|AlignmentProject
obj|Project|2
obj|MolList|2
obj|Object*|191
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\28:aotvoCD45_D2 (AAM48512) (3')|||||302453330|0|\36:CD45 phosphatase [Aotus vociferans].
end|2|2|
obj|String*|0
end
obj|String*|1|\31:Method: conceptual translation.
end
obj|String*|10|\34:REFERENCE   1  (residues 1 to 365)|\56:  AUTHORS   Montoya,G.E., Vernot,J.P. and Patarroyo,M.E.|\76:  TITLE     Partial characterization of the CD45 phosphatase cDNA in the owl|\35:            monkey Aotus vociferans|\23:  JOURNAL   Unpublished|\34:REFERENCE   2  (residues 1 to 365)|\56:  AUTHORS   Montoya,G.E., Vernot,J.P. and Patarroyo,M.E.|\29:  TITLE     Direct Submission|\75:  JOURNAL   Submitted (26-MAR-2001) Fisiologia Molecular, FIDIC, Avenida El|\58:            Dorado, Carrera 50. INEA, Bogota, DC, Colombia
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|300
obj|Object*|2
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|300|1|1|1|1|1..365
obj|String*|2|\28:/organism="Aotus vociferans"|\22:/db_xref="taxon:57176"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|300|1|1|1|1|<1..>365
obj|String*|1|\27:/product="CD45 phosphatase"
end|0||
obj|Object*|0
end
end
end|\300:nmkkrdppsepspleaefqrlpsyrswrtqhignqeenksknrnsnvipydfnrvplkhelemskesehdsdessdddsdseexskyinasfimxxwkpevmiaaqgplxetigdfwqmifqrkvkvivmltelkhgdqeicaqywgegkqtygdievdlkdtdksstytlrvfelrhskrkdsrtvyqyqytnwsvxxlpaxpkelismiqvxkqklpqknssegnkxhksxpllihcrdgsqqtgifcallnllesaeteevvdxfqvvkalrkarpgmxstfeqxqflydxiastyp|GenPept|
obj|String*|1|AAM48512
end||07-JUN-2002|\37:Aotus vociferans (noisy night monkey)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Aotus vociferans
end
obj|String*|0
end
obj|String*|0
end
obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Primates|Platyrrhini|Cebidae|Aotinae|Aotus
end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|\37:locus AF364095S2 accession AF364096.1
end
obj|String*|15|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29|\60:VNTI URL:vnti:protein/aotvoCD45_D2+%28AAM48512%29+%283%27%29
end
obj|String*|0
end
obj|String*|0
end
end|FBB7B0
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\22:bIA2_D1 (P56722) Ptprn|||||302454273|0|\94:Protein-tyrosine phosphatase-like N precursor (R-PTP-N) (Islet cell autoantigen 512) (ICA512).
end|2|2|
obj|String*|4|Receptor|Glycoprotein|Signal|Transmembrane
end
obj|String*|21|\67:-------------------------------------------------------------------|\60:This SWISS-PROT entry is copyright. It is produced through a|\63:collaboration between the Swiss Institute of Bioinformatics and|\60:the EMBL outstation - the European Bioinformatics Institute.|\63:The original entry is available from http://www.expasy.ch/sprot|\30:and http://www.ebi.ac.uk/sprot|\67:------------------------------------------------------------------.|\67:[FUNCTION] Implicated in neuroendocrine secretory processes. May be|\67:involved in processes specific for neurosecretory granules, such as|\67:their biogenesis, trafficking or regulated exocytosis or may have a|\64:general role in neuroendocrine functions. Lacks intrinsic enzyme|\65:activity. May play a role in the regulation of secretory granules|\47:via its interaction with SNTB2 (By similarity).|\65:[SUBUNIT] Interacts with phosphorylated SNTB2, protecting it from|\66:protein cleavage by CAPN1. Dephosphorylation of SNTB2 upon insulin|\64:stimulation disrupts the interaction and results in its cleavage|(By similarity).|\62:[SUBCELLULAR LOCATION] Type I membrane protein. Neuroendocrine|secretory granules.|\21:[PTM] N-glycosylated.|\60:[SIMILARITY] CONTAINS 1 PROTEIN-TYROSINE PHOSPHATASE DOMAIN.
end
obj|String*|12|\34:REFERENCE   1  (residues 1 to 979)|\50:  AUTHORS   Hermel,J.-M., Dirkx,R. and Solimena,M.|\29:  TITLE     Direct Submission|\33:  JOURNAL   Submitted (~JUN-1999)|\30:  REMARK    SEQUENCE FROM N.A.|\34:REFERENCE   2  (residues 1 to 979)|\53:  AUTHORS   Hermel,J.M., Dirkx,R. Jr. and Solimena,M.|\75:  TITLE     Post-translational modifications of ICA512, a receptor tyrosine|\58:            phosphatase-like protein of secretory granules|\54:  JOURNAL   Eur. J. Neurosci. 11 (8), 2609-2620 (1999)|  MEDLINE   99388259|\57:  REMARK    SEQUENCE OF N-TERMINUS, AND CHARACTERIZATION.
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|279
obj|Object*|6
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|279|1|1|1|1|1..979
obj|String*|2|\22:/organism="Bos taurus"|\21:/db_xref="taxon:9913"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRN|||||0|0|
end|270|270|||0|1|279|1|1|1|1|1..979
obj|String*|2|/gene="PTPRN"|\56:/product="Protein-tyrosine phosphatase-like N precursor"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRN|||||0|0|\36:PROTEIN-TYROSINE PHOSPHATASE-LIKE N.
end|203|203|||0|1|279|1|1|1|1|35..979
obj|String*|2|/gene="PTPRN"|\27:/region_name="Mature chain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRN|||||0|0|\24:CYTOPLASMIC (POTENTIAL).
end|1004|1004|||0|1|279|1|1|1|1|601..979
obj|String*|2|/gene="PTPRN"|\21:/region_name="Domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRN|||||0|0|\34:PROTEIN-TYROSINE PHOSPHATASE-LIKE.
end|1000|1000|||0|4|279|1|1|1|1|696..979
obj|String*|2|/gene="PTPRN"|\21:/region_name="Domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRN|||||0|0|BY SIMILARITY.
end|220|220|||0|217|217|1|1|1|1|909
obj|String*|2|/gene="PTPRN"|/site_type="active"
end|0||
obj|Object*|0
end
end
end|\279:hmilaymedhlrnrdrlakewqalcayqaepntcataqgegnikknrhpdflpydhariklkvesspsrsdyinaspiiehdprmpayiatqgplshtiadfwqmvwesgctvivmltplvedgvkqcdrywpdegsslyhvyevnlvsehiwcedflvrsfylknvqtqetrtltqfhflswpaegtpastrplldfrrkvnkcyrgrscpiivhcsdgagrtgtyilidmvlnrmakgvkeidiaatlehvrdqrpglvrskdqfefaltavaeevn|GenPept|
obj|String*|1|P56722
end||15-JUN-2002|Bos taurus (cow)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|1| PTPRN
end
obj|String*|1|Bos taurus
end
obj|String*|0
end
obj|String*|0
end
obj|String*|15|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Cetartiodactyla|Ruminantia|Pecora|Bovoidea|Bovidae|Bovinae|Bos
end
obj|Object*|0
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obj|String*|0
end
obj|String*|0
end
obj|String*|9|\46:swissprot: locus PTPN_BOVIN, accession P56722;|class: standard.|\22:created: May 30, 2000.|\31:sequence updated: May 30, 2000.|\33:annotation updated: Jun 15, 2002.|\31:xrefs: gi: 5305475, gi: 5305476|\62:xrefs (non-sequence databases): HSSPQ06124, InterProIPR000387,|\60:InterProIPR000242, PfamPF00102, PRINTSPR00700, SMARTSM00194,|\46:PROSITEPS00383, PROSITEPS50056, PROSITEPS50055
end
obj|String*|33|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29|\42:VNTI URL:vnti:protein/bIA2_D1+%28P56722%29
end
obj|String*|0
end
obj|String*|0
end
end|33549E8
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\30:bPTPBA14_D1 (NP_777015) PTPN13|||||307067825|0|\106:protein tyrosine phosphatase, non-receptor type 13 [APO-1/CD95 (Fas)-associated phosphatase] [Bos taurus].
end|2|2|
obj|String*|0
end
obj|String*|2|\65:PROVISIONAL REFSEQ: This record has not yet been subject to final|\62:NCBI review. The reference sequence was derived from U20807.1.
end
obj|String*|4|\35:REFERENCE   1  (residues 1 to 2484)|\49:  AUTHORS   Vega,Q.C., Walton,K.M. and Dixon,J.E.|\54:  TITLE     Tyrosine Phosphatases and the Cytoskeleton|\23:  JOURNAL   Unpublished
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||JNA||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|275
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|275|1|1|1|1|1..275
obj|String*|4|\22:/organism="Bos taurus"|\21:/db_xref="taxon:9913"|/chromosome="6"|/map="6"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|275|1|1|1|1|1..275
obj|String*|2|\57:/product="protein tyrosine phosphatase, non-receptor type|\45:13 [APO-1/CD95 (Fas)-associated phosphatase]"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Region_2|||||0|0|PTPc
end|266|266|||0|20|274|1|1|1|1|20..274
obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
end|0||
obj|Object*|0
end
end
end|\275:aklksvirmlrglldqgipskelenlqelkpldqcligqtkenrrknryknilpydatrvplgdeggyinasfikipvgreefvyiacqgplpttvgdfwqmiweqnssviammtqevegekikcqrywpnvlgkstmvsnrlrlalvrvqqlkgfvvramtlediqtgevrhvshlnftawpdhdtpsqpddlltfisymrhvhrsgpiithcsagigrsgtlicidvvlglisqdlefdisdlvrcmrlqrhgmvqtedqyifcyqvilyvlt|GenPept|
obj|String*|1|NP_777015
end||2-JUL-2003|Bos taurus (cow).
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Bos taurus
end
obj|String*|0
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obj|String*|0
end
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end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|\29:REFSEQ: accession NM_174590.1
end
obj|String*|37|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13|\56:VNTI URL:vnti:protein/bPTPBA14_D1+%28NP_777015%29+PTPN13
end
obj|String*|0
end
obj|String*|0
end
end|2901148
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||cCD45_D1 (A54080)|||||302463475|0|\84:protein-tyrosine-phosphatase (EC 3.1.3.48), receptor type delta precursor - chicken.
end|2|2|
obj|String*|3|phosphoprotein|\30:phosphoric monoester hydrolase|\29:tyrosine-specific phosphatase
end
obj|String*|0
end
obj|String*|6|\35:REFERENCE   1  (residues 1 to 1237)|\58:  AUTHORS   Fang,K.S., Barker,K., Sudol,M. and Hanafusa,H.|\79:  TITLE     A transmembrane protein-tyrosine phosphatase contains spectrin-like|\47:            repeats in its extracellular domain|\55:  JOURNAL   J. Biol. Chem. 269 (19), 14056-14063 (1994)|  MEDLINE   94245724
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|279
obj|Object*|6
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|279|1|1|1|1|1..1237
obj|String*|2|\25:/organism="Gallus gallus"|\21:/db_xref="taxon:9031"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|279|1|1|1|1|1..1237
obj|String*|3|\53:/product="protein-tyrosine-phosphatase, receptor type|delta precursor"|\21:/EC_number="3.1.3.48"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||LAC|||||0|0|\61:leukocyte common antigen cytosolic domain homology #label LAC
end|1000|1000|||0|1|279|1|1|1|1|528..1170
obj|String*|1|\21:/region_name="domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTP|||||0|0|\48:protein-tyrosine-phosphatase homology #label PTP
end|1000|1000|||0|42|266|1|1|1|1|610..834
obj|String*|1|\21:/region_name="domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Active_Site_1|||||0|0|\34:Cys (phosphocysteine intermediate)
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obj|Feature
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obj|String*|1|A54080
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obj|String*|0
end|0
obj|String*|0
end|PRT
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obj|String*|9|pir: locus A54080;|\61:summary: #length 1237 #molecular-weight 139319 #checksum 1986|;|\63:superfamily: leukocyte common antigen; leukocyte common antigen|\64:cytosolic domain homology; protein-tyrosine-phosphatase homology|;|\66:PIR dates: 02-Aug-1994 #sequence_revision 02-Aug-1994 #text_change|21-Jan-2000|.
end
obj|String*|48|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D1+%28A54080%29
end
obj|String*|0
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end|270C440
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||cCD45_D2 (A54080)|||||302464996|0|\84:protein-tyrosine-phosphatase (EC 3.1.3.48), receptor type delta precursor - chicken.
end|2|2|
obj|String*|3|phosphoprotein|\30:phosphoric monoester hydrolase|\29:tyrosine-specific phosphatase
end
obj|String*|0
end
obj|String*|6|\35:REFERENCE   1  (residues 1 to 1237)|\58:  AUTHORS   Fang,K.S., Barker,K., Sudol,M. and Hanafusa,H.|\79:  TITLE     A transmembrane protein-tyrosine phosphatase contains spectrin-like|\47:            repeats in its extracellular domain|\55:  JOURNAL   J. Biol. Chem. 269 (19), 14056-14063 (1994)|  MEDLINE   94245724
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|308
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|308|1|1|1|1|1..1237
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obj|Feature
obj|DBObj||Protein_1|||||0|0|
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obj|String*|3|\53:/product="protein-tyrosine-phosphatase, receptor type|delta precursor"|\21:/EC_number="3.1.3.48"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||LAC|||||0|0|\61:leukocyte common antigen cytosolic domain homology #label LAC
end|1000|1000|||0|1|308|1|1|1|1|528..1170
obj|String*|1|\21:/region_name="domain"
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end||21-JAN-2000|\23:Gallus gallus (chicken)
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end|0
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obj|String*|9|pir: locus A54080;|\61:summary: #length 1237 #molecular-weight 139319 #checksum 1986|;|\63:superfamily: leukocyte common antigen; leukocyte common antigen|\64:cytosolic domain homology; protein-tyrosine-phosphatase homology|;|\66:PIR dates: 02-Aug-1994 #sequence_revision 02-Aug-1994 #text_change|21-Jan-2000|.
end
obj|String*|15|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29|\43:VNTI URL:vnti:protein/cCD45_D2+%28A54080%29
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obj|String*|0
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obj|String*|0
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end|FB7768
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||cPTP1B_D1 (O13016)|||||302464650|0|\101:Protein-tyrosine phosphatase, non-receptor type 1 (Protein-tyrosine phosphatase 1B) (PTP-1B) (CPTP1).
end|2|2|
obj|String*|1|Hydrolase
end
obj|String*|14|\67:-------------------------------------------------------------------|\60:This SWISS-PROT entry is copyright. It is produced through a|\63:collaboration between the Swiss Institute of Bioinformatics and|\60:the EMBL outstation - the European Bioinformatics Institute.|\63:The original entry is available from http://www.expasy.ch/sprot|\30:and http://www.ebi.ac.uk/sprot|\67:------------------------------------------------------------------.|\65:[CATALYTIC ACTIVITY] PROTEIN TYROSINE PHOSPHATE + H(2)O = PROTEIN|\26:TYROSINE + ORTHOPHOSPHATE.|\66:[SUBCELLULAR LOCATION] ASSOCIATED TO THE ENDOPLASMIC RETICULUM VIA|\66:ITS C-TERMINAL DOMAIN WITH ITS PHOSPHATASE DOMAIN ORIENTED TOWARDS|\30:THE CYTOPLASM (BY SIMILARITY).|\53:[SIMILARITY] BELONGS TO THE NON-RECEPTOR CLASS OF THE|\36:PROTEIN-TYROSINE PHOSPHATASE FAMILY.
end
obj|String*|16|\34:REFERENCE   1  (residues 1 to 434)|\70:  AUTHORS   Balsamo,J., Leung,T., Ernst,H., Zanin,M.K., Hoffman,S. and|\21:            Lilien,J.|\78:  TITLE     Regulated binding of PTP1B-like phosphatase to N-cadherin: control|\78:            of cadherin-mediated adhesion by dephosphorylation of beta-catenin|\49:  JOURNAL   J. Cell Biol. 134 (3), 801-813 (1996)|  MEDLINE   96326683|\30:  REMARK    SEQUENCE FROM N.A.|\25:            TISSUE=Retina|\34:REFERENCE   2  (residues 1 to 434)|\46:  AUTHORS   Kim,C.W., Jung,E.J. and Kang,Y.-S.|\70:  TITLE     Cloning and characterization of a chicken protein tyrosine|\30:            phosphatase, CPTP1|\45:  JOURNAL   Exp. Mol. Med. 28, 207-213 (1996)|\40:  REMARK    SEQUENCE OF 14-369 FROM N.A.|\28:            TISSUE=Intestine
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|279
obj|Object*|6
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|279|1|1|1|1|1..434
obj|String*|2|\25:/organism="Gallus gallus"|\21:/db_xref="taxon:9031"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPN1|||||0|0|
end|270|270|||0|1|279|1|1|1|1|1..434
obj|String*|4|/gene="PTPN1"|\57:/product="Protein-tyrosine phosphatase, non-receptor type|1"|\21:/EC_number="3.1.3.48"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPN1|||||0|0|A -> R (IN REF. 2).
end|240|240|||0|14|14|1|1|1|1|14
obj|String*|2|/gene="PTPN1"|\23:/region_name="Conflict"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPN1|||||0|0|\29:PROTEIN-TYROSINE PHOSPHATASE.
end|1000|1000|||0|40|279|1|1|1|1|40..288
obj|String*|2|/gene="PTPN1"|\21:/region_name="Domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPN1|||||0|0|\21:GD -> RC (IN REF. 2).
end|240|240|||0|62|63|1|1|1|1|62..63
obj|String*|2|/gene="PTPN1"|\23:/region_name="Conflict"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPN1|||||0|0|
end|220|220|||0|215|215|1|1|1|1|215
obj|String*|2|/gene="PTPN1"|/site_type="active"
end|0||
obj|Object*|0
end
end
end|\279:meiekefhrldqaaswaaiyqdirheasdfpckvakhprnknrnryrdvspfdhsriklnqgdndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgsikcaqywprkeekemffedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpdfgvpespasflnflfkvresgslnpeygpvvvhcsagigrsgtfclvdtclllmdkrkdpssvdvkqvllemrkyrmgliqtadqlrfsylaviegak|GenPept|
obj|String*|1|O13016
end||16-OCT-2001|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|1| PTPN1
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obj|String*|0
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obj|String*|9|\46:swissprot: locus PTN1_CHICK, accession O13016;|class: standard.|\46:extra accessions:Q90704,created: Dec 15, 1998.|\31:sequence updated: Dec 15, 1998.|\33:annotation updated: Oct 16, 2001.|\57:xrefs: gi: 2058554, gi: 2058555, gi: 1209884, gi: 1209885|\62:xrefs (non-sequence databases): HSSPP18031, InterProIPR000387,|\60:InterProIPR000242, PfamPF00102, PRINTSPR00700, SMARTSM00194,|\46:PROSITEPS00383, PROSITEPS50056, PROSITEPS50055
end
obj|String*|35|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29|\44:VNTI URL:vnti:protein/cPTP1B_D1+%28O13016%29
end
obj|String*|0
end
obj|String*|0
end
end|342CB98
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\23:cPTPalpha_D1 (AAB04150)|||||302463254|0|\29:protein tyrosine phosphatase.
end|2|2|
obj|String*|0
end
obj|String*|1|\31:Method: conceptual translation.
end
obj|String*|5|\34:REFERENCE   1  (residues 1 to 807)|\21:  AUTHORS   Fang,K.S.|\78:  TITLE     Structural and functional characterization of two chicken tyrosine|\24:            phosphatases|\25:  JOURNAL   Thesis (1993)
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|280
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|280|1|1|1|1|1..807
obj|String*|5|\25:/organism="Gallus gallus"|\25:/sub_species="domesticus"|\21:/db_xref="taxon:9031"|/tissue_type="brain"|/dev_stage="E10"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|280|1|1|1|1|1..807
obj|String*|1|\39:/product="protein tyrosine phosphatase"
end|0||
obj|Object*|0
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obj|Feature
obj|DBObj||Chain_1|||||0|0|
end|203|203|||0|1|280|1|1|1|1|21..807
obj|String*|1|\39:/product="protein tyrosine phosphatase"
end|0||
obj|Object*|0
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end|\280:dkleeeinrrigddnklfreefnalpacpiqatceaaskeenkeknryvnilpydhsrvhltpvegvpdshyintsfinsyqeknkfiaaqgpkeetvndfwrmiweqntativmvtnlkerkeckcaqywpdqgcwtygnirvsvedvtvlvdytvrkfciqqvgdvtnkkpqrlvtqfhftswpdfgvpftpigmlkflkkvktcnpqyagaivvhcsagvgrtgtfividamldmmhaerkvdvygfvsriraqrcqmvqtdmqyvfiyqallehyl|GenPept|
obj|String*|1|AAB04150
end||23-JUL-1996|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Gallus gallus
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obj|String*|0
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obj|String*|0
end
obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Archosauria|Aves|Neognathae|Galliformes|Phasianidae|Phasianinae|Gallus
end
obj|Object*|0
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obj|String*|0
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obj|String*|0
end
obj|String*|1|\32:locus CHKPTPA accession L22437.1
end
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end
obj|String*|0
end
obj|String*|0
end
end|20FAF40
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\23:cPTPalpha_D2 (AAB04150)|||||302464946|0|\29:protein tyrosine phosphatase.
end|2|2|
obj|String*|0
end
obj|String*|1|\31:Method: conceptual translation.
end
obj|String*|5|\34:REFERENCE   1  (residues 1 to 807)|\21:  AUTHORS   Fang,K.S.|\78:  TITLE     Structural and functional characterization of two chicken tyrosine|\24:            phosphatases|\25:  JOURNAL   Thesis (1993)
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|281
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|281|1|1|1|1|1..807
obj|String*|5|\25:/organism="Gallus gallus"|\25:/sub_species="domesticus"|\21:/db_xref="taxon:9031"|/tissue_type="brain"|/dev_stage="E10"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|281|1|1|1|1|1..807
obj|String*|1|\39:/product="protein tyrosine phosphatase"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Chain_1|||||0|0|
end|203|203|||0|1|281|1|1|1|1|21..807
obj|String*|1|\39:/product="protein tyrosine phosphatase"
end|0||
obj|Object*|0
end
end
end|\281:tsleihlqkiynkvpgtssngleeefkkltsikiqndkmrtgnlpanmkknrvlqiipyefnrviipvkrgeentdyvnasfidgyrrrtptcqprpvqhtiedfwrmiwewkscsivmlteleergqekcaqywpsdgsvsygdinvelkkeeecesytvrdllvtntrenksrqirqfhfhgwpevgipsdgkgminiiaavqkqqqqsgnhpmhchcsagagrtgtfcalstvlervkaegildvfqtvkslrlqrphmvqtleqyefcykvvqeyid|GenPept|
obj|String*|1|AAB04150
end||23-JUL-1996|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Gallus gallus
end
obj|String*|0
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obj|String*|0
end
obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Archosauria|Aves|Neognathae|Galliformes|Phasianidae|Phasianinae|Gallus
end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|\32:locus CHKPTPA accession L22437.1
end
obj|String*|13|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29|\49:VNTI URL:vnti:protein/cPTPalpha_D2+%28AAB04150%29
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obj|String*|0
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obj|String*|0
end
end|24BC628
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\21:cPTPgamma_D1 (Q98936)|||||302464404|0|\59:Protein-tyrosine phosphatase gamma precursor (R-PTP-gamma).
end|2|2|
obj|String*|5|Glycoprotein|Transmembrane|Hydrolase|Repeat|Signal
end
obj|String*|14|\67:-------------------------------------------------------------------|\60:This SWISS-PROT entry is copyright. It is produced through a|\63:collaboration between the Swiss Institute of Bioinformatics and|\60:the EMBL outstation - the European Bioinformatics Institute.|\63:The original entry is available from http://www.expasy.ch/sprot|\30:and http://www.ebi.ac.uk/sprot|\67:------------------------------------------------------------------.|\65:[CATALYTIC ACTIVITY] Protein tyrosine phosphate + H(2)O = protein|\21:tyrosine + phosphate.|\58:[SUBCELLULAR LOCATION] Type I membrane protein (Probable).|\54:[SIMILARITY] IN THE N-TERMINAL SECTION; BELONGS TO THE|\42:EUKARYOTIC-TYPE CARBONIC ANHYDRASE FAMILY.|\61:[SIMILARITY] CONTAINS 2 PROTEIN-TYROSINE PHOSPHATASE DOMAINS.|\57:[SIMILARITY] CONTAINS 1 FIBRONECTIN TYPE III-LIKE DOMAIN.
end
obj|String*|7|\35:REFERENCE   1  (residues 1 to 1422)|\78:  AUTHORS   Qinghua,X., Xiaojun,G., Cong,S., Zong,S.M., Jong,Y.J., Chan,J. and|\22:            Wang,L.-H.|\29:  TITLE     Direct Submission|\33:  JOURNAL   Submitted (~OCT-1995)|\30:  REMARK    SEQUENCE FROM N.A.|\36:            TISSUE=Brain, and Kidney
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|291
obj|Object*|6
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|291|1|1|1|1|1..1422
obj|String*|2|\25:/organism="Gallus gallus"|\21:/db_xref="taxon:9031"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRG|||||0|0|
end|270|270|||0|1|291|1|1|1|1|1..1422
obj|String*|3|/gene="PTPRG"|\55:/product="Protein-tyrosine phosphatase gamma precursor"|\21:/EC_number="3.1.3.48"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRG|||||0|0|\35:PROTEIN-TYROSINE PHOSPHATASE GAMMA.
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obj|String*|2|/gene="PTPRG"|\27:/region_name="Mature chain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRG|||||0|0|\24:CYTOPLASMIC (POTENTIAL).
end|1004|1004|||0|1|291|1|1|1|1|769..1422
obj|String*|2|/gene="PTPRG"|\21:/region_name="Domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRG|||||0|0|\31:PROTEIN-TYROSINE PHOSPHATASE 1.
end|1000|1000|||0|39|291|1|1|1|1|846..1102
obj|String*|2|/gene="PTPRG"|\21:/region_name="Domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRG|||||0|0|BY SIMILARITY.
end|220|220|||0|230|230|1|1|1|1|1037
obj|String*|2|/gene="PTPRG"|/site_type="active"
end|0||
obj|Object*|0
end
end
end|\291:kqfvkhiselysnnqhgfsedfeevqrctadmnitaehsnhpdnkhknryinilaydhsrvklrplpgkdskhsdyinanyvsgynkakayiatqgplkstfedfwrmiwaqhtgiivmitnlvekgrrkcdqywptenseeygniivtlkstnihacytvrplhgqehkdekgserkpkgrqnertviqyhytqwpdmgvpeyalpvltfvrrssaartphmgpvvvhcsagvgrtgtyividsmlqqikdkstvnvlgflkhirtqrnylvqteeqyifihdalleail|GenPept|
obj|String*|1|Q98936
end||15-JUN-2002|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|1| PTPRG
end
obj|String*|1|Gallus gallus
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obj|String*|0
end
obj|String*|0
end
obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Archosauria|Aves|Neognathae|Galliformes|Phasianidae|Phasianinae|Gallus
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obj|String*|11|\46:swissprot: locus PTPG_CHICK, accession Q98936;|class: standard.|\22:created: Jul 15, 1999.|\31:sequence updated: Jul 15, 1999.|\33:annotation updated: Jun 15, 2002.|\31:xrefs: gi: 1617477, gi: 1617478|\62:xrefs (non-sequence databases): HSSPP18052, InterProIPR001148,|\56:InterProIPR003961, InterProIPR000387, InterProIPR000242,|\53:PfamPF00041, PfamPF00102, PfamPF00194, PRINTSPR00700,|\59:ProDomPD000865, SMARTSM00060, SMARTSM00194, PROSITEPS00383,|\30:PROSITEPS50056, PROSITEPS50055
end
obj|String*|49|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D1+%28Q98936%29
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end|21ED558
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\21:cPTPgamma_D2 (Q98936)|||||302464892|0|\59:Protein-tyrosine phosphatase gamma precursor (R-PTP-gamma).
end|2|2|
obj|String*|5|Glycoprotein|Transmembrane|Hydrolase|Repeat|Signal
end
obj|String*|14|\67:-------------------------------------------------------------------|\60:This SWISS-PROT entry is copyright. It is produced through a|\63:collaboration between the Swiss Institute of Bioinformatics and|\60:the EMBL outstation - the European Bioinformatics Institute.|\63:The original entry is available from http://www.expasy.ch/sprot|\30:and http://www.ebi.ac.uk/sprot|\67:------------------------------------------------------------------.|\65:[CATALYTIC ACTIVITY] Protein tyrosine phosphate + H(2)O = protein|\21:tyrosine + phosphate.|\58:[SUBCELLULAR LOCATION] Type I membrane protein (Probable).|\54:[SIMILARITY] IN THE N-TERMINAL SECTION; BELONGS TO THE|\42:EUKARYOTIC-TYPE CARBONIC ANHYDRASE FAMILY.|\61:[SIMILARITY] CONTAINS 2 PROTEIN-TYROSINE PHOSPHATASE DOMAINS.|\57:[SIMILARITY] CONTAINS 1 FIBRONECTIN TYPE III-LIKE DOMAIN.
end
obj|String*|7|\35:REFERENCE   1  (residues 1 to 1422)|\78:  AUTHORS   Qinghua,X., Xiaojun,G., Cong,S., Zong,S.M., Jong,Y.J., Chan,J. and|\22:            Wang,L.-H.|\29:  TITLE     Direct Submission|\33:  JOURNAL   Submitted (~OCT-1995)|\30:  REMARK    SEQUENCE FROM N.A.|\36:            TISSUE=Brain, and Kidney
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||JNA||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|283
obj|Object*|6
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|283|1|1|1|1|1..1422
obj|String*|2|\25:/organism="Gallus gallus"|\21:/db_xref="taxon:9031"
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obj|Object*|0
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obj|Feature
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obj|Feature
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obj|Feature
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end|0||
obj|Object*|0
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obj|Feature
obj|DBObj||PTPRG|||||0|0|\31:PROTEIN-TYROSINE PHOSPHATASE 2.
end|1000|1000|||0|1|283|1|1|1|1|1103..1422
obj|String*|2|/gene="PTPRG"|\21:/region_name="Domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRG|||||0|0|\22:ANCESTRAL ACTIVE SITE.
end|265|265|||0|222|222|1|1|1|1|1328
obj|String*|2|/gene="PTPRG"|\25:/site_type="unclassified"
end|0||
obj|Object*|0
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obj|String*|1|Q98936
end||15-JUN-2002|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
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obj|String*|11|\46:swissprot: locus PTPG_CHICK, accession Q98936;|class: standard.|\22:created: Jul 15, 1999.|\31:sequence updated: Jul 15, 1999.|\33:annotation updated: Jun 15, 2002.|\31:xrefs: gi: 1617477, gi: 1617478|\62:xrefs (non-sequence databases): HSSPP18052, InterProIPR001148,|\56:InterProIPR003961, InterProIPR000387, InterProIPR000242,|\53:PfamPF00041, PfamPF00102, PfamPF00194, PRINTSPR00700,|\59:ProDomPD000865, SMARTSM00060, SMARTSM00194, PROSITEPS00383,|\30:PROSITEPS50056, PROSITEPS50055
end
obj|String*|7|\47:VNTI URL:vnti:protein/cPTPgamma_D2+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D2+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D2+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D2+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D2+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D2+%28Q98936%29|\47:VNTI URL:vnti:protein/cPTPgamma_D2+%28Q98936%29
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end|28A56A8
end
obj|IxMolX
obj|Molecule
obj|BioObject
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end|2|2|
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end
obj|String*|0
end
obj|String*|6|\35:REFERENCE   1  (residues 1 to 1499)|\23:  AUTHORS   Stoker,A.W.|\76:  TITLE     Isoforms of a novel cell adhesion molecule-like protein tyrosine|\60:            phosphatase are implicated in neural development|\45:  JOURNAL   Mech. Dev. 46 (3), 201-217 (1994)|  MEDLINE   95001563
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
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obj|Feature
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obj|Feature
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end
obj|Feature
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end|1000|1000|||0|1|275|1|1|1|1|1..275
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end|0||
obj|Object*|0
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obj|Feature
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obj|Feature
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end|1007|1007|||0|220|220|1|1|1|1|220..220
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obj|String*|1|I50212
end||17-MAY-2003|\24:Gallus gallus (chicken).
obj|String*|0
end|0
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obj|String*|13|pir: locus I50212;|\61:summary: #length 1499 #molecular-weight 168570 #checksum 8393|;|\25:genetic: #gene CRYPalpha1|;|\64:superfamily: leukocyte antigen-related protein; fibronectin type|\62:III repeat homology; immunoglobulin homology; leukocyte common|\63:antigen cytosolic domain homology; protein-tyrosine-phosphatase|homology|;|\66:PIR dates: 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change|21-Jan-2000|.
end
obj|String*|54|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D1+%28I50212%29
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end|F89CF0
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\21:cPTPsigma_D2 (I50212)|||||302465404|0|\53:protein-tyrosine-phosphatase (EC 3.1.3.48) - chicken.
end|2|2|
obj|String*|3|phosphoprotein|\30:phosphoric monoester hydrolase|\29:tyrosine-specific phosphatase
end
obj|String*|0
end
obj|String*|6|\35:REFERENCE   1  (residues 1 to 1499)|\23:  AUTHORS   Stoker,A.W.|\76:  TITLE     Isoforms of a novel cell adhesion molecule-like protein tyrosine|\60:            phosphatase are implicated in neural development|\45:  JOURNAL   Mech. Dev. 46 (3), 201-217 (1994)|  MEDLINE   95001563
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||JNA||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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end|1|0|282
obj|Object*|6
obj|Feature
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end|269|269|||0|1|282|1|1|1|1|1..1499
obj|String*|2|\25:/organism="Gallus gallus"|\21:/db_xref="taxon:9031"
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obj|Object*|0
end
end
obj|Feature
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end|270|270|||0|1|282|1|1|1|1|1..1499
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end|0||
obj|Object*|0
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end
obj|Feature
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end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTP2|||||0|0|\49:protein-tyrosine-phosphatase homology #label PTP2
end|1000|1000|||0|47|269|1|1|1|1|1257..1479
obj|String*|1|\21:/region_name="domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Active_Site_2|||||0|0|\34:Cys (phosphocysteine intermediate)
end|220|220|||0|222|222|1|1|1|1|1432
obj|String*|1|/site_type="active"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Binding_2|||||0|0|\25:substrate phosphate (Arg)
end|1007|1007|||0|228|228|1|1|1|1|1438
obj|String*|1|/site_type="binding"
end|0||
obj|Object*|0
end
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end|\282:rnlytyiqklaqievgehvtgmelefkrlanskahtsrfisanlpcnkfknrlvnimpyettrvclqpirgvegsdyinasfidgyrqqkayiatqgplaettedfwrmlwennstivvmltklremgrekchqywpaersaryqyfvvdpmaeynmpqyilrefkvtdardgqsrtvrqfqftdwpeqgvpksgegfidfigqvhktkeqfgqdgpisvhcsagvgrtgvfitlsivlermryegvvdifqtvkmlrtqpamvqtedeyqfcyqaaleylg|GenPept|
obj|String*|1|I50212
end||21-JAN-2000|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Gallus gallus
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obj|String*|0
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obj|String*|0
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obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Archosauria|Aves|Neognathae|Galliformes|Phasianidae|Phasianinae|Gallus
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obj|String*|13|pir: locus I50212;|\61:summary: #length 1499 #molecular-weight 168570 #checksum 8393|;|\25:genetic: #gene CRYPalpha1|;|\64:superfamily: leukocyte antigen-related protein; fibronectin type|\62:III repeat homology; immunoglobulin homology; leukocyte common|\63:antigen cytosolic domain homology; protein-tyrosine-phosphatase|homology|;|\66:PIR dates: 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change|21-Jan-2000|.
