CPLM-010742

Genbank Nucleotide ID

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
9	GDVEKGKKIFIMKCS	ubiquitination	[1]
40	LHGLFGRKTGQAPGY	ubiquitination	[1, 2]
54	YSYTAANKNKGIIWG	ubiquitination	[2, 3]
56	YTAANKNKGIIWGED	ubiquitination	[1, 2]
73	MEYLENPKKYIPGTK	ubiquitination	[2]
80	KKYIPGTKMIFVGIK	ubiquitination	[1, 4]
87	KMIFVGIKKKEERAD	ubiquitination	[2, 4]
88	MIFVGIKKKEERADL	acetylation	[5]
89	IFVGIKKKEERADLI	acetylation	[5]
100	ADLIAYLKKATNE**	acetylation	[5, 6]
100	ADLIAYLKKATNE**	ubiquitination	[2, 4]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]

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.

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 (By similarity).
MOD_RES 98 98 Phosphotyrosine (By similarity).

3D-structure; Acetylation; Apoptosis; Complete proteome; Direct protein sequencing; Disease mutation; Electron transport; Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome; Respiratory chain; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IMP:UniProtKB.
GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO:0005758; C:mitochondrial intermembrane space; TAS:UniProtKB.
GO:0005634; C:nucleus; IDA:LIFEdb.
GO:0000159; C:protein phosphatase type 2A complex; TAS:UniProtKB.
GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; IDA:UniProtKB.
GO:0020037; F:heme binding; TAS:UniProtKB.
GO:0005506; F:iron ion binding; IEA:InterPro.
GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; TAS:UniProtKB.
GO:0006309; P:apoptotic DNA fragmentation; IMP:UniProtKB.
GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
GO:0044281; P:small molecule metabolic process; TAS:Reactome.

IPR002327; Cyt_c_1A/1B.
IPR009056; Cyt_c_dom.
IPR003088; Cyt_c_I.

PF00034; Cytochrom_C

PR00604; CYTCHRMECIAB.