M7AXS8 · M7AXS8_CHEMY

Function

function

Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.

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 Componentchromatin
Cellular Componentnucleus
Cellular ComponentPTW/PP1 phosphatase complex
Molecular Functionmetal ion binding
Molecular Functionprotein phosphatase 1 binding
Molecular Functionprotein phosphatase inhibitor activity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein phosphatase 1 regulatory subunit 10
  • Alternative names
    • MHC class I region proline-rich protein CAT53

Gene names

    • ORF names
      UY3_15037

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Testudinata > Testudines > Cryptodira > Durocryptodira > Americhelydia > Chelonioidea > Cheloniidae > Chelonia

Accessions

  • Primary accession
    M7AXS8

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Keywords

Interaction

Subunit

Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1CC. Interacts with PPP1CA, WDR82 and TOX4.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias, zinc finger.

Type
IDPosition(s)Description
Domain123-197TFIIS N-terminal
Region197-262Disordered
Compositional bias201-249Basic and acidic residues
Region290-319Disordered
Region351-448Disordered
Compositional bias414-434Polar residues
Region545-571Disordered
Region583-631Disordered
Compositional bias704-746Pro residues
Region704-761Disordered
Domain762-790C3H1-type
Zinc finger762-790C3H1-type

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    796
  • Mass (Da)
    86,729
  • Last updated
    2013-05-29 v1
  • Checksum
    F7DE9F5710BDC669
MSDCRARFVELLTLRTESDQQTLSNGDAQAVKKAADLILGWVCKEPELSIMGSGPIDPHELLKGLDCFLGRDGEVKNTEGVTKIFNFMKDAQKMVSRCIYLNILLQTRAQDILAKFIRVGGYKLLNTWLTSSKASSNVPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRRLASILVSDWMGVIRSQSSAQPAERDKKKRKEESKSKAPVQEKPQEAKAEAKAEETPEKKREKPKSLRTTAPSHAKFRSTGLELETPSLVPLKKNPNAVVVSEKYNLKPMPIKRQSTSAPSGDNPPVEKKYKPLNTTPNSTKEIKVKIIPAQPMEGLGFLDALNSAPIPGIKIKKKKKVLSPTAAKSSPFEGKPAPEASTAKPSSPEPATASEPMEVDRPGTPVPAVEVPELMETASSEQNSDAKPPESAADSTQLTKKGKKKKTVSWPEESKLREYFYFELDETERVNVNKIKDFGEAAKREMLKDREAFETARRLSHDAMEEKVPWVYPKLIDLPNPLVQPGNGSREKFTQAEREKGILQEIFLSKESVPDSPHEPDPESYEPLPPKLIPLDEECTMDEAAYQEGLDPAAASQSPDGAGASKLPPVLANLMGSMGAGKSPQGPNPSSSMNVQEILTSIMGGPNNHKTEELMKQPDYSDKIKHLLGNLQTQPPGPSGVPHGLLGPGPLANGFPPGPKNMQHFPPGGPGPMPGPHGGPGGPNMPPGPGMPGGPRMMGPPPPQRGEFWDPPDGGMRGNPHGDMSSRPVCRHFMLKGSCRYENNCAFYHPGVNGPPLP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias201-249Basic and acidic residues
Compositional bias414-434Polar residues
Compositional bias704-746Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KB566561
EMBL· GenBank· DDBJ
EMP27865.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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