end
obj|String*|9|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29|\47:VNTI URL:vnti:protein/cPTPsigma_D2+%28I50212%29
end
obj|String*|0
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obj|String*|0
end
end|28C7478
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\22:cPTPzeta_D1 (AAA49015)|||||302464518|0|\27:phosphotyrosyl phosphatase.
end|2|2|
obj|String*|0
end
obj|String*|1|\31:Method: conceptual translation.
end
obj|String*|8|\34:REFERENCE   1  (residues 1 to 832)|\72:  AUTHORS   Rowley,R.B., Lee,J.M., Corbeil,H.B., Charbonneau,R., Jue,K.,|\41:            Dankort,D.L. and Branton,P.E.|\78:  TITLE     Isolation of chicken phosphotyrosyl phosphatase cDNA sequences and|\75:            identification of a brain-specific species related to human PTP|            zeta|\56:  JOURNAL   Cell. Mol. Biol. Res. 39 (3), 209-219 (1993)|  MEDLINE   94122757
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obj|Object*|0
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|286
obj|Object*|2
obj|Feature
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obj|String*|6|\25:/organism="Gallus gallus"|\25:/sub_species="domesticus"|\21:/db_xref="taxon:9031"|\21:/tissue_type="embryo"|/dev_stage="10 day"|\30:/tissue_lib="Clontech CL1001b"
end|0||
obj|Object*|0
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obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|286|1|1|1|1|1..832
obj|String*|1|\37:/product="phosphotyrosyl phosphatase"
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obj|Object*|0
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end|\286:khfpkhvadlhasngfseefeeiqsctvdlgitsdssnhpdnknknryinivaydhtrvklaqlaekdgkltdyinanyvdgynkpkayiaaqgplkstaedfwrmiwehnvevivmitnllekgrrkcdqywpaegseeygnflvtqksvhvlayytvrnftlrntkikkgsqkgrssgrvvtqyhytqwpdmgvpeytlpvltfvrkashakrhavgpivvhcsagvgrtgtyvvldsmlqqiqhegtvnifgflkhirtqrnylvqteeqyifihdalveail|GenPept|
obj|String*|1|AAA49015
end||14-JAN-1994|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
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end
obj|String*|1|Gallus gallus
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obj|String*|0
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obj|String*|0
end
obj|String*|1|\35:locus CHKPHOPHOS accession L27625.1
end
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obj|IxMolX
obj|Molecule
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end
obj|String*|8|\34:REFERENCE   1  (residues 1 to 832)|\72:  AUTHORS   Rowley,R.B., Lee,J.M., Corbeil,H.B., Charbonneau,R., Jue,K.,|\41:            Dankort,D.L. and Branton,P.E.|\78:  TITLE     Isolation of chicken phosphotyrosyl phosphatase cDNA sequences and|\75:            identification of a brain-specific species related to human PTP|            zeta|\56:  JOURNAL   Cell. Mol. Biol. Res. 39 (3), 209-219 (1993)|  MEDLINE   94122757
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||JNA||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|282
obj|Object*|2
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|282|1|1|1|1|1..832
obj|String*|6|\25:/organism="Gallus gallus"|\25:/sub_species="domesticus"|\21:/db_xref="taxon:9031"|\21:/tissue_type="embryo"|/dev_stage="10 day"|\30:/tissue_lib="Clontech CL1001b"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|282|1|1|1|1|1..832
obj|String*|1|\37:/product="phosphotyrosyl phosphatase"
end|0||
obj|Object*|0
end
end
end|\282:thihayvnallipgptgktrlekqfkllsqsntqqcdystalkqcnreknrtssiipversrvgisslsgegtdyinasyimgyyqsnefiitqhpllhtikdfwrmiwdhnaqlivmlpdsqnmaedefvywpnkdepincetfkvtmiaeehkclskeekliiqdfileatqddyvlevrhfqcpkwpnpdspisktfelisiikeetsnrdgpmivhdehggvtagtfcalttlmhqlenensvdvyqvakminlmrpgvftdieqyqflykailslvs|GenPept|
obj|String*|1|AAA49015
end||14-JAN-1994|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Gallus gallus
end
obj|String*|0
end
obj|String*|0
end
obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Archosauria|Aves|Neognathae|Galliformes|Phasianidae|Phasianinae|Gallus
end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|\35:locus CHKPHOPHOS accession L27625.1
end
obj|String*|7|\48:VNTI URL:vnti:protein/cPTPzeta_D2+%28AAA49015%29|\48:VNTI URL:vnti:protein/cPTPzeta_D2+%28AAA49015%29|\48:VNTI URL:vnti:protein/cPTPzeta_D2+%28AAA49015%29|\48:VNTI URL:vnti:protein/cPTPzeta_D2+%28AAA49015%29|\48:VNTI URL:vnti:protein/cPTPzeta_D2+%28AAA49015%29|\48:VNTI URL:vnti:protein/cPTPzeta_D2+%28AAA49015%29|\48:VNTI URL:vnti:protein/cPTPzeta_D2+%28AAA49015%29
end
obj|String*|0
end
obj|String*|0
end
end|2991C90
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||cSHP2_D1 (JC5167)|||||302464602|0|\74:protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 11 - chicken.
end|2|2|
obj|String*|3|phosphoprotein|\30:phosphoric monoester hydrolase|\29:tyrosine-specific phosphatase
end
obj|String*|2|\65:This enzyme plays positive roles in mitogenic signaling and early|development.
end
obj|String*|7|\34:REFERENCE   1  (residues 1 to 593)|\66:  AUTHORS   Park,C.Y., LaMontagne,K.R., Tonks,N.K. and Hayman,M.J.|\78:  TITLE     Cloning and expression of the chicken protein tyrosine phosphatase|            SH-PTP2|\40:  JOURNAL   Gene 177 (1-2), 93-97 (1996)|  MEDLINE   97080506|\24:  REMARK    erythroblast
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|300
obj|Object*|5
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|300|1|1|1|1|1..593
obj|String*|2|\25:/organism="Gallus gallus"|\21:/db_xref="taxon:9031"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|\55:phosphotyrosine phosphatase; PTP1D; PTP2c; SH-PTP2; SyP
end|270|270|||0|1|300|1|1|1|1|1..593
obj|String*|3|\56:/product="protein-tyrosine-phosphatase, nonreceptor type|11"|\21:/EC_number="3.1.3.48"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTP|||||0|0|\48:protein-tyrosine-phosphatase homology #label PTP
end|1000|1000|||0|50|287|1|1|1|1|273..510
obj|String*|1|\21:/region_name="domain"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Active_Site_1|||||0|0|\34:Cys (phosphocysteine intermediate)
end|220|220|||0|236|236|1|1|1|1|459
obj|String*|1|/site_type="active"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Binding_1|||||0|0|\25:substrate phosphate (Arg)
end|1007|1007|||0|242|242|1|1|1|1|465
obj|String*|1|/site_type="binding"
end|0||
obj|Object*|0
end
end
end|\300:aeiesrvrelsklaettdkvkqgfweefetlqqqeckllysrkegqrqenknknryknilpfdhtrvvlhdgdpnepvsdyinaniimpefetkcnnskpkksyiatqgclqntvndfwrmvfqensrvivmttkevergkskcvkywpdeyslkeygvmrvrnvkesaahdytlrelklskvgqgntertvwqyhfrtwpdhgvpsdpggvldfleevhhkqesisdagpvvvhcsagigrtgtfividilidiirekgvdcdidvpktiqmvrsqrsgmvqteaqyrfiymavqhyie|GenPept|
obj|String*|1|JC5167
end||16-JUL-1999|\23:Gallus gallus (chicken)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Gallus gallus
end
obj|String*|0
end
obj|String*|0
end
obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Archosauria|Aves|Neognathae|Galliformes|Phasianidae|Phasianinae|Gallus
end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|9|pir: locus JC5167;|\59:summary: #length 593 #molecular-weight 67982 #checksum 3712|;|\62:superfamily: protein-tyrosine-phosphatase, nonreceptor type 6;|\51:protein-tyrosine-phosphatase homology; SH2 homology|;|\66:PIR dates: 21-Feb-1997 #sequence_revision 27-Feb-1997 #text_change|16-Jul-1999|.
end
obj|String*|51|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29|\43:VNTI URL:vnti:protein/cSHP2_D1+%28JC5167%29
end
obj|String*|0
end
obj|String*|0
end
end|2052590
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\23:cypcaCD45_D1 (BAA92179)|||||302454614|0|\23:CD45 [Cyprinus carpio].
end|2|2|
obj|String*|0
end
obj|String*|0
end
obj|String*|15|REFERENCE   1|\54:  AUTHORS   Fujiki,K., Shin,D.H., Nakao,M. and Yano,T.|\78:  TITLE     Molecular cloning of carp (Cyprinus carpio) leucocyte cell-derived|\77:            chemotaxin 2, glia maturation factor beta, CD45 and lysozyme C by|\56:            use of suppression subtractive hybridisation|\58:  JOURNAL   Fish Shellfish Immunol. 10 (7), 643-650 (2000)|  MEDLINE   20531692|\35:REFERENCE   2  (residues 1 to 1216)|\52:  AUTHORS   Fujiki,K., Nakao,M., Shin,D. and Yano,T.|\29:  TITLE     Direct Submission|\71:  JOURNAL   Submitted (24-AUG-1999) Kazuhiro Fujiki, Kyushu University,|\79:            Laboratory of Marine Biochemistry, Faculty of Agriculture; Hakozaki|\64:            6-10-1, Higashi-ku, Fukuoka, Fukuoka 812-8581, Japan|\67:            (E-mail:fujikik@agr.kyushu-u.ac.jp, Tel:81-92-642-2896,|\31:            Fax:81-92-642-2894)
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|276
obj|Object*|2
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|276|1|1|1|1|1..1216
obj|String*|3|\27:/organism="Cyprinus carpio"|\21:/db_xref="taxon:7962"|\23:/cell_type="leukocytes"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|276|1|1|1|1|1..1216
obj|String*|1|/product="CD45"
end|0||
obj|Object*|0
end
end
end|\276:gglveayknkiadegrlfmdefqsiprifsnytikeakksenqyknryvdilpydynrvtlstggednyinasfiegyrepkkyiaaqgpkdetvvdfwrmvweqkssiivmvtrceegnktkcaqywpsldreaeifeefvvkirseehcpdyvirhlilnnkrekgserevthiqfiswpdhgvpgdpslllklrrrvnsfknffsgpvvvhcsagvgrtgtymsidamiesleaegrvdiygfvaklrrqrclmvqveaqyilihtalieynq|GenPept|
obj|String*|1|BAA92179
end||17-APR-2002|\29:Cyprinus carpio (common carp)
obj|String*|0
end|0
obj|String*|0
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obj|String*|0
end
obj|String*|1|Cyprinus carpio
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obj|String*|0
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obj|String*|0
end
obj|String*|13|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Actinopterygii|Neopterygii|Teleostei|Ostariophysi|Cypriniformes|Cyprinidae|Cyprinus
end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|accession AB031424.1
end
obj|String*|48|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D1+%28BAA92179%29
end
obj|String*|0
end
obj|String*|0
end
end|270C158
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\23:cypcaCD45_D2 (BAA92179)|||||302454709|0|\23:CD45 [Cyprinus carpio].
end|2|2|
obj|String*|0
end
obj|String*|0
end
obj|String*|15|REFERENCE   1|\54:  AUTHORS   Fujiki,K., Shin,D.H., Nakao,M. and Yano,T.|\78:  TITLE     Molecular cloning of carp (Cyprinus carpio) leucocyte cell-derived|\77:            chemotaxin 2, glia maturation factor beta, CD45 and lysozyme C by|\56:            use of suppression subtractive hybridisation|\58:  JOURNAL   Fish Shellfish Immunol. 10 (7), 643-650 (2000)|  MEDLINE   20531692|\35:REFERENCE   2  (residues 1 to 1216)|\52:  AUTHORS   Fujiki,K., Nakao,M., Shin,D. and Yano,T.|\29:  TITLE     Direct Submission|\71:  JOURNAL   Submitted (24-AUG-1999) Kazuhiro Fujiki, Kyushu University,|\79:            Laboratory of Marine Biochemistry, Faculty of Agriculture; Hakozaki|\64:            6-10-1, Higashi-ku, Fukuoka, Fukuoka 812-8581, Japan|\67:            (E-mail:fujikik@agr.kyushu-u.ac.jp, Tel:81-92-642-2896,|\31:            Fax:81-92-642-2894)
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|302
obj|Object*|2
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|302|1|1|1|1|1..1216
obj|String*|3|\27:/organism="Cyprinus carpio"|\21:/db_xref="taxon:7962"|\23:/cell_type="leukocytes"
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obj|Feature
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end|270|270|||0|1|302|1|1|1|1|1..1216
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obj|Object*|0
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end|\302:sefhsvlntlrqkngsdpsllekefqklpkfkkwrtmntgssednkkknrdsavipydfnrvifrldiegnqtsdpedeeeyssdeeeesnqyinasfidgywcnksliaaqgplqstaeefllmlyqqqtktlvmltdcqedgkdycfqywgdekktygdmeievkktetfptyvrrhleiqslkkkevlkvdqyqflkwrgrelpenaqelvemasiirenghydnsktnrnvpivvhcnngssrtgifcalwnlldsayteklvdvlqevknlrklrqgmvetieqyqflytalegafp|GenPept|
obj|String*|1|BAA92179
end||17-APR-2002|\29:Cyprinus carpio (common carp)
obj|String*|0
end|0
obj|String*|0
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obj|String*|0
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end
obj|Object*|0
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obj|String*|0
end
obj|String*|1|accession AB031424.1
end
obj|String*|15|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29|\49:VNTI URL:vnti:protein/cypcaCD45_D2+%28BAA92179%29
end
obj|String*|0
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obj|String*|0
end
end|F9FA00
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||fuCD45_D1 (CAB96211)|||||302488418|0|\25:CD45 [Takifugu rubripes].
end|2|2|
obj|String*|0
end
obj|String*|0
end
obj|String*|12|REFERENCE   1|\58:  AUTHORS   Diaz del Pozo,E.M., Beverley,P.C. and Timon,M.|\74:  TITLE     Genomic structure and sequence of the leukocyte common antigen|\76:            (CD45) from the pufferfish Fugu rubripes and comparison with its|\31:            mammalian homologue|\23:  JOURNAL   Unpublished|\35:REFERENCE   2  (residues 1 to 1246)|\30:  AUTHORS   Diaz del Pozo,E.M.|\29:  TITLE     Direct Submission|\78:  JOURNAL   Submitted (25-JUN-1999) Diaz del Pozo E.M., CD45 Group, The Edward|\72:            Jenner Institute for Vaccine Research, High Street, Compton,|\56:            Newbury, Berkshire, RG20 7NN, UNITED KINGDOM
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|279
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|279|1|1|1|1|1..1246
obj|String*|4|\29:/organism="Takifugu rubripes"|\22:/db_xref="taxon:31033"|/clone="ptp-16"|\21:/tissue_type="spleen"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|279|1|1|1|1|1..1246
obj|String*|3|/product="CD45"|\21:/EC_number="3.1.3.48"|\40:/function="protein tyrosine phosphatase"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Chain_1|||||0|0|
end|203|203|||0|1|279|1|1|1|1|20..1246
obj|String*|2|/product="CD45"|\21:/EC_number="3.1.3.48"
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end|\279:etlldaykrkiadegrlflaefqsiprifskytvkeakkshnvpknryvdilpydynrvqlttgngsagcdyinasfidgfkelkkyiaaqgpkeetvsnfwrmiweqqtsiivmvsrceegnrikcaqywpsedrdteifeefivkltsedhypdyiirhlsltnkkdkgserevthiqfmswpdhgvpeeaqlllklrrrvnsfknffsgpivvhcsagvgrtgtyigidammesleaegrvdiygyvvmlrrqrclmvqveaqyilihqallehtq|GenPept|
obj|String*|1|CAB96211
end||03-JUL-2000|Takifugu rubripes
obj|String*|0
end|0
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end|PRT
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end
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end
obj|String*|0
end
obj|String*|0
end
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end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|\42:embl locus FRU243429, accession AJ243429.1
end
obj|String*|48|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D1+%28CAB96211%29
end
obj|String*|0
end
obj|String*|0
end
end|278FC28
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||fuCD45_D2 (CAB96211)|||||302488507|0|\25:CD45 [Takifugu rubripes].
end|2|2|
obj|String*|0
end
obj|String*|0
end
obj|String*|12|REFERENCE   1|\58:  AUTHORS   Diaz del Pozo,E.M., Beverley,P.C. and Timon,M.|\74:  TITLE     Genomic structure and sequence of the leukocyte common antigen|\76:            (CD45) from the pufferfish Fugu rubripes and comparison with its|\31:            mammalian homologue|\23:  JOURNAL   Unpublished|\35:REFERENCE   2  (residues 1 to 1246)|\30:  AUTHORS   Diaz del Pozo,E.M.|\29:  TITLE     Direct Submission|\78:  JOURNAL   Submitted (25-JUN-1999) Diaz del Pozo E.M., CD45 Group, The Edward|\72:            Jenner Institute for Vaccine Research, High Street, Compton,|\56:            Newbury, Berkshire, RG20 7NN, UNITED KINGDOM
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|301
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|301|1|1|1|1|1..1246
obj|String*|4|\29:/organism="Takifugu rubripes"|\22:/db_xref="taxon:31033"|/clone="ptp-16"|\21:/tissue_type="spleen"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|301|1|1|1|1|1..1246
obj|String*|3|/product="CD45"|\21:/EC_number="3.1.3.48"|\40:/function="protein tyrosine phosphatase"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Chain_1|||||0|0|
end|203|203|||0|1|301|1|1|1|1|20..1246
obj|String*|2|/product="CD45"|\21:/EC_number="3.1.3.48"
end|0||
obj|Object*|0
end
end
end|\301:qelhstlntlkqrssdneptlledeferlpnfknwrtfntgvteenkkknrtssvipydynrvllkldeekshesdpdpdddydtssyddiedsakyinasllsgywgphtfisaqtplpdtvadfwsmilqkrvsivvmlsdcsqgdedcvywgedkktvedievetestdnspnfilrnmmihhlktdahqqvkhfqflkwgdkevpekpqdladlikeikhrcgytwprstpiivhcndgssrsgafcalwnlldnaekekmvdvfqvvktlrkerqgmcpsleqyqflydalevvyp|GenPept|
obj|String*|1|CAB96211
end||03-JUL-2000|Takifugu rubripes
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Takifugu rubripes
end
obj|String*|0
end
obj|String*|0
end
obj|String*|18|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Actinopterygii|Neopterygii|Teleostei|Euteleostei|Neoteleostei|Acanthomorpha|Acanthopterygii|Percomorpha|Tetraodontiformes|Tetradontoidea|Tetraodontidae|Takifugu
end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|\42:embl locus FRU243429, accession AJ243429.1
end
obj|String*|15|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29|\46:VNTI URL:vnti:protein/fuCD45_D2+%28CAB96211%29
end
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end
obj|String*|0
end
end|F99150
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\27:hBDP1_D1 (NP_055184) PTPN18|||||302014800|0|\93:protein tyrosine phosphatase, non-receptor type 18; brain-derived phosphatase [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|14|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X79568.1 and BI261717.1.|\58:On Jan 25, 2002 this sequence version replaced gi:7657484.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\63:oncogenic transformation. This PTP contains a PEST motif, which|\64:often serves as a protein-protein interaction domain, and may be|\66:related to protein intracellular half-live. This gene was found to|\59:be expressed in brain, colon tissues, and several different|\64:tumor-derived cell lines. The bilogical function of this PTP has|\24:not yet been determined.
end
obj|String*|7|\34:REFERENCE   1  (residues 1 to 460)|\69:  AUTHORS   Kim,Y.W., Wang,H., Sures,I., Lammers,R., Martell,K.J. and|\22:            Ullrich,A.|\76:  TITLE     Characterization of the PEST family protein tyrosine phosphatase|            BDP1|\46:  JOURNAL   Oncogene 13 (10), 2275-2279 (1996)|  MEDLINE   97108674
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|288
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|288|1|1|1|1|1..460
obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="2"|/map="2q21.2"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|\25:brain-derived phosphatase
end|270|270|||0|1|288|1|1|1|1|1..460
obj|String*|3|\57:/product="protein tyrosine phosphatase, non-receptor type|18"|\21:/EC_number="3.1.3.48"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Region_1|||||0|0|PTPc
end|266|266|||0|21|287|1|1|1|1|26..292
obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
end|0||
obj|Object*|0
end
end
end|\288:dsarsflerlearggregavlagefsdiqacsaawkadgvcstvagsrpenvrknrykdvlpydqtrvilsllqeeghsdyingnfirgvdgslayiatqgplphtlldfwrlvwefgvkvilmacreiengrkrcerywaqeqeplqtglfcitlikekwlnedimlrtlkvtfqkesrsvyqlqymswpdrgvpsspdhmlamveearrlqgsgpeplcvhcsagcgrtgvlctvdyvrqllltqmippdfslfdvvlkmrkqrpaavqteeqyrflyhtvaqmfc|GenPept|
obj|String*|1|NP_055184
end||07-MAY-2003|Homo sapiens (human)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Homo sapiens
end
obj|String*|0
end
obj|String*|0
end
obj|String*|12|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Primates|Catarrhini|Hominidae|Homo
end
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obj|String*|0
end
obj|String*|1|\29:REFSEQ: accession NM_014369.2
end
obj|String*|44|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18|\53:VNTI URL:vnti:protein/hBDP1_D1+%28NP_055184%29+PTPN18
end
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obj|String*|0
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end|2927B70
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\26:hCD45_D1 (NP_002829) PTPRC|||||302014800|0|\306:protein tyrosine phosphatase, receptor type, C isoform 1 precursor; protein tyrosine phosphatase, receptor type, c polypeptide; leukocyte-common antigen; T200 glycoprotein; human homolog of severe combined immunodeficiency due to PTPRC deficiency; SCID due to PTPRC deficiency; CD45 antigen [Homo sapiens].
end|2|2|
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obj|String*|23|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\58:reference sequence was derived from Y00638.1 and Y00062.1.|\57:On Feb 8, 2002 this sequence version replaced gi:4506307.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\53:domain, a single transmembrane segment and two tandem|\64:intracytoplasmic catalytic domains, and thus belongs to receptor|\62:type PTP. This gene is specifically expressed in hematopoietic|\65:cells. This PTP has been shown to be an essential regulator of T-|\66:and B-cell antigen receptor signaling. It functions through either|\58:direct interaction with components of the antigen receptor|\67:complexes, or by activating various Src family kinases required for|\60:the antigen receptor signaling. This PTP also suppresses JAK|\63:kinases, and thus functions as a regulator of cytokine receptor|\66:signaling. Four alternatively spliced transcripts variants of this|\57:gene, which encode distinct isoforms, have been reported.||\64:Transcript Variant: This variant (1) encodes the longest isoform|(1).
end
obj|String*|212|\35:REFERENCE   1  (residues 1 to 1304)|\44:  AUTHORS   Baldwin,T.A. and Ostergaard,H.L.|\78:  TITLE     The protein-tyrosine phosphatase CD45 reaches the cell surface via|\53:            golgi-dependent and -independent pathways|\55:  JOURNAL   J. Biol. Chem. 277 (52), 50333-50340 (2002)|  MEDLINE   22384317|\69:  REMARK    GeneRIF: reaches the cell surface via Golgi-dependent and|\33:            -independent pathways|\35:REFERENCE   2  (residues 1 to 1304)|\71:  AUTHORS   Harashima,A., Suzuki,M., Okochi,A., Yamamoto,M., Matsuo,Y.,|\47:            Motoda,R., Yoshioka,T. and Orita,K.|\75:  TITLE     CD45 tyrosine phosphatase inhibits erythroid differentiation of|\70:            umbilical cord blood CD34+ cells associated with selective|\31:            inactivation of Lyn|\44:  JOURNAL   Blood 100 (13), 4440-4445 (2002)|  MEDLINE   22340750|\73:  REMARK    GeneRIF: CD45 may play a pivotal role in erythropoiesis. CD45|\70:            tyrosine phosphatase inhibits erythroid differentiation of|\70:            umbilical cord blood CD34+ cells associated with selective|\32:            inactivation of Lyn.|\35:REFERENCE   3  (residues 1 to 1304)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   4  (residues 1 to 1304)|\36:  AUTHORS   Pradhan,D. and Morrow,J.|\75:  TITLE     The spectrin-ankyrin skeleton controls CD45 surface display and|\36:            interleukin-2 production|\43:  JOURNAL   Immunity 17 (3), 303-315 (2002)|  MEDLINE   22241694|\72:  REMARK    GeneRIF: The spectrin-ankyrin skeleton controls CD45 surface|\49:            display and interleukin-2 production.|\35:REFERENCE   5  (residues 1 to 1304)|\73:  AUTHORS   Ballerini,C., Rosati,E., Salvetti,M., Ristori,G., Cannoni,S.,|\63:            Biagioli,T., Massacesi,L., Sorbi,S. and Vergelli,M.|\77:  TITLE     Protein tyrosine phosphatase receptor-type C exon 4 gene mutation|\68:            distribution in an Italian multiple sclerosis population|\51:  JOURNAL   Neurosci. Lett. 328 (3), 325-327 (2002)|  MEDLINE   22142931|\79:  REMARK    GeneRIF: Role of the C-->G mutation in position 77 of exon 4 of the|\77:            protein tyrosine phosphatase receptor-type C (PTPRC) gene, coding|\76:            for the CD45 molecule, for the development of multiple sclerosis|\26:            (MS) in Italy.|\35:REFERENCE   6  (residues 1 to 1304)|\52:  AUTHORS   Yamada,T., Zhu,D., Saxon,A. and Zhang,K.|\79:  TITLE     CD45 controls interleukin-4-mediated IgE class switch recombination|\79:            in human B cells through its function as a Janus kinase phosphatase|\55:  JOURNAL   J. Biol. Chem. 277 (32), 28830-28835 (2002)|  MEDLINE   22151051|\74:  REMARK    GeneRIF: CD45 controls interleukin-4-mediated IgE class switch|\42:            recombination in human B cells|\35:REFERENCE   7  (residues 1 to 1304)|\62:  AUTHORS   Yu,C., Yu,H.S., Sun,K.H., Hsieh,S.C. and Tsai,C.Y.|\70:  TITLE     Anti-CD45 isoform antibodies enhance phagocytosis and gene|\68:            expression of IL-8 and TNF-alpha in human neutrophils by|\76:            differential suppression on protein tyrosine phosphorylation and|\34:            p56lck tyrosine kinase|\53:  JOURNAL   Clin. Exp. Immunol. 129 (1), 78-85 (2002)|  MEDLINE   22095000|\77:  REMARK    GeneRIF: Biological functions of membrane expressed CD45 isoforms|\76:            on PMNs were studied. Cross-linking of CD45 isoforms by specific|\68:            MAbs stimulated different PMN activities by differential|\71:            suppression on protein tyrosine phosphorylation and p56lck.|\35:REFERENCE   8  (residues 1 to 1304)|\78:  AUTHORS   Jacobsen,M., Hoffmann,S., Cepok,S., Stei,S., Ziegler,A., Sommer,N.|\25:            and Hemmer,B.|\77:  TITLE     A novel mutation in PTPRC interferes with splicing and alters the|\48:            structure of the human CD45 molecule|\49:  JOURNAL   Immunogenetics 54 (3), 158-163 (2002)|  MEDLINE   22067726|\76:  REMARK    GeneRIF: a mutation in PTPRC interferes with splicing and alters|\46:            the structure of the CD45 molecule|\35:REFERENCE   9  (residues 1 to 1304)|\43:  AUTHORS   Tchilian,E.Z. and Beverley,P.C.|\38:  TITLE     CD45 in memory and disease|\67:  JOURNAL   Arch. Immunol. Ther. Exp. (Warsz.) 50 (2), 85-93 (2002)|  MEDLINE   22017393|\78:  REMARK    GeneRIF: Role of high and low molecular weight isoforms of CD45 in|\68:            the function of na##ve and memory T lymphocytes. Review.|\35:REFERENCE   10 (residues 1 to 1304)|\70:  AUTHORS   Fajka-Boja,R., Szemes,M., Ion,G., Legradi,A., Caron,M. and|\24:            Monostori,E.|\77:  TITLE     Receptor tyrosine phosphatase, CD45 binds galectin-1 but does not|\56:            mediate its apoptotic signal in T cell lines|\51:  JOURNAL   Immunol. Lett. 82 (1-2), 149-154 (2002)|  MEDLINE   22003829|\77:  REMARK    GeneRIF: Receptor tyrosine phosphatase, CD45 binds galectin-1 but|\65:            does not mediate its apoptotic signal in Jurkat cells|\35:REFERENCE   11 (residues 1 to 1304)|\79:  AUTHORS   Fukuhara,K., Okumura,M., Shiono,H., Inoue,M., Kadota,Y., Miyoshi,S.|\26:            and Matsuda,H.|\76:  TITLE     A study on CD45 isoform expression during T-cell development and|\48:            selection events in the human thymus|\48:  JOURNAL   Hum. Immunol. 63 (5), 394-404 (2002)|  MEDLINE   21972715|\70:  REMARK    GeneRIF: analysis of CD45 isoform expression during T-cell|\57:            development and selection in the human thymus|\35:REFERENCE   12 (residues 1 to 1304)|\38:  AUTHORS   Wu,L., Fu,J. and Shen,S.H.|\64:  TITLE     SKAP55 coupled with CD45 positively regulates T-cell|\48:            receptor-mediated gene transcription|\53:  JOURNAL   Mol. Cell. Biol. 22 (8), 2673-2686 (2002)|  MEDLINE   21907230|\73:  REMARK    GeneRIF: SKAP55 coupled with CD45 positively regulates T-cell|\49:            receptor-mediated gene transcription.|\35:REFERENCE   13 (residues 1 to 1304)|\77:  AUTHORS   Ishikawa,H., Tsuyama,N., Abroun,S., Liu,S., Li,F.J., Taniguchi,O.|\27:            and Kawano,M.M.|\79:  TITLE     Requirements of src family kinase activity associated with CD45 for|\55:            myeloma cell proliferation by interleukin-6|\42:  JOURNAL   Blood 99 (6), 2172-2178 (2002)|  MEDLINE   21866149|\79:  REMARK    GeneRIF: Requirements of src family kinase activity associated with|\64:            CD45 for myeloma cell proliferation by interleukin-6|\35:REFERENCE   14 (residues 1 to 1304)|\66:  AUTHORS   Tchilian,E.Z., Dawes,R., Ramaley,P.A., Whitworth,J.A.,|\72:            Yuldasheva,N., Wells,R.S., Watera,C., French,N., Gilks,C.F.,|\72:            Kunachiwa,W., Ruzibakiev,R., Leetrakool,N., Carrington,C.V.,|\78:            Ramdath,D.D., Gotch,F., Stephens,H.A., Hill,A.V. and Beverley,P.C.|\78:  TITLE     A CD45 polymorphism associated with abnormal splicing is absent in|\31:            African populations|\53:  JOURNAL   Immunogenetics 53 (10-11), 980-983 (2002)|  MEDLINE   21850514|\76:  REMARK    GeneRIF: we examined the frequency of the C77G allele in African|\79:            and Asian populations from countries with high or low prevalence of|\78:            HIV infection; Here we report that the variant CD45 C77G allele is|\41:            absent in African populations|\35:REFERENCE   15 (residues 1 to 1304)|\76:  AUTHORS   Wood,J.P., Bieda,K., Segni,M., Herwig,J., Krause,M., Usadel,K.H.|\28:            and Badenhoop,K.|\79:  TITLE     CD45 exon 4 point mutation does not confer susceptibility to type 1|\48:            diabetes mellitus or Graves' disease|\53:  JOURNAL   Eur. J. Immunogenet. 29 (1), 73-74 (2002)|  MEDLINE   21830605|\79:  REMARK    GeneRIF: CD45 variant (C77G, exon 4) does not confer susceptibility|\45:            to either IDDM or Graves' disease|\35:REFERENCE   16 (residues 1 to 1304)|\71:  AUTHORS   Moro,H., Iwai,K., Mori,N., Watanabe,M., Fukushi,M., Oie,M.,|\78:            Arai,M., Tanaka,Y., Miyawaki,T., Gejyo,F., Arakawa,M. and Fujii,M.|\77:  TITLE     Interleukin-2-dependent but not independent T-cell lines infected|\79:            with human T-cell leukemia virus type 1 selectively express CD45RO,|\53:            a marker for persistent infection in vivo|\46:  JOURNAL   Virus Genes 23 (3), 263-271 (2001)|  MEDLINE   21636965|\78:  REMARK    GeneRIF: role of CD45RO in the persistent HTLV-1 infection in vivo|\35:REFERENCE   17 (residues 1 to 1304)|\74:  AUTHORS   Irie-Sasaki,J., Sasaki,T., Matsumoto,W., Opavsky,A., Cheng,M.,|\79:            Welstead,G., Griffiths,E., Krawczyk,C., Richardson,C.D., Aitken,K.,|\74:            Iscove,N., Koretzky,G., Johnson,P., Liu,P., Rothstein,D.M. and|\26:            Penninger,J.M.|\71:  TITLE     CD45 is a JAK phosphatase and negatively regulates cytokine|\31:            receptor signalling|\45:  JOURNAL   Nature 409 (6818), 349-354 (2001)|  MEDLINE   21069057|\35:REFERENCE   18 (residues 1 to 1304)|\76:  AUTHORS   Goff,L.K., van Soest,S., Timon,M., Tchilian,E. and Beverley,P.C.|\79:  TITLE     Protein tyrosine phosphatase receptor type C polypeptide (PTPRC) on|\79:            human chromosome band 1q31-->q32 localizes with marker D1S413(1) on|\48:            a 610-kb yeast artificial chromosome|\59:  JOURNAL   Cytogenet. Cell Genet. 87 (3-4), 223-224 (1999)|  MEDLINE   20169194|\35:REFERENCE   19 (residues 1 to 1304)|\79:  AUTHORS   Petricoin,E.F. III, Ito,S., Williams,B.L., Audet,S., Stancato,L.F.,|\66:            Gamero,A., Clouse,K., Grimley,P., Weiss,A., Beeler,J.,|\66:            Finbloom,D.S., Shores,E.W., Abraham,R. and Larner,A.C.|\79:  TITLE     Antiproliferative action of interferon-alpha requires components of|\38:            T-cell-receptor signalling|\45:  JOURNAL   Nature 390 (6660), 629-632 (1997)|  MEDLINE   98065953|\35:REFERENCE   20 (residues 1 to 1304)|\74:  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,|\49:            Ricca,G., Jaye,M. and Schlessinger,J.|\76:  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene|\77:            family of receptor-linked protein-tyrosine-phosphatases expressed|            in brain|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990)|  MEDLINE   90384936|\35:REFERENCE   21 (residues 1 to 1304)|\63:  AUTHORS   Schraven,B., Samstag,Y., Altevogt,P. and Meuer,S.C.|\62:  TITLE     Association of CD2 and CD45 on human T lymphocytes|\43:  JOURNAL   Nature 345 (6270), 71-74 (1990)|  MEDLINE   90231464|\35:REFERENCE   22 (residues 1 to 1304)|\39:  AUTHORS   Pingel,J.T. and Thomas,M.L.|\70:  TITLE     Evidence that the leukocyte-common antigen is required for|\54:            antigen-induced T lymphocyte proliferation|\41:  JOURNAL   Cell 58 (6), 1055-1065 (1989)|  MEDLINE   89376557|\35:REFERENCE   23 (residues 1 to 1304)|\67:  AUTHORS   Charbonneau,H., Tonks,N.K., Walsh,K.A. and Fischer,E.H.|\75:  TITLE     The leukocyte common antigen (CD45): a putative receptor-linked|\40:            protein tyrosine phosphatase|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 85 (19), 7182-7186 (1988)|  MEDLINE   89017162|\35:REFERENCE   24 (residues 1 to 1304)|\72:  AUTHORS   Streuli,M., Hall,L.R., Saga,Y., Schlossman,S.F. and Saito,H.|\79:  TITLE     Differential usage of three exons generates at least five different|\58:            mRNAs encoding human leukocyte common antigens|\50:  JOURNAL   J. Exp. Med. 166 (5), 1548-1566 (1987)|  MEDLINE   88061067|\35:REFERENCE   25 (residues 1 to 1304)|\68:  AUTHORS   Ralph,S.J., Thomas,M.L., Morton,C.C. and Trowbridge,I.S.|\76:  TITLE     Structural variants of human T200 glycoprotein (leukocyte-common|            antigen)|\43:  JOURNAL   EMBO J. 6 (5), 1251-1257 (1987)|  MEDLINE   87275816
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="1"|/map="1q31-q32"
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obj|Feature
obj|DBObj||Protein_1|||||0|0|\222:protein tyrosine phosphatase, receptor type, c polypeptide; leukocyte-common antigen; T200 glycoprotein; human homolog of severe combined immunodeficiency due to PTPRC deficiency; SCID due to PTPRC deficiency; CD45 antigen
end|270|270|||0|1|279|1|1|1|1|1..1304
obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, C|isoform 1 precursor"|\21:/EC_number="3.1.3.48"
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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end|\279:dilletykrkiadegrlflaefqsiprvfskfpikearkpfnqnknryvdilpydynrvelseingdagsnyinasyidgfkeprkyiaaqgprdetvddfwrmiweqkatvivmvtrceegnrnkcaeywpsmeegtrafgdvvvkinqhkrcpdyiiqklnivnkkekatgrevthiqftswpdhgvpedphlllklrrrvnafsnffsgpivvhcsagvgrtgtyigidamlegleaenkvdvygyvvklrrqrclmvqveaqyilihqalveynq|GenPept|
obj|String*|1|NP_002829
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obj|String*|1|\29:REFSEQ: accession NM_002838.2
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obj|String*|48|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D1+%28NP_002829%29+PTPRC
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obj|DBObj||\26:hCD45_D2 (NP_002829) PTPRC|||||302014800|0|\306:protein tyrosine phosphatase, receptor type, C isoform 1 precursor; protein tyrosine phosphatase, receptor type, c polypeptide; leukocyte-common antigen; T200 glycoprotein; human homolog of severe combined immunodeficiency due to PTPRC deficiency; SCID due to PTPRC deficiency; CD45 antigen [Homo sapiens].
