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P23467

- PTPRB_HUMAN

UniProt

P23467 - PTPRB_HUMAN

Protein

Receptor-type tyrosine-protein phosphatase beta

Gene

PTPRB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1870 – 18701Substrate
    Active sitei1904 – 19041Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation
    Binding sitei1948 – 19481SubstrateBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. dephosphorylation Source: UniProtKB
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. phosphate-containing compound metabolic process Source: ProtInc
    5. protein dephosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Angiogenesis

    Enzyme and pathway databases

    SignaLinkiP23467.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase beta (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase beta
    Short name:
    R-PTP-beta
    Alternative name(s):
    Vascular endothelial protein tyrosine phosphatase
    Short name:
    VE-PTP
    Gene namesi
    Name:PTPRB
    Synonyms:PTPB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9665. PTPRB.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34010.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 19971975Receptor-type tyrosine-protein phosphatase betaPRO_0000025436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi652 – 6521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi829 – 8291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1040 – 10401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1096 – 10961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1163 – 11631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1185 – 11851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1212 – 12121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1274 – 12741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1367 – 13671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1470 – 14701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1474 – 14741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1518 – 15181N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP23467.
    PRIDEiP23467.

    PTM databases

    PhosphoSiteiP23467.

    Expressioni

    Inductioni

    Up-regulated by hypoxia.1 Publication

    Gene expression databases

    ArrayExpressiP23467.
    BgeeiP23467.
    CleanExiHS_PTPRB.
    GenevestigatoriP23467.

    Organism-specific databases

    HPAiCAB004782.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046262EBI-1265766,EBI-641062
    GHRP109123EBI-1265766,EBI-286316
    MAPK3P273612EBI-1265766,EBI-73995
    METP085812EBI-1265766,EBI-1039152
    TEKQ027633EBI-1265766,EBI-2257090

    Protein-protein interaction databases

    BioGridi111751. 6 interactions.
    IntActiP23467. 27 interactions.
    MINTiMINT-1349770.
    STRINGi9606.ENSP00000334928.

    Structurei

    Secondary structure

    1
    1997
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1685 – 16873
    Helixi1688 – 170922
    Turni1710 – 17167
    Turni1720 – 17234
    Helixi1728 – 17303
    Helixi1740 – 17423
    Beta strandi1743 – 17453
    Helixi1753 – 17564
    Beta strandi1757 – 17637
    Beta strandi1766 – 17694
    Beta strandi1771 – 17755
    Turni1780 – 17823
    Helixi1783 – 179210
    Beta strandi1797 – 18004
    Beta strandi1804 – 18063
    Beta strandi1818 – 18214
    Beta strandi1823 – 18253
    Beta strandi1828 – 183710
    Beta strandi1839 – 184911
    Beta strandi1856 – 186510
    Beta strandi1870 – 18723
    Helixi1877 – 189317
    Beta strandi1894 – 18963
    Beta strandi1900 – 19034
    Beta strandi1905 – 19084
    Helixi1909 – 192618
    Beta strandi1928 – 19303
    Helixi1932 – 19409
    Helixi1950 – 196516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP23467.
    SMRiP23467. Positions 1687-1967.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23467.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 16211599ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1643 – 1997355CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1622 – 164221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 11189Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini112 – 20796Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini203 – 28886Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini291 – 37888Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini379 – 47193Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini467 – 55286Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini556 – 64186Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini642 – 72988Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini730 – 829100Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini819 – 90688Fibronectin type-III 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini909 – 100193Fibronectin type-III 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini995 – 108389Fibronectin type-III 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1087 – 117589Fibronectin type-III 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1173 – 126088Fibronectin type-III 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1260 – 135697Fibronectin type-III 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1357 – 144892Fibronectin type-III 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1458 – 155497Fibronectin type-III 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1703 – 1963261Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1904 – 19107Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 17 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    HOGENOMiHOG000060224.
    HOVERGENiHBG053759.
    InParanoidiP23467.
    KOiK05694.
    OMAiPEQQHPL.
    OrthoDBiEOG7PCJFZ.
    PhylomeDBiP23467.
    TreeFamiTF351926.

    Family and domain databases

    Gene3Di2.60.40.10. 15 hits.
    3.90.190.10. 1 hit.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00041. fn3. 15 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 17 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 17 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS50853. FN3. 12 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23467-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLSHGAGLAL WITLSLLQTG LAEPERCNFT LAESKASSHS VSIQWRILGS     50
    PCNFSLIYSS DTLGAALCPT FRIDNTTYGC NLQDLQAGTI YNFRIISLDE 100
    ERTVVLQTDP LPPARFGVSK EKTTSTSLHV WWTPSSGKVT SYEVQLFDEN 150
    NQKIQGVQIQ ESTSWNEYTF FNLTAGSKYN IAITAVSGGK RSFSVYTNGS 200
    TVPSPVKDIG ISTKANSLLI SWSHGSGNVE RYRLMLMDKG ILVHGGVVDK 250
    HATSYAFHGL TPGYLYNLTV MTEAAGLQNY RWKLVRTAPM EVSNLKVTND 300
    GSLTSLKVKW QRPPGNVDSY NITLSHKGTI KESRVLAPWI TETHFKELVP 350
    GRLYQVTVSC VSGELSAQKM AVGRTFPDKV ANLEANNNGR MRSLVVSWSP 400
    PAGDWEQYRI LLFNDSVVLL NITVGKEETQ YVMDDTGLVP GRQYEVEVIV 450
    ESGNLKNSER CQGRTVPLAV LQLRVKHANE TSLSIMWQTP VAEWEKYIIS 500
    LADRDLLLIH KSLSKDAKEF TFTDLVPGRK YMATVTSISG DLKNSSSVKG 550
    RTVPAQVTDL HVANQGMTSS LFTNWTQAQG DVEFYQVLLI HENVVIKNES 600
    ISSETSRYSF HSLKSGSLYS VVVTTVSGGI SSRQVVVEGR TVPSSVSGVT 650
    VNNSGRNDYL SVSWLLAPGD VDNYEVTLSH DGKVVQSLVI AKSVRECSFS 700
    SLTPGRLYTV TITTRSGKYE NHSFSQERTV PDKVQGVSVS NSARSDYLRV 750
    SWVHATGDFD HYEVTIKNKN NFIQTKSIPK SENECVFVQL VPGRLYSVTV 800
    TTKSGQYEAN EQGNGRTIPE PVKDLTLRNR STEDLHVTWS GANGDVDQYE 850
    IQLLFNDMKV FPPFHLVNTA TEYRFTSLTP GRQYKILVLT ISGDVQQSAF 900
    IEGFTVPSAV KNIHISPNGA TDSLTVNWTP GGGDVDSYTV SAFRHSQKVD 950
    SQTIPKHVFE HTFHRLEAGE QYQIMIASVS GSLKNQINVV GRTVPASVQG 1000
    VIADNAYSSY SLIVSWQKAA GVAERYDILL LTENGILLRN TSEPATTKQH 1050
    KFEDLTPGKK YKIQILTVSG GLFSKEAQTE GRTVPAAVTD LRITENSTRH 1100
    LSFRWTASEG ELSWYNIFLY NPDGNLQERA QVDPLVQSFS FQNLLQGRMY 1150
    KMVIVTHSGE LSNESFIFGR TVPASVSHLR GSNRNTTDSL WFNWSPASGD 1200
    FDFYELILYN PNGTKKENWK DKDLTEWRFQ GLVPGRKYVL WVVTHSGDLS 1250
    NKVTAESRTA PSPPSLMSFA DIANTSLAIT WKGPPDWTDY NDFELQWLPR 1300
    DALTVFNPYN NRKSEGRIVY GLRPGRSYQF NVKTVSGDSW KTYSKPIFGS 1350
    VRTKPDKIQN LHCRPQNSTA IACSWIPPDS DFDGYSIECR KMDTQEVEFS 1400
    RKLEKEKSLL NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS TITMIDRPPP 1450
    PPPHIRVNEK DVLISKSSIN FTVNCSWFSD TNGAVKYFTV VVREADGSDE 1500
    LKPEQQHPLP SYLEYRHNAS IRVYQTNYFA SKCAENPNSN SKSFNIKLGA 1550
    EMESLGGKCD PTQQKFCDGP LKPHTAYRIS IRAFTQLFDE DLKEFTKPLY 1600
    SDTFFSLPIT TESEPLFGAI EGVSAGLFLI GMLVAVVALL ICRQKVSHGR 1650
    ERPSARLSIR RDRPLSVHLN LGQKGNRKTS CPIKINQFEG HFMKLQADSN 1700
    YLLSKEYEEL KDVGRNQSCD IALLPENRGK NRYNNILPYD ATRVKLSNVD 1750
    DDPCSDYINA SYIPGNNFRR EYIVTQGPLP GTKDDFWKMV WEQNVHNIVM 1800
    VTQCVEKGRV KCDHYWPADQ DSLYYGDLIL QMLSESVLPE WTIREFKICG 1850
    EEQLDAHRLI RHFHYTVWPD HGVPETTQSL IQFVRTVRDY INRSPGAGPT 1900
    VVHCSAGVGR TGTFIALDRI LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE 1950
    CQYVYLHQCV RDVLRARKLR SEQENPLFPI YENVNPEYHR DPVYSRH 1997
    Length:1,997
    Mass (Da):224,301
    Last modified:January 11, 2011 - v3
    Checksum:i76E67B4A6109AA0F
    GO
    Isoform 2 (identifier: P23467-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         377-466: Missing.

    Show »
    Length:1,907
    Mass (Da):214,209
    Checksum:iC8A61E610D7ECC31
    GO
    Isoform 3 (identifier: P23467-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MLSHGAGLALWITLSLLQ → MEAEFYMVIL...TQPFSSTTEE

    Show »
    Length:2,215
    Mass (Da):249,143
    Checksum:i605BB45BA4541F02
    GO
    Isoform 4 (identifier: P23467-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,907
    Mass (Da):214,505
    Checksum:i237BC55F05D696E7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611T → S in CAA38066. (PubMed:2170109)Curated
    Sequence conflicti666 – 6661L → V in CAA38066. (PubMed:2170109)Curated
    Sequence conflicti926 – 9261V → A in BX648245. (PubMed:17974005)Curated
    Sequence conflicti1559 – 15591C → R in CAA38066. (PubMed:2170109)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941R → K.2 Publications
    Corresponds to variant rs2252784 [ dbSNP | Ensembl ].
    VAR_062251
    Natural varianti127 – 1271S → G.1 Publication
    Corresponds to variant rs2465811 [ dbSNP | Ensembl ].
    VAR_062252
    Natural varianti395 – 3951V → A.
    Corresponds to variant rs36027530 [ dbSNP | Ensembl ].
    VAR_057135
    Natural varianti415 – 4151D → E.
    Corresponds to variant rs2165627 [ dbSNP | Ensembl ].
    VAR_057136
    Natural varianti939 – 9391T → M.
    Corresponds to variant rs2304821 [ dbSNP | Ensembl ].
    VAR_057137
    Natural varianti1032 – 10321T → I.
    Corresponds to variant rs34902691 [ dbSNP | Ensembl ].
    VAR_057138
    Natural varianti1934 – 19341G → A.
    Corresponds to variant rs17226367 [ dbSNP | Ensembl ].
    VAR_057139

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1818MLSHG…LSLLQ → MEAEFYMVILTCLIFRNSEG FQIVHVQKQQCLFKNEKVVV GSCNRTIQNQQWMWTEDEKL LHVKSALCLAISNSSRGPSR SAILDRCSQAPRWTCYDQEG FLEVENASLFLQKQGSRVVV KKARKYLHSWMKIDVNKEGK LVNESLCLQKAGLGAEVSVR STRNTAPPQILTTFNAVPDG LVFLIRNTTEAFIRNAAENY SQNSSERQHPNLHMTGITDT SWVLSTTQPFSSTTEE in isoform 3. 1 PublicationVSP_040484Add
    BLAST
    Alternative sequencei377 – 46690Missing in isoform 2. 1 PublicationVSP_038521Add
    BLAST
    Alternative sequencei997 – 108690Missing in isoform 4. 1 PublicationVSP_053944Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS44943.1. [P23467-3]
    CCDS44944.1. [P23467-1]
    CCDS55845.1. [P23467-2]
    CCDS55846.1. [P23467-4]
    PIRiS12050.
    RefSeqiNP_001103224.1. NM_001109754.2. [P23467-3]
    NP_001193900.1. NM_001206971.1. [P23467-2]
    NP_001193901.1. NM_001206972.1. [P23467-4]
    NP_002828.3. NM_002837.4. [P23467-1]
    UniGeneiHs.434375.

    Genome annotation databases

    GeneIDi5787.
    KEGGihsa:5787.
    UCSCiuc001swb.4. human. [P23467-1]
    uc001swc.4. human. [P23467-3]
    uc010stp.2. human. [P23467-2]

    Polymorphism databases

    DMDMi317373518.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS44943.1. [P23467-3 ]
    CCDS44944.1. [P23467-1 ]
    CCDS55845.1. [P23467-2 ]
    CCDS55846.1. [P23467-4 ]
    PIRi S12050.
    RefSeqi NP_001103224.1. NM_001109754.2. [P23467-3 ]
    NP_001193900.1. NM_001206971.1. [P23467-2 ]
    NP_001193901.1. NM_001206972.1. [P23467-4 ]
    NP_002828.3. NM_002837.4. [P23467-1 ]
    UniGenei Hs.434375.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AHS X-ray 2.10 A/B 1686-1971 [» ]
    2H02 X-ray 2.30 A/B 1662-1973 [» ]
    2H03 X-ray 1.65 A 1676-1970 [» ]
    2H04 X-ray 2.30 A 1662-1973 [» ]
    2HC1 X-ray 1.30 A 1676-1965 [» ]
    2HC2 X-ray 1.40 A 1676-1965 [» ]
    2I3R X-ray 1.85 A/B 1662-1973 [» ]
    2I3U X-ray 1.85 A 1662-1973 [» ]
    2I4E X-ray 1.75 A/B 1662-1973 [» ]
    2I4G X-ray 1.65 A 1662-1973 [» ]
    2I4H X-ray 2.15 A 1662-1973 [» ]
    2I5X X-ray 1.70 A/B 1662-1973 [» ]
    ProteinModelPortali P23467.
    SMRi P23467. Positions 1687-1967.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111751. 6 interactions.
    IntActi P23467. 27 interactions.
    MINTi MINT-1349770.
    STRINGi 9606.ENSP00000334928.

    Chemistry

    ChEMBLi CHEMBL2706.

    PTM databases

    PhosphoSitei P23467.

    Polymorphism databases

    DMDMi 317373518.

    Proteomic databases

    PaxDbi P23467.
    PRIDEi P23467.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5787.
    KEGGi hsa:5787.
    UCSCi uc001swb.4. human. [P23467-1 ]
    uc001swc.4. human. [P23467-3 ]
    uc010stp.2. human. [P23467-2 ]

    Organism-specific databases

    CTDi 5787.
    GeneCardsi GC12M070910.
    H-InvDB HIX0017674.
    HIX0037045.
    HGNCi HGNC:9665. PTPRB.
    HPAi CAB004782.
    MIMi 176882. gene.
    neXtProti NX_P23467.
    PharmGKBi PA34010.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5599.
    HOGENOMi HOG000060224.
    HOVERGENi HBG053759.
    InParanoidi P23467.
    KOi K05694.
    OMAi PEQQHPL.
    OrthoDBi EOG7PCJFZ.
    PhylomeDBi P23467.
    TreeFami TF351926.

    Enzyme and pathway databases

    SignaLinki P23467.

    Miscellaneous databases

    ChiTaRSi PTPRB. human.
    EvolutionaryTracei P23467.
    GeneWikii PTPRB.
    GenomeRNAii 5787.
    NextBioi 22514.
    PROi P23467.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23467.
    Bgeei P23467.
    CleanExi HS_PTPRB.
    Genevestigatori P23467.

    Family and domain databases

    Gene3Di 2.60.40.10. 15 hits.
    3.90.190.10. 1 hit.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view ]
    Pfami PF00041. fn3. 15 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 17 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 17 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS50853. FN3. 12 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiPTPRB_HUMAN
    AccessioniPrimary (citable) accession number: P23467
    Secondary accession number(s): B7ZKS8
    , B7ZKT0, C9JX87, F5H3G6, Q14D85, Q3MIV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3