PPP1CC
entrez
5501
canonical
uniprot
P36873
canonical
ensembl
ENSG00000186298
resolver
ensp
ENSP00000335084
resolver
ensp
ENSP00000341779
resolver
ensp
ENSP00000777972
resolver
ensp
ENSP00000777973
resolver
genesymbol
PPP1CC
resolver
hgnc
HGNC:9283
resolver
uniprot_entry
PP1G_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: Inactivated by binding to URI1. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress. {ECO:0000269|PubMed:15705855, ECO:0000269|PubMed:17936702}.
uniprot
proteins
amino_acid_sequence
MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
function
FUNCTION: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets (PubMed:17936702, PubMed:25012651). Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1 (PubMed:17936702). 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 Ca(2+)/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 (PubMed:20516061). In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation (PubMed:21712997). May dephosphorylate CSNK1D and CSNK1E (By similarity). Regulates the recruitment of the SKA complex to kinetochores (PubMed:28982702). Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Together with PPP1CA (PP1-alpha subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35831509). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35831509). Dephosphorylates MKI67 at the onset of anaphase (PubMed:25012651). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:35831509). {ECO:0000250|UniProtKB:P63087, ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997, ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23499489, ECO:0000269|PubMed:25012651, ECO:0000269|PubMed:28982702, ECO:0000269|PubMed:35768504, ECO:0000269|PubMed:35831509}.
uniprot
proteins
mass_dalton
36984
uniprot
proteins
mutagenesis
MUTAGEN 50; /note="P->R: Promotes SMP complex formation."; /evidence="ECO:0000269|PubMed:35768504"; MUTAGEN 125; /note="H->A: Loss of activity."; /evidence="ECO:0000269|PubMed:11739654"; MUTAGEN 273; /note="C->A,S,L: Abolishes interaction with microcystin toxin."; /evidence="ECO:0000269|PubMed:7556599
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by NEK2. {ECO:0000269|PubMed:15659832}.
uniprot
proteins
protein_family
PP-1 subfamily
uniprot
proteins
protein_family
PPP phosphatase family
uniprot
proteins
pubmed
11535607
uniprot
proteins
pubmed
11564868
uniprot
proteins
pubmed
11739654
uniprot
proteins
pubmed
12226088
uniprot
proteins
pubmed
12529430
uniprot
proteins
pubmed
15280359
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15659832
uniprot
proteins
pubmed
15705855
uniprot
proteins
pubmed
16492807
uniprot
proteins
pubmed
17283141
uniprot
proteins
pubmed
17936702
uniprot
proteins
pubmed
17965019
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19377461
uniprot
proteins
pubmed
20516061
uniprot
proteins
pubmed
20926688
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21712997
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23396208
uniprot
proteins
pubmed
23499489
uniprot
proteins
pubmed
23506001
uniprot
proteins
pubmed
23789093
uniprot
proteins
pubmed
23846654
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24336203
uniprot
proteins
pubmed
24867636
uniprot
proteins
pubmed
25012651
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28982702
uniprot
proteins
pubmed
30100357
uniprot
proteins
pubmed
34260926
uniprot
proteins
pubmed
35768504
uniprot
proteins
pubmed
35831509
uniprot
proteins
pubmed
7500362
uniprot
proteins
pubmed
7556599
uniprot
proteins
pubmed
8111128
uniprot
proteins
pubmed
8394140
uniprot
proteins
pubmed
9414128
uniprot
proteins
sequence_length
323
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11739654}. Nucleus. Nucleus, nucleolus {ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:20926688, ECO:0000269|PubMed:23789093}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11739654}. Nucleus speckle {ECO:0000269|PubMed:11739654}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12529430}. Cleavage furrow {ECO:0000269|PubMed:12529430}. Midbody {ECO:0000269|PubMed:12529430}. Mitochondrion {ECO:0000269|PubMed:17936702}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:23789093}. Note=Colocalizes with SPZ1 in the nucleus (By similarity). Colocalizes with URI1 at mitochondrion (PubMed:17936702). Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments (PubMed:11739654). Highly mobile in cells and can be relocalized through interaction with targeting subunits (PubMed:17965019). In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles (PubMed:11739654). Shows a dynamic targeting to specific sites throughout the cell cycle (PubMed:12529430). Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis (PubMed:12529430). Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase (PubMed:12529430). Also accumulates at the cleavage furrow and midbody by telophase (PubMed:12529430). Colocalizes with DYNLT4 in the microtubule organizing center (MTOC) (PubMed:23789093). {ECO:0000250|UniProtKB:P63087, ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:12529430, ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:17965019, ECO:0000269|PubMed:23789093}.
uniprot
proteins