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 27-MAR-2024, entry version 200. DE RecName: Full=Cytochrome c; GN Name=CYCS; Synonyms=CYC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 pseudogenes RT 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 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., 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., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA 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., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., 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., Mural R.J., RA 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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, and the RT 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., Walther T.C., RA 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., Buerckstuemmer T., RA 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 MUTAGENESIS OF LYS-6; PHE-11; CYS-15; CYS-18 AND HIS-19, AND HEME-BINDING. RX PubMed=23150584; DOI=10.1073/pnas.1213897109; RA San Francisco B., Bretsnyder E.C., Kranz R.G.; RT "Human mitochondrial holocytochrome c synthase's heme binding, maturation RT determinants, and complex formation with cytochrome c."; RL Proc. Natl. Acad. Sci. U.S.A. 110:E788-E797(2013). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] 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., Ayoub D., RA 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 [18] 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 [19] RP VARIANT THC4 SER-42, IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION RP OF VARIANT THC4 SER-42, AND X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF RP 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., Capron C., RA Ledgerwood E.C.; RT "A mutation of human cytochrome c enhances the intrinsic apoptotic pathway RT but causes only thrombocytopenia."; RL Nat. Genet. 40:387-389(2008). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome CC c heme group can accept an electron from the heme group of the CC cytochrome c1 subunit of cytochrome reductase. Cytochrome c then CC transfers this electron to the cytochrome oxidase complex, the final CC protein carrier in the mitochondrial electron-transport chain. CC -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic CC members or activation of the pro-apoptotic members of the Bcl-2 family CC leads to altered mitochondrial membrane permeability resulting in CC release of cytochrome c into the cytosol. Binding of cytochrome c to CC Apaf-1 triggers the activation of caspase-9, which then accelerates CC apoptosis by activating other caspases. CC -!- INTERACTION: CC P99999; O14727: APAF1; NbExp=6; IntAct=EBI-446479, EBI-446492; CC P99999; P05067: APP; NbExp=3; IntAct=EBI-446479, EBI-77613; CC P99999; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-446479, EBI-10254793; CC P99999; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-446479, EBI-10693038; CC P99999; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-446479, EBI-18036948; CC P99999; Q96BR5: COA7; NbExp=3; IntAct=EBI-446479, EBI-6269632; CC P99999; Q9UKG9-2: CROT; NbExp=3; IntAct=EBI-446479, EBI-25835363; CC P99999; O00303: EIF3F; NbExp=3; IntAct=EBI-446479, EBI-711990; CC P99999; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-446479, EBI-8468186; CC P99999; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-446479, EBI-6425864; CC P99999; P06241: FYN; NbExp=3; IntAct=EBI-446479, EBI-515315; CC P99999; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-446479, EBI-743960; CC P99999; Q6A162: KRT40; NbExp=6; IntAct=EBI-446479, EBI-10171697; CC P99999; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-446479, EBI-2510853; CC P99999; Q8IYG6: LRRC56; NbExp=3; IntAct=EBI-446479, EBI-14752528; CC P99999; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-446479, EBI-16439278; CC P99999; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-446479, EBI-25835557; CC P99999; Q9BUL5: PHF23; NbExp=3; IntAct=EBI-446479, EBI-722852; CC P99999; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-446479, EBI-25835994; CC P99999; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-446479, EBI-10248967; CC P99999; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-446479, EBI-9089805; CC P99999; P37840: SNCA; NbExp=3; IntAct=EBI-446479, EBI-985879; CC P99999; Q13573: SNW1; NbExp=3; IntAct=EBI-446479, EBI-632715; CC P99999; Q92797-2: SYMPK; NbExp=3; IntAct=EBI-446479, EBI-21560407; CC P99999; O43829: ZBTB14; NbExp=3; IntAct=EBI-446479, EBI-10176632; CC P99999; Q9FKS5: CYC1-2; Xeno; NbExp=2; IntAct=EBI-446479, EBI-1777995; CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely CC associated with the inner membrane. CC -!