Q54WH6 · PTPA2_DICDI

Function

function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular Componentprotein phosphatase type 2A complex
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functionprotein tyrosine phosphatase activator activity
Biological Processmitotic spindle organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable serine/threonine-protein phosphatase 2A activator 2
  • EC number
  • Alternative names
    • Peptidyl-prolyl cis-trans isomerase PTPA-2 (PPIase PTPA-2; Rotamase PTPA-2)
    • Phosphotyrosyl phosphatase activator 2

Gene names

    • Name
      ppp2r4B
    • ORF names
      DDB_G0279655

Organism names

Accessions

  • Primary accession
    Q54WH6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003284041-468Probable serine/threonine-protein phosphatase 2A activator 2

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias412-431Polar residues
Region412-468Disordered
Compositional bias451-468Pro residues

Sequence similarities

Belongs to the PTPA-type PPIase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    468
  • Mass (Da)
    53,913
  • Last updated
    2005-05-24 v1
  • MD5 Checksum
    5A9BF2E8ECA62985BBADD64687565173
MSENNNKIPSFGLKSNVNSTYNHLETVAKLSIDEKLVNEPPKFVDIKTITPLNVENNGIAQKRIISKRDLRSFHTSSTYSELLNFIIQLSLDIQGKSLKSNFTITKNINSIIVLLNQLDQYITDIPPKQIRTRFGNESFVEWFNKVEKETPKLLFNLINDNPLNTPITNEVPIIYNEISTYLQNSWGDKQRIDYGSGHELNFICFLLCLVKIKFIKREEYELLVLIIFNKYLNMMRRLQESYWLEPAGSHGVWGLDDYHFLPFLFGSSQLIEHKYIRPKSIRNDEIVNSSFSDEYMYLGCIRFIGKVKSGGSLLEHSPMLVDISGVKNWSKVNEGMIKMFKSEVLGKLPIMQHMFFASIIQYIDNPDIIETDEEINQRKPIVTHSFSSCGCINRVPSMFAVANTDKILASTSTTTNNNNNNITSGDHCNDNEQQCSETHNHDHNHNHNHNHNHPPPPPQQQRSYFPLD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias412-431Polar residues
Compositional bias451-468Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAFI02000032
EMBL· GenBank· DDBJ
EAL67602.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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