A0A8C0BQJ3 · A0A8C0BQJ3_9AVES

  • Protein
    Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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) + phosphate
    This 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) + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.16 (UniProtKB | ENZYME | Rhea)
  • H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.16 (UniProtKB | ENZYME | Rhea)
  • H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.48 (UniProtKB | ENZYME | Rhea)
  • a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.67 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site97Phosphocysteine intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentdendritic spine
Cellular ComponentPML body
Cellular Componentpostsynaptic density
Molecular Functioninositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity
Molecular Functionphosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity
Molecular Functionphosphatidylinositol-3,4-bisphosphate 3-phosphatase activity
Molecular Functionphosphatidylinositol-3-phosphate phosphatase activity
Molecular Functionprotein tyrosine phosphatase activity
Biological Processapoptotic process
Biological Processnegative regulation of cell population proliferation
Biological Processnervous system development
Biological Processphosphatidylinositol dephosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
  • EC number
  • Alternative names
    • Phosphatase and tensin homolog

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Accipitriformes > Accipitridae > Accipitrinae > Buteo

Accessions

  • Primary accession
    A0A8C0BQJ3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain1-158Phosphatase tensin-type
Domain75-146Tyrosine specific protein phosphatases
Domain163-323C2 tensin-type
Compositional bias326-343Polar residues
Region326-376Disordered
Compositional bias344-358Basic and acidic residues

Sequence similarities

Belongs to the PTEN phosphatase protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    376
  • Mass (Da)
    43,951
  • Last updated
    2022-01-19 v1
  • Checksum
    E8FF1862BCB9392F
MDIYPNIIAMGFPAERLEGVYRNNIDDVIFPCFLNPCLFFFFRCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSSGTCNPQFVVYQLKVKIFTSPSGPSRREDKYMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIGLDENSDKVENGSLVADQELDGIFSTERSDNDKEYLILTLTKNDLDKANKDKANRYFSPNFKVKLFFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias326-343Polar residues
Compositional bias344-358Basic and acidic residues

Keywords

Genome annotation databases

Similar Proteins

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