\
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: ATP synthase subunit beta

UniprotKB/SwissProt ID: A0A3Q7FVP3 (A0A3Q7FVP3)

Gene Name:

Organism: Solanum lycopersicum (Tomato)

Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits Produces ATP from ADP in the presence of a proton gradient across the membrane

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion inner membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR003593 AAA+_ATPase
IPR055190 ATP-synt_VA_C
IPR042079 ATP_synt_F1_beta_sf
IPR020971 ATP_synth_F1_beta_su
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR050053 ATPase_alpha/beta_chains
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
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase

The S-nitrosylation sites of A0A3Q7FVP3

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 310 KLGEKQSESK C ALVYGQMNEP