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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: PP1B_RABIT (P62143)

Gene Name: PPP1CB

Organism: Oryctolagus cuniculus (Rabbit).

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 (By similarity).

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm (By similarity). Nucleus (By similarity). Nucleus, nucleoplasm (By similarity). Nucleus, nucleolus (By similarity). Note=Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 reloca

Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR004843
IPR006186

The S-nitrosylation sites of PP1B_RABIT

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1126NFFLLRGNHE C ASINRIYGFY EEEEEECCCH H HHHHHHCCHH 2.53%N/A21278135in vitro
2201PTDVPDTGLL C DLLWSDPDKD CCCCCCHHHH H HHHHHCCCCC 4.10%N/A21278135in vitro
3244FLNRHDLDLI C RAHQVVEDGY HHHHCCCEEE E HHHHHHHHHH 4.01%N/A21278135in vitro