Q9NY27 · PP4R2_HUMAN
- ProteinSerine/threonine-protein phosphatase 4 regulatory subunit 2
- GenePPP4R2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids417 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair.
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 | centrosome | |
Cellular Component | chromatin | |
Cellular Component | cytoplasm | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | protein phosphatase 4 complex | |
Molecular Function | protein phosphatase regulator activity | |
Molecular Function | protein-macromolecule adaptor activity | |
Biological Process | mRNA processing | |
Biological Process | protein modification process | |
Biological Process | regulation of double-strand break repair | |
Biological Process | regulation of double-strand break repair via homologous recombination | |
Biological Process | RNA splicing |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase 4 regulatory subunit 2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NY27
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 99 | No effect on RPA2-binding; decrease in PPP4C-binding. | ||||
Sequence: F → A | ||||||
Mutagenesis | 103 | No effect on RPA2-binding; loss of PPP4C-binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 106 | No effect on RPA2-binding, nor on PPP4C-binding. | ||||
Sequence: E → A | ||||||
Natural variant | VAR_051749 | 174 | in dbSNP:rs2306983 | |||
Sequence: P → L | ||||||
Natural variant | VAR_034811 | 282 | in dbSNP:rs34742137 | |||
Sequence: S → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 441 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000299365 | 1-417 | UniProt | Serine/threonine-protein phosphatase 4 regulatory subunit 2 | |||
Sequence: MDVERLQEALKDFEKRGKKEVCPVLDQFLCHVAKTGETMIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNGIPFTIQRLCELLTDPRRNYTGTDKFLRGVEKNVMVVSCVYPSSEKNNSNSLNRMNGVMFPGNSPSYTERSNINGPGTPRPLNRPKVSLSAPMTTNGLPESTDSKEANLQQNEEKNHSDSSTSESEVSSVSPLKNKHPDEDAVEAEGHEVKRLRFDKEGEVRETASQTTSSEISSVMVGETEASSSSQDKDKDSRCTRQHCTEEDEEEDEEEEEESFMTSREMIPERKNQEKESDDALTVNEETSEENNQMEESDVSQAEKDLLHSEGSENEGPVSSSSSDCRETEELVGSNSSKTGEILSESSMENDDEATEVTDEPMEQD | |||||||
Modified residue | 159 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 173 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 183 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 226 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 386 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 388 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complexes PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A and PPP4C-PPP4R2-PPP4R3B. The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with DDX20/GEMIN3 and GEMIN4. Interacts with RPA2; this DNA damage-dependent interaction recruits PPP4C leading to RPA2 dephosphorylation.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NY27 | PPP4C P60510 | 16 | EBI-1048740, EBI-1046072 | |
BINARY | Q9NY27 | PTPA Q15257 | 2 | EBI-1048740, EBI-1774121 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 140-173 | Polar residues | ||||
Sequence: EKNNSNSLNRMNGVMFPGNSPSYTERSNINGPGT | ||||||
Region | 140-417 | Disordered | ||||
Sequence: EKNNSNSLNRMNGVMFPGNSPSYTERSNINGPGTPRPLNRPKVSLSAPMTTNGLPESTDSKEANLQQNEEKNHSDSSTSESEVSSVSPLKNKHPDEDAVEAEGHEVKRLRFDKEGEVRETASQTTSSEISSVMVGETEASSSSQDKDKDSRCTRQHCTEEDEEEDEEEEEESFMTSREMIPERKNQEKESDDALTVNEETSEENNQMEESDVSQAEKDLLHSEGSENEGPVSSSSSDCRETEELVGSNSSKTGEILSESSMENDDEATEVTDEPMEQD | ||||||
