A0A3P8XQB9 · A0A3P8XQB9_ESOLU
- ProteinPhosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids417 (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 | 126 | Phosphocysteine intermediate | |||
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 | protein 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
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Protacanthopterygii > Esociformes > Esocidae > Esox
Accessions
- Primary accessionA0A3P8XQB9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 16-187 | Phosphatase tensin-type | |||
Domain | 104-175 | Tyrosine specific protein phosphatases | |||
Domain | 192-364 | C2 tensin-type | |||
Compositional bias | 304-318 | Polar residues | |||
Region | 304-324 | Disordered | |||
Compositional bias | 366-384 | Polar residues | |||
Region | 366-417 | Disordered | |||
Compositional bias | 385-399 | Basic and acidic residues | |||
Sequence similarities
Belongs to the PTEN phosphatase protein family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length417
- Mass (Da)48,449
- Last updated2020-12-02 v2
- Checksum1F3239136EB7CA3B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6Q2YP68 | A0A6Q2YP68_ESOLU | 496 | |||
A0A3P8XSC4 | A0A3P8XSC4_ESOLU | 428 | |||
A0A3P8ZPL6 | A0A3P8ZPL6_ESOLU | 440 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 304-318 | Polar residues | |||
Compositional bias | 366-384 | Polar residues | |||
Compositional bias | 385-399 | Basic and acidic residues | |||
Keywords
- Technical term