- PTM: Binds 1 heme c group covalently 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-regulating CC mitochondrial respiration. {ECO:0000250}. CC -!- DISEASE: Thrombocytopenia 4 (THC4) [MIM:612004]: A form of CC thrombocytopenia, a hematologic disorder defined by a decrease in the CC number of platelets in circulating blood, resulting in the potential CC for increased bleeding and decreased ability for clotting. CC {ECO:0000269|PubMed:18345000}. Note=The disease is caused by variants CC affecting the gene 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 of CC November 2006; CC URL="https://web.expasy.org/spotlight/back_issues/076"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=An unexpected place - Issue CC 88 of November 2007; CC URL="https://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 PDB; 1J3S; NMR; -; A=2-105. DR PDB; 2N3Y; NMR; -; A=2-105. DR PDB; 2N9I; NMR; -; A=2-105. DR PDB; 2N9J; 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 PDB; 5EXQ; X-ray; 1.60 A; A/B=2-105. DR PDB; 5O10; X-ray; 1.36 A; A/B=2-105. DR PDB; 5TY3; X-ray; 1.25 A; A/B=2-105. DR PDB; 6DUJ; X-ray; 1.82 A; A/C=2-105. DR PDB; 6ECJ; X-ray; 2.70 A; A/B/C/D/E/F/G/H=2-105. DR PDB; 6XNK; X-ray; 2.08 A; A/C/E/G=2-105. DR PDBsum; 1J3S; -. DR PDBsum; 2N3Y; -. DR PDBsum; 2N9I; -. DR PDBsum; 2N9J; -. DR PDBsum; 3NWV; -. DR PDBsum; 3ZCF; -. DR PDBsum; 3ZOO; -. DR PDBsum; 5EXQ; -. DR PDBsum; 5O10; -. DR PDBsum; 5TY3; -. DR PDBsum; 6DUJ; -. DR PDBsum; 6ECJ; -. DR PDBsum; 6XNK; -. DR AlphaFoldDB; P99999; -. DR BMRB; P99999; -. DR SASBDB; P99999; -. DR SMR; P99999; -. DR BioGRID; 119922; 159. DR ComplexPortal; CPX-3762; Apoptosome. DR CORUM; P99999; -. DR DIP; DIP-29683N; -. DR IntAct; P99999; 68. DR MINT; P99999; -. DR STRING; 9606.ENSP00000307786; -. DR BindingDB; P99999; -. DR ChEMBL; CHEMBL2189163; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB03317; Ferroheme C. DR DrugBank; DB03366; Imidazole. DR DrugBank; DB01017; Minocycline. DR DrugBank; DB02110; Protoporphyrin Ix Containing Co. DR DrugBank; DB03977; Trimethyllysine. DR DrugBank; DB03934; Zinc protoporphyrin. DR DrugBank; DB04249; Zinc Substituted Heme C. DR DrugCentral; P99999; -. DR MoonDB; P99999; Curated. DR TCDB; 1.A.132.1.1; the azolectin:cytochrome c pore (accp) family. DR GlyGen; P99999; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P99999; -. DR PhosphoSitePlus; P99999; -. DR SwissPalm; P99999; -. DR BioMuta; CYCS; -. DR DMDM; 42560196; -. DR EPD; P99999; -. DR jPOST; P99999; -. DR MassIVE; P99999; -. DR MaxQB; P99999; -. DR PaxDb; 9606-ENSP00000307786; -. DR PeptideAtlas; P99999; -. DR ProteomicsDB; 57831; -. DR Pumba; P99999; -. DR TopDownProteomics; P99999; -. DR ABCD; P99999; 2 sequenced antibodies. DR Antibodypedia; 3917; 1613 antibodies from 47 providers. DR DNASU; 54205; -. DR Ensembl; ENST00000305786.7; ENSP00000307786.2; ENSG00000172115.9. DR Ensembl; ENST00000409409.5; ENSP00000386270.1; ENSG00000172115.9. DR Ensembl; ENST00000409764.5; ENSP00000387279.1; ENSG00000172115.9. DR GeneID; 54205; -. DR KEGG; hsa:54205; -. DR MANE-Select; ENST00000305786.7; ENSP00000307786.2; NM_018947.6; NP_061820.1. DR UCSC; uc003sxl.4; human. DR AGR; HGNC:19986; -. DR CTD; 54205; -. DR DisGeNET; 54205; -. DR GeneCards; CYCS; -. DR HGNC; HGNC:19986; CYCS. DR HPA; ENSG00000172115; Tissue enhanced (tongue). DR MalaCards; CYCS; -. DR MIM; 123970; gene. DR MIM; 612004; phenotype. DR neXtProt; NX_P99999; -. DR OpenTargets; ENSG00000172115; -. DR Orphanet; 168629; Autosomal thrombocytopenia with normal platelets. DR PharmGKB; PA134981636; -. DR VEuPathDB; HostDB:ENSG00000172115; -. DR eggNOG; KOG3453; Eukaryota. DR GeneTree; ENSGT00390000009405; -. DR InParanoid; P99999; -. DR OMA; WGCPASE; -. DR OrthoDB; 4150at2759; -. DR PhylomeDB; P99999; -. DR TreeFam; TF300226; -. DR BioCyc; MetaCyc:ENSG00000172115-MONOMER; -. DR PathwayCommons; P99999; -. 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-111463; SMAC (DIABLO) binds to IAPs. DR Reactome; R-HSA-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species. DR Reactome; R-HSA-5620971; Pyroptosis. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-611105; Respiratory electron transport. DR Reactome; R-HSA-9627069; Regulation of the apoptosome activity. DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. DR SignaLink; P99999; -. DR SIGNOR; P99999; -. DR BioGRID-ORCS; 54205; 529 hits in 1082 CRISPR screens. DR ChiTaRS; CYCS; human. DR EvolutionaryTrace; P99999; -. DR GeneWiki; Cytochrome_c; -. DR GenomeRNAi; 54205; -. DR Pharos; P99999; Tchem. DR PRO; PR:P99999; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P99999; Protein. DR Bgee; ENSG00000172115; Expressed in mucosa of transverse colon and 181 other cell types or tissues. DR ExpressionAtlas; P99999; baseline and differential. DR GO; GO:0043293; C:apoptosome; IPI:ComplexPortal. DR GO; GO:0005829; C:cytosol; IDA:ARUK-UCL. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:CAFA. DR GO; GO:0005739; C:mitochondrion; IDA:ARUK-UCL. DR GO; GO:0005634; C:nucleus; IDA:LIFEdb. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. 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:0045333; P:cellular respiration; TAS:UniProtKB. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; NAS:ComplexPortal. 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 Gene3D; 1.10.760.10; Cytochrome c-like domain; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR002327; Cyt_c_1A/1B. DR PANTHER; PTHR11961; CYTOCHROME C; 1. DR PANTHER; PTHR11961:SF29; CYTOCHROME C; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR SUPFAM; SSF46626; Cytochrome c; 1. DR PROSITE; PS51007; CYTC; 1. DR Genevisible; P99999; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; Direct protein sequencing; KW Disease variant; Electron transport; Heme; Iron; Metal-binding; KW Mitochondrion; Phosphoprotein; Reference proteome; Respiratory chain; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:13933734, FT ECO:0000269|PubMed:14063298" FT CHAIN 2..105 FT /note="Cytochrome c" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT /id="PRO_0000108218" FT BINDING 15 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, FT ECO:0000269|PubMed:23150584" FT BINDING 18 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, FT ECO:0000269|PubMed:23150584" FT BINDING 19 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433, FT ECO:0000269|PubMed:23150584" FT BINDING 81 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000269|PubMed:13933734" FT MOD_RES 49 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62894" FT MOD_RES 56 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P62897" FT MOD_RES 73 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62897" FT MOD_RES 73 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62897" FT MOD_RES 98 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62894" FT MOD_RES 100 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62897" FT VARIANT 42 FT /note="G -> S (in THC4; increases the pro-apoptotic FT function by triggering caspase activation more efficiently FT than wild-type; does not affect the redox function; FT dbSNP:rs121918552)" FT /evidence="ECO:0000269|PubMed:18345000" FT /id="VAR_044450" FT VARIANT 56 FT /note="K -> R (in dbSNP:rs11548795)" FT /id="VAR_048850" FT VARIANT 66 FT /note="M -> L" FT /id="VAR_002204" FT MUTAGEN 6 FT /note="K->A,D,R: No effect on covalent heme attachment." FT /evidence="ECO:0000269|PubMed:23150584" FT MUTAGEN 11 FT /note="F->A: Decreased covalent heme attachment." FT /evidence="ECO:0000269|PubMed:23150584" FT MUTAGEN 11 FT /note="F->Y: No effect on covalent heme attachment." FT /evidence="ECO:0000269|PubMed:23150584" FT MUTAGEN 15 FT /note="C->S: Decreased covalent heme attachment." FT /evidence="ECO:0000269|PubMed:23150584" FT MUTAGEN 18 FT /note="C->A: Decreased covalent heme attachment." FT /evidence="ECO:0000269|PubMed:23150584" FT MUTAGEN 19 FT /note="H->A: Loss of covalent heme attachment." FT /evidence="ECO:0000269|PubMed:23150584" FT CONFLICT 18 FT /note="C -> Y (in Ref. 8; AAH15130)" FT /evidence="ECO:0000305" FT CONFLICT 41 FT /note="T -> I (in Ref. 8; AAH68464)" FT /evidence="ECO:0000305" FT HELIX 4..14 FT /evidence="ECO:0007829|PDB:5TY3" FT TURN 15..18 FT /evidence="ECO:0007829|PDB:5TY3" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:1J3S" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1J3S" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:1J3S" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:2N9I" FT HELIX 51..55 FT /evidence="ECO:0007829|PDB:5TY3" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:2N3Y" FT HELIX 62..70 FT /evidence="ECO:0007829|PDB:5TY3" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:5TY3" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:2N3Y" FT HELIX 89..102 FT /evidence="ECO:0007829|PDB:5TY3" SQ SEQUENCE 105 AA; 11749 MW; 8EE9689E0102506B CRC64; MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGIIW GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE //