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Collapse Statistics
226 human active and 11 inactive phosphatases in total;
194 phosphatases have substrate data;
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305 protein substrates;
89 non-protein substrates;
1114 dephosphorylation interactions;
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213 KEGG pathways;
206 NCI Nature PID pathways
560 Reactome pathways;
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last update: 18 Feb, 2016

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PTPN22

Gene Name PTPN22 (QuickGO)
Structure of phosphatase catalytic domain

PDB ID: 2QCT
(LeftMouse - Rotate; Shift+Left - Scale; Ctrl+Left - Translate)
SynonymsPTPN22 PTPN8
Protein NameTyrosine-protein phosphatase non-receptor type 22
Alternative Name(s)
Tyrosine-protein phosphatase non-receptor type 22 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP) (Lymphoid phosphatase) (LyP)
Ensembl Gene IDENSG00000134242
EntrezGene ID26191
UniProt AC (Human)Q9Y2R2 (protein sequence)
Enzyme ClassEC 3.1.3.48 (BRENDA )
Molecular Weight91705
Protein Length807
Phosphatase activityactive
Protein DomainInterPro | Pfam3D Structure * PDB | PDBe | DrugPort
* ModBase | SwissModel
Structure-based FamilyFamily 1 (CATH: 3.90.190.10)Historical ClassPTPs >> Class I Cys-based PTPs >> Classical PTPs >> Non-receptor type PTPs (NRPTPs)
Localization cytoplasm; nucleus; plasma membrane (PubMed: 10940933, 10068674 | Europe PMC)
Catalytic SiteCatalytic Site Atlas Target by Small MoleculesChEMBL
Gene ExpressionGene Expression Atlas

The Human Protein Atlas

Function and DiseaseOMIM
Protein-protein Interaction Database STRING | IntAct | MINT
Kinase Database Phospho.ELM | PhosphoSite | NetworKIN
Function (UniProt annotation)
FUNCTION: Seems to act on Cbl. May play a role in regulating the function of Cbl and its associated protein kinases. Acts as negative regulator of T cell receptor (TCR) signaling. Dephosphorylates and inactivates the SRC family kinases.
Catalytic Activity (UniProt annotation)
CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
Protein Sequence
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS ETRTIYQFHY KNWPDHDVPS SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI DYTWMLLKDG IIPENFSVFS LIREMRTQRP SLVQTQEQYE LVYNAVLELF KRQMDVIRDK HSGTESQAKH CIPEKNHTLQ ADSYSPNLPK STTKAAKMMN QQRTKMEIKE SSSFDFRTSE ISAKEELVLH PAKSSTSFDF LELNYSFDKN ADTTMKWQTK AFPIVGEPLQ KHQSLDLGSL LFEGCSNSKP VNAAGRYFNS KVPITRTKST PFELIQQRET KEVDSKENFS YLESQPHDSC FVEMQAQKVM HVSSAELNYS LPYDSKHQIR NASNVKHHDS SALGVYSYIP LVENPYFSSW PPSGTSSKMS LDLPEKQDGT VFPSSLLPTS STSLFSYYNS HDSLSLNSPT NISSLLNQES AVLATAPRID DEIPPPLPVR TPESFIVVEE AGEFSPNVPK SLSSAVKVKI GTSLEWGGTS EPKKFDDSVI LRPSKSVKLR SPKSELHQDR SSPPPPLPER TLESFFLADE DCMQAQSIET YSTSYPDTME NSTSSKQTLK TPGKSFTRSK SLKILRNMKK SICNSCPPNK PAESVQSNNS SSFLNFGFAN RFSKPKGPRN PPPTWNI
ELM motif
N/A
Gene Ontology
GO:0017124SH3 domain binding
GO:0030217T cell differentiation
GO:0009898internal side of plasma membrane
GO:0019900kinase binding
GO:0050868negative regulation of T cell activation
GO:0050860negative regulation of T cell receptor signaling pathway
GO:0005634nucleus
GO:0048471perinuclear region of cytoplasm
GO:0035644phosphoanandamide dephosphorylation
GO:0004725protein tyrosine phosphatase activity
GO:0050855regulation of B cell receptor signaling pathway
GO:0032817regulation of natural killer cell proliferation

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