ID CYC_HUMAN Reviewed; 105 AA. AC P99999; A4D166; B2R4I1; P00001; Q6NUR2; Q6NX69; Q96BV4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 142. DE RecName: Full=Cytochrome c; GN Name=CYCS; Synonyms=CYC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2849112; DOI=10.1073/pnas.85.24.9625; RA Evans M.J., Scarpulla R.C.; RT "The human somatic cytochrome c gene: two classes of processed RT pseudogenes demarcate a period of rapid molecular evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 85:9625-9629(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow, Brain, Kidney, Lung, Skeletal muscle, Skin, RC Testis, and Urinary bladder; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2. RC TISSUE=Heart; RX PubMed=13933734; RA Matsubara H., Smith E.L.; RT "The amino acid sequence of human heart cytochrome c."; RL J. Biol. Chem. 237:3575-3576(1962). RN [10] RP PROTEIN SEQUENCE OF 2-105. RC TISSUE=Heart; RX PubMed=14063298; RA Matsubara H., Smith E.L.; RT "Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, RT and the complete amino acid sequence."; RL J. Biol. Chem. 238:2732-2753(1963). RN [11] RP REVIEW ON ROLE IN APOPTOSIS. RX PubMed=9515723; DOI=10.1016/S0014-5793(98)00061-1; RA Skulachev V.P.; RT "Cytochrome c in the apoptotic and antioxidant cascades."; RL FEBS Lett. 423:275-280(1998). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [16] RP STRUCTURE BY NMR. RA Jeng W.-Y., Shiu J.-H., Tsai Y.-H., Chuang W.-J.; RT "Solution structure of reduced recombinant human cytochrome c."; RL Submitted (FEB-2003) to the PDB data bank. RN [17] RP VARIANT THC4 SER-42, IDENTIFICATION BY MASS SPECTROMETRY, RP CHARACTERIZATION OF VARIANT THC4 SER-42, AND X-RAY CRYSTALLOGRAPHY RP (2.75 ANGSTROMS) OF VARIANT THC4 SER-42 AND WILD TYPE. RX PubMed=18345000; DOI=10.1038/ng.103; RA Morison I.M., Cramer Borde E.M.C., Cheesman E.J., Cheong P.L., RA Holyoake A.J., Fichelson S., Weeks R.J., Lo A., Davies S.M.K., RA Wilbanks S.M., Fagerlund R.D., Ludgate M.W., da Silva Tatley F.M., RA Coker M.S.A., Bockett N.A., Hughes G., Pippig D.A., Smith M.P., RA Capron C., Ledgerwood E.C.; RT "A mutation of human cytochrome c enhances the intrinsic apoptotic RT pathway but causes only thrombocytopenia."; RL Nat. Genet. 40:387-389(2008). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the CC cytochrome c heme group can accept an electron from the heme group CC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c CC then transfers this electron to the cytochrome oxidase complex, CC the final protein carrier in the mitochondrial electron-transport CC chain. CC -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti- CC apoptotic members or activation of the pro-apoptotic members of CC the Bcl-2 family leads to altered mitochondrial membrane CC permeability resulting in release of cytochrome c into the CC cytosol. Binding of cytochrome c to Apaf-1 triggers the activation CC of caspase-9, which then accelerates apoptosis by activating other CC caspases. CC -!- INTERACTION: CC O14727:APAF1; NbExp=6; IntAct=EBI-446479, EBI-446492; CC Q07817:BCL2L1; NbExp=2; IntAct=EBI-446479, EBI-78035; CC Q9FKS5:CYC12 (xeno); NbExp=2; IntAct=EBI-446479, EBI-1777995; CC Q6A162:KRT40; NbExp=3; IntAct=EBI-446479, EBI-10171697; CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. CC Note=Loosely associated with the inner membrane. CC -!- PTM: Binds 1 heme group per subunit. CC -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the CC turnover in the reaction with cytochrome c oxidase, down- CC regulating mitochondrial respiration. {ECO:0000250}. CC -!