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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: ATP synthase peripheral stalk subunit OSCP, mitochondrial

UniprotKB/SwissProt ID: Q9DB20 (Q9DB20)

Gene Name: Atp5po

Organism: Mus musculus (Mouse)

Function: Subunit OSCP, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (By similarity). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion. Mitochondrion inner membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR026015 ATP_synth_OSCP/delta_N_sf
IPR020781 ATPase_OSCP/d_CS
IPR000711 ATPase_OSCP/dsu

The S-nitrosylation sites of Q9DB20

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 141 IMSVHRGEVP C TVTTASPLDD  CCCCCCCCCH H HHHHCCHHHH  6.04% 22588120
21278135