Q3UUN5 · Q3UUN5_MOUSE
- ProteinPhosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- GenePten
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids407 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3.
Catalytic activity
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphateThis reaction proceeds in the forward direction.
- 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 128 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | dendritic spine | |
Cellular Component | plasma membrane | |
Cellular Component | PML body | |
Cellular Component | postsynaptic density | |
Molecular Function | inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity | |
Molecular Function | phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity | |
Molecular Function | phosphatidylinositol-3-phosphate phosphatase activity | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | apoptotic process | |
Biological Process | cell motility | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | nervous system development | |
Biological Process | phosphatidylinositol dephosphorylation | |
Biological Process | regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3UUN5
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-189 | Phosphatase tensin-type | ||||
Sequence: MLNGAGLDQAFKMSLPRRARIGASVGPVRSSAGYKKAEDEMSRATSVGDQLEAPARIIYLNQSHLNKFCDNRIRCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNH | ||||||
Domain | 106-177 | Tyrosine specific protein phosphatases | ||||
Sequence: KPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRR | ||||||
Domain | 194-354 | C2 tensin-type | ||||
Sequence: PVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKT | ||||||
Region | 356-407 | Disordered | ||||
Sequence: EEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHSQITKV | ||||||
Compositional bias | 357-374 | Polar residues | ||||
Sequence: EPSNPEASSSTSVTPDVS | ||||||
Compositional bias | 375-389 | Basic and acidic residues | ||||
Sequence: DNEPDHYRYSDTTDS |
Sequence similarities
Belongs to the PTEN phosphatase protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length407
- Mass (Da)46,893
- Last updated2005-10-11 v1
- ChecksumCFFA22CA270BB80E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 357-374 | Polar residues | ||||
Sequence: EPSNPEASSSTSVTPDVS | ||||||
Compositional bias | 375-389 | Basic and acidic residues | ||||
Sequence: DNEPDHYRYSDTTDS |