Q8R3G1 · PP1R8_MOUSE
- ProteinNuclear inhibitor of protein phosphatase 1
- GenePpp1r8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids351 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nuclear speck | |
Cellular Component | spliceosomal complex | |
Molecular Function | DNA binding | |
Molecular Function | mRNA binding | |
Molecular Function | protein phosphatase regulator activity | |
Molecular Function | protein serine/threonine phosphatase inhibitor activity | |
Biological Process | cell population proliferation | |
Biological Process | mRNA processing | |
Biological Process | negative regulation of protein dephosphorylation | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameNuclear inhibitor of protein phosphatase 1
- Short namesNIPP-1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8R3G1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mainly, but not exclusively, nuclear.
Keywords
- Cellular component
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.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000071506 | 1-351 | Nuclear inhibitor of protein phosphatase 1 | |||
Sequence: MAAAVNSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEKMGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRMEGSGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSETGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVAINPTPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI | ||||||
Modified residue | 161 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 178 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 199 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 204 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 249 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 264 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 335 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
May be inactivated by phosphorylation on Ser-199 or Ser-204.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-142 | Interaction with CDC5L, SF3B1 and MELK | ||||
Sequence: MAAAVNSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEK | ||||||
Domain | 49-101 | FHA | ||||
Sequence: YLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRL | ||||||
Region | 143-224 | Interaction with EED | ||||
Sequence: MGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRN | ||||||
Motif | 185-209 | Nuclear localization signal 1 | ||||
Sequence: GNLDIQRPKRKRKNSRVTFSEDDEI | ||||||
Region | 191-200 | Involved in PP-1 inhibition | ||||
Sequence: RPKRKRKNSR | ||||||
Region | 200-203 | Involved in PP-1 binding | ||||
Sequence: RVTF | ||||||
Motif | 210-240 | Nuclear localization signal 2 | ||||
Sequence: INPEDVDPSVGRFRNMVQTAVVPVKKKRMEG | ||||||
Region | 310-329 | Interaction with EED | ||||
Sequence: AVAINPTPNPAVYNPEAVNE | ||||||
Region | 314-351 | Disordered | ||||
Sequence: NPTPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI | ||||||
Region | 330-351 | RNA-binding | ||||
Sequence: PKKKKYAKEAWPGKKPTPSLLI | ||||||
Region | 331-337 | Involved in PP-1 inhibition | ||||
Sequence: KKKKYAK |
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 statusComplete
- Length351
- Mass (Da)38,528
- Last updated2002-06-01 v1
- ChecksumD3A3BC4B2DF467A2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A2ADR8 | A2ADR8_MOUSE | Ppp1r8 | 350 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC025479 EMBL· GenBank· DDBJ | AAH25479.1 EMBL· GenBank· DDBJ | mRNA | ||
AK032022 EMBL· GenBank· DDBJ | BAC27653.1 EMBL· GenBank· DDBJ | mRNA |