A0A8C0BQJ3 · A0A8C0BQJ3_9AVES
- ProteinPhosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids376 (go to sequence)
- Protein existenceInferred from homology
- 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 | 97 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | dendritic spine | |
Cellular Component | PML body | |
Cellular Component | postsynaptic density | |
Molecular Function | inositol-1,3,4,5-tetrakisphosphate 3-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 | negative regulation of cell population proliferation | |
Biological Process | nervous system development | |
Biological Process | phosphatidylinositol dephosphorylation |
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
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Accipitriformes > Accipitridae > Accipitrinae > Buteo
Accessions
- Primary accessionA0A8C0BQJ3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-158 | Phosphatase tensin-type | ||||
Sequence: MDIYPNIIAMGFPAERLEGVYRNNIDDVIFPCFLNPCLFFFFRCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNH | ||||||
Domain | 75-146 | Tyrosine specific protein phosphatases | ||||
Sequence: KPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRR | ||||||
Domain | 163-323 | C2 tensin-type | ||||
Sequence: PVALLFHKMMFETIPMFSSGTCNPQFVVYQLKVKIFTSPSGPSRREDKYMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIGLDENSDKVENGSLVADQELDGIFSTERSDNDKEYLILTLTKNDLDKANKDKANRYFSPNFKVKLFFTKT | ||||||
Compositional bias | 326-343 | Polar residues | ||||
Sequence: EPSNPEASSSTSVTPDVS | ||||||
Region | 326-376 | Disordered | ||||
Sequence: EPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV | ||||||
Compositional bias | 344-358 | Basic and acidic residues | ||||
Sequence: DNEPDHYRYSDTTDS |
Sequence similarities
Belongs to the PTEN phosphatase protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length376
- Mass (Da)43,951
- Last updated2022-01-19 v1
- ChecksumE8FF1862BCB9392F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 326-343 | Polar residues | ||||
Sequence: EPSNPEASSSTSVTPDVS | ||||||
Compositional bias | 344-358 | Basic and acidic residues | ||||
Sequence: DNEPDHYRYSDTTDS |
Keywords
- Technical term