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

spacer

PTEN

Gene Name PTEN (QuickGO)
Structure of phosphatase catalytic domain

PDB ID: 1D5R
(LeftMouse - Rotate; Shift+Left - Scale; Ctrl+Left - Translate)
SynonymsPTEN MMAC1 TEP1
Protein NamePhosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Alternative Name(s)
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)
Ensembl Gene IDENSG00000171862
EntrezGene ID5728
UniProt AC (Human)P60484 (protein sequence)
Enzyme ClassEC 3.1.3.16, 3.1.3.48, 3.1.3.67 (BRENDA )
Molecular Weight47166
Protein Length403
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 >> VH1-like or dual-specificity phosphatases (DSPs) >> PTENs
Localization cytoplasm; cytosol; nucleus; plasma membrane (PubMed: 10213484, 12847108, 12543774, 9356475, 9593664, 10760291, 9187108, 18716620 | Europe PMC)
Catalytic SiteCatalytic Site Atlas Target by Small MoleculesN/A
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: Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability.
Catalytic Activity (UniProt annotation)
CATALYTIC ACTIVITY: Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate.; CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein + phosphate.; CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
Protein Sequence
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHTQI TKV
ELM motif
CLV_C14_Caspase3-7Caspase-3 and Caspase-7 cleavage site.
MOD_CK2_1CK2 phosphorylation site
Gene Ontology
GO:0030165PDZ domain binding
GO:0016605PML body
GO:0050852T cell receptor signaling pathway
GO:0007092activation of mitotic anaphase-promoting complex activity
GO:0010997anaphase-promoting complex binding
GO:0006915apoptosis
GO:0060070canonical Wnt receptor signaling pathway
GO:0008283cell proliferation
GO:0007417central nervous system development
GO:0005829cytosol
GO:0019899enzyme binding
GO:0006917induction of apoptosis
GO:0046855inositol phosphate dephosphorylation
GO:0051717inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity
GO:0009898internal side of plasma membrane
GO:0008289lipid binding
GO:0000287magnesium ion binding
GO:2000134negative regulation of G1/S transition of mitotic cell cycle
GO:0030336negative regulation of cell migration
GO:0031658negative regulation of cyclin-dependent protein kinase activity involved in G1/S
GO:0051895negative regulation of focal adhesion assembly
GO:0051898negative regulation of protein kinase B signaling cascade
GO:0001933negative regulation of protein phosphorylation
GO:0048011nerve growth factor receptor signaling pathway
GO:0046856phosphatidylinositol dephosphorylation
GO:0016314phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity
GO:0051800phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity
GO:0004438phosphatidylinositol-3-phosphatase activity
GO:0048015phosphatidylinositol-mediated signaling
GO:2000060positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process
GO:0051091positive regulation of sequence-specific DNA binding transcription factor activity
GO:0004722protein serine/threonine phosphatase activity
GO:0050821protein stabilization
GO:0004725protein tyrosine phosphatase activity
GO:0008138protein tyrosine/serine/threonine phosphatase activity
GO:0010975regulation of neuron projection development

spacer
spacer