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obj|String*|23|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\58:reference sequence was derived from Y00638.1 and Y00062.1.|\57:On Feb 8, 2002 this sequence version replaced gi:4506307.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\53:domain, a single transmembrane segment and two tandem|\64:intracytoplasmic catalytic domains, and thus belongs to receptor|\62:type PTP. This gene is specifically expressed in hematopoietic|\65:cells. This PTP has been shown to be an essential regulator of T-|\66:and B-cell antigen receptor signaling. It functions through either|\58:direct interaction with components of the antigen receptor|\67:complexes, or by activating various Src family kinases required for|\60:the antigen receptor signaling. This PTP also suppresses JAK|\63:kinases, and thus functions as a regulator of cytokine receptor|\66:signaling. Four alternatively spliced transcripts variants of this|\57:gene, which encode distinct isoforms, have been reported.||\64:Transcript Variant: This variant (1) encodes the longest isoform|(1).
end
obj|String*|212|\35:REFERENCE   1  (residues 1 to 1304)|\44:  AUTHORS   Baldwin,T.A. and Ostergaard,H.L.|\78:  TITLE     The protein-tyrosine phosphatase CD45 reaches the cell surface via|\53:            golgi-dependent and -independent pathways|\55:  JOURNAL   J. Biol. Chem. 277 (52), 50333-50340 (2002)|  MEDLINE   22384317|\69:  REMARK    GeneRIF: reaches the cell surface via Golgi-dependent and|\33:            -independent pathways|\35:REFERENCE   2  (residues 1 to 1304)|\71:  AUTHORS   Harashima,A., Suzuki,M., Okochi,A., Yamamoto,M., Matsuo,Y.,|\47:            Motoda,R., Yoshioka,T. and Orita,K.|\75:  TITLE     CD45 tyrosine phosphatase inhibits erythroid differentiation of|\70:            umbilical cord blood CD34+ cells associated with selective|\31:            inactivation of Lyn|\44:  JOURNAL   Blood 100 (13), 4440-4445 (2002)|  MEDLINE   22340750|\73:  REMARK    GeneRIF: CD45 may play a pivotal role in erythropoiesis. CD45|\70:            tyrosine phosphatase inhibits erythroid differentiation of|\70:            umbilical cord blood CD34+ cells associated with selective|\32:            inactivation of Lyn.|\35:REFERENCE   3  (residues 1 to 1304)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   4  (residues 1 to 1304)|\36:  AUTHORS   Pradhan,D. and Morrow,J.|\75:  TITLE     The spectrin-ankyrin skeleton controls CD45 surface display and|\36:            interleukin-2 production|\43:  JOURNAL   Immunity 17 (3), 303-315 (2002)|  MEDLINE   22241694|\72:  REMARK    GeneRIF: The spectrin-ankyrin skeleton controls CD45 surface|\49:            display and interleukin-2 production.|\35:REFERENCE   5  (residues 1 to 1304)|\73:  AUTHORS   Ballerini,C., Rosati,E., Salvetti,M., Ristori,G., Cannoni,S.,|\63:            Biagioli,T., Massacesi,L., Sorbi,S. and Vergelli,M.|\77:  TITLE     Protein tyrosine phosphatase receptor-type C exon 4 gene mutation|\68:            distribution in an Italian multiple sclerosis population|\51:  JOURNAL   Neurosci. Lett. 328 (3), 325-327 (2002)|  MEDLINE   22142931|\79:  REMARK    GeneRIF: Role of the C-->G mutation in position 77 of exon 4 of the|\77:            protein tyrosine phosphatase receptor-type C (PTPRC) gene, coding|\76:            for the CD45 molecule, for the development of multiple sclerosis|\26:            (MS) in Italy.|\35:REFERENCE   6  (residues 1 to 1304)|\52:  AUTHORS   Yamada,T., Zhu,D., Saxon,A. and Zhang,K.|\79:  TITLE     CD45 controls interleukin-4-mediated IgE class switch recombination|\79:            in human B cells through its function as a Janus kinase phosphatase|\55:  JOURNAL   J. Biol. Chem. 277 (32), 28830-28835 (2002)|  MEDLINE   22151051|\74:  REMARK    GeneRIF: CD45 controls interleukin-4-mediated IgE class switch|\42:            recombination in human B cells|\35:REFERENCE   7  (residues 1 to 1304)|\62:  AUTHORS   Yu,C., Yu,H.S., Sun,K.H., Hsieh,S.C. and Tsai,C.Y.|\70:  TITLE     Anti-CD45 isoform antibodies enhance phagocytosis and gene|\68:            expression of IL-8 and TNF-alpha in human neutrophils by|\76:            differential suppression on protein tyrosine phosphorylation and|\34:            p56lck tyrosine kinase|\53:  JOURNAL   Clin. Exp. Immunol. 129 (1), 78-85 (2002)|  MEDLINE   22095000|\77:  REMARK    GeneRIF: Biological functions of membrane expressed CD45 isoforms|\76:            on PMNs were studied. Cross-linking of CD45 isoforms by specific|\68:            MAbs stimulated different PMN activities by differential|\71:            suppression on protein tyrosine phosphorylation and p56lck.|\35:REFERENCE   8  (residues 1 to 1304)|\78:  AUTHORS   Jacobsen,M., Hoffmann,S., Cepok,S., Stei,S., Ziegler,A., Sommer,N.|\25:            and Hemmer,B.|\77:  TITLE     A novel mutation in PTPRC interferes with splicing and alters the|\48:            structure of the human CD45 molecule|\49:  JOURNAL   Immunogenetics 54 (3), 158-163 (2002)|  MEDLINE   22067726|\76:  REMARK    GeneRIF: a mutation in PTPRC interferes with splicing and alters|\46:            the structure of the CD45 molecule|\35:REFERENCE   9  (residues 1 to 1304)|\43:  AUTHORS   Tchilian,E.Z. and Beverley,P.C.|\38:  TITLE     CD45 in memory and disease|\67:  JOURNAL   Arch. Immunol. Ther. Exp. (Warsz.) 50 (2), 85-93 (2002)|  MEDLINE   22017393|\78:  REMARK    GeneRIF: Role of high and low molecular weight isoforms of CD45 in|\68:            the function of na##ve and memory T lymphocytes. Review.|\35:REFERENCE   10 (residues 1 to 1304)|\70:  AUTHORS   Fajka-Boja,R., Szemes,M., Ion,G., Legradi,A., Caron,M. and|\24:            Monostori,E.|\77:  TITLE     Receptor tyrosine phosphatase, CD45 binds galectin-1 but does not|\56:            mediate its apoptotic signal in T cell lines|\51:  JOURNAL   Immunol. Lett. 82 (1-2), 149-154 (2002)|  MEDLINE   22003829|\77:  REMARK    GeneRIF: Receptor tyrosine phosphatase, CD45 binds galectin-1 but|\65:            does not mediate its apoptotic signal in Jurkat cells|\35:REFERENCE   11 (residues 1 to 1304)|\79:  AUTHORS   Fukuhara,K., Okumura,M., Shiono,H., Inoue,M., Kadota,Y., Miyoshi,S.|\26:            and Matsuda,H.|\76:  TITLE     A study on CD45 isoform expression during T-cell development and|\48:            selection events in the human thymus|\48:  JOURNAL   Hum. Immunol. 63 (5), 394-404 (2002)|  MEDLINE   21972715|\70:  REMARK    GeneRIF: analysis of CD45 isoform expression during T-cell|\57:            development and selection in the human thymus|\35:REFERENCE   12 (residues 1 to 1304)|\38:  AUTHORS   Wu,L., Fu,J. and Shen,S.H.|\64:  TITLE     SKAP55 coupled with CD45 positively regulates T-cell|\48:            receptor-mediated gene transcription|\53:  JOURNAL   Mol. Cell. Biol. 22 (8), 2673-2686 (2002)|  MEDLINE   21907230|\73:  REMARK    GeneRIF: SKAP55 coupled with CD45 positively regulates T-cell|\49:            receptor-mediated gene transcription.|\35:REFERENCE   13 (residues 1 to 1304)|\77:  AUTHORS   Ishikawa,H., Tsuyama,N., Abroun,S., Liu,S., Li,F.J., Taniguchi,O.|\27:            and Kawano,M.M.|\79:  TITLE     Requirements of src family kinase activity associated with CD45 for|\55:            myeloma cell proliferation by interleukin-6|\42:  JOURNAL   Blood 99 (6), 2172-2178 (2002)|  MEDLINE   21866149|\79:  REMARK    GeneRIF: Requirements of src family kinase activity associated with|\64:            CD45 for myeloma cell proliferation by interleukin-6|\35:REFERENCE   14 (residues 1 to 1304)|\66:  AUTHORS   Tchilian,E.Z., Dawes,R., Ramaley,P.A., Whitworth,J.A.,|\72:            Yuldasheva,N., Wells,R.S., Watera,C., French,N., Gilks,C.F.,|\72:            Kunachiwa,W., Ruzibakiev,R., Leetrakool,N., Carrington,C.V.,|\78:            Ramdath,D.D., Gotch,F., Stephens,H.A., Hill,A.V. and Beverley,P.C.|\78:  TITLE     A CD45 polymorphism associated with abnormal splicing is absent in|\31:            African populations|\53:  JOURNAL   Immunogenetics 53 (10-11), 980-983 (2002)|  MEDLINE   21850514|\76:  REMARK    GeneRIF: we examined the frequency of the C77G allele in African|\79:            and Asian populations from countries with high or low prevalence of|\78:            HIV infection; Here we report that the variant CD45 C77G allele is|\41:            absent in African populations|\35:REFERENCE   15 (residues 1 to 1304)|\76:  AUTHORS   Wood,J.P., Bieda,K., Segni,M., Herwig,J., Krause,M., Usadel,K.H.|\28:            and Badenhoop,K.|\79:  TITLE     CD45 exon 4 point mutation does not confer susceptibility to type 1|\48:            diabetes mellitus or Graves' disease|\53:  JOURNAL   Eur. J. Immunogenet. 29 (1), 73-74 (2002)|  MEDLINE   21830605|\79:  REMARK    GeneRIF: CD45 variant (C77G, exon 4) does not confer susceptibility|\45:            to either IDDM or Graves' disease|\35:REFERENCE   16 (residues 1 to 1304)|\71:  AUTHORS   Moro,H., Iwai,K., Mori,N., Watanabe,M., Fukushi,M., Oie,M.,|\78:            Arai,M., Tanaka,Y., Miyawaki,T., Gejyo,F., Arakawa,M. and Fujii,M.|\77:  TITLE     Interleukin-2-dependent but not independent T-cell lines infected|\79:            with human T-cell leukemia virus type 1 selectively express CD45RO,|\53:            a marker for persistent infection in vivo|\46:  JOURNAL   Virus Genes 23 (3), 263-271 (2001)|  MEDLINE   21636965|\78:  REMARK    GeneRIF: role of CD45RO in the persistent HTLV-1 infection in vivo|\35:REFERENCE   17 (residues 1 to 1304)|\74:  AUTHORS   Irie-Sasaki,J., Sasaki,T., Matsumoto,W., Opavsky,A., Cheng,M.,|\79:            Welstead,G., Griffiths,E., Krawczyk,C., Richardson,C.D., Aitken,K.,|\74:            Iscove,N., Koretzky,G., Johnson,P., Liu,P., Rothstein,D.M. and|\26:            Penninger,J.M.|\71:  TITLE     CD45 is a JAK phosphatase and negatively regulates cytokine|\31:            receptor signalling|\45:  JOURNAL   Nature 409 (6818), 349-354 (2001)|  MEDLINE   21069057|\35:REFERENCE   18 (residues 1 to 1304)|\76:  AUTHORS   Goff,L.K., van Soest,S., Timon,M., Tchilian,E. and Beverley,P.C.|\79:  TITLE     Protein tyrosine phosphatase receptor type C polypeptide (PTPRC) on|\79:            human chromosome band 1q31-->q32 localizes with marker D1S413(1) on|\48:            a 610-kb yeast artificial chromosome|\59:  JOURNAL   Cytogenet. Cell Genet. 87 (3-4), 223-224 (1999)|  MEDLINE   20169194|\35:REFERENCE   19 (residues 1 to 1304)|\79:  AUTHORS   Petricoin,E.F. III, Ito,S., Williams,B.L., Audet,S., Stancato,L.F.,|\66:            Gamero,A., Clouse,K., Grimley,P., Weiss,A., Beeler,J.,|\66:            Finbloom,D.S., Shores,E.W., Abraham,R. and Larner,A.C.|\79:  TITLE     Antiproliferative action of interferon-alpha requires components of|\38:            T-cell-receptor signalling|\45:  JOURNAL   Nature 390 (6660), 629-632 (1997)|  MEDLINE   98065953|\35:REFERENCE   20 (residues 1 to 1304)|\74:  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,|\49:            Ricca,G., Jaye,M. and Schlessinger,J.|\76:  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene|\77:            family of receptor-linked protein-tyrosine-phosphatases expressed|            in brain|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990)|  MEDLINE   90384936|\35:REFERENCE   21 (residues 1 to 1304)|\63:  AUTHORS   Schraven,B., Samstag,Y., Altevogt,P. and Meuer,S.C.|\62:  TITLE     Association of CD2 and CD45 on human T lymphocytes|\43:  JOURNAL   Nature 345 (6270), 71-74 (1990)|  MEDLINE   90231464|\35:REFERENCE   22 (residues 1 to 1304)|\39:  AUTHORS   Pingel,J.T. and Thomas,M.L.|\70:  TITLE     Evidence that the leukocyte-common antigen is required for|\54:            antigen-induced T lymphocyte proliferation|\41:  JOURNAL   Cell 58 (6), 1055-1065 (1989)|  MEDLINE   89376557|\35:REFERENCE   23 (residues 1 to 1304)|\67:  AUTHORS   Charbonneau,H., Tonks,N.K., Walsh,K.A. and Fischer,E.H.|\75:  TITLE     The leukocyte common antigen (CD45): a putative receptor-linked|\40:            protein tyrosine phosphatase|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 85 (19), 7182-7186 (1988)|  MEDLINE   89017162|\35:REFERENCE   24 (residues 1 to 1304)|\72:  AUTHORS   Streuli,M., Hall,L.R., Saga,Y., Schlossman,S.F. and Saito,H.|\79:  TITLE     Differential usage of three exons generates at least five different|\58:            mRNAs encoding human leukocyte common antigens|\50:  JOURNAL   J. Exp. Med. 166 (5), 1548-1566 (1987)|  MEDLINE   88061067|\35:REFERENCE   25 (residues 1 to 1304)|\68:  AUTHORS   Ralph,S.J., Thomas,M.L., Morton,C.C. and Trowbridge,I.S.|\76:  TITLE     Structural variants of human T200 glycoprotein (leukocyte-common|            antigen)|\43:  JOURNAL   EMBO J. 6 (5), 1251-1257 (1987)|  MEDLINE   87275816
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obj|DBObj||\26:hDEP1_D1 (NP_002834) PTPRJ|||||302014800|0|\185:protein tyrosine phosphatase, receptor type, J precursor; protein tyrosine phosphatase, receptor type, J polypeptide; human density enhanced phosphatase-1; CD148 antigen [Homo sapiens].
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obj|String*|18|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from U10886.1.|\58:On Feb 22, 2002 this sequence version replaced gi:4506315.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\61:region containing five fibronectin type III repeats, a single|\61:transmembrane region, and a single intracytoplasmic catalytic|\60:domain, and thus represents a receptor-type PTP. This PTP is|\66:present in all hematopoietic lineages, and was shown to negatively|\63:regulate T cell receptor signaling possibly through interfering|\63:with the phosphorylation of Phospholipase C Gamma 1 (PLCG1) and|\66:Linker for Activation of T Cells (LAT). This PTP was also found to|\58:dephosphorylate PDGF beta receptor, and may be involved in|\31:UV-induced signal transduction.
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obj|String*|61|\35:REFERENCE   1  (residues 1 to 1337)|\76:  AUTHORS   Ruivenkamp,C.A., van Wezel,T., Zanon,C., Stassen,A.P., Vlcek,C.,|\75:            Csikos,T., Klous,A.M., Tripodis,N., Perrakis,A., Boerrigter,L.,|\74:            Groot,P.C., Lindeman,J., Mooi,W.J., Meijjer,G.A., Scholten,G.,|\70:            Dauwerse,H., Paces,V., van Zandwijk,N., van Ommen,G.J. and|\21:            Demant,P.|\74:  TITLE     Ptprj is a candidate for the mouse colon-cancer susceptibility|\65:            locus Scc1 and is frequently deleted in human cancers|\46:  JOURNAL   Nat. Genet. 31 (3), 295-300 (2002)|  MEDLINE   22084388|\71:  REMARK    GeneRIF: This protein is frequently deleted in human breast|            cancers.|\35:REFERENCE   2  (residues 1 to 1337)|\59:  AUTHORS   Baker,J.E., Majeti,R., Tangye,S.G. and Weiss,A.|\76:  TITLE     Protein tyrosine phosphatase CD148-mediated inhibition of T-cell|\75:            receptor signal transduction is associated with reduced LAT and|\49:            phospholipase Cgamma1 phosphorylation|\53:  JOURNAL   Mol. Cell. Biol. 21 (7), 2393-2403 (2001)|  MEDLINE   21160271|\35:REFERENCE   3  (residues 1 to 1337)|\72:  AUTHORS   Kovalenko,M., Denner,K., Sandstrom,J., Persson,C., Gross,S.,|\57:            Jandt,E., Vilella,R., Bohmer,F. and Ostman,A.|\75:  TITLE     Site-selective dephosphorylation of the platelet-derived growth|\70:            factor beta-receptor by the receptor-like protein-tyrosine|\29:            phosphatase DEP-1|\55:  JOURNAL   J. Biol. Chem. 275 (21), 16219-16226 (2000)|  MEDLINE   20283660|\35:REFERENCE   4  (residues 1 to 1337)|\68:  AUTHORS   Gross,S., Knebel,A., Tenev,T., Neininger,A., Gaestel,M.,|\39:            Herrlich,P. and Bohmer,F.D.|\73:  TITLE     Inactivation of protein-tyrosine phosphatases as mechanism of|\42:            UV-induced signal transduction|\55:  JOURNAL   J. Biol. Chem. 274 (37), 26378-26386 (1999)|  MEDLINE   99403084|\35:REFERENCE   5  (residues 1 to 1337)|\70:  AUTHORS   Tangye,S.G., Phillips,J.H., Lanier,L.L., de Vries,J.E. and|\21:            Aversa,G.|\79:  TITLE     CD148: a receptor-type protein tyrosine phosphatase involved in the|\49:            regulation of human T cell activation|\49:  JOURNAL   J. Immunol. 161 (7), 3249-3255 (1998)|  MEDLINE   98430639|\35:REFERENCE   6  (residues 1 to 1337)|\73:  AUTHORS   de la Fuente-Garcia,M.A., Nicolas,J.M., Freed,J.H., Palou,E.,|\57:            Thomas,A.P., Vilella,R., Vives,J. and Gaya,A.|\75:  TITLE     CD148 is a membrane protein tyrosine phosphatase present in all|\76:            hematopoietic lineages and is involved in signal transduction on|\23:            lymphocytes|\42:  JOURNAL   Blood 91 (8), 2800-2809 (1998)|  MEDLINE   98200586|\35:REFERENCE   7  (residues 1 to 1337)|\68:  AUTHORS   Honda,H., Inazawa,J., Nishida,J., Yazaki,Y. and Hirai,H.|\77:  TITLE     Molecular cloning, characterization, and chromosomal localization|\61:            of a novel protein-tyrosine phosphatase, HPTP eta|\43:  JOURNAL   Blood 84 (12), 4186-4194 (1994)|  MEDLINE   95086212|\35:REFERENCE   8  (residues 1 to 1337)|\45:  AUTHORS   Ostman,A., Yang,Q. and Tonks,N.K.|\78:  TITLE     Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase,|\52:            is enhanced with increasing cell density|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 91 (21), 9680-9684 (1994)|  MEDLINE   95024024
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obj|String*|12|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Primates|Catarrhini|Hominidae|Homo
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obj|String*|1|\29:REFSEQ: accession NM_002843.2
end
obj|String*|47|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ|\52:VNTI URL:vnti:protein/hDEP1_D1+%28NP_002834%29+PTPRJ
end
obj|String*|0
end
obj|String*|0
end
end|26F7320
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\28:hGLEPP1_D1 (NP_109592) PTPRO|||||302014800|0|\201:receptor-type protein tyrosine phosphatase O isoform a precursor; glomerular epithelial protein-1; protein tyrosine phosphatase PTP-U2; phosphotyrosine phosphatase U2; PTPase U2; PTPROt [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|17|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\58:reference sequence was derived from Z48541.1 and U20489.1.||\59:Summary: This gene encodes a receptor-type protein tyrosine|\67:phosphatase containing a single intracellular catalytic domain with|\63:a characteristic signature motif. The gene product, which has a|\62:transmembrane domain, is an integral membrane protein. Several|\63:alternatively spliced transcript variants, some of which encode|\61:different isoforms of the protein, have been described. These|\44:variants exhibit tissue-specific expression.||\64:Transcript Variant: This variant (1) encodes the longest isoform|\64:(a) known to date. The encoded protein has a large extracellular|\65:domain containing 8 repeats of a fibronectin type III-like motif.|\67:This variant is expressed in the glomerulus of kidney and in brain.|\65:In kidney, it may play a role in regulating glomerular epithelial|\42:cell (podocyte) structure and/or function.
end
obj|String*|22|\35:REFERENCE   1  (residues 1 to 1216)|\77:  AUTHORS   Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Tiwari,S., Freeman,G.J.|\26:            and Shipp,M.A.|\74:  TITLE     PTPROt: an alternatively spliced and developmentally regulated|\61:            B-lymphoid phosphatase that promotes G0/G1 arrest|\42:  JOURNAL   Blood 94 (7), 2403-2413 (1999)|  MEDLINE   99428326|\35:REFERENCE   2  (residues 1 to 1216)|\59:  AUTHORS   Seimiya,H., Sawabe,T., Inazawa,J. and Tsuruo,T.|\76:  TITLE     Cloning, expression and chromosomal localization of a novel gene|\72:            for protein tyrosine phosphatase (PTP-U2) induced by various|\43:            differentiation-inducing agents|\45:  JOURNAL   Oncogene 10 (9), 1731-1738 (1995)|  MEDLINE   95273089|\35:REFERENCE   3  (residues 1 to 1216)|\78:  AUTHORS   Wiggins,R.C., Wiggins,J.E., Goyal,M., Wharram,B.L. and Thomas,P.E.|\72:  TITLE     Molecular cloning of cDNAs encoding human GLEPP1, a membrane|\72:            protein tyrosine phosphatase: characterization of the GLEPP1|\77:            protein distribution in human kidney and assignment of the GLEPP1|\46:            gene to human chromosome 12p12-p13|\43:  JOURNAL   Genomics 27 (1), 174-181 (1995)|  MEDLINE   95394455
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||JNA||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|277
obj|Object*|2
obj|Feature
obj|DBObj||Region_2|||||0|0|PTPc
end|266|266|||0|17|272|1|1|1|1|937..1192
obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
end|0||
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end
end
obj|Feature
obj|DBObj||Dom_Misc_3|||||0|0|
end|1000|1000|||0|214|224|1|1|1|1|1134..1144
obj|String*|1|\47:/region_name="catalytic domain signature motif"
end|0||
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end
end
end|\277:ddfdayikdmakdsdykfslqfeelkligldiphfaadlplnrcknrytnilpydfsrvrlvsmneeegadyinanyipgynspqeyiatqgplpetrndfwkmvlqqksqiivmltqcnekrrvkcdhywpfteepiaygditvemiseeeqddwacrhfrinyademqdvmhfnytawpdhgvptanaaesilqfvhmvrqqatkskgpmiihcsagvgrtgtfialdrllqhirdhefvdilglvsemrsyrmsmvqteeqyifihqcvqlmwm|GenPept|
obj|String*|1|NP_109592
end||06-APR-2003|Homo sapiens (human)
obj|String*|0
end|0
obj|String*|0
end|PRT
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end
obj|String*|1|Homo sapiens
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end
obj|String*|0
end
obj|String*|12|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Primates|Catarrhini|Hominidae|Homo
end
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end
obj|String*|1|\29:REFSEQ: accession NM_030667.1
end
obj|String*|47|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO|\54:VNTI URL:vnti:protein/hGLEPP1_D1+%28NP_109592%29+PTPRO
end
obj|String*|0
end
obj|String*|0
end
end|26F6030
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\28:hHDPTP_D1 (NP_056281) PTPN23|||||302014800|0|\107:protein tyrosine phosphatase, non-receptor type 23; His-domain protein tyrosine phosphatase [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|3|\62:PREDICTED REFSEQ: The mRNA record is supported by experimental|\66:evidence; however, the coding sequence is predicted. The reference|\37:sequence was derived from AF290614.1.
end
obj|String*|12|\35:REFERENCE   1  (residues 1 to 1636)|\79:  AUTHORS   Qu,X., Zhai,Y., Wei,H., Zhang,C., Xing,G., Lu,C., Wang,M. and He,F.|\76:  TITLE     Cloning, chromosomal assignment and tissue expression of a novel|\62:            human protein tyrosine phosphatase (PTP-TD14) gene|\38:  JOURNAL   I Chuan 23 (6), 1-9 (2001)|\35:REFERENCE   2  (residues 1 to 1636)|\71:  AUTHORS   Toyooka,S., Ouchida,M., Jitsumori,Y., Tsukuda,K., Sakai,A.,|\50:            Nakamura,A., Shimizu,N. and Shimizu,K.|\70:  TITLE     HD-PTP: A novel protein tyrosine phosphatase gene on human|\29:            chromosome 3p21.3|\66:  JOURNAL   Biochem. Biophys. Res. Commun. 278 (3), 671-678 (2000)|  MEDLINE   20549011
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|286
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|286|1|1|1|1|1..1636
obj|String*|7|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="3"|/map="3p21.3"|/clone="F2896"|/tissue_type="liver"|/dev_stage="fetus"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|\39:His-domain protein tyrosine phosphatase
end|270|270|||0|1|286|1|1|1|1|1..1636
obj|String*|2|\57:/product="protein tyrosine phosphatase, non-receptor type|23"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Region_2|||||0|0|PTPc
end|266|266|||0|23|286|1|1|1|1|1191..1454
obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
end|0||
obj|Object*|0
end
end
end|\286:erlrqlqqeleafrgqlgdvgaldtvwrelqdaqehdargrsiaiarcyslknrhqdvmpydsnrvvlrsgkddyinascveglspycpplvatqaplpgtaadfwlmvheqkvsvivmlvseaemekqkvaryfptergqpmvhgalslalssvrstethvervlslqfrdqslkrslvhlhfptwpelglpdspsnllrfiqevhahylhqrplhtpiivhcssgvgrtgafallyaavqeveagngipelpqlvrrmrqqrkhmlqeklhlrfcyeavvrhve|GenPept|
obj|String*|1|NP_056281
end||06-APR-2003|Homo sapiens (human)
obj|String*|0
end|0
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end|PRT
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obj|String*|1|Homo sapiens
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end
obj|String*|1|\29:REFSEQ: accession NM_015466.1
end
obj|String*|33|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23|\54:VNTI URL:vnti:protein/hHDPTP_D1+%28NP_056281%29+PTPN23
end
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end|3401DF0
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\27:hHePTP_D1 (NP_002823) PTPN7|||||302014800|0|\182:protein tyrosine phosphatase, non-receptor type 7 isoform 1; protein-tyrosine phoshatase, nonreceptor-type, stress induced; hematopoietic protein-tyrosine phosphatase [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|23|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\59:reference sequence was derived from BC001746.1, BG340453.1,|\22:D11327.1 and M64322.1.|\58:On Jan 25, 2002 this sequence version replaced gi:4506299.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\66:oncogenic transformation. This gene is preferentially expressed in|\66:a variety of hematopoietic cells, and is an early response gene in|\64:lymphokine stimulated cells. The noncatalytic N-terminus of this|\61:PTP can interact with MAP kinases and suppress the MAP kinase|\66:activities. This PTP was shown to be involved in the regulation of|\61:T cell antigen receptor (TCR) signaling, which was thought to|\63:function through dephosphorylating the molecules related to MAP|\66:kinase pathway. Three alternatively spliced transcript variants of|\60:this gene, which encode two distinct isoforms, are reported.||\60:Transcript Variant: This variant (1) contains a different 5'|\66:region, which includes a part of the coding sequence when compared|\58:to variant 2. It thus encodes a protein that has a shorter|\37:N-terminus, as compared to isoform 2.
end
obj|String*|47|\34:REFERENCE   1  (residues 1 to 360)|\76:  AUTHORS   Oh-hora,M., Ogata,M., Mori,Y., Adachi,M., Imai,K., Kosugi,A. and|\22:            Hamaoka,T.|\74:  TITLE     Direct suppression of TCR-mediated activation of extracellular|\78:            signal-regulated kinase by leukocyte protein tyrosine phosphatase,|\43:            a tyrosine-specific phosphatase|\49:  JOURNAL   J. Immunol. 163 (3), 1282-1288 (1999)|  MEDLINE   99343735|\34:REFERENCE   2  (residues 1 to 360)|\76:  AUTHORS   Saxena,M., Williams,S., Brockdorff,J., Gilman,J. and Mustelin,T.|\71:  TITLE     Inhibition of T cell signaling by mitogen-activated protein|\70:            kinase-targeted hematopoietic tyrosine phosphatase (HePTP)|\55:  JOURNAL   J. Biol. Chem. 274 (17), 11693-11700 (1999)|  MEDLINE   99223488|\34:REFERENCE   3  (residues 1 to 360)|\61:  AUTHORS   Saxena,M., Williams,S., Gilman,J. and Mustelin,T.|\78:  TITLE     Negative regulation of T cell antigen receptor signal transduction|\57:            by hematopoietic tyrosine phosphatase (HePTP)|\55:  JOURNAL   J. Biol. Chem. 273 (25), 15340-15344 (1998)|  MEDLINE   98288260|\34:REFERENCE   4  (residues 1 to 360)|\71:  AUTHORS   Swieter,M., Berenstein,E.H., Swaim,W.D. and Siraganian,R.P.|\77:  TITLE     Aggregation of IgE receptors in rat basophilic leukemia 2H3 cells|\78:            induces tyrosine phosphorylation of the cytosolic protein-tyrosine|\29:            phosphatase HePTP|\55:  JOURNAL   J. Biol. Chem. 270 (37), 21902-21906 (1995)|  MEDLINE   95394959|\34:REFERENCE   5  (residues 1 to 360)|\75:  AUTHORS   Adachi,M., Sekiya,M., Isobe,M., Kumura,Y., Ogita,Z., Hinoda,Y.,|\32:            Imai,K. and Yachi,A.|\64:  TITLE     Molecular cloning and chromosomal mapping of a human|\47:            protein-tyrosine phosphatase LC-PTP|\68:  JOURNAL   Biochem. Biophys. Res. Commun. 186 (3), 1607-1615 (1992)|  MEDLINE   92378634|\34:REFERENCE   6  (residues 1 to 360)|\78:  AUTHORS   Adachi,M., Sekiya,M., Arimura,Y., Takekawa,M., Itoh,F., Hinoda,Y.,|\32:            Imai,K. and Yachi,A.|\72:  TITLE     Protein-tyrosine phosphatase expression in pre-B cell NALM-6|\46:  JOURNAL   Cancer Res. 52 (3), 737-740 (1992)|  MEDLINE   92119637|\22:REFERENCE   7  (sites)|\78:  AUTHORS   Zanke,B., Suzuki,H., Kishihara,K., Mizzen,L., Minden,M., Pawson,A.|\24:            and Mak,T.W.|\77:  TITLE     Cloning and expression of an inducible lymphoid-specific, protein|\43:            tyrosine phosphatase (HePTPase)|\51:  JOURNAL   Eur. J. Immunol. 22 (1), 235-239 (1992)|  MEDLINE   92111631
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|Feature
obj|DBObj||Protein_1|||||0|0|\105:protein-tyrosine phoshatase, nonreceptor-type, stress induced; hematopoietic protein-tyrosine phosphatase
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obj|String*|1|\29:REFSEQ: accession NM_002832.2
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obj|String*|45|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7|\53:VNTI URL:vnti:protein/hHePTP_D1+%28NP_002823%29+PTPN7
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end|283A868
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\25:hIA2_D1 (NP_002837) PTPRN|||||302014800|0|\191:protein tyrosine phosphatase, receptor type, N precursor; islet cell antigen 2; islet cell antigen 512; islet cell autoantigen 3; protein tyrosine phosphatase-like N precursor [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|14|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from L18983.1, AF042285.4 and|BC007713.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\61:region, a single transmembrane region, and a single catalytic|\67:domain, and thus represents a receptor-type PTP. This PTP was found|\60:to be an autoantigen that is reactive with insulin-dependent|\66:diabetes mellitus (IDDM) patient sera, and thus may be a potential|\44:target of autoimmunity in diabetes mellitus.
end
obj|String*|59|\34:REFERENCE   1  (residues 1 to 979)|\60:  AUTHORS   Sanjeevi,C.B., Das,A.K. and Shtauvere-Brameus,A.|\75:  TITLE     BCG vaccination and GAD65 and IA-2 autoantibodies in autoimmune|\38:            diabetes in southern India|\53:  JOURNAL   Ann. N. Y. Acad. Sci. 958, 293-296 (2002)|  MEDLINE   22015049|\73:  REMARK    GeneRIF: BCG vaccination and GAD65 and IA-2 autoantibodies in|\50:            autoimmune diabetes in southern India.|\34:REFERENCE   2  (residues 1 to 979)|\76:  AUTHORS   Kawasaki,E., Yamaguchi,H., Hattori,H., Egashira,T. and Eguchi,K.|\78:  TITLE     Autoantibodies to IA-2 in type 1 diabetes: measurements with a new|\45:            enzyme-linked immunosorbent assay|\53:  JOURNAL   Ann. N. Y. Acad. Sci. 958, 241-246 (2002)|  MEDLINE   22015037|\76:  REMARK    GeneRIF: Autoantibodies to IA-2 in type 1 diabetes: measurements|\57:            with a new enzyme-linked immunosorbent assay.|\34:REFERENCE   3  (residues 1 to 979)|\71:  AUTHORS   Miao,D., Yu,L., Tiberti,C., Cuthbertson,D.D., Rewers,M., di|\50:            Mario,U., Eisenbarth,G.S. and Dotta,F.|\75:  TITLE     ICA512(IA-2) epitope specific assays distinguish transient from|\46:            diabetes associated autoantibodies|\48:  JOURNAL   J. Autoimmun. 18 (2), 191-196 (2002)|  MEDLINE   21906940|\79:  REMARK    GeneRIF: ICA512(IA-2) epitope specific assays distinguish transient|\52:            from diabetes associated autoantibodies.|\34:REFERENCE   4  (residues 1 to 979)|\42:  AUTHORS   Mikulecky,M. and Michalkova,D.|\73:  TITLE     Secular and seasonal cycling of IA2-ab autoantibody in Slovak|\29:            diabetic children|\62:  JOURNAL   Biomed. Pharmacother. 55 Suppl 1, 106S-109S (2001)|  MEDLINE   21630621|\34:REFERENCE   5  (residues 1 to 979)|\75:  AUTHORS   Cui,L., Yu,W.P., DeAizpurua,H.J., Schmidli,R.S. and Pallen,C.J.|\70:  TITLE     Cloning and characterization of islet cell antigen-related|\77:            protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and|\53:            autoantigen in insulin-dependent diabetes|\55:  JOURNAL   J. Biol. Chem. 271 (40), 24817-24823 (1996)|  MEDLINE   96394649|\34:REFERENCE   6  (residues 1 to 979)|\71:  AUTHORS   van den Maagdenberg,A.M., Olde Weghuis,D., Rijss,J., van de|\78:            Wetering,R.A., Wieringa,B., Geurts van Kessel,A. and Hendriks,W.J.|\75:  TITLE     Assignment of the human gene for receptor-type protein tyrosine|\76:            phosphatase IA-2 (PTPRN) to chromosome region 2q35 --> q36.1 and|\58:            identification of an intragenic genetic marker|\59:  JOURNAL   Cytogenet. Cell Genet. 73 (1-2), 145-148 (1996)|  MEDLINE   96244610|\34:REFERENCE   7  (residues 1 to 979)|\53:  AUTHORS   Lan,M.S., Lu,J., Goto,Y. and Notkins,A.L.|\75:  TITLE     Molecular cloning and identification of a receptor-type protein|\61:            tyrosine phosphatase, IA-2, from human insulinoma|\49:  JOURNAL   DNA Cell Biol. 13 (5), 505-514 (1994)|  MEDLINE   94296553|\34:REFERENCE   8  (residues 1 to 979)|\75:  AUTHORS   Rabin,D.U., Pleasic,S.M., Shapiro,J.A., Yoo-Warren,H., Oles,J.,|\51:            Hicks,J.M., Goldstein,D.E. and Rae,P.M.|\75:  TITLE     Islet cell antigen 512 is a diabetes-specific islet autoantigen|\52:            related to protein tyrosine phosphatases|\49:  JOURNAL   J. Immunol. 152 (6), 3183-3188 (1994)|  MEDLINE   94194080
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="2"|/map="2q35-q36.1"
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obj|Feature
obj|DBObj||Protein_1|||||0|0|\117:islet cell antigen 2; islet cell antigen 512; islet cell autoantigen 3; protein tyrosine phosphatase-like N precursor
end|270|270|||0|1|279|1|1|1|1|1..979
obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, N|precursor"|\21:/EC_number="3.1.3.48"
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|1|NP_002837
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obj|String*|1|\29:REFSEQ: accession NM_002846.2
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obj|String*|33|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN|\51:VNTI URL:vnti:protein/hIA2_D1+%28NP_002837%29+PTPRN
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end|333B7C0
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\30:hIA2beta_D1 (NP_002838) PTPRN2|||||302014800|0|\227:protein tyrosine phosphatase, receptor type, N polypeptide 2 isoform 1 precursor; protein tyrosine phosphatase receptor pi; phogrin; tyrosine phosphatase IA-2 beta; IAR/receptor-like protein-tyrosine phosphatase [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|18|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from U66702.1 and AF007555.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\65:region, a single transmembrane region, and a single intracellular|\62:catalytic domain, and thus represents a receptor-type PTP. The|\55:catalytic domain of this PTP is most closely related to|\61:PTPRN/IA-2beta. This PTP and PTPRN are both found to be major|\65:autoantigens associated with insulin-dependent diabetes mellitus.|\67:Three alternatively spliced transcript variants of this gene, which|\45:encode distinct proteins, have been reported.||\64:Transcript Variant: This variant (1) encodes the longest isoform|(1).
end
obj|String*|44|\35:REFERENCE   1  (residues 1 to 1015)|\78:  AUTHORS   van den Maagdenberg,A.M., Schepens,J.T., Schepens,M.T., Pepers,B.,|\58:            Wieringa,B., van Kessel,A.G. and Hendriks,W.J.|\73:  TITLE     Assignment of Ptprn2, the gene encoding receptor-type protein|\65:            tyrosine phosphatase IA-2beta, a major autoantigen in|\79:            insulin-dependent diabetes mellitus, to mouse chromosome region 12F|\59:  JOURNAL   Cytogenet. Cell Genet. 82 (3-4), 153-155 (1998)|  MEDLINE   99077744|\35:REFERENCE   2  (residues 1 to 1015)|\68:  AUTHORS   Schmidli,R.S., Colman,P.G., Cui,L., Yu,W.P., Kewming,K.,|\74:            Jankulovski,C., Harrison,L.C., Pallen,C.J. and DeAizpurua,H.J.|\76:  TITLE     Antibodies to the protein tyrosine phosphatases IAR and IA-2 are|\79:            associated with progression to insulin-dependent diabetes (IDDM) in|\51:            first-degree relatives at-risk for IDDM|\45:  JOURNAL   Autoimmunity 28 (1), 15-23 (1998)|  MEDLINE   98425805|\35:REFERENCE   3  (residues 1 to 1015)|\66:  AUTHORS   Li,Q., Borovitskaya,A.E., DeSilva,M.G., Wasserfall,C.,|\52:            Maclaren,N.K., Notkins,A.L. and Lan,M.S.|\74:  TITLE     Autoantigens in insulin-dependent diabetes mellitus: molecular|\59:            cloning and characterization of human IA-2 beta|\63:  JOURNAL   Proc. Assoc. Am. Physicians 109 (4), 429-439 (1997)|  MEDLINE   97364262|\35:REFERENCE   4  (residues 1 to 1015)|\69:  AUTHORS   Smith,P.D., Barker,K.T., Wang,J., Lu,Y.J., Shipley,J. and|\25:            Crompton,M.R.|\76:  TITLE     ICAAR, a novel member of a new family of transmembrane, tyrosine|\37:            phosphatase-like proteins|\66:  JOURNAL   Biochem. Biophys. Res. Commun. 229 (2), 402-411 (1996)|  MEDLINE   97127415|\35:REFERENCE   5  (residues 1 to 1015)|\56:  AUTHORS   Kawasaki,E., Hutton,J.C. and Eisenbarth,G.S.|\77:  TITLE     Molecular cloning and characterization of the human transmembrane|\78:            protein tyrosine phosphatase homologue, phogrin, an autoantigen of|\27:            type 1 diabetes|\66:  JOURNAL   Biochem. Biophys. Res. Commun. 227 (2), 440-447 (1996)|  MEDLINE   97032784|\35:REFERENCE   6  (residues 1 to 1015)|\75:  AUTHORS   Cui,L., Yu,W.P., DeAizpurua,H.J., Schmidli,R.S. and Pallen,C.J.|\70:  TITLE     Cloning and characterization of islet cell antigen-related|\77:            protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and|\53:            autoantigen in insulin-dependent diabetes|\55:  JOURNAL   J. Biol. Chem. 271 (40), 24817-24823 (1996)|  MEDLINE   96394649
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|33|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2|\56:VNTI URL:vnti:protein/hIA2beta_D1+%28NP_002838%29+PTPRN2
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obj|DBObj||\25:hLAR_D1 (NP_002831) PTPRF|||||302014800|0|\253:protein tyrosine phosphatase, receptor type, F isoform 1 precursor; protein tyrosine phosphatase, receptor type, F polypeptide; receptor-linked protein-tyrosine phosphatase LAR; leukocyte antigen-related tyrosine phosphatase; LCA-homolog [Homo sapiens].
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obj|String*|25|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from Y00815.1 and BI711143.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\53:region, a single transmembrane region, and two tandem|\57:intracytoplasmic catalytic domains, and thus represents a|\66:receptor-type PTP. The extracellular region contains three Ig-like|\56:domains, and nine non-Ig like domains similar to that of|\64:neural-cell adhesion molecule. This PTP was shown to function in|\60:the regulation of epithelial cell-cell contacts at adherents|\66:junctions, as well as in the control of beta-catenin signaling. An|\59:increased expression level of this protein was found in the|\66:insulin-responsive tissue of obese, insulin-resistant individuals,|\65:and may contribute to the pathogenesis of insulin resistance. Two|\61:alternatively spliced transcript variants of this gene, which|\45:encode distinct proteins, have been reported.||\63:Transcript Variant: This variant (1) contains an extra internal|\64:fragment within the coding region when compared to variant 2. It|\66:thus encodes a protein that has a 9 aa internal fragment absent in|isoform 2.
end
obj|String*|68|\35:REFERENCE   1  (residues 1 to 1897)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   2  (residues 1 to 1897)|\51:  AUTHORS   Symons,J.R., LeVea,C.M. and Mooney,R.A.|\77:  TITLE     Expression of the leucocyte common antigen-related (LAR) tyrosine|\71:            phosphatase is regulated by cell density through functional|\32:            E-cadherin complexes|\50:  JOURNAL   Biochem. J. 365 (Pt 2), 513-519 (2002)|  MEDLINE   22090243|\69:  REMARK    GeneRIF: regulation of expression by cell density through|\43:            functional E-cadherin complexes|\35:REFERENCE   3  (residues 1 to 1897)|\71:  AUTHORS   Zabolotny,J.M., Kim,Y.B., Peroni,O.D., Kim,J.K., Pani,M.A.,|\74:            Boss,O., Klaman,L.D., Kamatkar,S., Shulman,G.I., Kahn,B.B. and|\21:            Neel,B.G.|\65:  TITLE     Overexpression of the LAR (leukocyte antigen-related)|\76:            protein-tyrosine phosphatase in muscle causes insulin resistance|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 98 (9), 5187-5192 (2001)|  MEDLINE   21221100|\35:REFERENCE   4  (residues 1 to 1897)|\62:  AUTHORS   Muller,T., Choidas,A., Reichmann,E. and Ullrich,A.|\74:  TITLE     Phosphorylation and free pool of beta-catenin are regulated by|\77:            tyrosine kinases and tyrosine phosphatases during epithelial cell|\21:            migration|\55:  JOURNAL   J. Biol. Chem. 274 (15), 10173-10183 (1999)|  MEDLINE   99214576|\35:REFERENCE   5  (residues 1 to 1897)|\39:  AUTHORS   Ahmad,F. and Goldstein,B.J.|\71:  TITLE     Functional association between the insulin receptor and the|\74:            transmembrane protein-tyrosine phosphatase LAR in intact cells|\50:  JOURNAL   J. Biol. Chem. 272 (1), 448-457 (1997)|  MEDLINE   97150746|\35:REFERENCE   6  (residues 1 to 1897)|\53:  AUTHORS   Harder,K.W., Saw,J., Miki,N. and Jirik,F.|\77:  TITLE     Coexisting amplifications of the chromosome 1p32 genes (PTPRF and|\75:            MYCL1) encoding protein tyrosine phosphatase LAR and L-myc in a|\39:            small cell lung cancer line|\43:  JOURNAL   Genomics 27 (3), 552-553 (1995)|  MEDLINE   96047346|\35:REFERENCE   7  (residues 1 to 1897)|\69:  AUTHORS   Schaapveld,R.Q., van den Maagdenberg,A.M., Schepens,J.T.,|\77:            Weghuis,D.O., Geurts van Kessel,A., Wieringa,B. and Hendriks,W.J.|\78:  TITLE     The mouse gene Ptprf encoding the leukocyte common antigen-related|\68:            molecule LAR: cloning, characterization, and chromosomal|\24:            localization|\43:  JOURNAL   Genomics 27 (1), 124-130 (1995)|  MEDLINE   95394448|\35:REFERENCE   8  (residues 1 to 1897)|\61:  AUTHORS   O'Grady,P., Krueger,N.X., Streuli,M. and Saito,H.|\78:  TITLE     Genomic organization of the human LAR protein tyrosine phosphatase|\74:            gene and alternative splicing in the extracellular fibronectin|\28:            type-III domains|\55:  JOURNAL   J. Biol. Chem. 269 (40), 25193-25199 (1994)|  MEDLINE   95014301|\35:REFERENCE   9  (residues 1 to 1897)|\77:  AUTHORS   Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H.|\69:  TITLE     A new member of the immunoglobulin superfamily that has a|\73:            cytoplasmic region homologous to the leukocyte common antigen|\50:  JOURNAL   J. Exp. Med. 168 (5), 1523-1530 (1988)|  MEDLINE   89035978
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|25|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from Y00815.1 and BI711143.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\53:region, a single transmembrane region, and two tandem|\57:intracytoplasmic catalytic domains, and thus represents a|\66:receptor-type PTP. The extracellular region contains three Ig-like|\56:domains, and nine non-Ig like domains similar to that of|\64:neural-cell adhesion molecule. This PTP was shown to function in|\60:the regulation of epithelial cell-cell contacts at adherents|\66:junctions, as well as in the control of beta-catenin signaling. An|\59:increased expression level of this protein was found in the|\66:insulin-responsive tissue of obese, insulin-resistant individuals,|\65:and may contribute to the pathogenesis of insulin resistance. Two|\61:alternatively spliced transcript variants of this gene, which|\45:encode distinct proteins, have been reported.||\63:Transcript Variant: This variant (1) contains an extra internal|\64:fragment within the coding region when compared to variant 2. It|\66:thus encodes a protein that has a 9 aa internal fragment absent in|isoform 2.
end
obj|String*|68|\35:REFERENCE   1  (residues 1 to 1897)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   2  (residues 1 to 1897)|\51:  AUTHORS   Symons,J.R., LeVea,C.M. and Mooney,R.A.|\77:  TITLE     Expression of the leucocyte common antigen-related (LAR) tyrosine|\71:            phosphatase is regulated by cell density through functional|\32:            E-cadherin complexes|\50:  JOURNAL   Biochem. J. 365 (Pt 2), 513-519 (2002)|  MEDLINE   22090243|\69:  REMARK    GeneRIF: regulation of expression by cell density through|\43:            functional E-cadherin complexes|\35:REFERENCE   3  (residues 1 to 1897)|\71:  AUTHORS   Zabolotny,J.M., Kim,Y.B., Peroni,O.D., Kim,J.K., Pani,M.A.,|\74:            Boss,O., Klaman,L.D., Kamatkar,S., Shulman,G.I., Kahn,B.B. and|\21:            Neel,B.G.|\65:  TITLE     Overexpression of the LAR (leukocyte antigen-related)|\76:            protein-tyrosine phosphatase in muscle causes insulin resistance|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 98 (9), 5187-5192 (2001)|  MEDLINE   21221100|\35:REFERENCE   4  (residues 1 to 1897)|\62:  AUTHORS   Muller,T., Choidas,A., Reichmann,E. and Ullrich,A.|\74:  TITLE     Phosphorylation and free pool of beta-catenin are regulated by|\77:            tyrosine kinases and tyrosine phosphatases during epithelial cell|\21:            migration|\55:  JOURNAL   J. Biol. Chem. 274 (15), 10173-10183 (1999)|  MEDLINE   99214576|\35:REFERENCE   5  (residues 1 to 1897)|\39:  AUTHORS   Ahmad,F. and Goldstein,B.J.|\71:  TITLE     Functional association between the insulin receptor and the|\74:            transmembrane protein-tyrosine phosphatase LAR in intact cells|\50:  JOURNAL   J. Biol. Chem. 272 (1), 448-457 (1997)|  MEDLINE   97150746|\35:REFERENCE   6  (residues 1 to 1897)|\53:  AUTHORS   Harder,K.W., Saw,J., Miki,N. and Jirik,F.|\77:  TITLE     Coexisting amplifications of the chromosome 1p32 genes (PTPRF and|\75:            MYCL1) encoding protein tyrosine phosphatase LAR and L-myc in a|\39:            small cell lung cancer line|\43:  JOURNAL   Genomics 27 (3), 552-553 (1995)|  MEDLINE   96047346|\35:REFERENCE   7  (residues 1 to 1897)|\69:  AUTHORS   Schaapveld,R.Q., van den Maagdenberg,A.M., Schepens,J.T.,|\77:            Weghuis,D.O., Geurts van Kessel,A., Wieringa,B. and Hendriks,W.J.|\78:  TITLE     The mouse gene Ptprf encoding the leukocyte common antigen-related|\68:            molecule LAR: cloning, characterization, and chromosomal|\24:            localization|\43:  JOURNAL   Genomics 27 (1), 124-130 (1995)|  MEDLINE   95394448|\35:REFERENCE   8  (residues 1 to 1897)|\61:  AUTHORS   O'Grady,P., Krueger,N.X., Streuli,M. and Saito,H.|\78:  TITLE     Genomic organization of the human LAR protein tyrosine phosphatase|\74:            gene and alternative splicing in the extracellular fibronectin|\28:            type-III domains|\55:  JOURNAL   J. Biol. Chem. 269 (40), 25193-25199 (1994)|  MEDLINE   95014301|\35:REFERENCE   9  (residues 1 to 1897)|\77:  AUTHORS   Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H.|\69:  TITLE     A new member of the immunoglobulin superfamily that has a|\73:            cytoplasmic region homologous to the leukocyte common antigen|\50:  JOURNAL   J. Exp. Med. 168 (5), 1523-1530 (1988)|  MEDLINE   89035978
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="1"|/map="1p34"
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obj|Feature
obj|DBObj||Protein_1|||||0|0|\169:protein tyrosine phosphatase, receptor type, F polypeptide; receptor-linked protein-tyrosine phosphatase LAR; leukocyte antigen-related tyrosine phosphatase; LCA-homolog
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obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, F|isoform 1 precursor"|\21:/EC_number="3.1.3.48"
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obj|Feature
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|1|\29:REFSEQ: accession NM_002840.2
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obj|String*|9|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF|\51:VNTI URL:vnti:protein/hLAR_D2+%28NP_002831%29+PTPRF
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\28:hLyPTP_D1 (NP_057051) PTPN22|||||302014800|0|\158:lymphoid-specific protein tyrosine phosphatase isoform 1; lymphoid-specific protein tyrosine phosphatase; protein tyrosine phosphatase homolog [Homo sapiens].
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obj|String*|13|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\62:reference sequence was derived from AF077031.1 and AF001846.1.||\66:Summary: This gene encodes a protein tyrosine phosphatase which is|\63:expressed primarily in lymphoid tissues. This enzyme associates|\61:with the molecular adapter protein CBL and may be involved in|\65:regulating CBL function in the T-cell receptor signaling pathway.|\59:Alternative splicing of this gene results in two transcript|\36:variants encoding distinct isoforms.||\67:Transcript Variant: This variant (1) encodes the longer isoform (1)|\56:which is 116 aa longer than isoform 2 and has a distinct|C-terminus.
end
obj|String*|16|\34:REFERENCE   1  (residues 1 to 807)|\78:  AUTHORS   Hill,R.J., Zozulya,S., Lu,Y.L., Ward,K., Gishizky,M. and Jallal,B.|\76:  TITLE     The lymphoid protein tyrosine phosphatase Lyp interacts with the|\74:            adaptor molecule Grb2 and functions as a negative regulator of|\29:            T-cell activation|\48:  JOURNAL   Exp. Hematol. 30 (3), 237-244 (2002)|  MEDLINE   21876996|\77:  REMARK    GeneRIF: data demonstrate a novel interaction between Lyp and the|\79:            adaptor Grb2 and are consistent with a negative regulatory role for|\36:            Lyp in T-cell signaling.|\34:REFERENCE   2  (residues 1 to 807)|\68:  AUTHORS   Cohen,S., Dadi,H., Shaoul,E., Sharfe,N. and Roifman,C.M.|\74:  TITLE     Cloning and characterization of a lymphoid-specific, inducible|\51:            human protein tyrosine phosphatase, Lyp|\42:  JOURNAL   Blood 93 (6), 2013-2024 (1999)|  MEDLINE   99168989
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||JNA||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="1"|/map="1p13.3-p13.1"
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obj|Object*|0
end
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obj|DBObj||Protein_1|||||0|0|\84:lymphoid-specific protein tyrosine phosphatase; protein tyrosine phosphatase homolog
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obj|String*|2|\56:/product="lymphoid-specific protein tyrosine phosphatase|isoform 1"
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obj|DBObj||Region_1|||||0|0|PTPc
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|1|NP_057051
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obj|String*|1|\29:REFSEQ: accession NM_015967.2
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obj|String*|44|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22|\54:VNTI URL:vnti:protein/hLyPTP_D1+%28NP_057051%29+PTPN22
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end|21AAEB8
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\26:hMEG1_D1 (NP_002821) PTPN4|||||302014800|0|\184:protein tyrosine phosphatase, non-receptor type 4; megakaryocyte phosphatase; PTPase-MEG1; protein tyrosine phosphatase MEG1; megakaryocyte protein-tyrosine phosphatase [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|13|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from M68941.1 and BC010674.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\64:oncogenic transformation. This protein contains a C-terminal PTP|\58:domain and an N-terminal domain homologous to the band 4.1|\66:superfamily of cytoskeletal-associated proteins. This PTP has been|\61:shown to interact with glutamate receptor delta 2 and epsilon|\67:subunits, and is thought to play a role in signalling downstream of|\59:the glutamate receptors through tyrosine dephosphorylation.
end
obj|String*|25|\34:REFERENCE   1  (residues 1 to 926)|\74:  AUTHORS   Hironaka,K., Umemori,H., Tezuka,T., Mishina,M. and Yamamoto,T.|\76:  TITLE     The protein-tyrosine phosphatase PTPMEG interacts with glutamate|\49:            receptor delta 2 and epsilon subunits|\55:  JOURNAL   J. Biol. Chem. 275 (21), 16167-16173 (2000)|  MEDLINE   20283654|\34:REFERENCE   2  (residues 1 to 926)|\43:  AUTHORS   Gu,M., Meng,K. and Majerus,P.W.|\76:  TITLE     The effect of overexpression of the protein tyrosine phosphatase|\79:            PTPMEG on cell growth and on colony formation in soft agar in COS-7|            cells|\69:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 93 (23), 12980-12985 (1996)|  MEDLINE   97075104|\34:REFERENCE   3  (residues 1 to 926)|\34:  AUTHORS   Gu,M. and Majerus,P.W.|\69:  TITLE     The properties of the protein tyrosine phosphatase PTPMEG|\55:  JOURNAL   J. Biol. Chem. 271 (44), 27751-27759 (1996)|  MEDLINE   97066967|\34:REFERENCE   4  (residues 1 to 926)|\62:  AUTHORS   Gu,M.X., York,J.D., Warshawsky,I. and Majerus,P.W.|\66:  TITLE     Identification, cloning, and expression of a cytosolic|\77:            megakaryocyte protein-tyrosine-phosphatase with sequence homology|\39:            to cytoskeletal protein 4.1|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 88 (13), 5867-5871 (1991)|  MEDLINE   91288564
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="2"|/map="2q14.1"
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obj|Feature
obj|DBObj||Protein_1|||||0|0|\117:megakaryocyte phosphatase; PTPase-MEG1; protein tyrosine phosphatase MEG1; megakaryocyte protein-tyrosine phosphatase
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obj|String*|3|\57:/product="protein tyrosine phosphatase, non-receptor type|4"|\21:/EC_number="3.1.3.48"
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obj|DBObj||Region_1|||||0|0|PTPc
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obj|String*|1|NP_002821
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obj|String*|1|\29:REFSEQ: accession NM_002830.2
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obj|DBObj||\26:hMEG2_D1 (NP_002824) PTPN9|||||302014800|0|\113:protein tyrosine phosphatase, non-receptor type 9; protein-tyrosine phosphatase MEG2; PTPase-MEG2 [Homo sapiens].
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obj|String*|13|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from M83738.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\64:oncogenic transformation. This PTP contains an N-terminal domain|\65:that shares a significant similarity with yeast SEC14, which is a|\62:protein that has phosphatidylinositol transfer activity and is|\66:required for protein secretion through the Golgi complex in yeast.|\66:This PTP was found to be activated by polyphosphoinositide, and is|\67:thought to be involved in signaling events regulating phagocytosis.
end
obj|String*|23|\34:REFERENCE   1  (residues 1 to 593)|\69:  AUTHORS   Qi,Y., Zhao,R., Cao,H., Sui,X., Krantz,S.B. and Zhao,Z.J.|\77:  TITLE     Purification and characterization of protein tyrosine phosphatase|            PTP-MEG2|\50:  JOURNAL   J. Cell. Biochem. 86 (1), 79-89 (2002)|  MEDLINE   22106294|\74:  REMARK    GeneRIF: Purification and characterization of protein tyrosine|\32:            phosphatase PTP-MEG2|\34:REFERENCE   2  (residues 1 to 593)|\78:  AUTHORS   Kruger,J.M., Fukushima,T., Cherepanov,V., Borregaard,N., Loeve,C.,|\72:            Shek,C., Sharma,K., Tanswell,A.K., Chow,C.W. and Downey,G.P.|\67:  TITLE     Protein-tyrosine phosphatase MEG2 is expressed by human|\72:            neutrophils. Localization to the phagosome and activation by|\33:            polyphosphoinositides|\52:  JOURNAL   J. Biol. Chem. 277 (4), 2620-2628 (2002)|  MEDLINE   21659736|\34:REFERENCE   3  (residues 1 to 593)|\49:  AUTHORS   Gu,M., Warshawsky,I. and Majerus,P.W.|\63:  TITLE     Cloning and expression of a cytosolic megakaryocyte|\66:            protein-tyrosine-phosphatase with sequence homology to|\58:            retinaldehyde-binding protein and yeast SEC14p|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 89 (7), 2980-2984 (1992)|  MEDLINE   92212952
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="15"|/map="15q23"
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obj|DBObj||Protein_1|||||0|0|\46:protein-tyrosine phosphatase MEG2; PTPase-MEG2
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obj|String*|3|\57:/product="protein tyrosine phosphatase, non-receptor type|9"|\21:/EC_number="3.1.3.48"
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obj|DBObj||Region_1|||||0|0|PTPc
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|1|NP_002824
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obj|String*|1|\29:REFSEQ: accession NM_002833.2
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obj|String*|34|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9|\52:VNTI URL:vnti:protein/hMEG2_D1+%28NP_002824%29+PTPN9
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end|351FA78
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\28:hPCPTP1_D1 (NP_002840) PTPRR|||||302014800|0|\234:protein tyrosine phosphatase, receptor type, R isoform 1 precursor; protein tyrosine phosphatase, receptor type, Q; protein-tyrosine phosphatase NC-PTPCOM1; protein tyrosine phosphatase Cr1PTPase precursor; Ch-1 PTPase [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|20|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from D64053.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\65:region, a single transmembrane region, and a single intracellular|\63:catalytic domains, and thus represents a receptor-type PTP. The|\64:similar gene predominately expressed in mouse brain was found to|\59:associate with, and thus regulate the activity and cellular|\65:localization of MAP kinases. The rat counterpart of this gene was|\58:reported to be regulated by the nerve growth factor, which|\58:suggested the function of this gene in neuronal growth and|differentiation.||\64:Transcript Variant: This variant (1) contains a different 5' end|\65:region when compared to variant 2. It thus encodes a protein that|\50:has a longer N-terminus, as compared to isoform 2.
end
obj|String*|26|\34:REFERENCE   1  (residues 1 to 657)|\55:  AUTHORS   Blanco-Aparicio,C., Torres,J. and Pulido,R.|\78:  TITLE     A novel regulatory mechanism of MAP kinases activation and nuclear|\77:            translocation mediated by PKA and the PTP-SL tyrosine phosphatase|\51:  JOURNAL   J. Cell Biol. 147 (6), 1129-1136 (1999)|  MEDLINE   20069779|\34:REFERENCE   2  (residues 1 to 657)|\77:  AUTHORS   Shiozuka,K., Watanabe,Y., Ikeda,T., Hashimoto,S. and Kawashima,H.|\70:  TITLE     Cloning and expression of PCPTP1 encoding protein tyrosine|\23:            phosphatase|\40:  JOURNAL   Gene 162 (2), 279-284 (1995)|  MEDLINE   96032358|\48:  REMARK    founctional study of the rat homolog|\34:REFERENCE   3  (residues 1 to 657)|\57:  AUTHORS   Ogata,M., Sawada,M., Fujino,Y. and Hamaoka,T.|\78:  TITLE     cDNA cloning and characterization of a novel receptor-type protein|\69:            tyrosine phosphatase expressed predominantly in the brain|\52:  JOURNAL   J. Biol. Chem. 270 (5), 2337-2343 (1995)|  MEDLINE   95138207|\49:  REMARK    functional study of the mouse homolog|\34:REFERENCE   4  (residues 1 to 657)|\39:  AUTHORS   Sharma,E. and Lombroso,P.J.|\75:  TITLE     A neuronal protein tyrosine phosphatase induced by nerve growth|            factor|\48:  JOURNAL   J. Biol. Chem. 270 (1), 49-53 (1995)|  MEDLINE   95113874
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="12"|/map="12q15"
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obj|DBObj||Protein_1|||||0|0|\150:protein tyrosine phosphatase, receptor type, Q; protein-tyrosine phosphatase NC-PTPCOM1; protein tyrosine phosphatase Cr1PTPase precursor; Ch-1 PTPase
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obj|String*|2|\56:/product="protein tyrosine phosphatase, receptor type, R|isoform 1 precursor"
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obj|String*|1|\29:REFSEQ: accession NM_002849.2
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obj|IxMolX
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obj|String*|17|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from M93425.1.|\58:On Jan 25, 2002 this sequence version replaced gi:4506287.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP contains a C-terminal PEST|\64:motif, which serves as a protein-protein interaction domain, and|\63:may be related to protein intracellular half-life. This PTP was|\64:found to bind and dephosphorylate the product of oncogene c-ABL,|\67:thus may play a role in oncogenesis. This PTP was shown to interact|\59:with, and dephosphorylate, various of cytoskeleton and cell|\67:adhesion molecules, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and|\66:paxillin, which suggested its regulatory roles in controlling cell|shape and mobility.
end
obj|String*|54|\34:REFERENCE   1  (residues 1 to 780)|\67:  AUTHORS   Lyons,P.D., Dunty,J.M., Schaefer,E.M. and Schaller,M.D.|\77:  TITLE     Inhibition of the catalytic activity of cell adhesion kinase beta|\75:            by protein-tyrosine phosphatase-PEST-mediated dephosphorylation|\55:  JOURNAL   J. Biol. Chem. 276 (26), 24422-24431 (2001)|  MEDLINE   21316574|\34:REFERENCE   2  (residues 1 to 780)|\76:  AUTHORS   Cong,F., Spencer,S., Cote,J.F., Wu,Y., Tremblay,M.L., Lasky,L.A.|\25:            and Goff,S.P.|\79:  TITLE     Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine|\76:            phosphatase to the c-Abl kinase to mediate Abl dephosphorylation|\45:  JOURNAL   Mol. Cell 6 (6), 1413-1423 (2000)|  MEDLINE   21111050|\34:REFERENCE   3  (residues 1 to 780)|\79:  AUTHORS   Shen,Y., Lyons,P., Cooley,M., Davidson,D., Veillette,A., Salgia,R.,|\42:            Griffin,J.D. and Schaller,M.D.|\72:  TITLE     The noncatalytic domain of protein-tyrosine phosphatase-PEST|\58:            targets paxillin for dephosphorylation in vivo|\52:  JOURNAL   J. Biol. Chem. 275 (2), 1405-1413 (2000)|  MEDLINE   20092920|\34:REFERENCE   4  (residues 1 to 780)|\79:  AUTHORS   Nishiya,N., Iwabuchi,Y., Shibanuma,M., Cote,J.F., Tremblay,M.L. and|            Nose,K.|\70:  TITLE     Hic-5, a paxillin homologue, binds to the protein-tyrosine|\64:            phosphatase PEST (PTP-PEST) through its LIM 3 domain|\53:  JOURNAL   J. Biol. Chem. 274 (14), 9847-9853 (1999)|  MEDLINE   99194842|\34:REFERENCE   5  (residues 1 to 780)|\38:  AUTHORS   Garton,A.J. and Tonks,N.K.|\69:  TITLE     Regulation of fibroblast motility by the protein tyrosine|\32:            phosphatase PTP-PEST|\52:  JOURNAL   J. Biol. Chem. 274 (6), 3811-3818 (1999)|  MEDLINE   99121127|\34:REFERENCE   6  (residues 1 to 780)|\79:  AUTHORS   Takekawa,M., Itoh,F., Hinoda,Y., Adachi,M., Ariyama,T., Inazawa,J.,|\32:            Imai,K. and Yachi,A.|\75:  TITLE     Chromosomal localization of the protein tyrosine phosphatase G1|\74:            gene and characterization of the aberrant transcripts in human|\30:            colon cancer cells|\46:  JOURNAL   FEBS Lett. 339 (3), 222-228 (1994)|  MEDLINE   94156037|\34:REFERENCE   7  (residues 1 to 780)|\56:  AUTHORS   Yang,Q., Co,D., Sommercorn,J. and Tonks,N.K.|\63:  TITLE     Cloning and expression of PTP-PEST. A novel, human,|\57:            nontransmembrane protein tyrosine phosphatase|\52:  JOURNAL   J. Biol. Chem. 268 (9), 6622-6628 (1993)|  MEDLINE   93203262|\34:REFERENCE   8  (residues 1 to 780)|\78:  AUTHORS   Takekawa,M., Itoh,F., Hinoda,Y., Arimura,Y., Toyota,M., Sekiya,M.,|\43:            Adachi,M., Imai,K. and Yachi,A.|\73:  TITLE     Cloning and characterization of a human cDNA encoding a novel|\61:            putative cytoplasmic protein-tyrosine-phosphatase|\68:  JOURNAL   Biochem. Biophys. Res. Commun. 189 (2), 1223-1230 (1992)|  MEDLINE   93112015
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|DBObj||\27:hPTP1B_D1 (NP_002818) PTPN1|||||302014800|0|\173:protein tyrosine phosphatase, non-receptor type 1; non-receptor tyrosine phophatase 1; protein tyrosine phophatase 1B; protein tyrosine phophatase, placental [Homo sapiens].
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obj|String*|18|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from M33689.1 and AU117677.1.||\67:Summary: The protein encoded by this gene is the founding member of|\65:the protein tyrosine phosphatase (PTP) family, which was isolated|\61:and identified based on its enzymatic activity and amino acid|\66:sequence. PTPs catalyze the hydrolysis of the phosphate monoesters|\66:specifically on tyrosine residues. Members of the PTP family share|\62:a highly conserved catalytic motif, which is essential for the|\65:catalytic activity. PTPs are known to be signaling molecules that|\63:regulate a variety of cellular processes including cell growth,|\66:differentiation, mitotic cycle, and oncogenic transformation. This|\60:PTP has been shown to act as a negative regulator of insulin|\62:signaling by dephosphorylating the phosphotryosine residues of|\54:insulin receptor kinase. This PTP was also reported to|\67:dephosphorylate epidermal growth factor receptor kinase, as well as|\63:JAK2 and TYK2 kinases, which implicated the role of this PTP in|\65:cell growth control, and cell response to interferon stimulation.
end
obj|String*|115|\34:REFERENCE   1  (residues 1 to 435)|\34:  AUTHORS   Li,S. and Whorton,A.R.|\76:  TITLE     Regulation of protein tyrosine phosphatase 1B in intact cells by|\27:            S-nitrosothiols|\59:  JOURNAL   Arch. Biochem. Biophys. 410 (2), 269-279 (2003)|  MEDLINE   22461115|\79:  REMARK    GeneRIF: PTP1B inhibition by S-nitrosylation is caused by formation|\32:            of a mixed disulfide|\34:REFERENCE   2  (residues 1 to 435)|\36:  AUTHORS   Fukada,T. and Tonks,N.K.|\70:  TITLE     Identification of YB-1 as a regulator of PTP1B expression:|\73:            implications for regulation of insulin and cytokine signaling|\42:  JOURNAL   EMBO J. 22 (3), 479-493 (2003)|  MEDLINE   22441887|\71:  REMARK    GeneRIF: Data show that Y box-binding protein-1 (YB-1) is a|\76:            regulator of protein tyrosine phosphatase 1B (PTP1B) expression,|\71:            and highlight PTP1B as a critical regulator of insulin- and|\50:            cytokine-mediated signal transduction.|\34:REFERENCE   3  (residues 1 to 435)|\77:  AUTHORS   Yigzaw,Y., Poppleton,H.M., Sreejayan,N., Hassid,A. and Patel,T.B.|\79:  TITLE     Protein-tyrosine phosphatase-1B (PTP1B) mediates the anti-migratory|\30:            actions of Sprouty|\50:  JOURNAL   J. Biol. Chem. 278 (1), 284-288 (2003)|  MEDLINE   22393490|\75:  REMARK    GeneRIF: Data show that an increase in soluble protein-tyrosine|\78:            phosphatase 1B activity contributes to the anti-migratory, but not|\55:            anti-mitogenic, actions of human Sprouty 2.|\34:REFERENCE   4  (residues 1 to 435)|\73:  AUTHORS   Di Paola,R., Frittitta,L., Miscio,G., Bozzali,M., Baratta,R.,|\66:            Centra,M., Spampinato,D., Santagati,M.G., Ercolino,T.,|\75:            Cisternino,C., Soccio,T., Mastroianno,S., Tassi,V., Almgren,P.,|\52:            Pizzuti,A., Vigneri,R. and Trischitta,V.|\78:  TITLE     A variation in 3' UTR of hPTP1B increases specific gene expression|\50:            and associates with insulin resistance|\53:  JOURNAL   Am. J. Hum. Genet. 70 (3), 806-812 (2002)|  MEDLINE   21832513|\74:  REMARK    GeneRIF: variation in 3' UTR of hPTP1B increases specific gene|\61:            expression and associates with insulin resistance|\34:REFERENCE   5  (residues 1 to 435)|\77:  AUTHORS   Myers,M.P., Andersen,J.N., Cheng,A., Tremblay,M.L., Horvath,C.M.,|\64:            Parisien,J.P., Salmeen,A., Barford,D. and Tonks,N.K.|\75:  TITLE     TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B|\55:  JOURNAL   J. Biol. Chem. 276 (51), 47771-47774 (2001)|  MEDLINE   21611285|\34:REFERENCE   6  (residues 1 to 435)|\58:  AUTHORS   Wang,J., Cheung,A.T., Kolls,J.K., Starks,W.W.,|\62:            Martinez-Hernandez,A., Dietzen,D. and Bryer-Ash,M.|\76:  TITLE     Effects of adenovirus-mediated liver-selective overexpression of|\74:            protein tyrosine phosphatase-1b on insulin sensitivity in vivo|\53:  JOURNAL   Diabetes Obes Metab 3 (5), 367-380 (2001)|  MEDLINE   21560532|\78:  REMARK    GeneRIF: Moderate overabundance of PTP-1B in liver tissue does not|\78:            alter insulin action on glucose metabolism, and the site of action|\74:            of PTP-1B is presumably at insulin-responsive target tissue or|\41:            tissues other than the liver.|\34:REFERENCE   7  (residues 1 to 435)|\45:  AUTHORS   Dadke,S., Kusari,A. and Kusari,J.|\74:  TITLE     Phosphorylation and activation of protein tyrosine phosphatase|\40:            (PTP) 1B by insulin receptor|\57:  JOURNAL   Mol. Cell. Biochem. 221 (1-2), 147-154 (2001)|  MEDLINE   21396990|\34:REFERENCE   8  (residues 1 to 435)|\67:  AUTHORS   Egawa,K., Maegawa,H., Shimizu,S., Morino,K., Nishio,Y.,|\78:            Bryer-Ash,M., Cheung,A.T., Kolls,J.K., Kikkawa,R. and Kashiwagi,A.|\72:  TITLE     Protein-tyrosine phosphatase-1B negatively regulates insulin|\59:            signaling in l6 myocytes and Fao hepatoma cells|\55:  JOURNAL   J. Biol. Chem. 276 (13), 10207-10211 (2001)|  MEDLINE   21167830|\34:REFERENCE   9  (residues 1 to 435)|\76:  AUTHORS   Salmeen,A., Andersen,J.N., Myers,M.P., Tonks,N.K. and Barford,D.|\79:  TITLE     Molecular basis for the dephosphorylation of the activation segment|\70:            of the insulin receptor by protein tyrosine phosphatase 1B|\45:  JOURNAL   Mol. Cell 6 (6), 1401-1412 (2000)|  MEDLINE   21111049|\34:REFERENCE   10 (residues 1 to 435)|\65:  AUTHORS   Peters,G.H., Iversen,L.F., Branner,S., Andersen,H.S.,|\67:            Mortensen,S.B., Olsen,O.H., Moller,K.B. and Moller,N.P.|\72:  TITLE     Residue 259 is a key determinant of substrate specificity of|\54:            protein-tyrosine phosphatases 1B and alpha|\55:  JOURNAL   J. Biol. Chem. 275 (24), 18201-18209 (2000)|  MEDLINE   20309769|\34:REFERENCE   11 (residues 1 to 435)|\64:  AUTHORS   Ahmad,F., Li,P.M., Meyerovitch,J. and Goldstein,B.J.|\78:  TITLE     Osmotic loading of neutralizing antibodies demonstrates a role for|\73:            protein-tyrosine phosphatase 1B in negative regulation of the|\34:            insulin action pathway|\55:  JOURNAL   J. Biol. Chem. 270 (35), 20503-20508 (1995)|  MEDLINE   95386495|\34:REFERENCE   12 (residues 1 to 435)|\76:  AUTHORS   Milarski,K.L., Zhu,G., Pearl,C.G., McNamara,D.J., Dobrusin,E.M.,|\79:            MacLean,D., Thieme-Sefler,A., Zhang,Z.Y., Sawyer,T., Decker,S.J. et|            al.|\78:  TITLE     Sequence specificity in recognition of the epidermal growth factor|\55:            receptor by protein tyrosine phosphatase 1B|\55:  JOURNAL   J. Biol. Chem. 268 (31), 23634-23639 (1993)|  MEDLINE   94043167|\34:REFERENCE   13 (residues 1 to 435)|\69:  AUTHORS   Brown-Shimer,S., Johnson,K.A., Lawrence,J.B., Johnson,C.,|\48:            Bruskin,A., Green,N.R. and Hill,D.E.|\79:  TITLE     Molecular cloning and chromosome mapping of the human gene encoding|\49:            protein phosphotyrosyl phosphatase 1B|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (13), 5148-5152 (1990)|  MEDLINE   90311360|\34:REFERENCE   14 (residues 1 to 435)|\79:  AUTHORS   Chernoff,J., Schievella,A.R., Jost,C.A., Erikson,R.L. and Neel,B.G.|\76:  TITLE     Cloning of a cDNA for a major human protein-tyrosine-phosphatase|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (7), 2735-2739 (1990)|  MEDLINE   90207272|\34:REFERENCE   15 (residues 1 to 435)|\75:  AUTHORS   Charbonneau,H., Tonks,N.K., Kumar,S., Diltz,C.D., Harrylock,M.,|\62:            Cool,D.E., Krebs,E.G., Fischer,E.H. and Walsh,K.A.|\76:  TITLE     Human placenta protein-tyrosine-phosphatase: amino acid sequence|\66:            and relationship to a family of receptor-like proteins|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 86 (14), 5252-5256 (1989)|  MEDLINE   89315775
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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end|33946E8
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obj|BioObject
obj|DBObj||\30:hPTPalpha_D1 (NP_002827) PTPRA|||||302014800|0|\287:protein tyrosine phosphatase, receptor type, A isoform 1 precursor; protein tyrosine phosphatase, receptor type, alpha polypeptide; PTPase-alpha; Leukocyte common antigen-related peptide (protein tyrosine phosphate); tyrosine phosphatase alpha; PTPLCA-related phosphatase [Homo sapiens].
end|2|2|
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end
obj|String*|22|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from M34668.1 and AI284972.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\53:domain, a single transmembrane segment and two tandem|\57:intracytoplasmic catalytic domains, and thus represents a|\65:receptor-type PTP. This PTP has been shown to dephosphorylate and|\62:activate Src family tyrosine kinases, and is implicated in the|\66:regulation of integrin signaling, cell adhesion and proliferation.|\67:Three alternatively spliced variants of this gene, which encode two|\38:distinct isoforms, have been reported.||\61:Transcript Variant: This variant (1) contains a unique 5' UTR|\65:region when compared to other variants. The genomic exons forming|\61:the 5' end region of this transcript are also used to form an|\67:internal coding region in the transcripts of VPS16, a distinct gene|\57:located at the locus immediately upstream of this gene on|\60:chromosome 20. This variant encodes the longest isoform (1).
end
obj|String*|86|\34:REFERENCE   1  (residues 1 to 802)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\34:REFERENCE   2  (residues 1 to 802)|\37:  AUTHORS   Mustelin,T. and Hunter,T.|\74:  TITLE     Meeting at mitosis: cell cycle-specific regulation of c-Src by|\21:            RPTPalpha|\43:  JOURNAL   Sci STKE 2002 (115), PE3 (2002)|  MEDLINE   21655780|\78:  REMARK    GeneRIF: In entering mitosis the cell cycle-specific regulation of|\79:            c-Src by RPTPalpha can occur by dephosphorylation of phospho-Tyr527|\77:            that activates c-Src in a reaction catalyzed by the transmembrane|\65:            receptor-like protein tyrosine phosphatase RPTPalpha.|\34:REFERENCE   3  (residues 1 to 802)|\69:  AUTHORS   Ardini,E., Agresti,R., Tagliabue,E., Greco,M., Aiello,P.,|\43:            Yang,L.T., Menard,S. and Sap,J.|\75:  TITLE     Expression of protein tyrosine phosphatase alpha (RPTPalpha) in|\77:            human breast cancer correlates with low tumor grade, and inhibits|\50:            tumor cell growth in vitro and in vivo|\46:  JOURNAL   Oncogene 19 (43), 4979-4987 (2000)|  MEDLINE   20499263|\34:REFERENCE   4  (residues 1 to 802)|\65:  AUTHORS   Peters,G.H., Iversen,L.F., Branner,S., Andersen,H.S.,|\67:            Mortensen,S.B., Olsen,O.H., Moller,K.B. and Moller,N.P.|\72:  TITLE     Residue 259 is a key determinant of substrate specificity of|\54:            protein-tyrosine phosphatases 1B and alpha|\55:  JOURNAL   J. Biol. Chem. 275 (24), 18201-18209 (2000)|  MEDLINE   20309769|\34:REFERENCE   5  (residues 1 to 802)|\65:  AUTHORS   Harder,K.W., Moller,N.P., Peacock,J.W. and Jirik,F.R.|\79:  TITLE     Protein-tyrosine phosphatase alpha regulates Src family kinases and|\43:            alters cell-substratum adhesion|\55:  JOURNAL   J. Biol. Chem. 273 (48), 31890-31900 (1998)|  MEDLINE   99041953|\34:REFERENCE   6  (residues 1 to 802)|\47:  AUTHORS   Zheng,X.M., Wang,Y. and Pallen,C.J.|\77:  TITLE     Cell transformation and activation of pp60c-src by overexpression|\45:            of a protein tyrosine phosphatase|\45:  JOURNAL   Nature 359 (6393), 336-339 (1992)|  MEDLINE   93024881|\34:REFERENCE   7  (residues 1 to 802)|\73:  AUTHORS   Rao,V.V., Loffler,C., Sap,J., Schlessinger,J. and Hansmann,I.|\79:  TITLE     The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is|\76:            assigned to human chromosome 20p12-pter by in situ hybridization|\26:            (ISH and FISH)|\43:  JOURNAL   Genomics 13 (3), 906-907 (1992)|  MEDLINE   92347910|\34:REFERENCE   8  (residues 1 to 802)|\47:  AUTHORS   Ohagi,S., Nishi,M. and Steiner,D.F.|\67:  TITLE     Sequence of a cDNA encoding human LRP (leukocyte common|\36:            antigen-related peptide)|\51:  JOURNAL   Nucleic Acids Res. 18 (23), 7159 (1990)|  MEDLINE   91088320|\34:REFERENCE   9  (residues 1 to 802)|\65:  AUTHORS   Jirik,F.R., Janzen,N.M., Melhado,I.G. and Harder,K.W.|\74:  TITLE     Cloning and chromosomal assignment of a widely expressed human|\54:            receptor-like protein-tyrosine phosphatase|\48:  JOURNAL   FEBS Lett. 273 (1-2), 239-242 (1990)|  MEDLINE   91032191|\34:REFERENCE   10 (residues 1 to 802)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018|\34:REFERENCE   11 (residues 1 to 802)|\74:  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,|\49:            Ricca,G., Jaye,M. and Schlessinger,J.|\76:  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene|\77:            family of receptor-linked protein-tyrosine-phosphatases expressed|            in brain|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990)|  MEDLINE   90384936|\34:REFERENCE   12 (residues 1 to 802)|\64:  AUTHORS   Sap,J., D'Eustachio,P., Givol,D. and Schlessinger,J.|\74:  TITLE     Cloning and expression of a widely expressed receptor tyrosine|\23:            phosphatase|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (16), 6112-6116 (1990)|  MEDLINE   90349565
end
obj|Object*|0
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="20"|/map="20p13"
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obj|DBObj||Protein_1|||||0|0|\203:protein tyrosine phosphatase, receptor type, alpha polypeptide; PTPase-alpha; Leukocyte common antigen-related peptide (protein tyrosine phosphate); tyrosine phosphatase alpha; PTPLCA-related phosphatase
end|270|270|||0|1|280|1|1|1|1|1..802
obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, A|isoform 1 precursor"|\21:/EC_number="3.1.3.48"
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obj|DBObj||Region_1|||||0|0|PTPc
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|1|NP_002827
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obj|String*|12|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Primates|Catarrhini|Hominidae|Homo
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obj|String*|1|\29:REFSEQ: accession NM_002836.2
end
obj|String*|50|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D1+%28NP_002827%29+PTPRA
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end|201FA40
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\30:hPTPalpha_D2 (NP_002827) PTPRA|||||302014800|0|\287:protein tyrosine phosphatase, receptor type, A isoform 1 precursor; protein tyrosine phosphatase, receptor type, alpha polypeptide; PTPase-alpha; Leukocyte common antigen-related peptide (protein tyrosine phosphate); tyrosine phosphatase alpha; PTPLCA-related phosphatase [Homo sapiens].
end|2|2|
obj|String*|0
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obj|String*|22|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from M34668.1 and AI284972.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\53:domain, a single transmembrane segment and two tandem|\57:intracytoplasmic catalytic domains, and thus represents a|\65:receptor-type PTP. This PTP has been shown to dephosphorylate and|\62:activate Src family tyrosine kinases, and is implicated in the|\66:regulation of integrin signaling, cell adhesion and proliferation.|\67:Three alternatively spliced variants of this gene, which encode two|\38:distinct isoforms, have been reported.||\61:Transcript Variant: This variant (1) contains a unique 5' UTR|\65:region when compared to other variants. The genomic exons forming|\61:the 5' end region of this transcript are also used to form an|\67:internal coding region in the transcripts of VPS16, a distinct gene|\57:located at the locus immediately upstream of this gene on|\60:chromosome 20. This variant encodes the longest isoform (1).
end
obj|String*|86|\34:REFERENCE   1  (residues 1 to 802)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\34:REFERENCE   2  (residues 1 to 802)|\37:  AUTHORS   Mustelin,T. and Hunter,T.|\74:  TITLE     Meeting at mitosis: cell cycle-specific regulation of c-Src by|\21:            RPTPalpha|\43:  JOURNAL   Sci STKE 2002 (115), PE3 (2002)|  MEDLINE   21655780|\78:  REMARK    GeneRIF: In entering mitosis the cell cycle-specific regulation of|\79:            c-Src by RPTPalpha can occur by dephosphorylation of phospho-Tyr527|\77:            that activates c-Src in a reaction catalyzed by the transmembrane|\65:            receptor-like protein tyrosine phosphatase RPTPalpha.|\34:REFERENCE   3  (residues 1 to 802)|\69:  AUTHORS   Ardini,E., Agresti,R., Tagliabue,E., Greco,M., Aiello,P.,|\43:            Yang,L.T., Menard,S. and Sap,J.|\75:  TITLE     Expression of protein tyrosine phosphatase alpha (RPTPalpha) in|\77:            human breast cancer correlates with low tumor grade, and inhibits|\50:            tumor cell growth in vitro and in vivo|\46:  JOURNAL   Oncogene 19 (43), 4979-4987 (2000)|  MEDLINE   20499263|\34:REFERENCE   4  (residues 1 to 802)|\65:  AUTHORS   Peters,G.H., Iversen,L.F., Branner,S., Andersen,H.S.,|\67:            Mortensen,S.B., Olsen,O.H., Moller,K.B. and Moller,N.P.|\72:  TITLE     Residue 259 is a key determinant of substrate specificity of|\54:            protein-tyrosine phosphatases 1B and alpha|\55:  JOURNAL   J. Biol. Chem. 275 (24), 18201-18209 (2000)|  MEDLINE   20309769|\34:REFERENCE   5  (residues 1 to 802)|\65:  AUTHORS   Harder,K.W., Moller,N.P., Peacock,J.W. and Jirik,F.R.|\79:  TITLE     Protein-tyrosine phosphatase alpha regulates Src family kinases and|\43:            alters cell-substratum adhesion|\55:  JOURNAL   J. Biol. Chem. 273 (48), 31890-31900 (1998)|  MEDLINE   99041953|\34:REFERENCE   6  (residues 1 to 802)|\47:  AUTHORS   Zheng,X.M., Wang,Y. and Pallen,C.J.|\77:  TITLE     Cell transformation and activation of pp60c-src by overexpression|\45:            of a protein tyrosine phosphatase|\45:  JOURNAL   Nature 359 (6393), 336-339 (1992)|  MEDLINE   93024881|\34:REFERENCE   7  (residues 1 to 802)|\73:  AUTHORS   Rao,V.V., Loffler,C., Sap,J., Schlessinger,J. and Hansmann,I.|\79:  TITLE     The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is|\76:            assigned to human chromosome 20p12-pter by in situ hybridization|\26:            (ISH and FISH)|\43:  JOURNAL   Genomics 13 (3), 906-907 (1992)|  MEDLINE   92347910|\34:REFERENCE   8  (residues 1 to 802)|\47:  AUTHORS   Ohagi,S., Nishi,M. and Steiner,D.F.|\67:  TITLE     Sequence of a cDNA encoding human LRP (leukocyte common|\36:            antigen-related peptide)|\51:  JOURNAL   Nucleic Acids Res. 18 (23), 7159 (1990)|  MEDLINE   91088320|\34:REFERENCE   9  (residues 1 to 802)|\65:  AUTHORS   Jirik,F.R., Janzen,N.M., Melhado,I.G. and Harder,K.W.|\74:  TITLE     Cloning and chromosomal assignment of a widely expressed human|\54:            receptor-like protein-tyrosine phosphatase|\48:  JOURNAL   FEBS Lett. 273 (1-2), 239-242 (1990)|  MEDLINE   91032191|\34:REFERENCE   10 (residues 1 to 802)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018|\34:REFERENCE   11 (residues 1 to 802)|\74:  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,|\49:            Ricca,G., Jaye,M. and Schlessinger,J.|\76:  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene|\77:            family of receptor-linked protein-tyrosine-phosphatases expressed|            in brain|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990)|  MEDLINE   90384936|\34:REFERENCE   12 (residues 1 to 802)|\64:  AUTHORS   Sap,J., D'Eustachio,P., Givol,D. and Schlessinger,J.|\74:  TITLE     Cloning and expression of a widely expressed receptor tyrosine|\23:            phosphatase|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (16), 6112-6116 (1990)|  MEDLINE   90349565
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="20"|/map="20p13"
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obj|DBObj||Protein_1|||||0|0|\203:protein tyrosine phosphatase, receptor type, alpha polypeptide; PTPase-alpha; Leukocyte common antigen-related peptide (protein tyrosine phosphate); tyrosine phosphatase alpha; PTPLCA-related phosphatase
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obj|String*|1|\29:REFSEQ: accession NM_002836.2
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obj|String*|13|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA|\56:VNTI URL:vnti:protein/hPTPalpha_D2+%28NP_002827%29+PTPRA
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obj|DBObj||\29:hPTPBAS_D1 (NP_006255) PTPN13|||||302014800|0|\314:protein tyrosine phosphatase, non-receptor type 13 isoform 2; protein tyrosine phosphatase, nonreceptor type 13; protein tyrosine phosphatase 1E; Fas-associated phosphatase-1; protein-tyrosine phosphatase 1, Fas-associated; protein-tyrosine phophatase PTPL1; APO-1/CD95 (Fas)-associated phosphatase [Homo sapiens].
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obj|String*|24|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from D21210.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\58:oncogenic transformation. This PTP is a large protein that|\63:possesses a PTP domain at C-terminus, and multiple noncatalytic|\59:domains, which include a domain with similarity to band 4.1|\57:superfamily of cytoskeletal-associated proteins, a region|\64:consisting of five PDZ domains, and a leucine zipper motif. This|\65:PTP was found to interact with, and dephosphorylate Fas receptor,|\64:as well as IkappaBalpha through the PDZ domains, which suggested|\65:its role in Fas mediated programmed cell death. This PTP was also|\62:shown to interact with GTPase-activating protein, and thus may|\54:function as a regulator of Rho signaling pathway. Four|\64:alternatively spliced transcript variants, which encode distinct|\29:proteins, have been reported.||\63:Transcript Variant: This variant (2) lacks an internal fragment|\56:within the coding region when compared to variant 4. The|\59:translation remains in frame, and the encoded protein lacks|\41:internal 19 aa, as compared to isoform 4.
end
obj|String*|122|\35:REFERENCE   1  (residues 1 to 2466)|\78:  AUTHORS   Yoshida,S., Harada,H., Nagai,H., Fukino,K., Teramoto,A. and Emi,M.|\78:  TITLE     Head-to-head juxtaposition of Fas-associated phosphatase-1 (FAP-1)|\79:            and c-Jun NH2-terminal kinase 3 (JNK3) genes: genomic structure and|\49:            seven polymorphisms of the FAP-1 gene|\50:  JOURNAL   J. Hum. Genet. 47 (11), 614-619 (2002)|  MEDLINE   22323362|\74:  REMARK    GeneRIF: Shares a promoter region with the tightly linked gene|\58:            encoding stress-activated protein kinase JNK3.|\35:REFERENCE   2  (residues 1 to 2466)|\69:  AUTHORS   Bompard,G., Puech,C., Prebois,C., Vignon,F. and Freiss,G.|\74:  TITLE     Protein-tyrosine phosphatase PTPL1/FAP-1 triggers apoptosis in|\37:            human breast cancer cells|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47861-47869 (2002)|  MEDLINE   22344658|\75:  REMARK    GeneRIF: PTPL1/FAP-1 has a key role in the apoptotic process in|\79:            human breast cancer cells independent of Fas but associated with an|\52:            early inhibition of the insulin receptor|\61:            substrate-1/phosphatidylinositol 3-kinase pathway|\35:REFERENCE   3  (residues 1 to 2466)|\59:  AUTHORS   Kozlov,G., Banville,D., Gehring,K. and Ekiel,I.|\70:  TITLE     Solution structure of the PDZ2 domain from cytosolic human|\79:            phosphatase hPTP1E complexed with a peptide reveals contribution of|\66:            the beta2-beta3 loop to PDZ domain-ligand interactions|\49:  JOURNAL   J. Mol. Biol. 320 (4), 813-820 (2002)|  MEDLINE   22090786|\72:  REMARK    GeneRIF: PDZ2 domain from cytosolic human phosphatase hPTP1E|\73:            complexed with peptide, RA-GEF-2, reveals contribution of the|\62:            beta2-beta3 loop to PDZ domain-ligand interactions|\35:REFERENCE   4  (residues 1 to 2466)|\69:  AUTHORS   Walma,T., Spronk,C.A., Tessari,M., Aelen,J., Schepens,J.,|\40:            Hendriks,W. and Vuister,G.W.|\77:  TITLE     Structure, dynamics and binding characteristics of the second PDZ|\28:            domain of PTP-BL|\51:  JOURNAL   J. Mol. Biol. 316 (5), 1101-1110 (2002)|  MEDLINE   21881810|\75:  REMARK    GeneRIF: Structure, dynamics and binding characteristics of the|\39:            second PDZ domain of PTP-BL|\35:REFERENCE   5  (residues 1 to 2466)|\71:  AUTHORS   Marin,L., Minguela,A., Moya-Quiles,M.R., Torio,A., Muro,M.,|\73:            Garcia-Alonso,A.M., Sanchez-Bueno,F., Bru,M., Parrilla,P. and|\30:            Alvarez-Lopez,M.R.|\74:  TITLE     Expression of CD95 and apoptosis induction in peripheral blood|\45:            cells from liver graft recipients|\52:  JOURNAL   Transplant. Proc. 34 (1), 280-282 (2002)|  MEDLINE   21957524|\75:  REMARK    GeneRIF: expression and apoptosis induction in peripheral blood|\34:            cells from liver graft|\35:REFERENCE   6  (residues 1 to 2466)|\43:  AUTHORS   Nakai,Y., Irie,S. and Sato,T.A.|\75:  TITLE     Identification of IkappaBalpha as a substrate of Fas-associated|\25:            phosphatase-1|\55:  JOURNAL   Eur. J. Biochem. 267 (24), 7170-7175 (2000)|  MEDLINE   20558254|\35:REFERENCE   7  (residues 1 to 2466)|\76:  AUTHORS   Irie,S., Hachiya,T., Rabizadeh,S., Maruyama,W., Mukai,J., Li,Y.,|\50:            Reed,J.C., Bredesen,D.E. and Sato,T.A.|\79:  TITLE     Functional interaction of Fas-associated phosphatase-1 (FAP-1) with|\61:            p75(NTR) and their effect on NF-kappaB activation|\46:  JOURNAL   FEBS Lett. 460 (2), 191-198 (1999)|  MEDLINE   20012928|\35:REFERENCE   8  (residues 1 to 2466)|\70:  AUTHORS   Maekawa,K., Imagawa,N., Naito,A., Harada,S., Yoshie,O. and|\21:            Takagi,S.|\72:  TITLE     Association of protein-tyrosine phosphatase PTP-BAS with the|\72:            transcription-factor-inhibitory protein IkappaBalpha through|\67:            interaction between the PDZ1 domain and ankyrin repeats|\50:  JOURNAL   Biochem. J. 337 (Pt 2), 179-184 (1999)|  MEDLINE   99102074|\35:REFERENCE   9  (residues 1 to 2466)|\75:  AUTHORS   Saras,J., Franzen,P., Aspenstrom,P., Hellman,U., Gonez,L.J. and|\23:            Heldin,C.H.|\74:  TITLE     A novel GTPase-activating protein for Rho interacts with a PDZ|\60:            domain of the protein-tyrosine phosphatase PTPL1|\55:  JOURNAL   J. Biol. Chem. 272 (39), 24333-24338 (1997)|  MEDLINE   97450957|\35:REFERENCE   10 (residues 1 to 2466)|\61:  AUTHORS   Saras,J., Engstrom,U., Gonez,L.J. and Heldin,C.H.|\75:  TITLE     Characterization of the interactions between PDZ domains of the|\77:            protein-tyrosine phosphatase PTPL1 and the carboxyl-terminal tail|            of Fas|\55:  JOURNAL   J. Biol. Chem. 272 (34), 20979-20981 (1997)|  MEDLINE   97407871|\35:REFERENCE   11 (residues 1 to 2466)|\70:  AUTHORS   Yanagisawa,J., Takahashi,M., Kanki,H., Yano-Yanagisawa,H.,|\77:            Tazunoki,T., Sawa,E., Nishitoba,T., Kamishohara,M., Kobayashi,E.,|\34:            Kataoka,S. and Sato,T.|\79:  TITLE     The molecular interaction of Fas and FAP-1. A tripeptide blocker of|\75:            human Fas interaction with FAP-1 promotes Fas-induced apoptosis|\53:  JOURNAL   J. Biol. Chem. 272 (13), 8539-8545 (1997)|  MEDLINE   97236811|\35:REFERENCE   12 (residues 1 to 2466)|\74:  AUTHORS   Inazawa,J., Ariyama,T., Abe,T., Druck,T., Ohta,M., Huebner,K.,|\48:            Yanagisawa,J., Reed,J.C. and Sato,T.|\77:  TITLE     PTPN13, a fas-associated protein tyrosine phosphatase, is located|\57:            on the long arm of chromosome 4 at band q21.3|\43:  JOURNAL   Genomics 31 (2), 240-242 (1996)|  MEDLINE   96422192|\35:REFERENCE   13 (residues 1 to 2466)|\53:  AUTHORS   Sato,T., Irie,S., Kitada,S. and Reed,J.C.|\74:  TITLE     FAP-1: a protein tyrosine phosphatase that associates with Fas|\46:  JOURNAL   Science 268 (5209), 411-415 (1995)|  MEDLINE   95232528|\35:REFERENCE   14 (residues 1 to 2466)|\67:  AUTHORS   Saras,J., Claesson-Welsh,L., Heldin,C.H. and Gonez,L.J.|\69:  TITLE     Cloning and characterization of PTPL1, a protein tyrosine|\77:            phosphatase with similarities to cytoskeletal-associated proteins|\55:  JOURNAL   J. Biol. Chem. 269 (39), 24082-24089 (1994)|  MEDLINE   95014139|\35:REFERENCE   15 (residues 1 to 2466)|\58:  AUTHORS   Banville,D., Ahmad,S., Stocco,R. and Shen,S.H.|\74:  TITLE     A novel protein-tyrosine phosphatase with homology to both the|\60:            cytoskeletal proteins of the band 4.1 family and|\49:            junction-associated guanylate kinases|\55:  JOURNAL   J. Biol. Chem. 269 (35), 22320-22327 (1994)|  MEDLINE   94350988|\35:REFERENCE   16 (residues 1 to 2466)|\62:  AUTHORS   Maekawa,K., Imagawa,N., Nagamatsu,M. and Harada,S.|\69:  TITLE     Molecular cloning of a novel protein-tyrosine phosphatase|\65:            containing a membrane-binding domain and GLGF repeats|\46:  JOURNAL   FEBS Lett. 337 (2), 200-206 (1994)|  MEDLINE   94116679
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||JNA||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|DBObj||Protein_1|||||0|0|\236:protein tyrosine phosphatase, nonreceptor type 13; protein tyrosine phosphatase 1E; Fas-associated phosphatase-1; protein-tyrosine phosphatase 1, Fas-associated; protein-tyrosine phophatase PTPL1; APO-1/CD95 (Fas)-associated phosphatase
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obj|String*|3|\57:/product="protein tyrosine phosphatase, non-receptor type|13 isoform 2"|\21:/EC_number="3.1.3.48"
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obj|String*|1|\29:REFSEQ: accession NM_006264.1
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\29:hPTPbeta_D1 (NP_002828) PTPRB|||||302014800|0|\170:protein tyrosine phosphatase, receptor type, B precursor; protein tyrosine phosphatase, receptor type, beta polypeptide; protein tyrosine phosphatase beta [Homo sapiens].
end|2|2|
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obj|String*|19|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X54131.1 and BE042873.1.|\57:On Feb 4, 2002 this sequence version replaced gi:4506305.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\63:domain, a single transmembrane segment and one intracytoplasmic|\56:catalytic domain, thus belongs to receptor type PTP. The|\56:extracellular region of this PTP is composed of multiple|\62:fibronectin type_III repeats, which was shown to interact with|\64:neuronal receptor and cell adhesion molecules, such as contactin|\67:and tenascin C. This protein was also found to interact with sodium|\59:channels, and thus may regulate sodium channels by altering|\65:tyrosine phosphorylation status. The functions of the interaction|\64:partners of this protein implicate the roles of this PTP in cell|\55:adhesion, neurite growth, and neuronal differentiation.
end
obj|String*|49|\35:REFERENCE   1  (residues 1 to 1997)|\74:  AUTHORS   Adamsky,K., Schilling,J., Garwood,J., Faissner,A. and Peles,E.|\73:  TITLE     Glial tumor cell adhesion is mediated by binding of the FNIII|\78:            domain of receptor protein tyrosine phosphatase beta (RPTPbeta) to|\22:            tenascin C|\43:  JOURNAL   Oncogene 20 (5), 609-618 (2001)|  MEDLINE   21214455|\35:REFERENCE   2  (residues 1 to 1997)|\74:  AUTHORS   Ratcliffe,C.F., Qu,Y., McCormick,K.A., Tibbs,V.C., Dixon,J.E.,|\41:            Scheuer,T. and Catterall,W.A.|\72:  TITLE     A sodium channel signaling complex: modulation by associated|\54:            receptor protein tyrosine phosphatase beta|\48:  JOURNAL   Nat. Neurosci. 3 (5), 437-444 (2000)|  MEDLINE   20233995|\35:REFERENCE   3  (residues 1 to 1997)|\76:  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,|\34:            Peles,E. and Grumet,M.|\74:  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by|\77:            extracellular regions of glial receptor tyrosine phosphatase beta|\49:  JOURNAL   J. Cell Biol. 136 (4), 907-918 (1997)|  MEDLINE   97201469|\35:REFERENCE   4  (residues 1 to 1997)|\79:  AUTHORS   Peles,E., Nativ,M., Campbell,P.L., Sakurai,T., Martinez,R., Lev,S.,|\68:            Clary,D.O., Schilling,J., Barnea,G., Plowman,G.D. et al.|\79:  TITLE     The carbonic anhydrase domain of receptor tyrosine phosphatase beta|\75:            is a functional ligand for the axonal cell recognition molecule|\21:            contactin|\39:  JOURNAL   Cell 82 (2), 251-260 (1995)|  MEDLINE   95354206|\35:REFERENCE   5  (residues 1 to 1997)|\66:  AUTHORS   Harder,K.W., Anderson,L.L., Duncan,A.M. and Jirik,F.R.|\78:  TITLE     The gene for receptor-like protein tyrosine phosphatase (PTPRB) is|\46:            assigned to chromosome 12q15-->q21|\57:  JOURNAL   Cytogenet. Cell Genet. 61 (4), 269-270 (1992)|  MEDLINE   93137605|\35:REFERENCE   6  (residues 1 to 1997)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018|\35:REFERENCE   7  (residues 1 to 1997)|\74:  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,|\49:            Ricca,G., Jaye,M. and Schlessinger,J.|\76:  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene|\77:            family of receptor-linked protein-tyrosine-phosphatases expressed|            in brain|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990)|  MEDLINE   90384936
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="12"|/map="12q15-q21"
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obj|DBObj||Protein_1|||||0|0|\96:protein tyrosine phosphatase, receptor type, beta polypeptide; protein tyrosine phosphatase beta
end|270|270|||0|1|280|1|1|1|1|1..1997
obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, B|precursor"|\21:/EC_number="3.1.3.48"
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obj|DBObj||Region_1|||||0|0|PTPc
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obj|String*|1|NP_002828
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obj|String*|1|\29:REFSEQ: accession NM_002837.2
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obj|String*|47|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB|\55:VNTI URL:vnti:protein/hPTPbeta_D1+%28NP_002828%29+PTPRB
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\28:hPTPD1_D1 (NP_008970) PTPN21|||||302014800|0|\99:protein tyrosine phosphatase, non-receptor type 21; protein tyrosine phosphatase D1 [Homo sapiens].
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obj|String*|16|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X79510.1 and AI800682.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\65:oncogenic transformation. This PTP contains an N-terminal domain,|\64:similar to cytoskeletal- associated proteins including band 4.1,|\59:ezrin, merlin, and radixin. This PTP was shown to specially|\61:interact with BMX/ETK, a member of Tec tyrosine kinase family|\65:characterized by a multimodular structures including PH, SH3, and|\66:SH2 domains. The interaction of this PTP with BMX kinase was found|\66:to increase the activation of STAT3, but not STAT2 kinase. Studies|\64:of the similar gene in mice suggested the possible roles of this|\46:PTP in liver regeneration and spermatogenesis.
end
obj|String*|30|\35:REFERENCE   1  (residues 1 to 1174)|\75:  AUTHORS   Jui,H.Y., Tseng,R.J., Wen,X., Fang,H.I., Huang,L.M., Chen,K.Y.,|\45:            Kung,H.J., Ann,D.K. and Shih,H.M.|\79:  TITLE     Protein-tyrosine phosphatase D1, a potential regulator and effector|\34:            for Tec family kinases|\55:  JOURNAL   J. Biol. Chem. 275 (52), 41124-41132 (2000)|  MEDLINE   20576274|\35:REFERENCE   2  (residues 1 to 1174)|\78:  AUTHORS   Tokuchi,H., Higashitsuji,H., Nishiyama,H., Nonoguchi,K., Nagao,T.,|\53:            Xue,J.H., Itoh,K., Ogawa,O. and Fujita,J.|\79:  TITLE     Expression of protein tyrosine phosphatase PTP-RL10 and its isoform|\31:            in the mouse testis|\45:  JOURNAL   Int J Urol 6 (11), 572-577 (1999)|  MEDLINE   20049818|\35:REFERENCE   3  (residues 1 to 1174)|\73:  AUTHORS   Higashitsuji,H., Arii,S., Furutani,M., Imamura,M., Kaneko,Y.,|\50:            Takenawa,J., Nakayama,H. and Fujita,J.|\76:  TITLE     Enhanced expression of multiple protein tyrosine phosphatases in|\72:            the regenerating mouse liver: isolation of PTP-RL10, a novel|\79:            cytoplasmic-type phosphatase with sequence homology to cytoskeletal|\23:            protein 4.1|\43:  JOURNAL   Oncogene 10 (2), 407-414 (1995)|  MEDLINE   95140431|\35:REFERENCE   4  (residues 1 to 1174)|\76:  AUTHORS   Moller,N.P., Moller,K.B., Lammers,R., Kharitonenkov,A., Sures,I.|\26:            and Ullrich,A.|\74:  TITLE     Src kinase associates with a member of a distinct subfamily of|\73:            protein-tyrosine phosphatases containing an ezrin-like domain|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 91 (16), 7477-7481 (1994)|  MEDLINE   94329538
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|1|\29:REFSEQ: accession NM_007039.2
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obj|String*|42|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21|\54:VNTI URL:vnti:protein/hPTPD1_D1+%28NP_008970%29+PTPN21
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obj|DBObj||\28:hPTPD2_D1 (NP_005392) PTPN14|||||302014800|0|\120:protein tyrosine phosphatase, non-receptor type 14; cytoskeletal-associated protein tyrosine phosphatase [Homo sapiens].
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obj|String*|12|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X82676.1 and BC017300.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\57:oncogenic transformation. This PTP contains an N-terminal|\59:noncatalytic domain similar to that of band 4.1 superfamily|\65:cytoskeleton-associated proteins, which suggested the membrane or|\67:cytoskeleton localization of this protein. The specific function of|\37:this PTP has not yet been determined.
end
obj|String*|34|\35:REFERENCE   1  (residues 1 to 1187)|\66:  AUTHORS   Wadham,C., Gamble,J.R., Vadas,M.A. and Khew-Goodall,Y.|\76:  TITLE     Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to|\74:            the nucleus is associated with induction of cell proliferation|\55:  JOURNAL   J. Cell. Sci. 113 (Pt 17), 3117-3123 (2000)|  MEDLINE   20394014|\35:REFERENCE   2  (residues 1 to 1187)|\45:  AUTHORS   Aoyama,K., Matsuda,T. and Aoki,N.|\77:  TITLE     Characterization of newly identified four isoforms for a putative|\56:            cytosolic protein tyrosine phosphatase PTP36|\66:  JOURNAL   Biochem. Biophys. Res. Commun. 266 (2), 523-531 (1999)|  MEDLINE   20068798|\35:REFERENCE   3  (residues 1 to 1187)|\73:  AUTHORS   Ogata,M., Takada,T., Mori,Y., Uchida,Y., Miki,T., Okuyama,A.,|\59:            Kosugi,A., Sawada,M., Oh-hora,M. and Hamaoka,T.|\76:  TITLE     Regulation of phosphorylation level and distribution of PTP36, a|\77:            putative protein tyrosine phosphatase, by cell-substrate adhesion|\55:  JOURNAL   J. Biol. Chem. 274 (29), 20717-20724 (1999)|  MEDLINE   99329094|\35:REFERENCE   4  (residues 1 to 1187)|\75:  AUTHORS   Ogata,M., Takada,T., Mori,Y., Oh-hora,M., Uchida,Y., Kosugi,A.,|\36:            Miyake,K. and Hamaoka,T.|\75:  TITLE     Effects of overexpression of PTP36, a putative protein tyrosine|\76:            phosphatase, on cell adhesion, cell growth, and cytoskeletons in|\22:            HeLa cells|\55:  JOURNAL   J. Biol. Chem. 274 (18), 12905-12909 (1999)|  MEDLINE   99230323|\35:REFERENCE   5  (residues 1 to 1187)|\78:  AUTHORS   Smith,A.L., Mitchell,P.J., Shipley,J., Gusterson,B.A., Rogers,M.V.|\29:            and Crompton,M.R.|\78:  TITLE     Pez: a novel human cDNA encoding protein tyrosine phosphatase- and|\30:            ezrin-like domains|\66:  JOURNAL   Biochem. Biophys. Res. Commun. 209 (3), 959-965 (1995)|  MEDLINE   95251727
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|1|\29:REFSEQ: accession NM_005401.2
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obj|String*|42|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14|\54:VNTI URL:vnti:protein/hPTPD2_D1+%28NP_005392%29+PTPN14
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obj|DBObj||\31:hPTPdelta _D1 (NP_002830) PTPRD|||||302014800|0|\182:protein tyrosine phosphatase, receptor type, D isoform 1 precursor; protein tyrosine phosphatase, receptor type, delta polypeptide; protein tyrosine phosphatase delta [Homo sapiens].
end|2|2|
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obj|String*|19|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from L38929.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\53:region, a single transmembrane segment and two tandem|\67:intracytoplasmic catalytic domains, thus represents a receptor-type|\66:PTP. The extracellular region of this protein is composed of three|\67:Ig-like and eight fibronectin type III-like domains. Studies of the|\65:similar genes in chick and fly suggest the role of this PTP is in|\63:promoting neurite growth, and regulating neurons axon guidance.|\66:Multiple tissue specific alternatively spliced transcript variants|\32:of this gene have been reported.||\64:Transcript Variant: This variant (1) encodes the longest isoform|(1).
end
obj|String*|32|\35:REFERENCE   1  (residues 1 to 1912)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   2  (residues 1 to 1912)|\61:  AUTHORS   Pulido,R., Serra-Pages,C., Tang,M. and Streuli,M.|\66:  TITLE     The LAR/PTP delta/PTP sigma subfamily of transmembrane|\77:            protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and|\76:            PTP sigma isoforms are expressed in a tissue-specific manner and|\60:            associate with the LAR-interacting protein LIP.1|\69:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 92 (25), 11686-11690 (1995)|  MEDLINE   96102179|\35:REFERENCE   3  (residues 1 to 1912)|\76:  AUTHORS   Pulido,R., Krueger,N.X., Serra-Pages,C., Saito,H. and Streuli,M.|\65:  TITLE     Molecular characterization of the human transmembrane|\76:            protein-tyrosine phosphatase delta. Evidence for tissue-specific|\74:            expression of alternative human transmembrane protein-tyrosine|\38:            phosphatase delta isoforms|\53:  JOURNAL   J. Biol. Chem. 270 (12), 6722-6728 (1995)|  MEDLINE   95204468|\35:REFERENCE   4  (residues 1 to 1912)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018
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obj|IxMolX
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obj|DBObj||\30:hPTPdelta_D2 (NP_002830) PTPRD|||||302014800|0|\182:protein tyrosine phosphatase, receptor type, D isoform 1 precursor; protein tyrosine phosphatase, receptor type, delta polypeptide; protein tyrosine phosphatase delta [Homo sapiens].
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obj|String*|19|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from L38929.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\53:region, a single transmembrane segment and two tandem|\67:intracytoplasmic catalytic domains, thus represents a receptor-type|\66:PTP. The extracellular region of this protein is composed of three|\67:Ig-like and eight fibronectin type III-like domains. Studies of the|\65:similar genes in chick and fly suggest the role of this PTP is in|\63:promoting neurite growth, and regulating neurons axon guidance.|\66:Multiple tissue specific alternatively spliced transcript variants|\32:of this gene have been reported.||\64:Transcript Variant: This variant (1) encodes the longest isoform|(1).
end
obj|String*|32|\35:REFERENCE   1  (residues 1 to 1912)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   2  (residues 1 to 1912)|\61:  AUTHORS   Pulido,R., Serra-Pages,C., Tang,M. and Streuli,M.|\66:  TITLE     The LAR/PTP delta/PTP sigma subfamily of transmembrane|\77:            protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and|\76:            PTP sigma isoforms are expressed in a tissue-specific manner and|\60:            associate with the LAR-interacting protein LIP.1|\69:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 92 (25), 11686-11690 (1995)|  MEDLINE   96102179|\35:REFERENCE   3  (residues 1 to 1912)|\76:  AUTHORS   Pulido,R., Krueger,N.X., Serra-Pages,C., Saito,H. and Streuli,M.|\65:  TITLE     Molecular characterization of the human transmembrane|\76:            protein-tyrosine phosphatase delta. Evidence for tissue-specific|\74:            expression of alternative human transmembrane protein-tyrosine|\38:            phosphatase delta isoforms|\53:  JOURNAL   J. Biol. Chem. 270 (12), 6722-6728 (1995)|  MEDLINE   95204468|\35:REFERENCE   4  (residues 1 to 1912)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|DBObj||Protein_1|||||0|0|\98:protein tyrosine phosphatase, receptor type, delta polypeptide; protein tyrosine phosphatase delta
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obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, D|isoform 1 precursor"|\21:/EC_number="3.1.3.48"
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obj|DBObj||Region_5|||||0|0|PTPc
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|9|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD|\56:VNTI URL:vnti:protein/hPTPdelta_D2+%28NP_002830%29+PTPRD
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obj|IxMolX
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obj|BioObject
obj|DBObj||\32:hPTPepsilon_D1 (NP_006495) PTPRE|||||302014800|0|\240:protein tyrosine phosphatase, receptor type, E isoform 1 precursor; protein tyrosine phosphatase, receptor type, epsilon; protein tyrosine phosphatase, receptor type, epsilon polypeptide; protein tyrosine phosphatase epsilon [Homo sapiens].
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obj|String*|24|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X54134.1, AJ315969.1 and|BI559814.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\62:oncogenic transformation. Two alternatively spliced transcript|\64:variants of this gene have been reported, one of which encodes a|\64:receptor-type PTP that possesses a short extracellular domain, a|\60:single transmembrane region, and two tandem intracytoplasmic|\60:catalytic domains; Another one encodes a PTP that contains a|\54:distinct hydrophilic N-terminus, and thus represents a|\65:nonreceptor-type isoform of this PTP. Studies of the similar gene|\65:in mice suggested the regulatory roles of this PTP in RAS related|\66:signal transduction pathways, cytokines induced SATA signaling, as|\52:well as the activation of voltage-gated K+ channels.||\64:Transcript Variant: This variant (1) contains a different 5' end|\66:region that includes a part of the coding region, when compared to|\56:variant 2. It thus encodes a protein that has a distinct|\62:N-terminus, as compared to isoform 2. The encoded protein is a|\34:receptor type isoform of this PTP.
end
obj|String*|72|\34:REFERENCE   1  (residues 1 to 700)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\34:REFERENCE   2  (residues 1 to 700)|\63:  AUTHORS   Wabakken,T., Hauge,H., Funderud,S. and Aasheim,H.C.|\74:  TITLE     Characterization, expression and functional aspects of a novel|\56:            protein tyrosine phosphatase epsilon isoform|\53:  JOURNAL   Scand. J. Immunol. 56 (3), 276-285 (2002)|  MEDLINE   22181756|\78:  REMARK    GeneRIF: Characterization, expression and functional aspects of an|\79:            alternative spliced isoform of protein tyrosine phosphatase epsilon|\34:REFERENCE   3  (residues 1 to 700)|\74:  AUTHORS   Wabakken,T., Hauge,H., Finne,E.F., Wiedlocha,A. and Aasheim,H.|\71:  TITLE     Expression of human protein tyrosine phosphatase epsilon in|\70:            leucocytes: a potential ERK pathway-regulating phosphatase|\53:  JOURNAL   Scand. J. Immunol. 56 (2), 195-203 (2002)|  MEDLINE   22118122|\79:  REMARK    GeneRIF: Transfection of cells with different PTPepsilon constructs|\78:            and activator protein-1 reporter gene indicates that the catalytic|\71:            activity of PTPepsilon is involved in the regulation of the|\53:            mitogen-activated protein kinase cascade.|\34:REFERENCE   4  (residues 1 to 700)|\59:  AUTHORS   Tanuma,N., Nakamura,K., Shima,H. and Kikuchi,K.|\71:  TITLE     Protein-tyrosine phosphatase PTPepsilon C inhibits Jak-STAT|\79:            signaling and differentiation induced by interleukin-6 and leukemia|\50:            inhibitory factor in M1 leukemia cells|\55:  JOURNAL   J. Biol. Chem. 275 (36), 28216-28221 (2000)|  MEDLINE   20428741|\49:  REMARK    functional study of the mouse homolog|\34:REFERENCE   5  (residues 1 to 700)|\71:  AUTHORS   Peretz,A., Gil-Henn,H., Sobko,A., Shinder,V., Attali,B. and|            Elson,A.|\72:  TITLE     Hypomyelination and increased activity of voltage-gated K(+)|\73:            channels in mice lacking protein tyrosine phosphatase epsilon|\45:  JOURNAL   EMBO J. 19 (15), 4036-4045 (2000)|  MEDLINE   20380937|\49:  REMARK    functional study of the mouse homolog|\34:REFERENCE   6  (residues 1 to 700)|\47:  AUTHORS   Toledano-Katchalski,H. and Elson,A.|\72:  TITLE     The transmembranal and cytoplasmic forms of protein tyrosine|\78:            phosphatase epsilon physically associate with the adaptor molecule|            Grb2|\46:  JOURNAL   Oncogene 18 (36), 5024-5031 (1999)|  MEDLINE   99422037|\49:  REMARK    functional study of the mouse homolog|\34:REFERENCE   7  (residues 1 to 700)|\33:  AUTHORS   Elson,A. and Leder,P.|\79:  TITLE     Identification of a cytoplasmic, phorbol ester-inducible isoform of|\48:            protein tyrosine phosphatase epsilon|\69:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 92 (26), 12235-12239 (1995)|  MEDLINE   96109240|\34:REFERENCE   8  (residues 1 to 700)|\68:  AUTHORS   van den Maagdenberg,A.M., van den Hurk,H.H., Weghuis,D.,|\63:            Wieringa,B., Geurts van Kessel,A. and Hendriks,W.J.|\72:  TITLE     Assignment of the human protein tyrosine phosphatase epsilon|\68:            (PTPRE) gene to chromosome 10q26 by fluorescence in situ|\25:            hybridization|\43:  JOURNAL   Genomics 30 (1), 128-129 (1995)|  MEDLINE   96129319|\34:REFERENCE   9  (residues 1 to 700)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018
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obj|DBObj||\32:hPTPepsilon_D2 (NP_006495) PTPRE|||||302014800|0|\240:protein tyrosine phosphatase, receptor type, E isoform 1 precursor; protein tyrosine phosphatase, receptor type, epsilon; protein tyrosine phosphatase, receptor type, epsilon polypeptide; protein tyrosine phosphatase epsilon [Homo sapiens].
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obj|String*|24|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X54134.1, AJ315969.1 and|BI559814.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\62:oncogenic transformation. Two alternatively spliced transcript|\64:variants of this gene have been reported, one of which encodes a|\64:receptor-type PTP that possesses a short extracellular domain, a|\60:single transmembrane region, and two tandem intracytoplasmic|\60:catalytic domains; Another one encodes a PTP that contains a|\54:distinct hydrophilic N-terminus, and thus represents a|\65:nonreceptor-type isoform of this PTP. Studies of the similar gene|\65:in mice suggested the regulatory roles of this PTP in RAS related|\66:signal transduction pathways, cytokines induced SATA signaling, as|\52:well as the activation of voltage-gated K+ channels.||\64:Transcript Variant: This variant (1) contains a different 5' end|\66:region that includes a part of the coding region, when compared to|\56:variant 2. It thus encodes a protein that has a distinct|\62:N-terminus, as compared to isoform 2. The encoded protein is a|\34:receptor type isoform of this PTP.
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obj|String*|72|\34:REFERENCE   1  (residues 1 to 700)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\34:REFERENCE   2  (residues 1 to 700)|\63:  AUTHORS   Wabakken,T., Hauge,H., Funderud,S. and Aasheim,H.C.|\74:  TITLE     Characterization, expression and functional aspects of a novel|\56:            protein tyrosine phosphatase epsilon isoform|\53:  JOURNAL   Scand. J. Immunol. 56 (3), 276-285 (2002)|  MEDLINE   22181756|\78:  REMARK    GeneRIF: Characterization, expression and functional aspects of an|\79:            alternative spliced isoform of protein tyrosine phosphatase epsilon|\34:REFERENCE   3  (residues 1 to 700)|\74:  AUTHORS   Wabakken,T., Hauge,H., Finne,E.F., Wiedlocha,A. and Aasheim,H.|\71:  TITLE     Expression of human protein tyrosine phosphatase epsilon in|\70:            leucocytes: a potential ERK pathway-regulating phosphatase|\53:  JOURNAL   Scand. J. Immunol. 56 (2), 195-203 (2002)|  MEDLINE   22118122|\79:  REMARK    GeneRIF: Transfection of cells with different PTPepsilon constructs|\78:            and activator protein-1 reporter gene indicates that the catalytic|\71:            activity of PTPepsilon is involved in the regulation of the|\53:            mitogen-activated protein kinase cascade.|\34:REFERENCE   4  (residues 1 to 700)|\59:  AUTHORS   Tanuma,N., Nakamura,K., Shima,H. and Kikuchi,K.|\71:  TITLE     Protein-tyrosine phosphatase PTPepsilon C inhibits Jak-STAT|\79:            signaling and differentiation induced by interleukin-6 and leukemia|\50:            inhibitory factor in M1 leukemia cells|\55:  JOURNAL   J. Biol. Chem. 275 (36), 28216-28221 (2000)|  MEDLINE   20428741|\49:  REMARK    functional study of the mouse homolog|\34:REFERENCE   5  (residues 1 to 700)|\71:  AUTHORS   Peretz,A., Gil-Henn,H., Sobko,A., Shinder,V., Attali,B. and|            Elson,A.|\72:  TITLE     Hypomyelination and increased activity of voltage-gated K(+)|\73:            channels in mice lacking protein tyrosine phosphatase epsilon|\45:  JOURNAL   EMBO J. 19 (15), 4036-4045 (2000)|  MEDLINE   20380937|\49:  REMARK    functional study of the mouse homolog|\34:REFERENCE   6  (residues 1 to 700)|\47:  AUTHORS   Toledano-Katchalski,H. and Elson,A.|\72:  TITLE     The transmembranal and cytoplasmic forms of protein tyrosine|\78:            phosphatase epsilon physically associate with the adaptor molecule|            Grb2|\46:  JOURNAL   Oncogene 18 (36), 5024-5031 (1999)|  MEDLINE   99422037|\49:  REMARK    functional study of the mouse homolog|\34:REFERENCE   7  (residues 1 to 700)|\33:  AUTHORS   Elson,A. and Leder,P.|\79:  TITLE     Identification of a cytoplasmic, phorbol ester-inducible isoform of|\48:            protein tyrosine phosphatase epsilon|\69:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 92 (26), 12235-12239 (1995)|  MEDLINE   96109240|\34:REFERENCE   8  (residues 1 to 700)|\68:  AUTHORS   van den Maagdenberg,A.M., van den Hurk,H.H., Weghuis,D.,|\63:            Wieringa,B., Geurts van Kessel,A. and Hendriks,W.J.|\72:  TITLE     Assignment of the human protein tyrosine phosphatase epsilon|\68:            (PTPRE) gene to chromosome 10q26 by fluorescence in situ|\25:            hybridization|\43:  JOURNAL   Genomics 30 (1), 128-129 (1995)|  MEDLINE   96129319|\34:REFERENCE   9  (residues 1 to 700)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|BioObject
obj|DBObj||\30:hPTPgamma_D1 (NP_002832) PTPRG|||||302014800|0|\250:protein tyrosine phosphatase, receptor type, G precursor; protein tyrosine phosphatase, receptor type, gamma polypeptide; protein tyrosine phosphatase gamma; receptor-type protein phosphatase gamma; receptor tyrosine phosphatase gamma [Homo sapiens].
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obj|String*|18|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from L09247.1, AI872451.1 and|U46089.1.|\59:On Feb 22, 2002 this sequence version replaced gi:11386169.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\53:region, a single transmembrane region, and two tandem|\57:intracytoplasmic catalytic domains, and thus represents a|\66:receptor-type PTP. The extracellular region of this PTP contains a|\64:carbonic anhydrase-like (CAH) domain, which is also found in the|\64:extracellular region of PTPRBETA/ZETA. This gene is located in a|\59:chromosomal region that is frequently deleted in renal cell|\63:carcinoma and lung carcinoma, thus is thought to be a candidate|\22:tumor suppressor gene.
end
obj|String*|51|\35:REFERENCE   1  (residues 1 to 1445)|\76:  AUTHORS   Liu,S., Sugimoto,Y., Kulp,S.K., Jiang,J., Chang,H.L., Park,K.Y.,|\35:            Kashida,Y. and Lin,Y.C.|\76:  TITLE     Estrogenic down-regulation of protein tyrosine phosphatase gamma|\76:            (PTP gamma) in human breast is associated with estrogen receptor|            alpha|\53:  JOURNAL   Anticancer Res. 22 (6C), 3917-3923 (2002)|  MEDLINE   22441179|\79:  REMARK    GeneRIF: Estrogenic down-regulation of protein tyrosine phosphatase|\73:            gamma (PTP gamma) in human breast is associated with estrogen|\27:            receptor alpha.|\35:REFERENCE   2  (residues 1 to 1445)|\77:  AUTHORS   Liu,S., Kulp,S.K., Sugimoto,Y., Jiang,J., Chang,H.L. and Lin,Y.C.|\72:  TITLE     Involvement of breast epithelial-stromal interactions in the|\76:            regulation of protein tyrosine phosphatase-gamma (PTPgamma) mRNA|\54:            expression by estrogenically active agents|\58:  JOURNAL   Breast Cancer Res. Treat. 71 (1), 21-35 (2002)|  MEDLINE   21848634|\72:  REMARK    GeneRIF: both estradiol-17beta and zeranol regulate PTPgamma|\78:            expression in human breast; epithelial-stromal cell interaction is|\76:            important in regulation of PTPgamma expression by estrogenically|\25:            active agents|\35:REFERENCE   3  (residues 1 to 1445)|\76:  AUTHORS   Kastury,K., Ohta,M., Lasota,J., Moir,D., Dorman,T., LaForgia,S.,|\35:            Druck,T. and Huebner,K.|\75:  TITLE     Structure of the human receptor tyrosine phosphatase gamma gene|\70:            (PTPRG) and relation to the familial RCC t(3;8) chromosome|\25:            translocation|\43:  JOURNAL   Genomics 32 (2), 225-235 (1996)|  MEDLINE   96429999|\35:REFERENCE   4  (residues 1 to 1445)|\79:  AUTHORS   Barnea,G., Silvennoinen,O., Shaanan,B., Honegger,A.M., Canoll,P.D.,|\79:            D'Eustachio,P., Morse,B., Levy,J.B., Laforgia,S., Huebner,K. et al.|\69:  TITLE     Identification of a carbonic anhydrase-like domain in the|\73:            extracellular region of RPTP gamma defines a new subfamily of|\42:            receptor tyrosine phosphatases|\53:  JOURNAL   Mol. Cell. Biol. 13 (3), 1497-1506 (1993)|  MEDLINE   93180796|\35:REFERENCE   5  (residues 1 to 1445)|\78:  AUTHORS   LaForgia,S., Morse,B., Levy,J., Barnea,G., Cannizzaro,L.A., Li,F.,|\70:            Nowell,P.C., Boghosian-Sell,L., Glick,J., Weston,A. et al.|\76:  TITLE     Receptor protein-tyrosine phosphatase gamma is a candidate tumor|\59:            suppressor gene at human chromosome region 3p21|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 88 (11), 5036-5040 (1991)|  MEDLINE   91271326|\35:REFERENCE   6  (residues 1 to 1445)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018
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obj|IxMolX
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obj|DBObj||\30:hPTPgamma_D2 (NP_002832) PTPRG|||||302014800|0|\250:protein tyrosine phosphatase, receptor type, G precursor; protein tyrosine phosphatase, receptor type, gamma polypeptide; protein tyrosine phosphatase gamma; receptor-type protein phosphatase gamma; receptor tyrosine phosphatase gamma [Homo sapiens].
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obj|String*|18|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from L09247.1, AI872451.1 and|U46089.1.|\59:On Feb 22, 2002 this sequence version replaced gi:11386169.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\53:region, a single transmembrane region, and two tandem|\57:intracytoplasmic catalytic domains, and thus represents a|\66:receptor-type PTP. The extracellular region of this PTP contains a|\64:carbonic anhydrase-like (CAH) domain, which is also found in the|\64:extracellular region of PTPRBETA/ZETA. This gene is located in a|\59:chromosomal region that is frequently deleted in renal cell|\63:carcinoma and lung carcinoma, thus is thought to be a candidate|\22:tumor suppressor gene.
