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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 F(1) complex subunit alpha, mitochondrial

UniprotKB/SwissProt ID: P25705 (P25705)

Gene Name: ATP5F1A

Organism: Homo sapiens (Human)

Function: Subunit alpha, 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 (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). 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 (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain (PubMed:37244256). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion. Mitochondrion inner membrane. Cell membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR023366 ATP_synth_asu-like_sf
IPR000793 ATP_synth_asu_C
IPR038376 ATP_synth_asu_C_sf
IPR033732 ATP_synth_F1_a_nt-bd_dom
IPR005294 ATP_synth_F1_asu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR027417 P-loop_NTPase

The S-nitrosylation sites of P25705

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 244 DGSDEKKKLY C IYVAIGQKRS  CCHHHHHHHH H HHCHHHCCCC  2.34% 24105792
37478858
2 294 PLQYLAPYSG C SMGEYFRDNG  CCHHHHHHHH H HHCHHHCCCC  1.76%