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Reviewed, UniProtKB/Swiss-Prot P23467 (PTPRB_HUMAN)

Last modified October 13, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Gene names
Name: PTPRB
Synonyms: PTPB
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with MAGI3 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

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.

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Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein amino acid dephosphorylation Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentintegral to plasma membrane Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

transmembrane receptor protein tyrosine phosphatase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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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 – 164221 Potential
Topological domain1643 – 1997355Cytoplasmic Potential
Domain23 – 10886Fibronectin type-III 1
Domain110 – 20192Fibronectin type-III 2
Domain203 – 28886Fibronectin type-III 3
Domain289 – 37587Fibronectin type-III 4
Domain377 – 46589Fibronectin type-III 5
Domain467 – 55286Fibronectin type-III 6
Domain554 – 64188Fibronectin type-III 7
Domain643 – 73088Fibronectin type-III 8
Domain731 – 81787Fibronectin type-III 9
Domain819 – 90688Fibronectin type-III 10
Domain907 – 99387Fibronectin type-III 11
Domain995 – 108389Fibronectin type-III 12
Domain1085 – 117288Fibronectin type-III 13
Domain1173 – 126088Fibronectin type-III 14
Domain1261 – 135393Fibronectin type-III 15
Domain1355 – 144389Fibronectin type-III 16
Domain1448 – 1550103Fibronectin type-III 17
Domain1703 – 1963261Tyrosine-protein phosphatase

Sites

Active site19041Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue10671Phosphothreonine Ref.2
Modified residue10691Phosphoserine Ref.2
Modified residue16471Phosphoserine Ref.3
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

Natural variant3951V → A: dbSNP rs36027530.
VAR_057135
Natural variant4151D → E: dbSNP rs2165627.
VAR_057136
Natural variant9391T → M: dbSNP rs2304821.
VAR_057137
Natural variant10321T → I: dbSNP rs34902691.
VAR_057138
Natural variant19341G → A: dbSNP rs17226367.
VAR_057139

Secondary structure

1 .................................................... 1997
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P23467-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 691E99BA7A1515DD

FASTA1,997224,268
        10         20         30         40         50         60 
MLSHGAGLAL WITLSLLQTG LAEPERCNFT LAESKASSHS VSIQWRILGS PCNFSLIYSS 

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

       130        140        150        160        170        180 
EKTTSTGLHV 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 SPGYLYNLTV 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 
SVSWLVAPGD 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 EMESLGGKRD 

      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

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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: 2170109] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"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: 15144186] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1067 AND SER-1069, MASS SPECTROMETRY.
Tissue: T-cell.
[3]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1647, MASS SPECTROMETRY.
Tissue: Epithelium.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X54131 mRNA. Translation: CAA38066.1.
IPIIPI00295577.
PIRS12050.
RefSeqNP_002828.3.
UniGeneHs.434375

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP23467. 22 interactions.
STRINGP23467.

PTM databases

PhosphoSiteP23467.

Proteomic databases

PRIDEP23467.

Genome annotation databases

EnsemblENST00000261266; ENSP00000261266; ENSG00000127329; Homo sapiens. [Genome view]
ENST00000334414; ENSP00000334928; ENSG00000127329; Homo sapiens. [Genome view]
ENST00000451516; ENSP00000393028; ENSG00000127329; Homo sapiens. [Genome view]
GeneID5787.

Organism-specific databases

CTD5787.
GeneCardsGC12M069201.
H-InvDBHIX0017674.
HIX0037045.
HGNCHGNC:9665. PTPRB.
HPACAB004782.
MIM176882. gene.
PharmGKBPA34010.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP23467.
HOVERGENP23467.

Enzyme and pathway databases

BRENDA3.1.3.48. 247.

Gene expression databases

ArrayExpressP23467.
BgeeP23467.
CleanExHS_PTPRB.
GenevestigatorP23467.
GermOnlineENSG00000127329. Homo sapiens.

Family and domain databases

InterProIPR000387. Dual-sp/Tyr_phosphatase.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 14 hits.
PfamPF00041. fn3. 16 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
PROSITEPS50853. FN3. 17 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio22514.
SOURCESearch...

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Entry information

Entry namePTPRB_HUMAN
AccessionPrimary (citable) accession number: P23467
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 13, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents