P63088 · PP1G_RAT
- ProteinSerine/threonine-protein phosphatase PP1-gamma catalytic subunit
- GenePpp1cc
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids323 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Regulates the recruitment of the SKA complex to kinetochores (By similarity).
Isoform 2
Required for normal male fertility.
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Activity regulation
Inactivated by binding to URI1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 66 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 92 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 124 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 125 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 173 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 248 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase PP1-gamma catalytic subunit
- EC number
- Short namesPP-1G
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP63088
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with SPZ1 in the nucleus. Colocalizes with URI1 at mitochondrion. Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments. Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles. Shows a dynamic targeting to specific sites throughout the cell cycle. Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis. Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase. Also accumulates at the cleavage furrow and midbody by telophase.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000058789 | 2-323 | Serine/threonine-protein phosphatase PP1-gamma catalytic subunit | |||
Sequence: ADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK | ||||||
Modified residue | 307 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 311 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated by NEK2.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 2 is expressed only in testis, in the late spermatocytes and early spematids (at protein level).
Gene expression databases
Interaction
Subunit
PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in sliver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R3B, PPP1R7 and CDCA2. Isoform 2 interacts with SPZ1. Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with NOM1 and PPP1R8. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8 (By similarity).
Interacts with NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner (By similarity).
Interacts with FOXP3 (By similarity).
Interacts with TMEM225 (via RVxF motif) (By similarity).
Interacts with MKI67 (By similarity).
Interacts with RRP1B; this targets PPP1CC to the nucleolus (By similarity).
Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity) (PubMed:10504266, PubMed:10585469, PubMed:7720853, PubMed:9841883).
Interacts with DYNLT4 (By similarity).
Interacts (via RVxF motif) with FIRRM; regulates PLK1 kinase activity (By similarity).
Interacts with NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner (By similarity).
Interacts with FOXP3 (By similarity).
Interacts with TMEM225 (via RVxF motif) (By similarity).
Interacts with MKI67 (By similarity).
Interacts with RRP1B; this targets PPP1CC to the nucleolus (By similarity).
Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity) (PubMed:10504266, PubMed:10585469, PubMed:7720853, PubMed:9841883).
Interacts with DYNLT4 (By similarity).
Interacts (via RVxF motif) with FIRRM; regulates PLK1 kinase activity (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P63088 | Grm1 P23385 | 15 | EBI-80049, EBI-4410410 | |
BINARY | P63088 | Grm5 P31424 | 19 | EBI-80049, EBI-2902734 | |
BINARY | P63088 | Grm7 P35400 | 4 | EBI-80049, EBI-6936416 | |
BINARY | P63088 | mGluR7 Q63337 | 11 | EBI-80049, EBI-6935714 | |
XENO | P63088 | OGT O15294 | 3 | EBI-80049, EBI-539828 | |
BINARY | P63088 | Ppp1r9a O35867 | 2 | EBI-80049, EBI-7092421 | |
BINARY | P63088 | Ppp1r9b O35274 | 3 | EBI-80049, EBI-80022 | |
BINARY | P63088 | Tor1aip1 Q5PQX1 | 2 | EBI-80049, EBI-15644430 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 302-323 | Disordered | ||||
Sequence: KKPNATRPVTPPRGMITKQAKK |
Sequence similarities
Belongs to the PPP phosphatase family. PP-1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P63088-1
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
- SynonymsGamma-1
- Length323
- Mass (Da)36,984
- Last updated2004-09-13 v1
- Checksum4E28412C16898615
P63088-2
- Name2
- SynonymsGamma-2
- Differences from canonical
- 315-323: GMITKQAKK → VGSGLNPSIQKASNYRNNTVLYE
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JVK2 | A0A0G2JVK2_RAT | Ppp1cc | 332 | ||
A0A8I6ACH2 | A0A8I6ACH2_RAT | Ppp1cc | 311 | ||
A0A8I5ZX24 | A0A8I5ZX24_RAT | Ppp1cc | 328 | ||
A0A8I5ZJ60 | A0A8I5ZJ60_RAT | Ppp1cc | 308 | ||
A0A8I5ZSW1 | A0A8I5ZSW1_RAT | Ppp1cc | 332 |
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D90165 EMBL· GenBank· DDBJ | BAA14196.1 EMBL· GenBank· DDBJ | mRNA | ||
D90166 EMBL· GenBank· DDBJ | BAA14197.1 EMBL· GenBank· DDBJ | mRNA |