- DISEASE: Thrombocytopenia 4 (THC4) [MIM:612004]: Thrombocytopenia CC is defined by a decrease in the number of platelets in circulating CC blood, resulting in the potential for increased bleeding and CC decreased ability for clotting. {ECO:0000269|PubMed:18345000}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 CC of November 2006; CC URL="http://web.expasy.org/spotlight/back_issues/076"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=An unexpected place - CC Issue 88 of November 2007; CC URL="http://web.expasy.org/spotlight/back_issues/088/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M22877; AAA35732.1; -; Genomic_DNA. DR EMBL; BT006946; AAP35592.1; -; mRNA. DR EMBL; AK311836; BAG34778.1; -; mRNA. DR EMBL; AL713681; CAD28485.1; -; mRNA. DR EMBL; AC007487; AAQ96844.1; -; Genomic_DNA. DR EMBL; CH236948; EAL24239.1; -; Genomic_DNA. DR EMBL; CH471073; EAW93822.1; -; Genomic_DNA. DR EMBL; BC005299; AAH05299.1; -; mRNA. DR EMBL; BC008475; AAH08475.1; -; mRNA. DR EMBL; BC008477; AAH08477.1; -; mRNA. DR EMBL; BC009578; AAH09578.1; -; mRNA. DR EMBL; BC009579; AAH09579.1; -; mRNA. DR EMBL; BC009582; AAH09582.1; -; mRNA. DR EMBL; BC009587; AAH09587.1; -; mRNA. DR EMBL; BC009602; AAH09602.1; -; mRNA. DR EMBL; BC009607; AAH09607.1; -; mRNA. DR EMBL; BC014359; AAH14359.1; -; mRNA. DR EMBL; BC014361; AAH14361.1; -; mRNA. DR EMBL; BC015130; AAH15130.1; -; mRNA. DR EMBL; BC016006; AAH16006.1; -; mRNA. DR EMBL; BC021994; AAH21994.1; -; mRNA. DR EMBL; BC022330; AAH22330.1; -; mRNA. DR EMBL; BC067222; AAH67222.1; -; mRNA. DR EMBL; BC068464; AAH68464.1; -; mRNA. DR EMBL; BC070156; AAH70156.1; -; mRNA. DR EMBL; BC070346; AAH70346.1; -; mRNA. DR EMBL; BC071761; AAH71761.1; -; mRNA. DR CCDS; CCDS5393.1; -. DR PIR; A31764; CCHU. DR RefSeq; NP_061820.1; NM_018947.5. DR UniGene; Hs.437060; -. DR UniGene; Hs.617193; -. DR PDB; 1J3S; NMR; -; A=2-105. DR PDB; 3NWV; X-ray; 1.90 A; A/B/C/D=2-105. DR PDB; 3ZCF; X-ray; 1.65 A; A/B/C/D=2-105. DR PDB; 3ZOO; X-ray; 1.35 A; A/B/C/D=2-105. DR PDBsum; 1J3S; -. DR PDBsum; 3NWV; -. DR PDBsum; 3ZCF; -. DR PDBsum; 3ZOO; -. DR ProteinModelPortal; P99999; -. DR SMR; P99999; 2-105. DR BioGrid; 119922; 30. DR DIP; DIP-29683N; -. DR IntAct; P99999; 14. DR MINT; MINT-3023956; -. DR STRING; 9606.ENSP00000307786; -. DR DrugBank; DB01017; Minocycline. DR PhosphoSite; P99999; -. DR BioMuta; CYCS; -. DR DMDM; 42560196; -. DR MaxQB; P99999; -. DR PaxDb; P99999; -. DR PeptideAtlas; P99999; -. DR PRIDE; P99999; -. DR DNASU; 54205; -. DR Ensembl; ENST00000305786; ENSP00000307786; ENSG00000172115. DR Ensembl; ENST00000409409; ENSP00000386270; ENSG00000172115. DR Ensembl; ENST00000409764; ENSP00000387279; ENSG00000172115. DR GeneID; 54205; -. DR KEGG; hsa:54205; -. DR UCSC; uc003sxl.3; human. DR CTD; 54205; -. DR GeneCards; CYCS; -. DR HGNC; HGNC:19986; CYCS. DR HPA; CAB004222; -. DR HPA; CAB005126; -. DR HPA; CAB018597; -. DR MalaCards; CYCS; -. DR MIM; 123970; gene. DR MIM; 612004; phenotype. DR neXtProt; NX_P99999; -. DR Orphanet; 168629; Autosomal thrombocytopenia with normal platelets. DR PharmGKB; PA134981636; -. DR eggNOG; KOG3453; Eukaryota. DR eggNOG; COG3474; LUCA. DR GeneTree; ENSGT00390000009405; -. DR HOGENOM; HOG000009762; -. DR HOVERGEN; HBG003023; -. DR InParanoid; P99999; -. DR KO; K08738; -. DR OMA; HEYLRNP; -. DR OrthoDB; EOG761BWX; -. DR PhylomeDB; P99999; -. DR TreeFam; TF300226; -. DR Reactome; R-HSA-111457; Release of apoptotic factors from the mitochondria. DR Reactome; R-HSA-111458; Formation of apoptosome. DR Reactome; R-HSA-111459; Activation of caspases through apoptosome-mediated cleavage. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-611105; Respiratory electron transport. DR ChiTaRS; CYCS; human. DR EvolutionaryTrace; P99999; -. DR GeneWiki; Cytochrome_c; -. DR GenomeRNAi; 54205; -. DR NextBio; 56526; -. DR PRO; PR:P99999; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; P99999; -. DR CleanEx; HS_CYCS; -. DR ExpressionAtlas; P99999; baseline and differential. DR Genevisible; P99999; HS. DR GO; GO:0005829; C:cytosol; IMP:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:UniProtKB. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity; IDA:UniProtKB. DR GO; GO:0020037; F:heme binding; TAS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; TAS:UniProtKB. DR GO; GO:0006309; P:apoptotic DNA fragmentation; IMP:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central. DR GO; GO:0044237; P:cellular metabolic process; TAS:Reactome. DR GO; GO:0045333; P:cellular respiration; TAS:UniProtKB. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central. DR GO; GO:0007005; P:mitochondrion organization; TAS:Reactome. DR GO; GO:0006996; P:organelle organization; TAS:Reactome. DR GO; GO:0012501; P:programmed cell death; TAS:Reactome. DR GO; GO:0006470; P:protein dephosphorylation; TAS:GOC. DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome. DR GO; GO:0000302; P:response to reactive oxygen species; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR Gene3D; 1.10.760.10; -; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR002327; Cyt_c_1A/1B. DR PANTHER; PTHR11961; PTHR11961; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR SUPFAM; SSF46626; SSF46626; 1. DR PROSITE; PS51007; CYTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; Complete proteome; KW Direct protein sequencing; Disease mutation; Electron transport; Heme; KW Iron; Metal-binding; Mitochondrion; Phosphoprotein; Polymorphism; KW Reference proteome; Respiratory chain; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:13933734, FT ECO:0000269|PubMed:14063298}. FT CHAIN 2 105 Cytochrome c. FT /FTId=PRO_0000108218. FT METAL 19 19 Iron (heme axial ligand). FT METAL 81 81 Iron (heme axial ligand). FT BINDING 15 15 Heme (covalent). FT BINDING 18 18 Heme (covalent). FT MOD_RES 2 2 N-acetylglycine. FT {ECO:0000269|PubMed:13933734}. FT MOD_RES 49 49 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P62894}. FT MOD_RES 98 98 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P62894}. FT VARIANT 42 42 G -> S (in THC4; increases the pro- FT apoptotic function by triggering caspase FT activation more efficiently than wild- FT type; does not affect the redox FT function). {ECO:0000269|PubMed:18345000}. FT /FTId=VAR_044450. FT VARIANT 56 56 K -> R (in dbSNP:rs11548795). FT /FTId=VAR_048850. FT VARIANT 66 66 M -> L (in 10% of the molecules). FT /FTId=VAR_002204. FT CONFLICT 18 18 C -> Y (in Ref. 8; AAH15130). FT {ECO:0000305}. FT CONFLICT 41 41 T -> I (in Ref. 8; AAH68464). FT {ECO:0000305}. FT HELIX 4 14 {ECO:0000244|PDB:3ZOO}. FT TURN 15 18 {ECO:0000244|PDB:3ZOO}. FT STRAND 23 25 {ECO:0000244|PDB:1J3S}. FT STRAND 28 30 {ECO:0000244|PDB:1J3S}. FT TURN 36 38 {ECO:0000244|PDB:1J3S}. FT HELIX 51 55 {ECO:0000244|PDB:3ZOO}. FT HELIX 62 70 {ECO:0000244|PDB:3ZOO}. FT HELIX 72 75 {ECO:0000244|PDB:3ZOO}. FT HELIX 89 102 {ECO:0000244|PDB:3ZOO}. SQ SEQUENCE 105 AA; 11749 MW; 8EE9689E0102506B CRC64; MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGIIW GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE //