PTPRB_HUMAN
ID PTPRB_HUMAN Reviewed; 1997 AA.
AC P23467; B7ZKS8; B7ZKT0; C9JX87; F5H3G6; Q14D85; Q3MIV7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase beta;
DE Short=Protein-tyrosine phosphatase beta;
DE Short=R-PTP-beta;
DE EC=3.1.3.48;
DE AltName: Full=Vascular endothelial protein tyrosine phosphatase;
DE Short=VE-PTP;
DE Flags: Precursor;
GN Name=PTPRB; Synonyms=PTPB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-94 AND GLY-127.
RC TISSUE=Placenta;
RX PubMed=2170109; DOI=10.1002/j.1460-2075.1990.tb07523.x;
RA Krueger N.X., Streuli M., Saito H.;
RT "Structural diversity and evolution of human receptor-like protein tyrosine
RT phosphatases.";
RL EMBO J. 9:3241-3252(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND VARIANT
RP LYS-94.
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=19116766; DOI=10.1007/s10456-008-9126-0;
RA Yacyshyn O.K., Lai P.F.H., Forse K., Teichert-Kuliszewska K., Jurasz P.,
RA Stewart D.J.;
RT "Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in human
RT endothelial cells.";
RL Angiogenesis 12:25-33(2009).
RN [8]
RP FUNCTION.
RX PubMed=19136612; DOI=10.1096/fj.08-123810;
RA Mellberg S., Dimberg A., Bahram F., Hayashi M., Rennel E., Ameur A.,
RA Westholm J.O., Larsson E., Lindahl P., Cross M.J., Claesson-Welsh L.;
RT "Transcriptional profiling reveals a critical role for tyrosine phosphatase
RT VE-PTP in regulation of VEGFR2 activity and endothelial cell
RT morphogenesis.";
RL FASEB J. 23:1490-1502(2009).
RN [9]
RP INTERACTION WITH TEK.
RX PubMed=19451274; DOI=10.1083/jcb.200811159;
RA Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F.,
RA Deutsch U., Nottebaum A.F., Vestweber D.;
RT "VE-PTP controls blood vessel development by balancing Tie-2 activity.";
RL J. Cell Biol. 185:657-671(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1676-1965 IN COMPLEX WITH
RP INHIBITOR SULFAMIC ACID, SUBUNIT, AND ACTIVE SITE.
RX PubMed=17139078; DOI=10.1107/s0907444906037784;
RA Evdokimov A.G., Pokross M., Walter R., Mekel M., Cox B., Li C., Bechard R.,
RA Genbauffe F., Andrews R., Diven C., Howard B., Rastogi V., Gray J.,
RA Maier M., Peters K.G.;
RT "Engineering the catalytic domain of human protein tyrosine phosphatase
RT beta for structure-based drug discovery.";
RL Acta Crystallogr. D 62:1435-1445(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1662-1973 IN COMPLEX WITH
RP INHIBITOR SULFAMIC ACID.
RX PubMed=16759857; DOI=10.1016/j.bmcl.2006.05.074;
RA Amarasinghe K.K.D., Evdokimov A.G., Xu K., Clark C.M., Maier M.B.,
RA Srivastava A., Colson A.-O., Gerwe G.S., Stake G.E., Howard B.W.,
RA Pokross M.E., Gray J.L., Peters K.G.;
RT "Design and synthesis of potent, non-peptidic inhibitors of HPTPbeta.";
RL Bioorg. Med. Chem. Lett. 16:4252-4256(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1686-1971.
RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT "Large-scale structural analysis of the classical human protein tyrosine
RT phosphatome.";
RL Cell 136:352-363(2009).
CC -!- FUNCTION: Plays an important role in blood vessel remodeling and
CC angiogenesis. Not necessary for the initial formation of blood vessels,
CC but is essential for their maintenance and remodeling. Can induce
CC dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2.
CC Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a
CC negative regulator of TIE2, and controls TIE2 driven endothelial cell
CC proliferation, which in turn affects blood vessel remodeling during
CC embryonic development and determines blood vessel size during perinatal
CC growth. Essential for the maintenance of endothelial cell contact
CC integrity and for the adhesive function of VE-cadherin in endothelial
CC cells and this requires the presence of plakoglobin (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:19116766,
CC ECO:0000269|PubMed:19136612}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Monomer. Interacts with TEK (PubMed:19451274). Interacts via
CC fibronectin type-III 17 domain with CDH5. Detected in a complex with
CC CNTN1 and NRCAM (By similarity). Interacts (phosphorylated form) with
CC FYN and GRB2 (By similarity). {ECO:0000250|UniProtKB:B2RU80,
CC ECO:0000269|PubMed:19451274}.
