|AlignmentProject
obj|Project|2
obj|MolList|2
obj|Object*|58
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characterization of the CD45 phosphatase cDNA in the owl|\35:            monkey Aotus vociferans|\23:  JOURNAL   Unpublished|\34:REFERENCE   2  (residues 1 to 365)|\56:  AUTHORS   Montoya,G.E., Vernot,J.P. and Patarroyo,M.E.|\29:  TITLE     Direct Submission|\75:  JOURNAL   Submitted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*|3|\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|3EC1258
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
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|308|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|308|1|1|1|1|528..1170
obj|String*|1|\21:/region_name="domain"
end|0||
obj|Object*|0
end
end
end|\308:selhsylnnlkrkdppsepslleakfqrlpsykgwrtqntgnreenknknrsantipydfnrvpirseeeqskegehdsedssdedsdceessryinasfitgywgpkamiatqgplqetisdfwqmvfqrkvkvivmltelkegdqelcaqywgegrqtyddievqvtdvnccpsytirafdvthlkrketqkvyqyqyhkwngldvpedpkdlvdmilslkqkvpsrpasedsrnsrsvpfvihccdgsqqtwcvlclmtllesaeteevidvfqvvkalrrsrlgvvstfeqyqflydtiartyp|GenPept|
obj|String*|1|A54080
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
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 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*|3|\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
end
obj|String*|0
end
obj|String*|0
end
end|3EA9018
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
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|\32:locus CHKPTPA accession L22437.1
end
obj|String*|8|\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
end
obj|String*|0
end
obj|String*|0
end
end|1FA8180
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"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||PTPRG|||||0|0|
end|270|270|||0|1|283|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.
end|203|203|||0|1|283|1|1|1|1|20..1422
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|283|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 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
end
end
end|\283:nqlhsyvnsilipgiggktrlekqfklvtqcnakyvecfsaqkdcnkeknrnssvvpserarvglaplpgmkgtdyinasyimgyyrsnenvitqhplphttkdfwrmiwdhnaqiivmlpdnqslaedefvywpsreesmnceaftvtliskdrlclsneeqiiihdfileatqddyvlevrhfqcpkwpnpdapisstfelinvikeealtrdgptivhdeygavsagtlcalttlsqqlenenavdvfqvakminlmrpgvftdieqyqflykamlslvs|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
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*|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
end
obj|String*|0
end
obj|String*|0
end
end|20BF0C8
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/
end
end|1|0|282
obj|Object*|6
obj|Feature
obj|DBObj||Source_1|||||0|0|
end|269|269|||0|1|282|1|1|1|1|1..1499
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|282|1|1|1|1|1..1499
obj|String*|2|\39:/product="protein-tyrosine-phosphatase"|\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|282|1|1|1|1|881..1499
obj|String*|1|\21:/region_name="domain"
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
end
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
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*|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*|8|\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
end
obj|String*|0
end
end|1F91C28
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\22:cPTPzeta_D2 (AAA49015)|||||302464822|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
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|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|2067728
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"
end|0||
obj|Object*|0
end
end
obj|Feature
obj|DBObj||Protein_1|||||0|0|
end|270|270|||0|1|302|1|1|1|1|1..1216
obj|String*|1|/product="CD45"
end|0||
obj|Object*|0
end
end
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
end|PRT
obj|String*|0
end
obj|String*|1|Cyprinus carpio
end
obj|String*|0
end
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*|3|\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
end
obj|String*|0
end
end|3E8A620
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*|3|\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
obj|String*|0
end
obj|String*|0
end
end|3F1AD18
end
obj|IxMolX
obj|Molecule
obj|BioObject
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].
end|2|2|
obj|String*|0
end
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
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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="1"|/map="1q31-q32"
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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
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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*|1|\29:REFSEQ: accession NM_002838.2
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obj|String*|18|\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|\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
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obj|DBObj||\25:hLAR_D2 (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*|1|\29:REFSEQ: accession NM_002840.2
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obj|String*|18|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC|\52:VNTI URL:vnti:protein/hCD45_D2+%28NP_002829%29+PTPRC
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obj|IxMolX
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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|
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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|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).
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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|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|\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*|3|\53:/region_name="Protein tyrosine phosphatase, catalytic|domain"|\25:/db_xref="CDD:smart00194"
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obj|String*|18|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE|\58:VNTI URL:vnti:protein/hPTPepsilon_D2+%28NP_006495%29+PTPRE
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obj|IxMolX
obj|Molecule
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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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end
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
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/
end
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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|Feature
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_002841.2
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obj|String*|18|\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|\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|\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
end
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end
end|FAD028
end
obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\30:hPTPkappa_D2 (NP_002835) PTPRK|||||302014800|0|\206:protein tyrosine phosphatase, receptor type, K precursor; protein-tyrosine phosphatase, receptor type, kappa; protein-tyrosine phosphatase kappa; protein-tyrosine phosphatase kappa 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 L77886.1 and BI755683.1.|\58:On Feb 22, 2002 this sequence version replaced gi:4506317.||\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 was|\63:shown to mediate homophilic intercellular interaction, possibly|\64:through the interaction with beta- and gamma-catenin at adherens|\64:junctions. Expression of this gene was found to be stimulated by|\56:TGF-beta 1, which may be important for the inhibition of|\27:keratinocyte proliferation.
end
obj|String*|34|\35:REFERENCE   1  (residues 1 to 1440)|\72:  AUTHORS   Yang,Y., Gil,M.C., Choi,E.Y., Park,S.H., Pyun,K.H. and Ha,H.|\74:  TITLE     Molecular cloning and chromosomal localization of a human gene|\73:            homologous to the murine R-PTP-kappa, a receptor-type protein|\32:            tyrosine phosphatase|\38:  JOURNAL   Gene 186 (1), 77-82 (1997)|  MEDLINE   97199372|\35:REFERENCE   2  (residues 1 to 1440)|\68:  AUTHORS   Yang,Y., Gil,M., Byun,S.M., Choi,I., Pyun,K.H. and Ha,H.|\72:  TITLE     Transforming growth factor-beta1 inhibits human keratinocyte|\69:            proliferation by upregulation of a receptor-type tyrosine|\51:            phosphatase R-PTP-kappa gene expression|\66:  JOURNAL   Biochem. Biophys. Res. Commun. 228 (3), 807-812 (1996)|  MEDLINE   97096334|\35:REFERENCE   3  (residues 1 to 1440)|\58:  AUTHORS   Fuchs,M., Muller,T., Lerch,M.M. and Ullrich,A.|\72:  TITLE     Association of human protein-tyrosine phosphatase kappa with|\43:            members of the armadillo family|\55:  JOURNAL   J. Biol. Chem. 271 (28), 16712-16719 (1996)|  MEDLINE   96279245|\35:REFERENCE   4  (residues 1 to 1440)|\77:  AUTHORS   Zondag,G.C., Koningstein,G.M., Jiang,Y.P., Sap,J., Moolenaar,W.H.|\28:            and Gebbink,M.F.|\78:  TITLE     Homophilic interactions mediated by receptor tyrosine phosphatases|\73:            mu and kappa. A critical role for the novel extracellular MAM|            domain|\55:  JOURNAL   J. Biol. Chem. 270 (24), 14247-14250 (1995)|  MEDLINE   95301498|\35:REFERENCE   5  (residues 1 to 1440)|\77:  AUTHORS   Sap,J., Jiang,Y.P., Friedlander,D., Grumet,M. and Schlessinger,J.|\73:  TITLE     Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic|            binding|\47:  JOURNAL   Mol. Cell. Biol. 14 (1), 1-9 (1994)|  MEDLINE   94088505
end
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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|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].
end|2|2|
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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).
end
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|CreatorData|||||\28:jannik@noergaardandersen.com|||Jannik N Andersen||\56:http://ptp.cshl.edu & http://science.novonordisk.com/ptp
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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].
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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.
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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
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obj|String*|18|\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|\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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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.
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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
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obj|String*|18|\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|\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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obj|IxMolX
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obj|DBObj||\30:hPTPsigma_D2 (NP_002841) PTPRS|||||302014800|0|\125:protein tyrosine phosphatase, receptor type, sigma isoform 1 precursor; protein tyrosine phosphatase PTPsigma [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 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
obj|String*|60|\35:REFERENCE   1  (residues 1 to 1948)|\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 1948)|\77:  AUTHORS   Wallace,M.J., Batt,J., Fladd,C.A., Henderson,J.T., Skarnes,W. and|            Rotin,D.|\79:  TITLE     Neuronal defects and posterior pituitary hypoplasia in mice lacking|\54:            the receptor tyrosine phosphatase PTPsigma|\46:  JOURNAL   Nat. Genet. 21 (3), 334-338 (1999)|  MEDLINE   99178277|\49:  REMARK    functional study of the mouse homolog|\35:REFERENCE   3  (residues 1 to 1948)|\77:  AUTHORS   Elchebly,M., Wagner,J., Kennedy,T.E., Lanctot,C., Michaliszyn,E.,|\48:            Itie,A., Drouin,J. and Tremblay,M.L.|\69:  TITLE     Neuroendocrine dysplasia in mice lacking protein tyrosine|\29:            phosphatase sigma|\46:  JOURNAL   Nat. Genet. 21 (3), 330-333 (1999)|  MEDLINE   99178276|\49:  REMARK    functional study of the mouse homolog|\35:REFERENCE   4  (residues 1 to 1948)|\68:  AUTHORS   Haworth,K., Shu,K.K., Stokes,A., Morris,R. and Stoker,A.|\77:  TITLE     The expression of receptor tyrosine phosphatases is responsive to|\31:            sciatic nerve crush|\54:  JOURNAL   Mol. Cell. Neurosci. 12 (3), 93-104 (1998)|  MEDLINE   99009170|\47:  REMARK    functional study of the rat homolog|\35:REFERENCE   5  (residues 1 to 1948)|\75:  AUTHORS   Wagner,J., Gordon,L.A., Heng,H.H., Tremblay,M.L. and Olsen,A.S.|\74:  TITLE     Physical mapping of receptor type protein tyrosine phosphatase|\53:            sigma (PTPRS) to human chromosome 19p13.3|\41:  JOURNAL   Genomics 38 (1), 76-78 (1996)|  MEDLINE   97124849|\35:REFERENCE   6  (residues 1 to 1948)|\71:  AUTHORS   Endo,N., Rutledge,S.J., Opas,E.E., Vogel,R., Rodan,G.A. and|\22:            Schmidt,A.|\78:  TITLE     Human protein tyrosine phosphatase-sigma: alternative splicing and|\41:            inhibition by bisphosphonates|\54:  JOURNAL   J. Bone Miner. Res. 11 (4), 535-543 (1996)|  MEDLINE   96255038|\35:REFERENCE   7  (residues 1 to 1948)|\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   8  (residues 1 to 1948)|\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
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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="19"|/map="19p13.3"
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obj|DBObj||Protein_1|||||0|0|\37:protein tyrosine phosphatase PTPsigma
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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*|1|\29:REFSEQ: accession NM_002850.2
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obj|String*|18|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS|\56:VNTI URL:vnti:protein/hPTPsigma_D2+%28NP_002841%29+PTPRS
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obj|IxMolX
obj|Molecule
obj|BioObject
obj|DBObj||\30:hPTPzeta_D2 (NP_002842) PTPRZ1|||||302014800|0|\187:protein tyrosine phosphatase, receptor-type, Z polypeptide 1; protein tyrosine phosphatase, receptor-type, zeta polypeptide 1; receptor-type tyrosine phosphatase beta/zeta [Homo sapiens].
end|2|2|
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obj|String*|2|\65:PROVISIONAL REFSEQ: This record has not yet been subject to final|\62:NCBI review. The reference sequence was derived from M93426.1.
end
obj|String*|69|\35:REFERENCE   1  (residues 1 to 2314)|\76:  AUTHORS   Harroch,S., Furtado,G.C., Brueck,W., Rosenbluth,J., Lafaille,J.,|\53:            Chao,M., Buxbaum,J.D. and Schlessinger,J.|\78:  TITLE     A critical role for the protein tyrosine phosphatase receptor type|\63:            Z in functional recovery from demyelinating lesions|\46:  JOURNAL   Nat. Genet. 32 (3), 411-414 (2002)|  MEDLINE   22297719|\73:  REMARK    GeneRIF: PTPRZ1 has a role in oligodendrocyte survival and in|\47:            recovery from demyelinating disease|\35:REFERENCE   2  (residues 1 to 2314)|\76:  AUTHORS   Thomaidou,D., Coquillat,D., Meintanis,S., Noda,M., Rougon,G. and|\21:            Matsas,R.|\73:  TITLE     Soluble forms of NCAM and F3 neuronal cell adhesion molecules|\78:            promote Schwann cell migration: identification of protein tyrosine|\74:            phosphatases zeta/beta as the putative F3 receptors on Schwann|            cells|\48:  JOURNAL   J. Neurochem. 78 (4), 767-778 (2001)|  MEDLINE   21412137|\35:REFERENCE   3  (residues 1 to 2314)|\57:  AUTHORS   Kawachi,H., Fujikawa,A., Maeda,N. and Noda,M.|\75:  TITLE     Identification of GIT1/Cat-1 as a substrate molecule of protein|\75:            tyrosine phosphatase zeta /beta by the yeast substrate-trapping|            system|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 98 (12), 6593-6598 (2001)|  MEDLINE   21287250|\35:REFERENCE   4  (residues 1 to 2314)|\79:  AUTHORS   Meng,K., Rodriguez-Pena,A., Dimitrov,T., Chen,W., Yamin,M., Noda,M.|\26:            and Deuel,T.F.|\75:  TITLE     Pleiotrophin signals increased tyrosine phosphorylation of beta|\72:            beta-catenin through inactivation of the intrinsic catalytic|\70:            activity of the receptor-type protein tyrosine phosphatase|\21:            beta/zeta|\66:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 97 (6), 2603-2608 (2000)|  MEDLINE   20183934|\35:REFERENCE   5  (residues 1 to 2314)|\73:  AUTHORS   Kawachi,H., Tamura,H., Watakabe,I., Shintani,T., Maeda,N. and|            Noda,M.|\69:  TITLE     Protein tyrosine phosphatase zeta/RPTPbeta interacts with|\31:            PSD-95/SAP90 family|\59:  JOURNAL   Brain Res. Mol. Brain Res. 72 (1), 47-54 (1999)|  MEDLINE   99453345|\35:REFERENCE   6  (residues 1 to 2314)|\75:  AUTHORS   Onyango,P., Lubyova,B., Gardellin,P., Kurzbauer,R. and Weith,A.|\76:  TITLE     Molecular cloning and expression analysis of five novel genes in|\27:            chromosome 1p36|\43:  JOURNAL   Genomics 50 (2), 187-198 (1998)|  MEDLINE   98317532|\35:REFERENCE   7  (residues 1 to 2314)|\71:  AUTHORS   Ariyama,T., Hasegawa,K., Inazawa,J., Mizuno,K., Ogimoto,M.,|\37:            Katagiri,T. and Yakura,H.|\65:  TITLE     Assignment of the human protein tyrosine phosphatase,|\70:            receptor-type, zeta (PTPRZ) gene to chromosome band 7q31.3|\57:  JOURNAL   Cytogenet. Cell Genet. 70 (1-2), 52-54 (1995)|  MEDLINE   95254878|\35:REFERENCE   8  (residues 1 to 2314)|\73:  AUTHORS   Levy,J.B., Canoll,P.D., Silvennoinen,O., Barnea,G., Morse,B.,|\78:            Honegger,A.M., Huang,J.T., Cannizzaro,L.A., Park,S.H., Druck,T. et|            al.|\71:  TITLE     The cloning of a receptor-type protein tyrosine phosphatase|\51:            expressed in the central nervous system|\55:  JOURNAL   J. Biol. Chem. 268 (14), 10573-10581 (1993)|  MEDLINE   93252948|\35:REFERENCE   9  (residues 1 to 2314)|\37:  AUTHORS   Krueger,N.X. and Saito,H.|\76:  TITLE     A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is|\79:            expressed in brain and has an N-terminal receptor domain homologous|\34:            to carbonic anhydrases|\67:  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 89 (16), 7417-7421 (1992)|  MEDLINE   92366472
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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_002851.1
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