A0A6B0QTZ0 · A0A6B0QTZ0_9CETA

  • 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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site72Phosphocysteine 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

Gene names

    • ORF names
      E5288_WYG009068

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • WY2019
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    A0A6B0QTZ0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain, compositional bias, region.

Type
IDPosition(s)Description
Domain1-133Phosphatase tensin-type
Domain50-121Tyrosine specific protein phosphatases
Domain138-298C2 tensin-type
Compositional bias302-318Polar residues
Region302-351Disordered
Compositional bias319-333Basic and acidic residues

Sequence similarities

Belongs to the PTEN phosphatase protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    351
  • Mass (Da)
    40,893
  • Last updated
    2020-06-17 v1
  • Checksum
    0584C813AC80C862
MHKLTVVPGIAWHIKCWLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEESSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias302-318Polar residues
Compositional bias319-333Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VBQZ03000005
EMBL· GenBank· DDBJ
MXQ80540.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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