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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.

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

UniprotKB/SwissProt ID: P62140 (P62140)

Gene Name: PPP1CB

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. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. 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. 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). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35831509, PubMed:36175670). 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, PubMed:36175670). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:36175670)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus

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 P62140

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 126 NFFLLRGNHE C ASINRIYGFY   
2 139 INRIYGFYDE C KRRFNIKLWK   
3 154 NIKLWKTFTD C FNCLPIAAIV   
4 157 LWKTFTDCFN C LPIAAIVDEK   
5 170 IAAIVDEKIF C CHGGLSPDLQ   
6 171 AAIVDEKIFC C HGGLSPDLQS   
7 201 PTDVPDTGLL C DLLWSDPDKD   
8 244 FLNRHDLDLI C RAHQVVEDGY   
9 61 LLELEAPLKI C GDIHGQYTDL