A0AA97IQ11 · A0AA97IQ11_DROMI

  • Protein
    Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
  • Gene
    DmirGB2_Pten-PH
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

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 )

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 Functionphosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity
Molecular Functionphosphatidylinositol-3,4-bisphosphate 3-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
    • Inositol polyphosphate 3-phosphatase
    • Phosphatase and tensin homolog

Gene names

    • Name
      DmirGB2_Pten-PH
    • Synonyms
      DmirGB2_Pten-PB
      , DmirGB2_Pten-PD
      , DmirGB2_Pten-PG

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    A0AA97IQ11

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain21-193Phosphatase tensin-type
Domain110-167Tyrosine specific protein phosphatases
Domain181-338C2 tensin-type
Region376-396Disordered
Region448-469Disordered
Compositional bias453-469Basic and acidic residues

Sequence similarities

Belongs to the PTEN phosphatase protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    469
  • Mass (Da)
    53,797
  • Last updated
    2024-03-27 v1
  • Checksum
    A59550EC1CE529A2
MANTISLMSNVIRNVVSKNRIRYKGERFDLDLTYIYDNIIAMGYPAPDKLEGMYRNCQEDVLKFLDEKHGDHYKIYNLCLERSYDTNKFHGRVAIFPFEDHNPPTIELIQKFCKDVDSWLKEDVLNVVAVHCKAGKGRTGTMICAYLLYSGLQKSADEALAWYDEKRTKDRKGVTIPSQRRYVQYFSNLVCSSVPYSKKMFKVCEIRFSESSLLKNLGTVQCKVFVLQDSTTENVKAHRPKTWTFDFQESCVLNINNPSLSVAGDIKFEFAQKSSQKAICHFWLNTFFVQNSSVCESDGTLLKCTYTLKKSEIDGVHKDRKHKSFSEDFKISILFEGEACFNDETKSKKQPKAALENQDISTKIQYDTTTNLKNVSTASKRKQPNNIPLASNLNNDSTGMDLKKIHTFKPPSITKSNLTTWENGEINITSDTRSINDNKHINYDSYITYKQSSPKDGEEDWESGESTRL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias453-469Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BK064498
EMBL· GenBank· DDBJ
DBA35776.1
EMBL· GenBank· DDBJ
mRNA
BK064499
EMBL· GenBank· DDBJ
DBA35777.1
EMBL· GenBank· DDBJ
mRNA
BK064500
EMBL· GenBank· DDBJ
DBA35778.1
EMBL· GenBank· DDBJ
mRNA
BK064501
EMBL· GenBank· DDBJ
DBA35779.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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