Q8R3G1 · PP1R8_MOUSE

  • Protein
    Nuclear inhibitor of protein phosphatase 1
  • Gene
    Ppp1r8
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Essential for cell proliferation and early embryonic development.

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 Componentnuclear speck
Cellular Componentspliceosomal complex
Molecular FunctionDNA binding
Molecular FunctionmRNA binding
Molecular Functionprotein phosphatase regulator activity
Molecular Functionprotein serine/threonine phosphatase inhibitor activity
Biological Processcell population proliferation
Biological ProcessmRNA processing
Biological Processnegative regulation of protein dephosphorylation
Biological ProcessRNA splicing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Nuclear inhibitor of protein phosphatase 1
  • Short names
    NIPP-1
  • Alternative names
    • Protein phosphatase 1 regulatory inhibitor subunit 8

Gene names

    • Name
      Ppp1r8
    • Synonyms
      Nipp1

Organism names

  • Taxonomic identifier
  • Strains
    • FVB/N
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8R3G1
  • Secondary accessions
    • Q8C087

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Nucleus speckle
Note: Mainly, but not exclusively, nuclear.

Keywords

Phenotypes & Variants

Disruption phenotype

Mice display a retarded growth and embryonic lethality at E6.5, due to defects in proliferation rate.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000715061-351Nuclear inhibitor of protein phosphatase 1
Modified residue161Phosphothreonine
Modified residue178Phosphoserine
Modified residue199Phosphoserine
Modified residue204Phosphoserine
Modified residue249Phosphoserine
Modified residue264Phosphotyrosine
Modified residue335Phosphotyrosine

Post-translational modification

May be inactivated by phosphorylation on Ser-199 or Ser-204.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with phosphorylated CDC5L, SF3B1 and MELK. Part of the spliceosome. Interacts with PPP1CA, PPP1CB and PPP1CC (By similarity).
Interacts with EED. Part of a complex consisting of PPP1R8, EED, HDAC2 and PP-1

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain, motif.

TypeIDPosition(s)Description
Region1-142Interaction with CDC5L, SF3B1 and MELK
Domain49-101FHA
Region143-224Interaction with EED
Motif185-209Nuclear localization signal 1
Region191-200Involved in PP-1 inhibition
Region200-203Involved in PP-1 binding
Motif210-240Nuclear localization signal 2
Region310-329Interaction with EED
Region314-351Disordered
Region330-351RNA-binding
Region331-337Involved in PP-1 inhibition

Domain

Has a basic N- and C-terminal and an acidic central domain.
The FHA domain mediates interactions with threonine-phosphorylated MELK.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    351
  • Mass (Da)
    38,528
  • Last updated
    2002-06-01 v1
  • Checksum
    D3A3BC4B2DF467A2
MAAAVNSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEKMGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRMEGSGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSETGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVAINPTPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A2ADR8A2ADR8_MOUSEPpp1r8350

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC025479
EMBL· GenBank· DDBJ
AAH25479.1
EMBL· GenBank· DDBJ
mRNA
AK032022
EMBL· GenBank· DDBJ
BAC27653.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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