CC -!- INTERACTION:
CC P23467; P00533: EGFR; NbExp=3; IntAct=EBI-1265766, EBI-297353;
CC P23467; P04626: ERBB2; NbExp=2; IntAct=EBI-1265766, EBI-641062;
CC P23467; P10912: GHR; NbExp=3; IntAct=EBI-1265766, EBI-286316;
CC P23467; P27361: MAPK3; NbExp=2; IntAct=EBI-1265766, EBI-73995;
CC P23467; P08581: MET; NbExp=2; IntAct=EBI-1265766, EBI-1039152;
CC P23467; Q02763: TEK; NbExp=3; IntAct=EBI-1265766, EBI-2257090;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P23467-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23467-2; Sequence=VSP_038521;
CC Name=3;
CC IsoId=P23467-3; Sequence=VSP_040484;
CC Name=4;
CC IsoId=P23467-4; Sequence=VSP_053944;
CC -!- INDUCTION: Up-regulated by hypoxia. {ECO:0000269|PubMed:19116766}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54131; CAA38066.1; -; mRNA.
DR EMBL; BX648245; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC025569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97254.1; -; Genomic_DNA.
DR EMBL; BC101679; AAI01680.1; -; mRNA.
DR EMBL; BC113463; AAI13464.1; -; mRNA.
DR EMBL; BC143356; AAI43357.1; -; mRNA.
DR EMBL; BC143360; AAI43361.1; -; mRNA.
DR CCDS; CCDS44943.1; -. [P23467-3]
DR CCDS; CCDS44944.1; -. [P23467-1]
DR CCDS; CCDS55845.1; -. [P23467-2]
DR CCDS; CCDS55846.1; -. [P23467-4]
DR PIR; S12050; S12050.
DR RefSeq; NP_001103224.1; NM_001109754.3. [P23467-3]
DR RefSeq; NP_001193900.1; NM_001206971.2. [P23467-2]
DR RefSeq; NP_001193901.1; NM_001206972.2. [P23467-4]
DR RefSeq; NP_001317133.1; NM_001330204.1.
DR RefSeq; NP_002828.3; NM_002837.5. [P23467-1]
DR PDB; 2AHS; X-ray; 2.10 A; A/B=1686-1971.
DR PDB; 2H02; X-ray; 2.30 A; A/B=1662-1973.
DR PDB; 2H03; X-ray; 1.65 A; A=1676-1970.
DR PDB; 2H04; X-ray; 2.30 A; A=1662-1973.
DR PDB; 2HC1; X-ray; 1.30 A; A=1676-1970.
DR PDB; 2HC2; X-ray; 1.40 A; A=1676-1970.
DR PDB; 2I3R; X-ray; 1.85 A; A/B=1662-1973.
DR PDB; 2I3U; X-ray; 1.85 A; A=1662-1973.
DR PDB; 2I4E; X-ray; 1.75 A; A/B=1662-1973.
DR PDB; 2I4G; X-ray; 1.65 A; A=1662-1973.
DR PDB; 2I4H; X-ray; 2.15 A; A=1662-1973.
DR PDB; 2I5X; X-ray; 1.70 A; A/B=1662-1973.
DR PDBsum; 2AHS; -.
DR PDBsum; 2H02; -.
DR PDBsum; 2H03; -.
DR PDBsum; 2H04; -.
DR PDBsum; 2HC1; -.
DR PDBsum; 2HC2; -.
DR PDBsum; 2I3R; -.
DR PDBsum; 2I3U; -.
DR PDBsum; 2I4E; -.
DR PDBsum; 2I4G; -.
DR PDBsum; 2I4H; -.
DR PDBsum; 2I5X; -.
DR AlphaFoldDB; P23467; -.
DR SMR; P23467; -.
DR BioGRID; 111751; 29.
DR CORUM; P23467; -.
DR IntAct; P23467; 38.
DR MINT; P23467; -.
