CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009611
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytochrome c 
Protein Synonyms/Alias
  
Gene Name
 CYCS 
Gene Synonyms/Alias
 CYC 
Created Date
 July 27, 2013 
Organism
 Bos taurus (Bovine) 
NCBI Taxa ID
 9913 
Lysine Modification
Position
Peptide
Type
References
6**MGDVEKGKKIFVQacetylation[1]
8MGDVEKGKKIFVQKCacetylation[1]
9GDVEKGKKIFVQKCAacetylation[1]
14GKKIFVQKCAQCHTVacetylation[1]
23AQCHTVEKGGKHKTGacetylation[1, 2]
26HTVEKGGKHKTGPNLacetylation[1]
28VEKGGKHKTGPNLHGacetylation[1]
40LHGLFGRKTGQAPGFacetylation[1]
54FSYTDANKNKGITWGacetylation[1]
56YTDANKNKGITWGEEacetylation[1]
73MEYLENPKKYIPGTKacetylation[1]
74EYLENPKKYIPGTKMacetylation[1]
80KKYIPGTKMIFAGIKacetylation[1]
87KMIFAGIKKKGEREDacetylation[1]
88MIFAGIKKKGEREDLacetylation[1]
89IFAGIKKKGEREDLIacetylation[1, 3]
100EDLIAYLKKATNE**acetylation[1]
101DLIAYLKKATNE***acetylation[1]
Reference
 [1] Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc1, and cytochrome c1. Differential acetylation of lysyl residues in free and complexed cytochrome c.
 Rieder R, Bosshard HR.
 J Biol Chem. 1980 May 25;255(10):4732-9. [PMID: 6246081]
 [2] Studies on chemically modified cytochrome c. I. The acetylated cytochrome c.
 Wada K, Okunuki K.
 J Biochem. 1968 Nov;64(5):667-81. [PMID: 4303654]
 [3] Partial acetylation of lysine residues improves intraprotein cross-linking.
 Guo X, Bandyopadhyay P, Schilling B, Young MM, Fujii N, Aynechi T, Guy RK, Kuntz ID, Gibson BW.
 Anal Chem. 2008 Feb 15;80(4):951-60. [PMID: 18201069
Functional Description
 Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. 
Sequence Annotation
 METAL 19 19 Iron (heme axial ligand).
 METAL 81 81 Iron (heme axial ligand).
 BINDING 15 15 Heme (covalent).
 BINDING 18 18 Heme (covalent).
 MOD_RES 2 2 N-acetylglycine.
 MOD_RES 49 49 Phosphotyrosine.
 MOD_RES 98 98 Phosphotyrosine.  
Keyword
 3D-structure; Acetylation; Apoptosis; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome; Respiratory chain; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 105 AA 
Protein Sequence
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW 60
GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE 105 
Gene Ontology
 GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
 GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 
Interpro
 IPR002327; Cyt_c_1A/1B.
 IPR009056; Cyt_c_dom.
 IPR003088; Cyt_c_I. 
Pfam
 PF00034; Cytochrom_C 
SMART
  
PROSITE
 PS51007; CYTC 
PRINTS
 PR00604; CYTCHRMECIAB.