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M3WPL8 · M3WPL8_FELCA

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 site124Phosphocysteine intermediate

GO annotations

AspectTerm
Cellular Componentapical plasma membrane
Cellular Componentcell projection
Cellular Componentcytoplasmic side of plasma membrane
Cellular Componentcytosol
Cellular Componentdendritic spine
Cellular Componentnucleus
Cellular Componentplasma membrane
Cellular ComponentPML body
Cellular Componentpostsynaptic density
Molecular Functionanaphase-promoting complex binding
Molecular Functionidentical protein binding
Molecular Functioninositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity
Molecular Functioninositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity
Molecular Functionmyosin phosphatase activity
Molecular FunctionPDZ domain binding
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
Molecular Functionubiquitin-specific protease binding
Biological Processapoptotic process
Biological Processcanonical Wnt signaling pathway
Biological Processcell motility
Biological Processcellular response to electrical stimulus
Biological Processnegative regulation of cell population proliferation
Biological Processnegative regulation of cyclin-dependent protein serine/threonine kinase activity
Biological Processnegative regulation of epithelial to mesenchymal transition
Biological Processnegative regulation of focal adhesion assembly
Biological Processnegative regulation of G1/S transition of mitotic cell cycle
Biological Processnegative regulation of keratinocyte migration
Biological Processnegative regulation of osteoblast differentiation
Biological Processnegative regulation of peptidyl-serine phosphorylation
Biological Processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processnegative regulation of vascular associated smooth muscle cell proliferation
Biological Processnegative regulation of wound healing, spreading of epidermal cells
Biological Processnervous system development
Biological Processphosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processphosphatidylinositol dephosphorylation
Biological Processpositive regulation of DNA-binding transcription factor activity
Biological Processpositive regulation of ubiquitin protein ligase activity
Biological Processpositive regulation of ubiquitin-dependent protein catabolic process
Biological Processprotein dephosphorylation
Biological Processprotein stabilization
Biological Processregulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processspindle assembly involved in female meiosis

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

    • Name
      PTEN

Organism names

  • Taxonomic identifier
  • Strain
    • Abyssinian
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Feliformia > Felidae > Felinae > Felis

Accessions

  • Primary accession
    M3WPL8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain14-185Phosphatase tensin-type
Domain102-173Tyrosine specific protein phosphatases
Domain190-350C2 tensin-type
Region352-403Disordered
Compositional bias353-370Polar residues
Compositional bias371-385Basic and acidic residues

Sequence similarities

Belongs to the PTEN phosphatase protein family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    403
  • Mass (Da)
    47,166
  • Last updated
    2018-10-10 v3
  • MD5 Checksum
    F6916C76DD8BC97E8B7E846A37DECA0E
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias353-370Polar residues
Compositional bias371-385Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AANG04003211
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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