DR STRING; 9606.ENSP00000334928; -.
DR BindingDB; P23467; -.
DR ChEMBL; CHEMBL2706; -.
DR DrugBank; DB08678; (4-ETHYLPHENYL)SULFAMIC ACID.
DR DrugBank; DB07068; (4-{4-[(TERT-BUTOXYCARBONYL)AMINO]-2,2-BIS(ETHOXYCARBONYL)BUTYL}PHENYL)SULFAMIC ACID.
DR DrugBank; DB16353; Razuprotafib.
DR DrugBank; DB07127; {4-[2,2-BIS(5-METHYL-1,2,4-OXADIAZOL-3-YL)-3-PHENYLPROPYL]PHENYL}SULFAMIC ACID.
DR DrugBank; DB06989; {4-[2-BENZYL-3-METHOXY-2-(METHOXYCARBONYL)-3-OXOPROPYL]PHENYL}SULFAMIC ACID.
DR GuidetoPHARMACOLOGY; 1851; -.
DR DEPOD; PTPRB; -.
DR GlyGen; P23467; 26 sites.
DR iPTMnet; P23467; -.
DR PhosphoSitePlus; P23467; -.
DR BioMuta; PTPRB; -.
DR DMDM; 317373518; -.
DR EPD; P23467; -.
DR jPOST; P23467; -.
DR MassIVE; P23467; -.
DR MaxQB; P23467; -.
DR PaxDb; P23467; -.
DR PeptideAtlas; P23467; -.
DR PRIDE; P23467; -.
DR ProteomicsDB; 26267; -.
DR ProteomicsDB; 54098; -. [P23467-1]
DR ProteomicsDB; 54099; -. [P23467-2]
DR ProteomicsDB; 54100; -. [P23467-3]
DR Antibodypedia; 29475; 104 antibodies from 24 providers.
DR DNASU; 5787; -.
DR Ensembl; ENST00000261266.9; ENSP00000261266.5; ENSG00000127329.16. [P23467-1]
DR Ensembl; ENST00000334414.11; ENSP00000334928.6; ENSG00000127329.16. [P23467-3]
DR Ensembl; ENST00000538708.5; ENSP00000438927.1; ENSG00000127329.16. [P23467-4]
DR Ensembl; ENST00000550857.5; ENSP00000447302.1; ENSG00000127329.16. [P23467-2]
DR GeneID; 5787; -.
DR KEGG; hsa:5787; -.
DR MANE-Select; ENST00000334414.11; ENSP00000334928.6; NM_001109754.4; NP_001103224.1. [P23467-3]
DR UCSC; uc001swb.6; human. [P23467-1]
DR CTD; 5787; -.
DR DisGeNET; 5787; -.
DR GeneCards; PTPRB; -.
DR HGNC; HGNC:9665; PTPRB.
DR HPA; ENSG00000127329; Low tissue specificity.
DR MIM; 176882; gene.
DR neXtProt; NX_P23467; -.
DR OpenTargets; ENSG00000127329; -.
DR PharmGKB; PA34010; -.
DR VEuPathDB; HostDB:ENSG00000127329; -.
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000156088; -.
DR HOGENOM; CLU_000787_0_0_1; -.
DR InParanoid; P23467; -.
DR OMA; SATWEFP; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P23467; -.
DR TreeFam; TF351926; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P23467; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P23467; -.
DR SIGNOR; P23467; -.
DR BioGRID-ORCS; 5787; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; PTPRB; human.
DR EvolutionaryTrace; P23467; -.
DR GeneWiki; PTPRB; -.
DR GenomeRNAi; 5787; -.
DR Pharos; P23467; Tchem.
DR PRO; PR:P23467; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P23467; protein.
DR Bgee; ENSG00000127329; Expressed in endothelial cell and 181 other tissues.
DR ExpressionAtlas; P23467; baseline and differential.
DR Genevisible; P23467; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; IPI:ARUK-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0008347; P:glial cell migration; IEA:Ensembl.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
DR CDD; cd00063; FN3; 14.
DR Gene3D; 2.60.40.10; -; 15.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041201; PTPRJ_TM.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 15.
DR Pfam; PF18861; PTP_tm; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 17.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 16.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 12.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Glycoprotein; Hydrolase;
KW Membrane; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1997
FT /note="Receptor-type tyrosine-protein phosphatase beta"
FT /id="PRO_0000025436"
FT TOPO_DOM 23..1621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1622..1642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1643..1997
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..111
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 112..207
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 203..288
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 291..378
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 379..471
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 467..552
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 556..641
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 642..729
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 730..829
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 819..906
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 909..1001
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 995..1083
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1087..1175
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1173..1260
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1260..1356
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1357..1448
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1458..1554
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1703..1963
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1904
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044,
FT ECO:0000269|PubMed:17139078"
FT BINDING 1870
FT /ligand="substrate"
FT BINDING 1904..1910
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1948
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1981
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:B2RU80"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1096
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..18
FT /note="MLSHGAGLALWITLSLLQ -> MEAEFYMVILTCLIFRNSEGFQIVHVQKQQ
FT CLFKNEKVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSRGPSRSAILDRCSQ
FT APRWTCYDQEGFLEVENASLFLQKQGSRVVVKKARKYLHSWMKIDVNKEGKLVNESLCL
FT QKAGLGAEVSVRSTRNTAPPQILTTFNAVPDGLVFLIRNTTEAFIRNAAENYSQNSSER
FT QHPNLHMTGITDTSWVLSTTQPFSSTTEE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040484"
FT VAR_SEQ 377..466
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038521"
FT VAR_SEQ 997..1086
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053944"
FT VARIANT 94
FT /note="R -> K (in dbSNP:rs2252784)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2170109"
FT /id="VAR_062251"
FT VARIANT 127
FT /note="S -> G (in dbSNP:rs2465811)"
FT /evidence="ECO:0000269|PubMed:2170109"
FT /id="VAR_062252"
FT VARIANT 395
FT /note="V -> A (in dbSNP:rs36027530)"
FT /id="VAR_057135"
FT VARIANT 415
FT /note="D -> E (in dbSNP:rs2165627)"
FT /id="VAR_057136"
FT VARIANT 939
FT /note="T -> M (in dbSNP:rs2304821)"
FT /id="VAR_057137"
FT VARIANT 1032
FT /note="T -> I (in dbSNP:rs34902691)"
FT /id="VAR_057138"
FT VARIANT 1934
FT /note="G -> A (in dbSNP:rs17226367)"
FT /id="VAR_057139"
FT CONFLICT 261
FT /note="T -> S (in Ref. 1; CAA38066)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="L -> V (in Ref. 1; CAA38066)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="V -> A (in Ref. 2; BX648245)"
FT /evidence="ECO:0000305"
FT CONFLICT 1559
FT /note="C -> R (in Ref. 1; CAA38066)"
FT /evidence="ECO:0000305"
FT HELIX 1685..1687
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1688..1709
FT /evidence="ECO:0007829|PDB:2HC1"
FT TURN 1710..1716
FT /evidence="ECO:0007829|PDB:2HC1"
FT TURN 1720..1723
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1728..1730
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1740..1742
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1743..1745
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1753..1756
FT /evidence="ECO:0007829|PDB:2AHS"
FT STRAND 1757..1763
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1766..1769
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1771..1775
FT /evidence="ECO:0007829|PDB:2HC1"
FT TURN 1780..1782
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1783..1792
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1797..1800
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1804..1806
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1818..1821
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1823..1825
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1828..1837
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1839..1849
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1856..1865
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1870..1872
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1877..1893
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1894..1896
FT /evidence="ECO:0007829|PDB:2H03"
FT STRAND 1900..1903
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1905..1908
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1909..1926
FT /evidence="ECO:0007829|PDB:2HC1"
FT STRAND 1928..1930
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1932..1940
FT /evidence="ECO:0007829|PDB:2HC1"
FT HELIX 1950..1968
FT /evidence="ECO:0007829|PDB:2HC1"
SQ SEQUENCE 1997 AA; 224301 MW; 76E67B4A6109AA0F CRC64;
MLSHGAGLAL WITLSLLQTG LAEPERCNFT LAESKASSHS VSIQWRILGS PCNFSLIYSS
DTLGAALCPT FRIDNTTYGC NLQDLQAGTI YNFRIISLDE ERTVVLQTDP LPPARFGVSK
EKTTSTSLHV WWTPSSGKVT SYEVQLFDEN NQKIQGVQIQ ESTSWNEYTF FNLTAGSKYN
IAITAVSGGK RSFSVYTNGS TVPSPVKDIG ISTKANSLLI SWSHGSGNVE RYRLMLMDKG
ILVHGGVVDK HATSYAFHGL TPGYLYNLTV MTEAAGLQNY RWKLVRTAPM EVSNLKVTND
GSLTSLKVKW QRPPGNVDSY NITLSHKGTI KESRVLAPWI TETHFKELVP GRLYQVTVSC
VSGELSAQKM AVGRTFPDKV ANLEANNNGR MRSLVVSWSP PAGDWEQYRI LLFNDSVVLL
NITVGKEETQ YVMDDTGLVP GRQYEVEVIV ESGNLKNSER CQGRTVPLAV LQLRVKHANE
TSLSIMWQTP VAEWEKYIIS LADRDLLLIH KSLSKDAKEF TFTDLVPGRK YMATVTSISG
DLKNSSSVKG RTVPAQVTDL HVANQGMTSS LFTNWTQAQG DVEFYQVLLI HENVVIKNES
ISSETSRYSF HSLKSGSLYS VVVTTVSGGI SSRQVVVEGR TVPSSVSGVT VNNSGRNDYL
SVSWLLAPGD VDNYEVTLSH DGKVVQSLVI AKSVRECSFS SLTPGRLYTV TITTRSGKYE
NHSFSQERTV PDKVQGVSVS NSARSDYLRV SWVHATGDFD HYEVTIKNKN NFIQTKSIPK
SENECVFVQL VPGRLYSVTV TTKSGQYEAN EQGNGRTIPE PVKDLTLRNR STEDLHVTWS
GANGDVDQYE IQLLFNDMKV FPPFHLVNTA TEYRFTSLTP GRQYKILVLT ISGDVQQSAF
IEGFTVPSAV KNIHISPNGA TDSLTVNWTP GGGDVDSYTV SAFRHSQKVD SQTIPKHVFE
HTFHRLEAGE QYQIMIASVS GSLKNQINVV GRTVPASVQG VIADNAYSSY SLIVSWQKAA
GVAERYDILL LTENGILLRN TSEPATTKQH KFEDLTPGKK YKIQILTVSG GLFSKEAQTE
GRTVPAAVTD LRITENSTRH LSFRWTASEG ELSWYNIFLY NPDGNLQERA QVDPLVQSFS
FQNLLQGRMY KMVIVTHSGE LSNESFIFGR TVPASVSHLR GSNRNTTDSL WFNWSPASGD
FDFYELILYN PNGTKKENWK DKDLTEWRFQ GLVPGRKYVL WVVTHSGDLS NKVTAESRTA
PSPPSLMSFA DIANTSLAIT WKGPPDWTDY NDFELQWLPR DALTVFNPYN NRKSEGRIVY
GLRPGRSYQF NVKTVSGDSW KTYSKPIFGS VRTKPDKIQN LHCRPQNSTA IACSWIPPDS
DFDGYSIECR KMDTQEVEFS RKLEKEKSLL NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS
TITMIDRPPP PPPHIRVNEK DVLISKSSIN FTVNCSWFSD TNGAVKYFTV VVREADGSDE
LKPEQQHPLP SYLEYRHNAS IRVYQTNYFA SKCAENPNSN SKSFNIKLGA EMESLGGKCD
PTQQKFCDGP LKPHTAYRIS IRAFTQLFDE DLKEFTKPLY SDTFFSLPIT TESEPLFGAI
EGVSAGLFLI GMLVAVVALL ICRQKVSHGR ERPSARLSIR RDRPLSVHLN LGQKGNRKTS
CPIKINQFEG HFMKLQADSN YLLSKEYEEL KDVGRNQSCD IALLPENRGK NRYNNILPYD
ATRVKLSNVD DDPCSDYINA SYIPGNNFRR EYIVTQGPLP GTKDDFWKMV WEQNVHNIVM
VTQCVEKGRV KCDHYWPADQ DSLYYGDLIL QMLSESVLPE WTIREFKICG EEQLDAHRLI
RHFHYTVWPD HGVPETTQSL IQFVRTVRDY INRSPGAGPT VVHCSAGVGR TGTFIALDRI
LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE CQYVYLHQCV RDVLRARKLR SEQENPLFPI
YENVNPEYHR DPVYSRH