Compositional bias | 183-201 | Polar residues | ||||
Sequence: SLSAPMTTNGLPESTDSKE | ||||||
Compositional bias | 202-216 | Basic and acidic residues | ||||
Sequence: ANLQQNEEKNHSDSS | ||||||
Compositional bias | 228-258 | Basic and acidic residues | ||||
Sequence: LKNKHPDEDAVEAEGHEVKRLRFDKEGEVRE | ||||||
Compositional bias | 259-279 | Polar residues | ||||
Sequence: TASQTTSSEISSVMVGETEAS | ||||||
Compositional bias | 280-297 | Basic and acidic residues | ||||
Sequence: SSSQDKDKDSRCTRQHCT | ||||||
Compositional bias | 298-312 | Acidic residues | ||||
Sequence: EEDEEEDEEEEEESF | ||||||
Compositional bias | 313-334 | Basic and acidic residues | ||||
Sequence: MTSREMIPERKNQEKESDDALT | ||||||
Compositional bias | 349-363 | Basic and acidic residues | ||||
Sequence: SDVSQAEKDLLHSEG | ||||||
Compositional bias | 365-396 | Polar residues | ||||
Sequence: ENEGPVSSSSSDCRETEELVGSNSSKTGEILS | ||||||
Compositional bias | 398-417 | Acidic residues | ||||
Sequence: SSMENDDEATEVTDEPMEQD |
Sequence similarities
Belongs to the PPP4R2 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9NY27-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length417
- Mass (Da)46,898
- Last updated2007-09-11 v3
- Checksum75298CD34A202F40
Q9NY27-2
- Name2
- Differences from canonical
- 39-96: MIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNG → I
Q9NY27-3
- Name3
- Differences from canonical
- 1-56: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_027612 | 1-56 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_027613 | 39-96 | in isoform 2 | |||
Sequence: MIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNG → I | ||||||
Compositional bias | 140-173 | Polar residues | ||||
Sequence: EKNNSNSLNRMNGVMFPGNSPSYTERSNINGPGT | ||||||
Compositional bias | 183-201 | Polar residues | ||||
Sequence: SLSAPMTTNGLPESTDSKE | ||||||
Compositional bias | 202-216 | Basic and acidic residues | ||||
Sequence: ANLQQNEEKNHSDSS | ||||||
Compositional bias | 228-258 | Basic and acidic residues | ||||
Sequence: LKNKHPDEDAVEAEGHEVKRLRFDKEGEVRE | ||||||
Compositional bias | 259-279 | Polar residues | ||||
Sequence: TASQTTSSEISSVMVGETEAS | ||||||
Compositional bias | 280-297 | Basic and acidic residues | ||||
Sequence: SSSQDKDKDSRCTRQHCT | ||||||
Compositional bias | 298-312 | Acidic residues | ||||
Sequence: EEDEEEDEEEEEESF | ||||||
Compositional bias | 313-334 | Basic and acidic residues | ||||
Sequence: MTSREMIPERKNQEKESDDALT | ||||||
Compositional bias | 349-363 | Basic and acidic residues | ||||
Sequence: SDVSQAEKDLLHSEG | ||||||
Compositional bias | 365-396 | Polar residues | ||||
Sequence: ENEGPVSSSSSDCRETEELVGSNSSKTGEILS | ||||||
Compositional bias | 398-417 | Acidic residues | ||||
Sequence: SSMENDDEATEVTDEPMEQD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ271448 EMBL· GenBank· DDBJ | CAB93534.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF327345 EMBL· GenBank· DDBJ | AAL56006.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289901 EMBL· GenBank· DDBJ | BAF82590.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471055 EMBL· GenBank· DDBJ | EAW65530.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC100281 EMBL· GenBank· DDBJ | AAI00282.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC110889 EMBL· GenBank· DDBJ | AAI10890.1 EMBL· GenBank· DDBJ | mRNA | ||
BC128136 EMBL· GenBank· DDBJ | AAI28137.1 EMBL· GenBank· DDBJ | mRNA | ||
BC128137 EMBL· GenBank· DDBJ | AAI28138.1 EMBL· GenBank· DDBJ | mRNA |