\
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: Cytochrome c1, heme protein, mitochondrial

UniprotKB/SwissProt ID: P08574 (P08574)

Gene Name: CYC1

Organism: Homo sapiens (Human)

Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion inner membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR036909 Cyt_c-like_dom_sf
IPR002326 Cyt_c1
IPR021157 Cyt_c1_TM_anchor_C

The S-nitrosylation sites of P08574

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 139 FVAYRHLVGV C YTEDEAKELA   
2 219 DYVFSLLTGY C EPPTGVSLRE   
3 271 ATMSQIAKDV C TFLRWASEPE