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obj|String*|51|\35:REFERENCE   1  (residues 1 to 1445)|\76:  AUTHORS   Liu,S., Sugimoto,Y., Kulp,S.K., Jiang,J., Chang,H.L., Park,K.Y.,|\35:            Kashida,Y. and Lin,Y.C.|\76:  TITLE     Estrogenic down-regulation of protein tyrosine phosphatase gamma|\76:            (PTP gamma) in human breast is associated with estrogen receptor|            alpha|\53:  JOURNAL   Anticancer Res. 22 (6C), 3917-3923 (2002)|  MEDLINE   22441179|\79:  REMARK    GeneRIF: Estrogenic down-regulation of protein tyrosine phosphatase|\73:            gamma (PTP gamma) in human breast is associated with estrogen|\27:            receptor alpha.|\35:REFERENCE   2  (residues 1 to 1445)|\77:  AUTHORS   Liu,S., Kulp,S.K., Sugimoto,Y., Jiang,J., Chang,H.L. and Lin,Y.C.|\72:  TITLE     Involvement of breast epithelial-stromal interactions in the|\76:            regulation of protein tyrosine phosphatase-gamma (PTPgamma) mRNA|\54:            expression by estrogenically active agents|\58:  JOURNAL   Breast Cancer Res. Treat. 71 (1), 21-35 (2002)|  MEDLINE   21848634|\72:  REMARK    GeneRIF: both estradiol-17beta and zeranol regulate PTPgamma|\78:            expression in human breast; epithelial-stromal cell interaction is|\76:            important in regulation of PTPgamma expression by estrogenically|\25:            active agents|\35:REFERENCE   3  (residues 1 to 1445)|\76:  AUTHORS   Kastury,K., Ohta,M., Lasota,J., Moir,D., Dorman,T., LaForgia,S.,|\35:            Druck,T. and Huebner,K.|\75:  TITLE     Structure of the human receptor tyrosine phosphatase gamma gene|\70:            (PTPRG) and relation to the familial RCC t(3;8) chromosome|\25:            translocation|\43:  JOURNAL   Genomics 32 (2), 225-235 (1996)|  MEDLINE   96429999|\35:REFERENCE   4  (residues 1 to 1445)|\79:  AUTHORS   Barnea,G., Silvennoinen,O., Shaanan,B., Honegger,A.M., Canoll,P.D.,|\79:            D'Eustachio,P., Morse,B., Levy,J.B., Laforgia,S., Huebner,K. et al.|\69:  TITLE     Identification of a carbonic anhydrase-like domain in the|\73:            extracellular region of RPTP gamma defines a new subfamily of|\42:            receptor tyrosine phosphatases|\53:  JOURNAL   Mol. Cell. Biol. 13 (3), 1497-1506 (1993)|  MEDLINE   93180796|\35:REFERENCE   5  (residues 1 to 1445)|\78:  AUTHORS   LaForgia,S., Morse,B., Levy,J., Barnea,G., Cannizzaro,L.A., Li,F.,|\70:            Nowell,P.C., Boghosian-Sell,L., Glick,J., Weston,A. et al.|\76:  TITLE     Receptor protein-tyrosine phosphatase gamma is a candidate tumor|\59:            suppressor gene at human chromosome region 3p21|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 88 (11), 5036-5040 (1991)|  MEDLINE   91271326|\35:REFERENCE   6  (residues 1 to 1445)|\49:  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.|\77:  TITLE     Structural diversity and evolution of human receptor-like protein|\33:            tyrosine phosphatases|\44:  JOURNAL   EMBO J. 9 (10), 3241-3252 (1990)|  MEDLINE   91006018
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="3"|/map="3p21-p14"
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obj|DBObj||Protein_1|||||0|0|\176:protein tyrosine phosphatase, receptor type, gamma polypeptide; protein tyrosine phosphatase gamma; receptor-type protein phosphatase gamma; receptor tyrosine phosphatase gamma
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obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, G|precursor"|\21:/EC_number="3.1.3.48"
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obj|DBObj||Region_3|||||0|0|PTPc
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obj|String*|1|NP_002832
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obj|String*|1| PTPRG
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obj|String*|1|\29:REFSEQ: accession NM_002841.2
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obj|String*|7|\56:VNTI URL:vnti:protein/hPTPgamma_D2+%28NP_002832%29+PTPRG|\56:VNTI URL:vnti:protein/hPTPgamma_D2+%28NP_002832%29+PTPRG|\56:VNTI URL:vnti:protein/hPTPgamma_D2+%28NP_002832%29+PTPRG|\56:VNTI URL:vnti:protein/hPTPgamma_D2+%28NP_002832%29+PTPRG|\56:VNTI URL:vnti:protein/hPTPgamma_D2+%28NP_002832%29+PTPRG|\56:VNTI URL:vnti:protein/hPTPgamma_D2+%28NP_002832%29+PTPRG|\56:VNTI URL:vnti:protein/hPTPgamma_D2+%28NP_002832%29+PTPRG
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\27:hPTPH1_D1 (NP_002820) PTPN3|||||302014800|0|\151:protein tyrosine phosphatase, non-receptor type 3; protein tyrosin phosphatase H1; cytoskeletal-associated protein tyrosine phosphatase [Homo sapiens].
end|2|2|
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obj|String*|14|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\58:reference sequence was derived from M64572.1 and W15441.1.|\58:On Jan 10, 2002 this sequence version replaced gi:4506293.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\64:oncogenic transformation. This protein contains a C-terminal PTP|\58:domain and an N-terminal domain homologous to the band 4.1|\66:superfamily of cytoskeletal-associated proteins. P97, a cell cycle|\66:regulator involved in a variety of membrane related functions, has|\65:been shown to be a substrate of this PTP. This PTP was also found|\66:to interact with, and be regulated by adaptor protein 14-3-3 beta.
end
obj|String*|51|\34:REFERENCE   1  (residues 1 to 913)|\52:  AUTHORS   Zheng,Y., Schlondorff,J. and Blobel,C.P.|\64:  TITLE     Evidence for regulation of the tumor necrosis factor|\73:            alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1|\55:  JOURNAL   J. Biol. Chem. 277 (45), 42463-42470 (2002)|  MEDLINE   22301977|\58:  REMARK    GeneRIF: regulates TACE (tnf-alpha convertase}|\34:REFERENCE   2  (residues 1 to 913)|\59:  AUTHORS   Zhang,S.H., Liu,J., Kobayashi,R. and Tonks,N.K.|\75:  TITLE     Identification of the cell cycle regulator VCP (p97/CDC48) as a|\74:            substrate of the band 4.1-related protein-tyrosine phosphatase|            PTPH1|\55:  JOURNAL   J. Biol. Chem. 274 (25), 17806-17812 (1999)|  MEDLINE   99292748|\34:REFERENCE   3  (residues 1 to 913)|\71:  AUTHORS   Zhang,S.H., Kobayashi,R., Graves,P.R., Piwnica-Worms,H. and|\22:            Tonks,N.K.|\68:  TITLE     Serine phosphorylation-dependent association of the band|\74:            4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta|            protein|\55:  JOURNAL   J. Biol. Chem. 272 (43), 27281-27287 (1997)|  MEDLINE   98001710|\34:REFERENCE   4  (residues 1 to 913)|\78:  AUTHORS   Ikuta,S., Itoh,F., Hinoda,Y., Toyota,M., Makiguchi,Y., Imai,K. and|            Yachi,A.|\78:  TITLE     Expression of cytoskeletal-associated protein tyrosine phosphatase|\56:            PTPH1 mRNA in human hepatocellular carcinoma|\52:  JOURNAL   J. Gastroenterol. 29 (6), 727-732 (1994)|  MEDLINE   95179278|\34:REFERENCE   5  (residues 1 to 913)|\72:  AUTHORS   Itoh,F., Ikuta,S., Hinoda,Y., Arimura,Y., Ohe,M., Adachi,M.,|\56:            Ariyama,T., Inazawa,J., Imai,K. and Yachi,A.|\74:  TITLE     Expression and chromosomal assignment of PTPH1 gene encoding a|\64:            cytosolic protein tyrosine phosphatase homologous to|\44:            cytoskeletal-associated proteins|\49:  JOURNAL   Int. J. Cancer 55 (6), 947-951 (1993)|  MEDLINE   94075060|\34:REFERENCE   6  (residues 1 to 913)|\70:  AUTHORS   Arimura,Y., Hinoda,Y., Itoh,F., Takekawa,M., Tsujisaki,M.,|\43:            Adachi,M., Imai,K. and Yachi,A.|\74:  TITLE     cDNA cloning of new protein tyrosine phosphatases in the human|            colon|\47:  JOURNAL   Tumour Biol. 13 (3), 180-186 (1992)|  MEDLINE   92327504|\34:REFERENCE   7  (residues 1 to 913)|\34:  AUTHORS   Yang,Q. and Tonks,N.K.|\71:  TITLE     Isolation of a cDNA clone encoding a human protein-tyrosine|\77:            phosphatase with homology to the cytoskeletal-associated proteins|\38:            band 4.1, ezrin, and talin|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 88 (14), 5949-5953 (1991)|  MEDLINE   91296738
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|DBObj||\30:hPTPlamda_D1 (NP_005695) PTPRU|||||302014800|0|\161:protein tyrosine phosphatase, receptor type, U isoform 3 precursor; protein tyrosine phosphatase J; protein tyrosine phosphatase receptor omicron [Homo sapiens].
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obj|String*|22|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\58:reference sequence was derived from X97198.1 and X95712.1.|\58:On Mar 26, 2002 this sequence version replaced gi:5032003.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\67:region, a single transmembrane region, and two tandem intracellular|\63:catalytic domains, and thus represents a receptor-type PTP. The|\67:extracellular region contains a meprin-A5 antigen-PTP (MAM) domain,|\67:Ig-like and fibronectin type III-like repeats. This PTP was thought|\67:to play roles in cell-cell recognition and adhesion. Studies of the|\67:similar gene in mice suggested the role of this PTP in early neural|\59:development. The expression of this gene was reported to be|\65:regulated by phorbol myristate acetate (PMA) or calcium ionophore|\66:in Jurkat T lymphoma cells. Three alternatively spliced transcript|\61:variants, which encode distinct proteins, have been reported.||\64:Transcript Variant: This variant (3) encodes the longest isoform|(3).
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obj|String*|44|\35:REFERENCE   1  (residues 1 to 1446)|\78:  AUTHORS   Yan,H.X., He,Y.Q., Dong,H., Zhang,P., Zeng,J.Z., Cao,H.F., Wu,M.C.|\25:            and Wang,H.Y.|\77:  TITLE     Physical and functional interaction between receptor-like protein|\55:            tyrosine phosphatase PCP-2 and beta-catenin|\52:  JOURNAL   Biochemistry 41 (52), 15854-15860 (2002)|  MEDLINE   22389441|\73:  REMARK    GeneRIF: Expressed in a cell density-dependent fashion, PCP-2|\78:            interacts directly with its substrate beta-catenin, independent of|\63:            the tyrosine phosphorylation state of beta-catenin.|\35:REFERENCE   2  (residues 1 to 1446)|\70:  AUTHORS   Wang,B., Kishihara,K., Zhang,D., Sakamoto,T. and Nomoto,K.|\69:  TITLE     Transcriptional regulation of a receptor protein tyrosine|\73:            phosphatase gene hPTP-J by PKC-mediated signaling pathways in|\46:            Jurkat and Molt-4 T lymphoma cells|\59:  JOURNAL   Biochim. Biophys. Acta 1450 (3), 331-340 (1999)|  MEDLINE   99326162|\35:REFERENCE   3  (residues 1 to 1446)|\75:  AUTHORS   Avraham,S., London,R., Tulloch,G.A., Ellis,M., Fu,Y., Jiang,S.,|\67:            White,R.A., Painter,C., Steinberger,A.A. and Avraham,H.|\75:  TITLE     Characterization and chromosomal localization of PTPRO, a novel|\77:            receptor protein tyrosine phosphatase, expressed in hematopoietic|\22:            stem cells|\39:  JOURNAL   Gene 204 (1-2), 5-16 (1997)|  MEDLINE   98094249|\35:REFERENCE   4  (residues 1 to 1446)|\66:  AUTHORS   Wang,B., Kishihara,K., Zhang,D., Hara,H. and Nomoto,K.|\76:  TITLE     Molecular cloning and characterization of a novel human receptor|\78:            protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene|\78:            expression by PMA and calcium ionophore in Jurkat T lymphoma cells|\64:  JOURNAL   Biochem. Biophys. Res. Commun. 231 (1), 77-81 (1997)|  MEDLINE   97223402|\35:REFERENCE   5  (residues 1 to 1446)|\54:  AUTHORS   Crossland,S., Smith,P.D. and Crompton,M.R.|\69:  TITLE     Molecular cloning and characterization of PTP pi, a novel|\54:            receptor-like protein-tyrosine phosphatase|\50:  JOURNAL   Biochem. J. 319 (Pt 1), 249-254 (1996)|  MEDLINE   97024447|\35:REFERENCE   6  (residues 1 to 1446)|\72:  AUTHORS   Wang,H., Lian,Z., Lerch,M.M., Chen,Z., Xie,W. and Ullrich,A.|\72:  TITLE     Characterization of PCP-2, a novel receptor protein tyrosine|\48:            phosphatase of the MAM domain family|\46:  JOURNAL   Oncogene 12 (12), 2555-2562 (1996)|  MEDLINE   96293401
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\30:hPTPlamda_D2 (NP_005695) PTPRU|||||302014800|0|\161:protein tyrosine phosphatase, receptor type, U isoform 3 precursor; protein tyrosine phosphatase J; protein tyrosine phosphatase receptor omicron [Homo sapiens].
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obj|String*|22|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\58:reference sequence was derived from X97198.1 and X95712.1.|\58:On Mar 26, 2002 this sequence version replaced gi:5032003.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\67:region, a single transmembrane region, and two tandem intracellular|\63:catalytic domains, and thus represents a receptor-type PTP. The|\67:extracellular region contains a meprin-A5 antigen-PTP (MAM) domain,|\67:Ig-like and fibronectin type III-like repeats. This PTP was thought|\67:to play roles in cell-cell recognition and adhesion. Studies of the|\67:similar gene in mice suggested the role of this PTP in early neural|\59:development. The expression of this gene was reported to be|\65:regulated by phorbol myristate acetate (PMA) or calcium ionophore|\66:in Jurkat T lymphoma cells. Three alternatively spliced transcript|\61:variants, which encode distinct proteins, have been reported.||\64:Transcript Variant: This variant (3) encodes the longest isoform|(3).
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obj|String*|44|\35:REFERENCE   1  (residues 1 to 1446)|\78:  AUTHORS   Yan,H.X., He,Y.Q., Dong,H., Zhang,P., Zeng,J.Z., Cao,H.F., Wu,M.C.|\25:            and Wang,H.Y.|\77:  TITLE     Physical and functional interaction between receptor-like protein|\55:            tyrosine phosphatase PCP-2 and beta-catenin|\52:  JOURNAL   Biochemistry 41 (52), 15854-15860 (2002)|  MEDLINE   22389441|\73:  REMARK    GeneRIF: Expressed in a cell density-dependent fashion, PCP-2|\78:            interacts directly with its substrate beta-catenin, independent of|\63:            the tyrosine phosphorylation state of beta-catenin.|\35:REFERENCE   2  (residues 1 to 1446)|\70:  AUTHORS   Wang,B., Kishihara,K., Zhang,D., Sakamoto,T. and Nomoto,K.|\69:  TITLE     Transcriptional regulation of a receptor protein tyrosine|\73:            phosphatase gene hPTP-J by PKC-mediated signaling pathways in|\46:            Jurkat and Molt-4 T lymphoma cells|\59:  JOURNAL   Biochim. Biophys. Acta 1450 (3), 331-340 (1999)|  MEDLINE   99326162|\35:REFERENCE   3  (residues 1 to 1446)|\75:  AUTHORS   Avraham,S., London,R., Tulloch,G.A., Ellis,M., Fu,Y., Jiang,S.,|\67:            White,R.A., Painter,C., Steinberger,A.A. and Avraham,H.|\75:  TITLE     Characterization and chromosomal localization of PTPRO, a novel|\77:            receptor protein tyrosine phosphatase, expressed in hematopoietic|\22:            stem cells|\39:  JOURNAL   Gene 204 (1-2), 5-16 (1997)|  MEDLINE   98094249|\35:REFERENCE   4  (residues 1 to 1446)|\66:  AUTHORS   Wang,B., Kishihara,K., Zhang,D., Hara,H. and Nomoto,K.|\76:  TITLE     Molecular cloning and characterization of a novel human receptor|\78:            protein tyrosine phosphatase gene, hPTP-J: down-regulation of gene|\78:            expression by PMA and calcium ionophore in Jurkat T lymphoma cells|\64:  JOURNAL   Biochem. Biophys. Res. Commun. 231 (1), 77-81 (1997)|  MEDLINE   97223402|\35:REFERENCE   5  (residues 1 to 1446)|\54:  AUTHORS   Crossland,S., Smith,P.D. and Crompton,M.R.|\69:  TITLE     Molecular cloning and characterization of PTP pi, a novel|\54:            receptor-like protein-tyrosine phosphatase|\50:  JOURNAL   Biochem. J. 319 (Pt 1), 249-254 (1996)|  MEDLINE   97024447|\35:REFERENCE   6  (residues 1 to 1446)|\72:  AUTHORS   Wang,H., Lian,Z., Lerch,M.M., Chen,Z., Xie,W. and Ullrich,A.|\72:  TITLE     Characterization of PCP-2, a novel receptor protein tyrosine|\48:            phosphatase of the MAM domain family|\46:  JOURNAL   Oncogene 12 (12), 2555-2562 (1996)|  MEDLINE   96293401
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="1"|/map="1p35.3-p35.1"
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obj|Feature
obj|DBObj||Protein_1|||||0|0|\77:protein tyrosine phosphatase J; protein tyrosine phosphatase receptor omicron
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obj|String*|2|\56:/product="protein tyrosine phosphatase, receptor type, U|isoform 3 precursor"
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obj|String*|2|\57:/product="protein tyrosine phosphatase, receptor type, U,|isoform 3"
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obj|DBObj||Region_3|||||0|0|PTPc
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|1|\29:REFSEQ: accession NM_005704.2
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obj|String*|13|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU|\56:VNTI URL:vnti:protein/hPTPlamda_D2+%28NP_005695%29+PTPRU
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end|F90F48
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\27:hPTPmu_D1 (NP_002836) PTPRM|||||302014800|0|\176:protein tyrosine phosphatase, receptor type, M precursor; protein tyrosine phosphatase, receptor type, mu polypeptide; protein tyrosine phosphatase mu precursor [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|18|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X58288.1 and AA281524.1.|\58:On Feb 22, 2002 this sequence version replaced gi:4506319.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\63:region, a single transmembrane region, and two tandem catalytic|\67:domains, and thus represents a receptor-type PTP. The extracellular|\67:region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like|\63:domain and four fibronectin type III-like repeats. This PTP has|\67:been shown to mediate cell-cell aggregation through the interaction|\67:with another molecule of this PTP on an adjacent cell. This PTP can|\60:interact with scaffolding protein RACK1/GNB2L1, which may be|\63:necessary for the downstream signaling in response to cell-cell|adhesion.
end
obj|String*|52|\35:REFERENCE   1  (residues 1 to 1452)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   2  (residues 1 to 1452)|\77:  AUTHORS   Mourton,T., Hellberg,C.B., Burden-Gulley,S.M., Hinman,J., Rhee,A.|\33:            and Brady-Kalnay,S.M.|\73:  TITLE     The PTPmu protein-tyrosine phosphatase binds and recruits the|\59:            scaffolding protein RACK1 to cell-cell contacts|\55:  JOURNAL   J. Biol. Chem. 276 (18), 14896-14901 (2001)|  MEDLINE   21226727|\35:REFERENCE   3  (residues 1 to 1452)|\69:  AUTHORS   Feiken,E., van Etten,I., Gebbink,M.F., Moolenaar,W.H. and|\23:            Zondag,G.C.|\76:  TITLE     Intramolecular interactions between the juxtamembrane domain and|\72:            phosphatase domains of receptor protein-tyrosine phosphatase|\52:            RPTPmu. Regulation of catalytic activity|\55:  JOURNAL   J. Biol. Chem. 275 (20), 15350-15356 (2000)|  MEDLINE   20270248|\35:REFERENCE   4  (residues 1 to 1452)|\44:  AUTHORS   Brady-Kalnay,S.M. and Tonks,N.K.|\73:  TITLE     Identification of the homophilic binding site of the receptor|\47:            protein tyrosine phosphatase PTP mu|\55:  JOURNAL   J. Biol. Chem. 269 (45), 28472-28477 (1994)|  MEDLINE   95050637|\35:REFERENCE   5  (residues 1 to 1452)|\74:  AUTHORS   Suijkerbuijk,R.F., Gebbink,M.F., Moolenaar,W.H. and Geurts van|\21:            Kessel,A.|\68:  TITLE     Fine mapping of the human receptor-like protein tyrosine|\71:            phosphatase gene (PTPRM) to 18p11.2 by fluorescence in situ|\25:            hybridization|\59:  JOURNAL   Cytogenet. Cell Genet. 64 (3-4), 245-246 (1993)|  MEDLINE   94007972|\35:REFERENCE   6  (residues 1 to 1452)|\56:  AUTHORS   Brady-Kalnay,S.M., Flint,A.J. and Tonks,N.K.|\74:  TITLE     Homophilic binding of PTP mu, a receptor-type protein tyrosine|\58:            phosphatase, can mediate cell-cell aggregation|\49:  JOURNAL   J. Cell Biol. 122 (4), 961-972 (1993)|  MEDLINE   93352709|\35:REFERENCE   7  (residues 1 to 1452)|\69:  AUTHORS   Gebbink,M.F., van Etten,I., Hateboer,G., Suijkerbuijk,R.,|\71:            Beijersbergen,R.L., Geurts van Kessel,A. and Moolenaar,W.H.|\78:  TITLE     Cloning, expression and chromosomal localization of a new putative|\54:            receptor-like protein tyrosine phosphatase|\48:  JOURNAL   FEBS Lett. 290 (1-2), 123-130 (1991)|  MEDLINE   92008644
end
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end|2038790
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\27:hPTPmu_D2 (NP_002836) PTPRM|||||302014800|0|\176:protein tyrosine phosphatase, receptor type, M precursor; protein tyrosine phosphatase, receptor type, mu polypeptide; protein tyrosine phosphatase mu precursor [Homo sapiens].
end|2|2|
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obj|String*|18|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from X58288.1 and AA281524.1.|\58:On Feb 22, 2002 this sequence version replaced gi:4506319.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\63:region, a single transmembrane region, and two tandem catalytic|\67:domains, and thus represents a receptor-type PTP. The extracellular|\67:region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like|\63:domain and four fibronectin type III-like repeats. This PTP has|\67:been shown to mediate cell-cell aggregation through the interaction|\67:with another molecule of this PTP on an adjacent cell. This PTP can|\60:interact with scaffolding protein RACK1/GNB2L1, which may be|\63:necessary for the downstream signaling in response to cell-cell|adhesion.
end
obj|String*|52|\35:REFERENCE   1  (residues 1 to 1452)|\74:  AUTHORS   Blanchetot,C., Tertoolen,L.G., Overvoorde,J. and den Hertog,J.|\72:  TITLE     Intra- and intermolecular interactions between intracellular|\61:            domains of receptor protein-tyrosine phosphatases|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47263-47269 (2002)|  MEDLINE   22344739|\78:  REMARK    GeneRIF: interactions between RPTP-domain1s and RPTP-domain 2s are|\75:            a common but specific mechanism that is likely to be regulated-|\73:            domain2s and the wedge structures are crucial determinants of|\73:            binding specificity, thus regulating cross-talk between RPTPs|\35:REFERENCE   2  (residues 1 to 1452)|\77:  AUTHORS   Mourton,T., Hellberg,C.B., Burden-Gulley,S.M., Hinman,J., Rhee,A.|\33:            and Brady-Kalnay,S.M.|\73:  TITLE     The PTPmu protein-tyrosine phosphatase binds and recruits the|\59:            scaffolding protein RACK1 to cell-cell contacts|\55:  JOURNAL   J. Biol. Chem. 276 (18), 14896-14901 (2001)|  MEDLINE   21226727|\35:REFERENCE   3  (residues 1 to 1452)|\69:  AUTHORS   Feiken,E., van Etten,I., Gebbink,M.F., Moolenaar,W.H. and|\23:            Zondag,G.C.|\76:  TITLE     Intramolecular interactions between the juxtamembrane domain and|\72:            phosphatase domains of receptor protein-tyrosine phosphatase|\52:            RPTPmu. Regulation of catalytic activity|\55:  JOURNAL   J. Biol. Chem. 275 (20), 15350-15356 (2000)|  MEDLINE   20270248|\35:REFERENCE   4  (residues 1 to 1452)|\44:  AUTHORS   Brady-Kalnay,S.M. and Tonks,N.K.|\73:  TITLE     Identification of the homophilic binding site of the receptor|\47:            protein tyrosine phosphatase PTP mu|\55:  JOURNAL   J. Biol. Chem. 269 (45), 28472-28477 (1994)|  MEDLINE   95050637|\35:REFERENCE   5  (residues 1 to 1452)|\74:  AUTHORS   Suijkerbuijk,R.F., Gebbink,M.F., Moolenaar,W.H. and Geurts van|\21:            Kessel,A.|\68:  TITLE     Fine mapping of the human receptor-like protein tyrosine|\71:            phosphatase gene (PTPRM) to 18p11.2 by fluorescence in situ|\25:            hybridization|\59:  JOURNAL   Cytogenet. Cell Genet. 64 (3-4), 245-246 (1993)|  MEDLINE   94007972|\35:REFERENCE   6  (residues 1 to 1452)|\56:  AUTHORS   Brady-Kalnay,S.M., Flint,A.J. and Tonks,N.K.|\74:  TITLE     Homophilic binding of PTP mu, a receptor-type protein tyrosine|\58:            phosphatase, can mediate cell-cell aggregation|\49:  JOURNAL   J. Cell Biol. 122 (4), 961-972 (1993)|  MEDLINE   93352709|\35:REFERENCE   7  (residues 1 to 1452)|\69:  AUTHORS   Gebbink,M.F., van Etten,I., Hateboer,G., Suijkerbuijk,R.,|\71:            Beijersbergen,R.L., Geurts van Kessel,A. and Moolenaar,W.H.|\78:  TITLE     Cloning, expression and chromosomal localization of a new putative|\54:            receptor-like protein tyrosine phosphatase|\48:  JOURNAL   FEBS Lett. 290 (1-2), 123-130 (1991)|  MEDLINE   92008644
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="18"|/map="18p11.2"
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obj|DBObj||Protein_1|||||0|0|\102:protein tyrosine phosphatase, receptor type, mu polypeptide; protein tyrosine phosphatase mu precursor
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obj|String*|3|\56:/product="protein tyrosine phosphatase, receptor type, M|precursor"|\21:/EC_number="3.1.3.48"
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obj|String*|13|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM|\53:VNTI URL:vnti:protein/hPTPmu_D2+%28NP_002836%29+PTPRM
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end
obj|IxMolX
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obj|BioObject
obj|DBObj||\28:hPTPrho_D1 (NP_573400) PTPRT|||||302014800|0|\121:protein tyrosine phosphatase, receptor type, T isoform 1 precursor; receptor protein tyrosine phosphatase [Homo sapiens].
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end
obj|String*|22|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from AF043644.4 and R50970.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\67:region, a single transmembrane region, and two tandem intracellular|\63:catalytic domains, and thus represents a receptor-type PTP. The|\67:extracellular region contains a meprin-A5 antigen-PTP (MAM) domain,|\65:Ig-like and fibronectin type III-like repeats. The protein domain|\64:structure and the expression pattern of the mouse counterpart of|\67:this PTP suggest its roles in both signal transduction and cellular|\65:adhesion in the central nervous system. Two alternatively spliced|\65:transcript variants of this gene, which encode distinct proteins,|have been reported.||\59:Transcript Variant: This variant (1) contains an additional|\65:fragment within the coding region when compared to variant 2, and|\66:thus encodes a protein that contains an extra internal segment, as|\22:compared to isoform 2.
end
obj|String*|30|\35:REFERENCE   1  (residues 1 to 1463)|\78:  AUTHORS   Besco,J.A., Frostholm,A., Popesco,M.C., Burghes,A.H. and Rotter,A.|\74:  TITLE     Genomic organization and alternative splicing of the human and|\31:            mouse RPTPrho genes|\40:  JOURNAL   BMC Genomics 2 (1), 1 (2001)|\35:REFERENCE   2  (residues 1 to 1463)|\79:  AUTHORS   McAndrew,P.E., Frostholm,A., White,R.A., Rotter,A. and Burghes,A.H.|\73:  TITLE     Identification and characterization of RPTP rho, a novel RPTP|\69:            mu/kappa-like receptor protein tyrosine phosphatase whose|\66:            expression is restricted to the central nervous system|\60:  JOURNAL   Brain Res. Mol. Brain Res. 56 (1-2), 9-21 (1998)|  MEDLINE   98267260|\35:REFERENCE   3  (residues 1 to 1463)|\77:  AUTHORS   McAndrew,P.E., Frostholm,A., Evans,J.E., Zdilar,D., Goldowitz,D.,|\49:            Chiu,I.M., Burghes,A.H. and Rotter,A.|\76:  TITLE     Novel receptor protein tyrosine phosphatase (RPTPrho) and acidic|\68:            fibroblast growth factor (FGF-1) transcripts delineate a|\73:            rostrocaudal boundary in the granule cell layer of the murine|\29:            cerebellar cortex|\52:  JOURNAL   J. Comp. Neurol. 391 (4), 444-455 (1998)|  MEDLINE   98146229|\35:REFERENCE   4  (residues 1 to 1463)|\75:  AUTHORS   Hillier,L.D., Lennon,G., Becker,M., Bonaldo,M.F., Chiapelli,B.,|\69:            Chissoe,S., Dietrich,N., DuBuque,T., Favello,A., Gish,W.,|\69:            Hawkins,M., Hultman,M., Kucaba,T., Lacy,M., Le,M., Le,N.,|\77:            Mardis,E., Moore,B., Morris,M., Parsons,J., Prange,C., Rifkin,L.,|\57:            Rohlfing,T., Schellenberg,K., Marra,M. et al.|\76:  TITLE     Generation and analysis of 280,000 human expressed sequence tags|\45:  JOURNAL   Genome Res. 6 (9), 807-828 (1996)|  MEDLINE   97044478
end
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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end|203C5A8
end
obj|IxMolX
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obj|DBObj||\28:hPTPrho_D2 (NP_573400) PTPRT|||||302014800|0|\121:protein tyrosine phosphatase, receptor type, T isoform 1 precursor; receptor protein tyrosine phosphatase [Homo sapiens].
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obj|String*|22|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from AF043644.4 and R50970.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\67:region, a single transmembrane region, and two tandem intracellular|\63:catalytic domains, and thus represents a receptor-type PTP. The|\67:extracellular region contains a meprin-A5 antigen-PTP (MAM) domain,|\65:Ig-like and fibronectin type III-like repeats. The protein domain|\64:structure and the expression pattern of the mouse counterpart of|\67:this PTP suggest its roles in both signal transduction and cellular|\65:adhesion in the central nervous system. Two alternatively spliced|\65:transcript variants of this gene, which encode distinct proteins,|have been reported.||\59:Transcript Variant: This variant (1) contains an additional|\65:fragment within the coding region when compared to variant 2, and|\66:thus encodes a protein that contains an extra internal segment, as|\22:compared to isoform 2.
end
obj|String*|30|\35:REFERENCE   1  (residues 1 to 1463)|\78:  AUTHORS   Besco,J.A., Frostholm,A., Popesco,M.C., Burghes,A.H. and Rotter,A.|\74:  TITLE     Genomic organization and alternative splicing of the human and|\31:            mouse RPTPrho genes|\40:  JOURNAL   BMC Genomics 2 (1), 1 (2001)|\35:REFERENCE   2  (residues 1 to 1463)|\79:  AUTHORS   McAndrew,P.E., Frostholm,A., White,R.A., Rotter,A. and Burghes,A.H.|\73:  TITLE     Identification and characterization of RPTP rho, a novel RPTP|\69:            mu/kappa-like receptor protein tyrosine phosphatase whose|\66:            expression is restricted to the central nervous system|\60:  JOURNAL   Brain Res. Mol. Brain Res. 56 (1-2), 9-21 (1998)|  MEDLINE   98267260|\35:REFERENCE   3  (residues 1 to 1463)|\77:  AUTHORS   McAndrew,P.E., Frostholm,A., Evans,J.E., Zdilar,D., Goldowitz,D.,|\49:            Chiu,I.M., Burghes,A.H. and Rotter,A.|\76:  TITLE     Novel receptor protein tyrosine phosphatase (RPTPrho) and acidic|\68:            fibroblast growth factor (FGF-1) transcripts delineate a|\73:            rostrocaudal boundary in the granule cell layer of the murine|\29:            cerebellar cortex|\52:  JOURNAL   J. Comp. Neurol. 391 (4), 444-455 (1998)|  MEDLINE   98146229|\35:REFERENCE   4  (residues 1 to 1463)|\75:  AUTHORS   Hillier,L.D., Lennon,G., Becker,M., Bonaldo,M.F., Chiapelli,B.,|\69:            Chissoe,S., Dietrich,N., DuBuque,T., Favello,A., Gish,W.,|\69:            Hawkins,M., Hultman,M., Kucaba,T., Lacy,M., Le,M., Le,N.,|\77:            Mardis,E., Moore,B., Morris,M., Parsons,J., Prange,C., Rifkin,L.,|\57:            Rohlfing,T., Schellenberg,K., Marra,M. et al.|\76:  TITLE     Generation and analysis of 280,000 human expressed sequence tags|\45:  JOURNAL   Genome Res. 6 (9), 807-828 (1996)|  MEDLINE   97044478
end
obj|Object*|0
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|283
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end|269|269|||0|1|283|1|1|1|1|1..1463
obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="20"|/map="20q12-q13"
end|0||
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obj|DBObj||Protein_1|||||0|0|\37:receptor protein tyrosine phosphatase
end|270|270|||0|1|283|1|1|1|1|1..1463
obj|String*|2|\56:/product="protein tyrosine phosphatase, receptor type, T|isoform 1 precursor"
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obj|String*|2|\57:/product="protein tyrosine phosphatase, receptor type, T,|isoform 1"
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obj|Feature
obj|DBObj||Region_2|||||0|0|PTPc
end|266|266|||0|18|283|1|1|1|1|1196..1461
obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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end|\283:rslyynisrldpqtnssqikdefqtlnivtprvrpedcsigllprnhdknrsmdvlpldrclpflisvdgessnyinaalmdshkqpaafvvtqhplpntvadfwrlvfdyncssvvmlnemdtaqfcmqywpektsgcygpiqvefvsadidediihrifricnmarpqdgyrivqhlqyigwpayrdtppskrsllkvvrrlekwqeqydgregrtvvhclngggrsgtfcaicsvcemiqqqniidvfhivktlrnnksnmvetleqykfvyevaleyls|GenPept|
obj|String*|1|NP_573400
end||06-APR-2003|Homo sapiens (human)
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obj|String*|1|Homo sapiens
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end
obj|String*|12|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Primates|Catarrhini|Hominidae|Homo
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obj|String*|1|\29:REFSEQ: accession NM_133170.1
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obj|String*|13|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT|\54:VNTI URL:vnti:protein/hPTPrho_D2+%28NP_573400%29+PTPRT
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end|219B220
end
obj|IxMolX
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obj|DBObj||\29:hPTPS31_D1 (AR073855) PTPGMC1|||||302014800|0|\35:Translation of a fragment of delete
end|2|2|
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|276
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obj|String*|47|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1|\55:VNTI URL:vnti:protein/hPTPS31_D1+%28AR073855%29+PTPGMC1
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obj|IxMolX
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obj|DBObj||\30:hPTPsigma_D1 (NP_002841) PTPRS|||||302014800|0|\125:protein tyrosine phosphatase, receptor type, sigma isoform 1 precursor; protein tyrosine phosphatase PTPsigma [Homo sapiens].
end|2|2|
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obj|String*|22|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from U35234.1 and BI461316.1.|\58:On Mar 26, 2002 this sequence version replaced gi:4506327.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\60:oncogenic transformation. This PTP contains an extracellular|\53:region, a single transmembrane segment and two tandem|\57:intracytoplasmic catalytic domains, and thus represents a|\62:receptor-type PTP. The extracellular region of this protein is|\67:composed of multiple Ig-like and fibronectin type III-like domains.|\66:Studies of the similar gene in mice suggested that this PTP may be|\65:involved in cell-cell interaction, primary axonogenesis, and axon|\67:guidance during embryogenesis. This PTP has been also implicated in|\63:the molecular control of adult nerve repair. Four alternatively|\65:spliced transcript variants, which encode distinct proteins, have|been reported.||\64:Transcript Variant: This variant (1) encodes the longest isoform|(1).
end
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obj|IxMolX
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obj|DBObj||\26:hSAP1_D1 (NP_002833) PTPRH|||||302014800|0|\72:protein tyrosine phosphatase, receptor type, H precursor [Homo sapiens].
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obj|String*|16|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\45:reference sequence was derived from D15049.1.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\61:oncogenic transformation. This PTP possesses an extracellular|\51:region, a single transmembrane region, and a single|\56:intracytoplasmic catalytic domain, and thus represents a|\58:receptor-type PTP. The extracellular region contains eight|\62:fibronectin type III-like repeats and multiple N-glycosylation|\64:sites. The gene was shown to be expressed primarily in brain and|\67:liver, and at a lower level in heart and stomach. It was also found|\60:to be expressed in several cancer cell lines, but not in the|\29:corresponding normal tissues.
end
obj|String*|25|\35:REFERENCE   1  (residues 1 to 1118)|\71:  AUTHORS   Takada,T., Noguchi,T., Inagaki,K., Hosooka,T., Fukunaga,K.,|\57:            Yamao,T., Ogawa,W., Matozaki,T. and Kasuga,M.|\63:  TITLE     Induction of apoptosis by stomach cancer-associated|\42:            protein-tyrosine phosphatase-1|\55:  JOURNAL   J. Biol. Chem. 277 (37), 34359-34366 (2002)|  MEDLINE   22206505|\77:  REMARK    GeneRIF: SAP-1 induces apoptotic cell death by inhibition of cell|\72:            survival signaling mediated by PI 3-kinase, Akt, and ILK and|\67:            activation of a caspase-dependent proapoptotic pathway.|\35:REFERENCE   2  (residues 1 to 1118)|\74:  AUTHORS   Marneros,A.G., Mehenni,H., Reichenberger,E., Antonarakis,S.E.,|\35:            Krieg,T. and Olsen,B.R.|\78:  TITLE     Gene for the human transmembrane-type protein tyrosine phosphatase|\77:            H (PTPRH): genomic structure, fine-mapping and its exclusion as a|\48:            candidate for Peutz-Jeghers syndrome|\59:  JOURNAL   Cytogenet. Cell Genet. 92 (3-4), 213-216 (2001)|  MEDLINE   21328879|\35:REFERENCE   3  (residues 1 to 1118)|\70:  AUTHORS   Matozaki,T., Suzuki,T., Uchida,T., Inazawa,J., Ariyama,T.,|\76:            Matsuda,K., Horita,K., Noguchi,H., Mizuno,H., Sakamoto,C. et al.|\76:  TITLE     Molecular cloning of a human transmembrane-type protein tyrosine|\70:            phosphatase and its expression in gastrointestinal cancers|\52:  JOURNAL   J. Biol. Chem. 269 (3), 2075-2081 (1994)|  MEDLINE   94124561
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|1|\29:REFSEQ: accession NM_002842.1
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obj|BioObject
obj|DBObj||\26:hSHP1_D1 (NP_002822) PTPN6|||||302014800|0|\211:protein tyrosine phosphatase, non-receptor type 6 isoform 1; protein-tyrosine phosphatase 1C; hematopoietic cell phophatase; hematopoietic cell protein-tyrosine phosphatase; 70 kda SHP-1L protein [Homo sapiens].
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obj|String*|25|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from M77273.1, BC002523.1 and|U15536.1.|\58:On Jan 10, 2002 this sequence version replaced gi:4506297.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\66:oncogenic transformation. N-terminal part of this PTP contains two|\54:tandem Src homolog (SH2) domains, which act as protein|\64:phospho-tyrosine binding domains, and mediate the interaction of|\64:this PTP with its substrates. This PTP is expressed primarily in|\63:hematopoietic cells, and functions as an important regulator of|\64:multiple signaling pathways in hematopoietic cells. This PTP has|\67:been shown to interact with, and dephosphorylate a wide spectrum of|\64:phospho-proteins involved in hematopoietic cell signaling. Three|\66:alternatively spliced variants of this gene, which encode distinct|\29:isoforms, have been reported.||\63:Transcript Variant: This variant (1) lacks an internal fragment|\67:within the coding region, which leads to a translation frame change|\60:when compared to variant 3. It encodes a protein that has an|\63:identical N-terminus and a different C-terminus, as compared to|isoform 3.
end
obj|String*|148|\34:REFERENCE   1  (residues 1 to 595)|\68:  AUTHORS   Hanson,E.M., Dickensheets,H., Qu,C.K., Donnelly,R.P. and|\23:            Keegan,A.D.|\74:  TITLE     Regulation of the dephosphorylation of Stat6. Participation of|\69:            Tyr-713 in the interleukin-4 receptor alpha, the tyrosine|\49:            phosphatase SHP-1, and the proteasome|\52:  JOURNAL   J. Biol. Chem. 278 (6), 3903-3911 (2003)|  MEDLINE   22450671|\75:  REMARK    GeneRIF: participation in regulation of Stat6 dephosphorylation|\34:REFERENCE   2  (residues 1 to 595)|\76:  AUTHORS   Oka,T., Ouchida,M., Koyama,M., Ogama,Y., Takada,S., Nakatani,Y.,|\66:            Tanaka,T., Yoshino,T., Hayashi,K., Ohara,N., Kondo,E.,|\77:            Takahashi,K., Tsuchiyama,J., Tanimoto,M., Shimizu,K. and Akagi,T.|\76:  TITLE     Gene silencing of the tyrosine phosphatase SHP1 gene by aberrant|\46:            methylation in leukemias/lymphomas|\49:  JOURNAL   Cancer Res. 62 (22), 6390-6394 (2002)|  MEDLINE   22325693|\67:  REMARK    GeneRIF: Functional loss of SHP1 is associated with the|\48:            pathogenesis of leukemias/lymphomas.|\34:REFERENCE   3  (residues 1 to 595)|\67:  AUTHORS   Leon,F., Cespon,C., Franco,A., Lombardia,M., Roldan,E.,|\65:            Escribano,L., Harto,A., Gonzalez-Porque,P. and Roy,G.|\76:  TITLE     SHP-1 expression in peripheral T cells from patients with Sezary|\67:            syndrome and in the T cell line HUT-78: implications in|\35:            JAK3-mediated signaling|\45:  JOURNAL   Leukemia 16 (8), 1470-1477 (2002)|  MEDLINE   22140504|\75:  REMARK    GeneRIF: In the T cell line HUT-78, JAK3 was found to be highly|\78:            phosphorylated. These results suggest that SHP-1 might be involved|\77:            in maintaining the IL-2R/JAK3 signaling pathway under control and|\77:            point towards a role of SHP-1 in the pathogenesis of the disease.|\34:REFERENCE   4  (residues 1 to 595)|\75:  AUTHORS   Nikolova,M., Musette,P., Bagot,M., Boumsell,L. and Bensussan,A.|\76:  TITLE     Engagement of ILT2/CD85j in Sezary syndrome cells inhibits their|\29:            CD3/TCR signaling|\43:  JOURNAL   Blood 100 (3), 1019-1025 (2002)|  MEDLINE   22122461|\78:  REMARK    GeneRIF: ILT2 triggering on cutaneous T-cell lymphoma (CTCL) cells|\79:            leads to the recruitment of SHP-1 and to the specific inhibition of|\76:            CTCL malignant cell proliferation in S##zary syndrome induced by|\51:            CD3/T-cell receptor. (TCR) stimulation.|\34:REFERENCE   5  (residues 1 to 595)|\76:  AUTHORS   Angata,T., Kerr,S.C., Greaves,D.R., Varki,N.M., Crocker,P.R. and|            Varki,A.|\79:  TITLE     Cloning and characterization of human Siglec-11. A recently evolved|\77:            signaling that can interact with SHP-1 and SHP-2 and is expressed|\60:            by tissue macrophages, including brain microglia|\55:  JOURNAL   J. Biol. Chem. 277 (27), 24466-24474 (2002)|  MEDLINE   22086217|\45:  REMARK    GeneRIF: interacts with siglec-11|\34:REFERENCE   6  (residues 1 to 595)|\46:  AUTHORS   Vyas,Y.M., Maniar,H. and Dupont,B.|\70:  TITLE     Cutting edge: differential segregation of the SRC homology|\75:            2-containing protein tyrosine phosphatase-1 within the early NK|\73:            cell immune synapse distinguishes noncytolytic from cytolytic|\24:            interactions|\49:  JOURNAL   J. Immunol. 168 (7), 3150-3154 (2002)|  MEDLINE   21904490|\78:  REMARK    GeneRIF: SHP-1 is recruited to the NK cell immune synapse within 1|\77:            min in both cytolytic and noncytolytic conjugates, allowing clear|\79:            distinction between noncytolytic and cytolytic interactions at this|\23:            early time.|\34:REFERENCE   7  (residues 1 to 595)|\79:  AUTHORS   Kurita-Taniguchi,M., Hazeki,K., Murabayashi,N., Fukui,A., Tsuji,S.,|\50:            Matsumoto,M., Toyoshima,K. and Seya,T.|\74:  TITLE     Molecular assembly of CD46 with CD9, alpha3-beta1 integrin and|\75:            protein tyrosine phosphatase SHP-1 in human macrophages through|\37:            differentiation by GM-CSF|\48:  JOURNAL   Mol. Immunol. 38 (9), 689-700 (2002)|  MEDLINE   21848359|\74:  REMARK    GeneRIF: peripheral blood monocytes treated for 5--8 days with|\71:            GM-CSF (i.e. mature Mphi) acquired the capacity to assemble|\74:            tyrosine phosphatase SHP-1 with CD9, alpha3-beta1 integrin and|\23:            their CD46.|\34:REFERENCE   8  (residues 1 to 595)|\40:  AUTHORS   Blasioli,J. and Goodnow,C.C.|\63:  TITLE     Lyn/CD22/SHP-1 and their importance in autoimmunity|\51:  JOURNAL   Curr. Dir. Autoimmun. 5, 151-160 (2002)|  MEDLINE   21685428|\77:  REMARK    GeneRIF: The Lyn/CD22/SHP-1 pathway is important in autoimmunity.|\75:            Naive and tolerant B-cells differ in their calcium signaling in|\46:            response to antigenic stimulation.|\34:REFERENCE   9  (residues 1 to 595)|\47:  AUTHORS   Jin,Y.J., Yu,C.L. and Burakoff,S.J.|\75:  TITLE     Human 70-kDa SHP-1L differs from 68-kDa SHP-1 in its C-terminal|\44:            structure and catalytic activity|\55:  JOURNAL   J. Biol. Chem. 274 (40), 28301-28307 (1999)|  MEDLINE   99428497|\34:REFERENCE   10 (residues 1 to 595)|\78:  AUTHORS   Bousquet,C., Delesque,N., Lopez,F., Saint-Laurent,N., Esteve,J.P.,|\58:            Bedecs,K., Buscail,L., Vaysse,N. and Susini,C.|\78:  TITLE     sst2 somatostatin receptor mediates negative regulation of insulin|\69:            receptor signaling through the tyrosine phosphatase SHP-1|\53:  JOURNAL   J. Biol. Chem. 273 (12), 7099-7106 (1998)|  MEDLINE   98175983|\34:REFERENCE   11 (residues 1 to 595)|\70:  AUTHORS   Blery,M., Kubagawa,H., Chen,C.C., Vely,F., Cooper,M.D. and|\21:            Vivier,E.|\76:  TITLE     The paired Ig-like receptor PIR-B is an inhibitory receptor that|\59:            recruits the protein-tyrosine phosphatase SHP-1|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 95 (5), 2446-2451 (1998)|  MEDLINE   98151532|\34:REFERENCE   12 (residues 1 to 595)|\68:  AUTHORS   Ono,M., Okada,H., Bolland,S., Yanagi,S., Kurosaki,T. and|\24:            Ravetch,J.V.|\71:  TITLE     Deletion of SHIP or SHP-1 reveals two distinct pathways for|\32:            inhibitory signaling|\39:  JOURNAL   Cell 90 (2), 293-301 (1997)|  MEDLINE   97386454|\34:REFERENCE   13 (residues 1 to 595)|\70:  AUTHORS   Li,R.Y., Gaits,F., Ragab,A., Ragab-Thomas,J.M. and Chap,H.|\74:  TITLE     Tyrosine phosphorylation of an SH2-containing protein tyrosine|\70:            phosphatase is coupled to platelet thrombin receptor via a|\62:            pertussis toxin-sensitive heterotrimeric G-protein|\45:  JOURNAL   EMBO J. 14 (11), 2519-2526 (1995)|  MEDLINE   95300784|\34:REFERENCE   14 (residues 1 to 595)|\48:  AUTHORS   Banville,D., Stocco,R. and Shen,S.H.|\73:  TITLE     Human protein tyrosine phosphatase 1C (PTPN6) gene structure:|\72:            alternate promoter usage and exon skipping generate multiple|\23:            transcripts|\43:  JOURNAL   Genomics 27 (1), 165-173 (1995)|  MEDLINE   95394454|\34:REFERENCE   15 (residues 1 to 595)|\73:  AUTHORS   Plutzky,J., Neel,B.G., Rosenberg,R.D., Eddy,R.L., Byers,M.G.,|\39:            Jani-Sait,S. and Shows,T.B.|\78:  TITLE     Chromosomal localization of an SH2-containing tyrosine phosphatase|            (PTPN6)|\43:  JOURNAL   Genomics 13 (3), 869-872 (1992)|  MEDLINE   92347896|\34:REFERENCE   16 (residues 1 to 595)|\52:  AUTHORS   Plutzky,J., Neel,B.G. and Rosenberg,R.D.|\73:  TITLE     Isolation of a src homology 2-containing tyrosine phosphatase|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 89 (3), 1123-1127 (1992)|  MEDLINE   92141214|\34:REFERENCE   17 (residues 1 to 595)|\49:  AUTHORS   Yi,T.L., Cleveland,J.L. and Ihle,J.N.|\64:  TITLE     Protein tyrosine phosphatase containing SH2 domains:|\77:            characterization, preferential expression in hematopoietic cells,|\58:            and localization to human chromosome 12p12-p13|\51:  JOURNAL   Mol. Cell. Biol. 12 (2), 836-846 (1992)|  MEDLINE   92123209|\34:REFERENCE   18 (residues 1 to 595)|\62:  AUTHORS   Shen,S.H., Bastien,L., Posner,B.I. and Chretien,P.|\78:  TITLE     A protein-tyrosine phosphatase with sequence similarity to the SH2|\50:            domain of the protein-tyrosine kinases|\45:  JOURNAL   Nature 352 (6337), 736-739 (1991)|  MEDLINE   91343005
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obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|1|\29:REFSEQ: accession NM_002831.2
end
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end|20DB080
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\27:hSHP2_D1 (NP_002825) PTPN11|||||302014800|0|\180:protein tyrosine phosphatase, non-receptor type 11 isoform 1; protein-tyrosine phosphatase 2C; Noonan syndrome 1; protein tyrosine phosphatase, non-receptor type 11 [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|20|\64:REVIEWED REFSEQ: This record has been curated by NCBI staff. The|\60:reference sequence was derived from D13540.1 and BF515187.1.|\59:On Jan 25, 2002 this sequence version replaced gi:13430846.||\60:Summary: The protein encoded by this gene is a member of the|\63:protein tyrosine phosphatase (PTP) family. PTPs are known to be|\65:signaling molecules that regulate a variety of cellular processes|\58:including cell growth, differentiation, mitotic cycle, and|\58:oncogenic transformation. This PTP contains two tandem Src|\62:homology-2 domains, which function as phospho-tyrosine binding|\56:domains and mediate the interaction of this PTP with its|\66:substrates. This PTP is widely expressed in most tissues and plays|\59:a regulatory role in various cell signaling events that are|\62:important for a diversity of cell functions, such as mitogenic|\65:activation, metabolic control, transcription regulation, and cell|\64:migration. Two alternatively spliced transcript variants of this|\58:gene, which encode distinct isoforms, have been described.||\64:Transcript Variant: This variant (1) contains a different 3' end|\67:region, and encodes a longer isoform (1), as compared to variant 2.
end
obj|String*|233|\34:REFERENCE   1  (residues 1 to 593)|\68:  AUTHORS   Yamazaki,S., Yamakawa,A., Ito,Y., Ohtani,M., Higashi,H.,|\38:            Hatakeyama,M. and Azuma,T.|\72:  TITLE     The CagA protein of Helicobacter pylori is translocated into|\71:            epithelial cells and binds to SHP-2 in human gastric mucosa|\51:  JOURNAL   J. Infect. Dis. 187 (2), 334-337 (2003)|  MEDLINE   22439942|\76:  REMARK    GeneRIF: The CagA protein of Helicobacter pylori is translocated|\76:            into epithelial cells and binds to SHP-2 in human gastric mucosa|\34:REFERENCE   2  (residues 1 to 593)|\76:  AUTHORS   Lehmann,U., Schmitz,J., Weissenbach,M., Sobota,R.M., Hortner,M.,|\63:            Friederichs,K., Behrmann,I., Tsiaris,W., Sasaki,A.,|\77:            Schneider-Mergener,J., Yoshimura,A., Neel,B.G., Heinrich,P.C. and|\22:            Schaper,F.|\73:  TITLE     SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of|\49:            interleukin-6 signaling through gp130|\50:  JOURNAL   J. Biol. Chem. 278 (1), 661-671 (2003)|  MEDLINE   22393451|\77:  REMARK    GeneRIF: These data suggest, that there are two, largely distinct|\76:            modes of negative regulation of gp130 activity, despite the fact|\74:            that both SOCS3 and SHP2 are recruited to the same site within|            gp130.|\34:REFERENCE   3  (residues 1 to 593)|\78:  AUTHORS   Wu,T.R., Hong,Y.K., Wang,X.D., Ling,M.Y., Dragoi,A.M., Chung,A.S.,|\60:            Campbell,A.G., Han,Z.Y., Feng,G.S. and Chin,Y.E.|\69:  TITLE     SHP-2 is a dual-specificity phosphatase involved in Stat1|\76:            dephosphorylation at both tyrosine and serine residues in nuclei|\55:  JOURNAL   J. Biol. Chem. 277 (49), 47572-47580 (2002)|  MEDLINE   22344627|\77:  REMARK    GeneRIF: SHP-2 is a dual-specificity protein phosphatase involved|\79:            in Stat1 dephosphorylation at both tyrosine and serine residues and|\71:            plays an important role in modulating STAT function in gene|\22:            regulation|\34:REFERENCE   4  (residues 1 to 593)|\40:  AUTHORS   Maile,L.A. and Clemmons,D.R.|\75:  TITLE     The alphaVbeta3 integrin regulates insulin-like growth factor I|\68:            (IGF-I) receptor phosphorylation by altering the rate of|\72:            recruitment of the Src-homology 2-containing phosphotyrosine|\57:            phosphatase-2 to the activated IGF-I receptor|\52:  JOURNAL   Endocrinology 143 (11), 4259-4264 (2002)|  MEDLINE   22286240|\77:  REMARK    GeneRIF: activation state of alphaVbeta3 integrin is an important|\78:            regulator of the duration of insulin-like growth factor I receptor|\78:            phosphorylation and this regulation is mediated through changes in|\49:            the subcellular localization of SHP-2|\34:REFERENCE   5  (residues 1 to 593)|\72:  AUTHORS   Ion,A., Tartaglia,M., Song,X., Kalidas,K., van der Burgt,I.,|\79:            Shaw,A.C., Ming,J.E., Zampino,G., Zackai,E.H., Dean,J.C., Somer,M.,|\74:            Parenti,G., Crosby,A.H., Patton,M.A., Gelb,B.D. and Jeffery,S.|\75:  TITLE     Absence of PTPN11 mutations in 28 cases of cardiofaciocutaneous|\26:            (CFC) syndrome|\49:  JOURNAL   Hum. Genet. 111 (4-5), 421-427 (2002)|  MEDLINE   22271640|\73:  REMARK    GeneRIF: absence of mutation in cases of cardiofaciocutaneous|            syndrome|\34:REFERENCE   6  (residues 1 to 593)|\58:  AUTHORS   Cai,T., Nishida,K., Hirano,T. and Khavari,P.A.|\78:  TITLE     Gab1 and SHP-2 promote Ras/MAPK regulation of epidermal growth and|\27:            differentiation|\49:  JOURNAL   J. Cell Biol. 159 (1), 103-112 (2002)|  MEDLINE   22267353|\69:  REMARK    GeneRIF: Results indicate that Gab1 and SHP-2 promote the|\74:            undifferentiated epidermal cell state by facilitating Ras/MAPK|\22:            signaling.|\34:REFERENCE   7  (residues 1 to 593)|\71:  AUTHORS   Maheshwari,M., Belmont,J., Fernbach,S., Ho,T., Molinari,L.,|\76:            Yakub,I., Yu,F., Combes,A., Towbin,J., Craigen,W.J. and Gibbs,R.|\78:  TITLE     PTPN11 mutations in Noonan syndrome type I: detection of recurrent|\39:            mutations in exons 3 and 13|\46:  JOURNAL   Hum. Mutat. 20 (4), 298-304 (2002)|  MEDLINE   22236043|\78:  REMARK    GeneRIF: Mutations in PTPN11/SHP2 underlie a common form of Noonan|\75:            syndrome and confirm that the disease exhibits both allelic and|\32:            locus heterogeneity.|\34:REFERENCE   8  (residues 1 to 593)|\57:  AUTHORS   Legius,E., Schrander-Stumpel,C., Schollen,E.,|\62:            Pulles-Heintzberger,C., Gewillig,M. and Fryns,J.P.|\48:  TITLE     PTPN11 mutations in LEOPARD syndrome|\49:  JOURNAL   J. Med. Genet. 39 (8), 571-574 (2002)|  MEDLINE   22151430|\76:  REMARK    GeneRIF: Some PTPN11 mutations (e.g., Y279C) are associated with|\73:            both the Noonan syndrome phenotype and with skin pigmentation|\73:            anomalies, such as multiple lentigines or caf## au lait spots|\31:            (LEOPARD syndrome).|\34:REFERENCE   9  (residues 1 to 593)|\77:  AUTHORS   Kosaki,K., Suzuki,T., Muroya,K., Hasegawa,T., Sato,S., Matsuo,N.,|\57:            Kosaki,R., Nagai,T., Hasegawa,Y. and Ogata,T.|\70:  TITLE     PTPN11 (protein-tyrosine phosphatase, nonreceptor-type 11)|\69:            mutations in seven Japanese patients with Noonan syndrome|\64:  JOURNAL   J. Clin. Endocrinol. Metab. 87 (8), 3529-3533 (2002)|  MEDLINE   22151235|\78:  REMARK    GeneRIF: PTPN11 mutations are responsible for Noonan syndrome in a|\75:            substantial fraction of patients and that relatively infrequent|\78:            features of Noonan syndrome, such as sensory deafness and bleeding|\64:            diathesis, can also result from mutations of PTPN11.|\34:REFERENCE   10 (residues 1 to 593)|\76:  AUTHORS   Angata,T., Kerr,S.C., Greaves,D.R., Varki,N.M., Crocker,P.R. and|            Varki,A.|\79:  TITLE     Cloning and characterization of human Siglec-11. A recently evolved|\77:            signaling that can interact with SHP-1 and SHP-2 and is expressed|\60:            by tissue macrophages, including brain microglia|\55:  JOURNAL   J. Biol. Chem. 277 (27), 24466-24474 (2002)|  MEDLINE   22086217|\45:  REMARK    GeneRIF: interacts with siglec-11|\34:REFERENCE   11 (residues 1 to 593)|\78:  AUTHORS   Bordin,L., Brunati,A.M., Donella-Deana,A., Baggio,B., Toninello,A.|\24:            and Clari,G.|\71:  TITLE     Band 3 is an anchor protein and a target for SHP-2 tyrosine|\45:            phosphatase in human erythrocytes|\41:  JOURNAL   Blood 100 (1), 276-282 (2002)|  MEDLINE   22065093|\75:  REMARK    GeneRIF: Band 3 is an anchor protein for and a target for SHP-2|\55:            tyrosine phosphatase in human erythrocytes.|\34:REFERENCE   12 (residues 1 to 593)|\75:  AUTHORS   Tartaglia,M., Kalidas,K., Shaw,A., Song,X., Musat,D.L., van der|\68:            Burgt,I., Brunner,H.G., Bertola,D.R., Crosby,A., Ion,A.,|\68:            Kucherlapati,R.S., Jeffery,S., Patton,M.A. and Gelb,B.D.|\68:  TITLE     PTPN11 mutations in Noonan syndrome: molecular spectrum,|\72:            genotype-phenotype correlation, and phenotypic heterogeneity|\55:  JOURNAL   Am. J. Hum. Genet. 70 (6), 1555-1563 (2002)|  MEDLINE   21987645|\77:  REMARK    GeneRIF: PTPN11 mutations in Noonan syndrome: molecular spectrum,|\73:            genotype-phenotype correlation, and phenotypic heterogeneity.|\34:REFERENCE   13 (residues 1 to 593)|\71:  AUTHORS   Lacalle,R.A., Mira,E., Gomez-Mouton,C., Jimenez-Baranda,S.,|\38:            Martinez-A,C. and Manes,S.|\64:  TITLE     Specific SHP-2 partitioning in raft domains triggers|\58:            integrin-mediated signaling via Rho activation|\49:  JOURNAL   J. Cell Biol. 157 (2), 277-289 (2002)|  MEDLINE   21953171|\73:  REMARK    GeneRIF: Specific SHP-2 partitioning in raft domains triggers|\58:            integrin-mediated signaling via Rho activation|\34:REFERENCE   14 (residues 1 to 593)|\75:  AUTHORS   Ekman,S., Kallin,A., Engstrom,U., Heldin,C.H. and Ronnstrand,L.|\77:  TITLE     SHP-2 is involved in heterodimer specific loss of phosphorylation|\47:            of Tyr771 in the PDGF beta-receptor|\46:  JOURNAL   Oncogene 21 (12), 1870-1875 (2002)|  MEDLINE   21906255|\79:  REMARK    GeneRIF: SHP-2 modulates phosphorylation of PDGF receptors, thereby|\75:            controls RasGTP recruitment and Ras/MAP kinase signaling in the|\61:            heterodimeric configuration of the PDGF receptors|\34:REFERENCE   15 (residues 1 to 593)|\77:  AUTHORS   Higashi,H., Tsutsumi,R., Muto,S., Sugiyama,T., Azuma,T., Asaka,M.|\29:            and Hatakeyama,M.|\68:  TITLE     SHP-2 tyrosine phosphatase as an intracellular target of|\44:            Helicobacter pylori CagA protein|\46:  JOURNAL   Science 295 (5555), 683-686 (2002)|  MEDLINE   21669283|\76:  REMARK    GeneRIF: upon translocation, CagA perturbs cellular functions by|\30:            deregulating SHP-2|\34:REFERENCE   16 (residues 1 to 593)|\72:  AUTHORS   Fukunaga,K., Noguchi,T., Takeda,H., Matozaki,T., Hayashi,Y.,|\33:            Itoh,H. and Kasuga,M.|\65:  TITLE     Requirement for protein-tyrosine phosphatase SHP-2 in|\69:            insulin-induced activation of c-Jun NH(2)-terminal kinase|\52:  JOURNAL   J. Biol. Chem. 275 (7), 5208-5213 (2000)|  MEDLINE   20138272|\34:REFERENCE   17 (residues 1 to 593)|\47:  AUTHORS   Yu,C.L., Jin,Y.J. and Burakoff,S.J.|\76:  TITLE     Cytosolic tyrosine dephosphorylation of STAT5. Potential role of|\37:            SHP-2 in STAT5 regulation|\50:  JOURNAL   J. Biol. Chem. 275 (1), 599-604 (2000)|  MEDLINE   20085083|\34:REFERENCE   18 (residues 1 to 593)|\35:  AUTHORS   Li,C. and Friedman,J.M.|\71:  TITLE     Leptin receptor activation of SH2 domain containing protein|\76:            tyrosine phosphatase 2 modulates Ob receptor signal transduction|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (17), 9677-9682 (1999)|  MEDLINE   99380578|\34:REFERENCE   19 (residues 1 to 593)|\75:  AUTHORS   Manes,S., Mira,E., Gomez-Mouton,C., Zhao,Z.J., Lacalle,R.A. and|\25:            Martinez-A,C.|\79:  TITLE     Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion|\49:            kinase in regulation of cell motility|\53:  JOURNAL   Mol. Cell. Biol. 19 (4), 3125-3135 (1999)|  MEDLINE   99182500|\34:REFERENCE   20 (residues 1 to 593)|\71:  AUTHORS   Takada,T., Matozaki,T., Takeda,H., Fukunaga,K., Noguchi,T.,|\77:            Fujioka,Y., Okazaki,I., Tsuda,M., Yamao,T., Ochi,F. and Kasuga,M.|\66:  TITLE     Roles of the complex formation of SHPS-1 with SHP-2 in|\74:            insulin-stimulated mitogen-activated protein kinase activation|\53:  JOURNAL   J. Biol. Chem. 273 (15), 9234-9242 (1998)|  MEDLINE   98204923|\34:REFERENCE   21 (residues 1 to 593)|\69:  AUTHORS   Jamieson,C.R., van der Burgt,I., Brady,A.F., van Reen,M.,|\71:            Elsawi,M.M., Hol,F., Jeffery,S., Patton,M.A. and Mariman,E.|\79:  TITLE     Mapping a gene for Noonan syndrome to the long arm of chromosome 12|\45:  JOURNAL   Nat. Genet. 8 (4), 357-360 (1994)|  MEDLINE   95201801|\34:REFERENCE   22 (residues 1 to 593)|\54:  AUTHORS   Isobe,M., Hinoda,Y., Imai,K. and Adachi,M.|\78:  TITLE     Chromosomal localization of an SH2 containing tyrosine phosphatase|\48:            (SH-PTP3) gene to chromosome 12q24.1|\44:  JOURNAL   Oncogene 9 (6), 1751-1753 (1994)|  MEDLINE   94239755|\34:REFERENCE   23 (residues 1 to 593)|\59:  AUTHORS   Bastien,L., Ramachandran,C., Liu,S. and Adam,M.|\73:  TITLE     Cloning, expression and mutational analysis of SH-PTP2, human|\40:            protein-tyrosine phosphatase|\66:  JOURNAL   Biochem. Biophys. Res. Commun. 196 (1), 124-133 (1993)|  MEDLINE   94029983|\34:REFERENCE   24 (residues 1 to 593)|\70:  AUTHORS   Ahmad,S., Banville,D., Zhao,Z., Fischer,E.H. and Shen,S.H.|\76:  TITLE     A widely expressed human protein-tyrosine phosphatase containing|\34:            src homology 2 domains|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 90 (6), 2197-2201 (1993)|  MEDLINE   93211929|\34:REFERENCE   25 (residues 1 to 593)|\57:  AUTHORS   Vogel,W., Lammers,R., Huang,J. and Ullrich,A.|\67:  TITLE     Activation of a phosphotyrosine phosphatase by tyrosine|\27:            phosphorylation|\48:  JOURNAL   Science 259 (5101), 1611-1614 (1993)|  MEDLINE   93206095|\34:REFERENCE   26 (residues 1 to 593)|\76:  AUTHORS   Adachi,M., Sekiya,M., Miyachi,T., Matsuno,K., Hinoda,Y., Imai,K.|\24:            and Yachi,A.|\77:  TITLE     Molecular cloning of a novel protein-tyrosine phosphatase SH-PTP3|\65:            with sequence similarity to the src-homology region 2|\46:  JOURNAL   FEBS Lett. 314 (3), 335-339 (1992)|  MEDLINE   93106179|\34:REFERENCE   27 (residues 1 to 593)|\54:  AUTHORS   Freeman,R.M. Jr., Plutzky,J. and Neel,B.G.|\63:  TITLE     Identification of a human src homology 2-containing|\74:            protein-tyrosine-phosphatase: a putative homolog of Drosophila|\21:            corkscrew|\69:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 89 (23), 11239-11243 (1992)|  MEDLINE   93087502|\34:REFERENCE   28 (residues 1 to 593)|\78:  AUTHORS   Adachi,M., Sekiya,M., Arimura,Y., Takekawa,M., Itoh,F., Hinoda,Y.,|\32:            Imai,K. and Yachi,A.|\72:  TITLE     Protein-tyrosine phosphatase expression in pre-B cell NALM-6|\46:  JOURNAL   Cancer Res. 52 (3), 737-740 (1992)|  MEDLINE   92119637
end
obj|Object*|0
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obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
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obj|String*|4|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="12"|/map="12q24.1"
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obj|DBObj||Protein_1|||||0|0|\102:protein-tyrosine phosphatase 2C; Noonan syndrome 1; protein tyrosine phosphatase, non-receptor type 11
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obj|String*|3|\57:/product="protein tyrosine phosphatase, non-receptor type|11 isoform 1"|\21:/EC_number="3.1.3.48"
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obj|DBObj||Region_1|||||0|0|PTPc
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obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|1|\29:REFSEQ: accession NM_002834.2
end
obj|String*|51|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11|\53:VNTI URL:vnti:protein/hSHP2_D1+%28NP_002825%29+PTPN11
end
obj|String*|0
end
obj|String*|0
end
end|20DB368
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\26:hSTEP_D1 (NP_116170) PTPN5|||||302014800|0|\45:hypothetical protein FLJ14427 [Homo sapiens].
end|2|2|
obj|String*|0
end
obj|String*|4|\62:PREDICTED REFSEQ: The mRNA record is supported by experimental|\66:evidence; however, the coding sequence is predicted. The reference|\37:sequence was derived from AK090923.1.|\58:On Aug 5, 2002 this sequence version replaced gi:14249442.
end
obj|String*|12|REFERENCE   1|\68:  AUTHORS   Ninomiya,K., Wagatsuma,M., Kanda,K., Kondo,H., Yokoi,T.,|\78:            Kodaira,H., Furuya,T., Takahashi,M., Kikkawa,E., Omura,Y., Abe,K.,|\71:            Kamihara,K., Katsuta,N., Sato,K., Tanikawa,M., Yamazaki,M.,|\77:            Sugiyama,T., Irie,R., Otsuki,T., Sato,H., Wakamatsu,A., Ishii,S.,|\72:            Yamamoto,J., Isono,Y., Kawai-Hio,Y., Saito,K., Nishikawa,T.,|\71:            Kimura,K., Yamashita,H., Matsuo,K., Nakamura,Y., Sekine,M.,|\69:            Kikuchi,H., Murakawa,K., Kanehori,K., Takahashi-Fujii,A.,|\70:            Oshima,A., Sugiyama,A., Kawakami,B., Suzuki,Y., Sugano,S.,|\58:            Nagahari,K., Masuho,Y., Nagai,K. and Isogai,T.|\46:  TITLE     NEDO human cDNA sequencing project|\23:  JOURNAL   Unpublished
end
obj|Object*|0
end
obj|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
end
obj|CreatorData|\45:National Center for Biotechnology Information|\28:National Library of Medicine|\24:Building 38A, Room 8N805|\26:Bethesda, MD 20894, U.S.A.|\21:info@ncbi.nlm.nih.gov|(301)480-9241||NCBI Entrez|(301)496-2475|\36:http://www3.ncbi.nlm.nih.gov/Entrez/
end
end|1|0|276
obj|Object*|3
obj|Feature
obj|DBObj||Source_1|||||0|0|\25:cloning vector: pME18SFL3
end|269|269|||0|1|276|1|1|1|1|1..565
obj|String*|7|\24:/organism="Homo sapiens"|\21:/db_xref="taxon:9606"|/chromosome="11"|/map="11p15.1"|\21:/clone="BRAMY2015251"|\23:/tissue_type="amygdala"|/clone_lib="BRAMY2"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|276|1|1|1|1|1..565
obj|String*|1|\40:/product="hypothetical protein FLJ14427"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Region_1|||||0|0|PTPc
end|266|266|||0|18|274|1|1|1|1|299..555
obj|String*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
end|0||
obj|Object*|0
end
end
end|\276:srvlqaeelhekaldpfllqaeffeipmnfvdpkeydipglvrknryktilpnphsrvcltspdpddplssyinanyirgyggeekvyiatqgpivstvadfwrmvwqehtpiivmitnieemnekcteywpeeqvaydgveitvqkvihtedyrlrlislksgteerglkhywftswpdqktpdrappllhlvreveeaaqqegphcapiivhcsagigrtgcfiatsiccqqlrqegvvdilkttcqlrqdrggmiqtceqyqfvhhvmslyek|GenPept|
obj|String*|1|NP_116170
end||07-APR-2003|Homo sapiens (human)
obj|String*|0
end|0
obj|String*|0
end|PRT
obj|String*|0
end
obj|String*|1|Homo sapiens
end
obj|String*|0
end
obj|String*|0
end
obj|String*|12|Eukaryota|Metazoa|Chordata|Craniata|Vertebrata|Euteleostomi|Mammalia|Eutheria|Primates|Catarrhini|Hominidae|Homo
end
obj|Object*|0
end
obj|String*|0
end
obj|String*|0
end
obj|String*|1|\29:REFSEQ: accession NM_032781.2
end
obj|String*|45|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hSTEP_D1+%28NP_116170%29+PTPN5|\52:VNTI URL:vnti:protein/hST