A0A3P8XQB9 · A0A3P8XQB9_ESOLU

  • 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.
  • O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.16 (UniProtKB | ENZYME | Rhea)
  • O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.16 (UniProtKB | ENZYME | Rhea)
  • O-phospho-L-tyrosyl-[protein] + H2O = 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 site126Phosphocysteine intermediate

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentdendritic spine
Cellular Componentplasma membrane
Cellular ComponentPML body
Cellular Componentpostsynaptic density
Molecular Functioninositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity
Molecular Functionmyosin 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 Processcell motility
Biological Processnegative regulation of cell population proliferation
Biological Processnervous system development
Biological Processphosphatidylinositol dephosphorylation
Biological Processprotein dephosphorylation
Biological Processregulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction

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
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Protacanthopterygii > Esociformes > Esocidae > Esox

Accessions

  • Primary accession
    A0A3P8XQB9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Expression

Gene expression databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

Type
IDPosition(s)Description
Domain16-187Phosphatase tensin-type
Domain104-175Tyrosine specific protein phosphatases
Domain192-364C2 tensin-type
Compositional bias304-318Polar residues
Region304-324Disordered
Compositional bias366-384Polar residues
Region366-417Disordered
Compositional bias385-399Basic and acidic residues

Sequence similarities

Belongs to the PTEN phosphatase protein family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    417
  • Mass (Da)
    48,449
  • Last updated
    2020-12-02 v2
  • Checksum
    1F3239136EB7CA3B
VAMAAIIKEMVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKDHYKIYNLCAERHYDAAKFNCRVAQFPFEDHNPPQLELIKPFCEDLDQWLSKDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFQEAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSHLLKNKLDYKPVALLFHKMVFETLPMFSGGTCNPQFVVYQLKVKIHTSNPAHTRREEKHMLFEFPQPLPVCGDIKVEFFHKQNKMMKKDKMFHFWVNTFFIPGPPEESLEKVENGSVVVNDVDGVQNQPQGAPQLPQSAEHRDSDRDYLILALTKNDLDKANKDKANRYFSPNFKVMLYFTKTVEDSSNSEASTSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEEQHTQITKV

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A6Q2YP68A0A6Q2YP68_ESOLU496
A0A3P8XSC4A0A3P8XSC4_ESOLU428
A0A3P8ZPL6A0A3P8ZPL6_ESOLU440

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias304-318Polar residues
Compositional bias366-384Polar residues
Compositional bias385-399Basic and acidic residues

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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