Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23467 (PTPRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase beta

Short name=Protein-tyrosine phosphatase beta
Short name=R-PTP-beta
EC=3.1.3.48
Alternative name(s):
Vascular endothelial protein tyrosine phosphatase
Short name=VE-PTP
Gene names
Name:PTPRB
Synonyms:PTPB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1997 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin By similarity. Ref.7 Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Monomer. Interacts with TEK. Interacts via fibronectin type-III 17 domain with CDH5 By similarity. Ref.9 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Induction

Up-regulated by hypoxia. Ref.7

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.

Contains 17 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23467-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P23467-2)

The sequence of this isoform differs from the canonical sequence as follows:
     377-466: Missing.
Isoform 3 (identifier: P23467-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MLSHGAGLALWITLSLLQ → MEAEFYMVIL...TQPFSSTTEE
Isoform 4 (identifier: P23467-4)

The sequence of this isoform differs from the canonical sequence as follows:
     997-1086: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 19971975Receptor-type tyrosine-protein phosphatase beta
PRO_0000025436

Regions

Topological domain23 – 16211599Extracellular Potential
Transmembrane1622 – 164221Helical; Potential
Topological domain1643 – 1997355Cytoplasmic Potential
Domain23 – 11189Fibronectin type-III 1
Domain112 – 20796Fibronectin type-III 2
Domain203 – 28886Fibronectin type-III 3
Domain291 – 37888Fibronectin type-III 4
Domain379 – 47193Fibronectin type-III 5
Domain467 – 55286Fibronectin type-III 6
Domain556 – 64186Fibronectin type-III 7
Domain642 – 72988Fibronectin type-III 8
Domain730 – 829100Fibronectin type-III 9
Domain819 – 90688Fibronectin type-III 10
Domain909 – 100193Fibronectin type-III 11
Domain995 – 108389Fibronectin type-III 12
Domain1087 – 117589Fibronectin type-III 13
Domain1173 – 126088Fibronectin type-III 14
Domain1260 – 135697Fibronectin type-III 15
Domain1357 – 144892Fibronectin type-III 16
Domain1458 – 155497Fibronectin type-III 17
Domain1703 – 1963261Tyrosine-protein phosphatase
Region1904 – 19107Substrate binding By similarity

Sites

Active site19041Phosphocysteine intermediate Ref.10
Binding site18701Substrate
Binding site19481Substrate By similarity

Amino acid modifications

Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation5981N-linked (GlcNAc...) Potential
Glycosylation6521N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential
Glycosylation8291N-linked (GlcNAc...) Potential
Glycosylation10401N-linked (GlcNAc...) Potential
Glycosylation10961N-linked (GlcNAc...) Potential
Glycosylation11631N-linked (GlcNAc...) Potential
Glycosylation11851N-linked (GlcNAc...) Potential
Glycosylation12121N-linked (GlcNAc...) Potential
Glycosylation12741N-linked (GlcNAc...) Potential
Glycosylation13671N-linked (GlcNAc...) Potential
Glycosylation14701N-linked (GlcNAc...) Potential
Glycosylation14741N-linked (GlcNAc...) Potential
Glycosylation15181N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 1818MLSHG…LSLLQ → MEAEFYMVILTCLIFRNSEG FQIVHVQKQQCLFKNEKVVV GSCNRTIQNQQWMWTEDEKL LHVKSALCLAISNSSRGPSR SAILDRCSQAPRWTCYDQEG FLEVENASLFLQKQGSRVVV KKARKYLHSWMKIDVNKEGK LVNESLCLQKAGLGAEVSVR STRNTAPPQILTTFNAVPDG LVFLIRNTTEAFIRNAAENY SQNSSERQHPNLHMTGITDT SWVLSTTQPFSSTTEE in isoform 3.
VSP_040484
Alternative sequence377 – 46690Missing in isoform 2.
VSP_038521
Alternative sequence997 – 108690Missing in isoform 4.
VSP_053944
Natural variant941R → K. Ref.1 Ref.5
Corresponds to variant rs2252784 [ dbSNP | Ensembl ].
VAR_062251
Natural variant1271S → G. Ref.1
Corresponds to variant rs2465811 [ dbSNP | Ensembl ].
VAR_062252
Natural variant3951V → A.
Corresponds to variant rs36027530 [ dbSNP | Ensembl ].
VAR_057135
Natural variant4151D → E.
Corresponds to variant rs2165627 [ dbSNP | Ensembl ].
VAR_057136
Natural variant9391T → M.
Corresponds to variant rs2304821 [ dbSNP | Ensembl ].
VAR_057137
Natural variant10321T → I.
Corresponds to variant rs34902691 [ dbSNP | Ensembl ].
VAR_057138
Natural variant19341G → A.
Corresponds to variant rs17226367 [ dbSNP | Ensembl ].
VAR_057139

Experimental info

Sequence conflict2611T → S in CAA38066. Ref.1
Sequence conflict6661L → V in CAA38066. Ref.1
Sequence conflict9261V → A in BX648245. Ref.2
Sequence conflict15591C → R in CAA38066. Ref.1

Secondary structure

.................................................... 1997
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 76E67B4A6109AA0F

FASTA1,997224,301
        10         20         30         40         50         60 
MLSHGAGLAL WITLSLLQTG LAEPERCNFT LAESKASSHS VSIQWRILGS PCNFSLIYSS 

        70         80         90        100        110        120 
DTLGAALCPT FRIDNTTYGC NLQDLQAGTI YNFRIISLDE ERTVVLQTDP LPPARFGVSK 

       130        140        150        160        170        180 
EKTTSTSLHV WWTPSSGKVT SYEVQLFDEN NQKIQGVQIQ ESTSWNEYTF FNLTAGSKYN 

       190        200        210        220        230        240 
IAITAVSGGK RSFSVYTNGS TVPSPVKDIG ISTKANSLLI SWSHGSGNVE RYRLMLMDKG 

       250        260        270        280        290        300 
ILVHGGVVDK HATSYAFHGL TPGYLYNLTV MTEAAGLQNY RWKLVRTAPM EVSNLKVTND 

       310        320        330        340        350        360 
GSLTSLKVKW QRPPGNVDSY NITLSHKGTI KESRVLAPWI TETHFKELVP GRLYQVTVSC 

       370        380        390        400        410        420 
VSGELSAQKM AVGRTFPDKV ANLEANNNGR MRSLVVSWSP PAGDWEQYRI LLFNDSVVLL 

       430        440        450        460        470        480 
NITVGKEETQ YVMDDTGLVP GRQYEVEVIV ESGNLKNSER CQGRTVPLAV LQLRVKHANE 

       490        500        510        520        530        540 
TSLSIMWQTP VAEWEKYIIS LADRDLLLIH KSLSKDAKEF TFTDLVPGRK YMATVTSISG 

       550        560        570        580        590        600 
DLKNSSSVKG RTVPAQVTDL HVANQGMTSS LFTNWTQAQG DVEFYQVLLI HENVVIKNES 

       610        620        630        640        650        660 
ISSETSRYSF HSLKSGSLYS VVVTTVSGGI SSRQVVVEGR TVPSSVSGVT VNNSGRNDYL 

       670        680        690        700        710        720 
SVSWLLAPGD VDNYEVTLSH DGKVVQSLVI AKSVRECSFS SLTPGRLYTV TITTRSGKYE 

       730        740        750        760        770        780 
NHSFSQERTV PDKVQGVSVS NSARSDYLRV SWVHATGDFD HYEVTIKNKN NFIQTKSIPK 

       790        800        810        820        830        840 
SENECVFVQL VPGRLYSVTV TTKSGQYEAN EQGNGRTIPE PVKDLTLRNR STEDLHVTWS 

       850        860        870        880        890        900 
GANGDVDQYE IQLLFNDMKV FPPFHLVNTA TEYRFTSLTP GRQYKILVLT ISGDVQQSAF 

       910        920        930        940        950        960 
IEGFTVPSAV KNIHISPNGA TDSLTVNWTP GGGDVDSYTV SAFRHSQKVD SQTIPKHVFE 

       970        980        990       1000       1010       1020 
HTFHRLEAGE QYQIMIASVS GSLKNQINVV GRTVPASVQG VIADNAYSSY SLIVSWQKAA 

      1030       1040       1050       1060       1070       1080 
GVAERYDILL LTENGILLRN TSEPATTKQH KFEDLTPGKK YKIQILTVSG GLFSKEAQTE 

      1090       1100       1110       1120       1130       1140 
GRTVPAAVTD LRITENSTRH LSFRWTASEG ELSWYNIFLY NPDGNLQERA QVDPLVQSFS 

      1150       1160       1170       1180       1190       1200 
FQNLLQGRMY KMVIVTHSGE LSNESFIFGR TVPASVSHLR GSNRNTTDSL WFNWSPASGD 

      1210       1220       1230       1240       1250       1260 
FDFYELILYN PNGTKKENWK DKDLTEWRFQ GLVPGRKYVL WVVTHSGDLS NKVTAESRTA 

      1270       1280       1290       1300       1310       1320 
PSPPSLMSFA DIANTSLAIT WKGPPDWTDY NDFELQWLPR DALTVFNPYN NRKSEGRIVY 

      1330       1340       1350       1360       1370       1380 
GLRPGRSYQF NVKTVSGDSW KTYSKPIFGS VRTKPDKIQN LHCRPQNSTA IACSWIPPDS 

      1390       1400       1410       1420       1430       1440 
DFDGYSIECR KMDTQEVEFS RKLEKEKSLL NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS 

      1450       1460       1470       1480       1490       1500 
TITMIDRPPP PPPHIRVNEK DVLISKSSIN FTVNCSWFSD TNGAVKYFTV VVREADGSDE 

      1510       1520       1530       1540       1550       1560 
LKPEQQHPLP SYLEYRHNAS IRVYQTNYFA SKCAENPNSN SKSFNIKLGA EMESLGGKCD 

      1570       1580       1590       1600       1610       1620 
PTQQKFCDGP LKPHTAYRIS IRAFTQLFDE DLKEFTKPLY SDTFFSLPIT TESEPLFGAI 

      1630       1640       1650       1660       1670       1680 
EGVSAGLFLI GMLVAVVALL ICRQKVSHGR ERPSARLSIR RDRPLSVHLN LGQKGNRKTS 

      1690       1700       1710       1720       1730       1740 
CPIKINQFEG HFMKLQADSN YLLSKEYEEL KDVGRNQSCD IALLPENRGK NRYNNILPYD 

      1750       1760       1770       1780       1790       1800 
ATRVKLSNVD DDPCSDYINA SYIPGNNFRR EYIVTQGPLP GTKDDFWKMV WEQNVHNIVM 

      1810       1820       1830       1840       1850       1860 
VTQCVEKGRV KCDHYWPADQ DSLYYGDLIL QMLSESVLPE WTIREFKICG EEQLDAHRLI 

      1870       1880       1890       1900       1910       1920 
RHFHYTVWPD HGVPETTQSL IQFVRTVRDY INRSPGAGPT VVHCSAGVGR TGTFIALDRI 

      1930       1940       1950       1960       1970       1980 
LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE CQYVYLHQCV RDVLRARKLR SEQENPLFPI 

      1990 
YENVNPEYHR DPVYSRH 

« Hide

Isoform 2 [UniParc].

Checksum: C8A61E610D7ECC31
Show »

FASTA1,907214,209
Isoform 3 [UniParc].

Checksum: 605BB45BA4541F02
Show »

FASTA2,215249,143
Isoform 4 [UniParc].

Checksum: 237BC55F05D696E7
Show »

FASTA1,907214,505

References

« Hide 'large scale' references
[1]"Structural diversity and evolution of human receptor-like protein tyrosine phosphatases."
Krueger N.X., Streuli M., Saito H.
EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LYS-94 AND GLY-127.
Tissue: Placenta.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Fetal kidney.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), VARIANT LYS-94.
Tissue: Colon.
[6]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in human endothelial cells."
Yacyshyn O.K., Lai P.F.H., Forse K., Teichert-Kuliszewska K., Jurasz P., Stewart D.J.
Angiogenesis 12:25-33(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[8]"Transcriptional profiling reveals a critical role for tyrosine phosphatase VE-PTP in regulation of VEGFR2 activity and endothelial cell morphogenesis."
Mellberg S., Dimberg A., Bahram F., Hayashi M., Rennel E., Ameur A., Westholm J.O., Larsson E., Lindahl P., Cross M.J., Claesson-Welsh L.
FASEB J. 23:1490-1502(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"VE-PTP controls blood vessel development by balancing Tie-2 activity."
Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F., Deutsch U., Nottebaum A.F., Vestweber D.
J. Cell Biol. 185:657-671(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TEK.
[10]"Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery."
Evdokimov A.G., Pokross M., Walter R., Mekel M., Cox B., Li C., Bechard R., Genbauffe F., Andrews R., Diven C., Howard B., Rastogi V., Gray J., Maier M., Peters K.G.
Acta Crystallogr. D 62:1435-1445(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1676-1965 IN COMPLEX WITH INHIBITOR SULFAMIC ACID, SUBUNIT, ACTIVE SITE.
[11]"Design and synthesis of potent, non-peptidic inhibitors of HPTPbeta."
Amarasinghe K.K.D., Evdokimov A.G., Xu K., Clark C.M., Maier M.B., Srivastava A., Colson A.-O., Gerwe G.S., Stake G.E., Howard B.W., Pokross M.E., Gray J.L., Peters K.G.
Bioorg. Med. Chem. Lett. 16:4252-4256(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1662-1973 IN COMPLEX WITH INHIBITOR SULFAMIC ACID.
[12]"Large-scale structural analysis of the classical human protein tyrosine phosphatome."
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1686-1971.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54131 mRNA. Translation: CAA38066.1.
BX648245 mRNA. No translation available.
AC025569 Genomic DNA. No translation available.
AC083809 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97254.1.
BC101679 mRNA. Translation: AAI01680.1.
BC113463 mRNA. Translation: AAI13464.1.
BC143356 mRNA. Translation: AAI43357.1.
BC143360 mRNA. Translation: AAI43361.1.
PIRS12050.
RefSeqNP_001103224.1. NM_001109754.2.
NP_001193900.1. NM_001206971.1.
NP_001193901.1. NM_001206972.1.
NP_002828.3. NM_002837.4.
UniGeneHs.434375.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AHSX-ray2.10A/B1686-1971[»]
2H02X-ray2.30A/B1662-1973[»]
2H03X-ray1.65A1676-1970[»]
2H04X-ray2.30A1662-1973[»]
2HC1X-ray1.30A1676-1965[»]
2HC2X-ray1.40A1676-1965[»]
2I3RX-ray1.85A/B1662-1973[»]
2I3UX-ray1.85A1662-1973[»]
2I4EX-ray1.75A/B1662-1973[»]
2I4GX-ray1.65A1662-1973[»]
2I4HX-ray2.15A1662-1973[»]
2I5XX-ray1.70A/B1662-1973[»]
ProteinModelPortalP23467.
SMRP23467. Positions 1687-1967.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111751. 6 interactions.
IntActP23467. 27 interactions.
MINTMINT-1349770.
STRING9606.ENSP00000334928.

Chemistry

ChEMBLCHEMBL2706.

PTM databases

PhosphoSiteP23467.

Polymorphism databases

DMDM317373518.

Proteomic databases

PaxDbP23467.
PRIDEP23467.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261266; ENSP00000261266; ENSG00000127329. [P23467-1]
ENST00000334414; ENSP00000334928; ENSG00000127329. [P23467-3]
ENST00000538708; ENSP00000438927; ENSG00000127329.
ENST00000550857; ENSP00000447302; ENSG00000127329. [P23467-2]
GeneID5787.
KEGGhsa:5787.
UCSCuc001swb.4. human. [P23467-1]
uc001swc.4. human. [P23467-3]
uc010stp.2. human. [P23467-2]

Organism-specific databases

CTD5787.
GeneCardsGC12M070910.
H-InvDBHIX0017674.
HIX0037045.
HGNCHGNC:9665. PTPRB.
HPACAB004782.
MIM176882. gene.
neXtProtNX_P23467.
PharmGKBPA34010.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000060224.
HOVERGENHBG053759.
InParanoidP23467.
KOK05694.
OMAPEQQHPL.
OrthoDBEOG7PCJFZ.
PhylomeDBP23467.
TreeFamTF351926.

Enzyme and pathway databases

SignaLinkP23467.

Gene expression databases

ArrayExpressP23467.
BgeeP23467.
CleanExHS_PTPRB.
GenevestigatorP23467.

Family and domain databases

Gene3D2.60.40.10. 15 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 15 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 17 hits.
PROSITEPS50853. FN3. 12 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRB. human.
EvolutionaryTraceP23467.
GeneWikiPTPRB.
GenomeRNAi5787.
NextBio22514.
PROP23467.
SOURCESearch...

Entry information

Entry namePTPRB_HUMAN
AccessionPrimary (citable) accession number: P23467
Secondary accession number(s): B7ZKS8 expand/collapse secondary AC list , B7ZKT0, C9JX87, F5H3G6, Q14D85, Q3MIV7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM