\
logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

Read more...


Protein Name: Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

UniprotKB/SwissProt ID: P36873 (P36873)

Gene Name: PPP1CC

Organism: Homo sapiens (Human)

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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus speckle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Mitochondrion. Cytoplasm, cytoskeleton, microtubule organizing center

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR050341 PP1_catalytic_subunit
IPR006186 Ser/Thr-sp_prot-phosphatase
IPR031675 STPPase_N

The S-nitrosylation sites of P36873

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 127 NFFLLRGNHE C ASINRIYGFY  CCCHHHCCHH H HHHHHHHHHC  2.53% 19483679
2 140 INRIYGFYDE C KRRYNIKLWK  CCCHHHCCHH H HHHHHHHHHC  3.67%
3 155 NIKLWKTFTD C FNCLPIAAIV  CCCHHHCCHH H HHHHHHHHHC  2.1% 19483679
4 158 LWKTFTDCFN C LPIAAIVDEK  CCCHHHCCHH H HHHHHHHHHC  2.1% 19483679
5 171 IAAIVDEKIF C CHGGLSPDLQ  CCCHHHCCHH H HHHHHHHHHC  1.58%
6 172 AAIVDEKIFC C HGGLSPDLQS  CCCHHHCCHH H HHHHHHHHHC  2.02%
7 202 PTDVPDQGLL C DLLWSDPDKD  CCCHHHCCHH H HHHHHHHHHC  4.1%
8 245 FLHKHDLDLI C RAHQVVEDGY  CCCHHHCCHH H HHHHHHHHHC  4.01% 19483679
9 62 LLELEAPLKI C GDIHGQYYDL  CCCHHHCCHH H HHHHHHHHHC  3.71%