CYB_HUMAN
ID CYB_HUMAN Reviewed; 380 AA.
AC P00156; Q34786; Q8HBR6; Q8HNQ0; Q8HNQ1; Q8HNQ9; Q8HNR4; Q8HNR7; Q8W7V8;
AC Q8WCV9; Q8WCY2; Q8WCY7; Q8WCY8; Q9B1A6; Q9B1B6; Q9B1B8; Q9B1D4; Q9B1X6;
AC Q9B2V0; Q9B2V8; Q9B2W0; Q9B2W3; Q9B2W8; Q9B2X1; Q9B2X7; Q9B2X9; Q9B2Y3;
AC Q9B2Z0; Q9B2Z4; Q9T6H6; Q9T9Y0; Q9TEH4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Cytochrome b;
DE AltName: Full=Complex III subunit 3;
DE AltName: Full=Complex III subunit III;
DE AltName: Full=Cytochrome b-c1 complex subunit 3;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS Homo sapiens (Human).
OG Mitochondrion.
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 [LARGE SCALE GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=7219534; DOI=10.1038/290457a0;
RA Anderson S., Bankier A.T., Barrell B.G., de Bruijn M.H.L., Coulson A.R.,
RA Drouin J., Eperon I.C., Nierlich D.P., Roe B.A., Sanger F., Schreier P.H.,
RA Smith A.J.H., Staden R., Young I.G.;
RT "Sequence and organization of the human mitochondrial genome.";
RL Nature 290:457-465(1981).
RN [2]
RP SEQUENCE REVISION TO 7.
RX PubMed=10508508; DOI=10.1038/13779;
RA Andrews R.M., Kubacka I., Chinnery P.F., Lightowlers R.N., Turnbull D.M.,
RA Howell N.;
RT "Reanalysis and revision of the Cambridge reference sequence for human
RT mitochondrial DNA.";
RL Nat. Genet. 23:147-147(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-7 AND CARDIOMYOPATHY
RP HIS-255.
RC TISSUE=Heart;
RX PubMed=7623448; DOI=10.1007/bf00711378;
RA Marin-Garcia J., Ananthakrishnan R., Gonzalvo A., Goldenthal M.J.;
RT "Novel mutations in mitochondrial cytochrome b in fatal post partum
RT cardiomyopathy.";
RL J. Inherit. Metab. Dis. 18:77-78(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-7; THR-191; ALA-194 AND
RP THR-229.
RC TISSUE=Placenta;
RX PubMed=7530363; DOI=10.1073/pnas.92.2.532;
RA Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.;
RT "Recent African origin of modern humans revealed by complete sequences of
RT hominoid mitochondrial DNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:532-536(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378, AND VARIANTS ILE-7; SER-8;
RP LEU-18; VAL-39; THR-78; THR-122; ALA-123; THR-153; ALA-194; THR-229;
RP ILE-236; THR-306; THR-329; VAL-334; MET-353; MET-356 AND ILE-368.
RX PubMed=11130070; DOI=10.1038/35047064;
RA Ingman M., Kaessmann H., Paeaebo S., Gyllensten U.;
RT "Mitochondrial genome variation and the origin of modern humans.";
RL Nature 408:708-713(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378, AND VARIANTS ILE-7; SER-8;
RP LEU-18; THR-122; VAL-164; 189-VAL-THR-190; ALA-194; THR-229; ILE-236;
RP THR-330; ALA-360 AND ILE-368.
RX PubMed=11553319; DOI=10.1186/1471-2156-2-13;
RA Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.;
RT "Major genomic mitochondrial lineages delineate early human expansions.";
RL BMC Genet. 2:13-13(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378, AND VARIANTS ILE-7; THR-39;
RP VAL-78; THR-191; ALA-194 AND ASP-260.
RX PubMed=12022039; DOI=10.1086/341358;
RA Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K.,
RA Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M.,
RA Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.;
RT "Mitochondrial genome diversity of native Americans supports a single early
RT entry of founder populations into America.";
RL Am. J. Hum. Genet. 71:187-192(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 269-380.
RC TISSUE=Lymphoblast;
RX PubMed=6100559;
RA Spurr N.K., Bodmer W.F.;
RT "Serendipitous cloning of a mitochondrial cDNA and its polymorphism.";
RL Mol. Biol. Med. 2:239-249(1984).
RN [9]
RP DISEASE.
RX PubMed=11047755; DOI=10.1086/316900;
RA Keightley J.A., Anitori R., Burton M.D., Quan F., Buist N.R.M.,
RA Kennaway N.G.;
RT "Mitochondrial encephalomyopathy and complex III deficiency associated with
RT a stop-codon mutation in the cytochrome b gene.";
RL Am. J. Hum. Genet. 67:1400-1410(2000).
RN [10]
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 [11]
RP VARIANTS ILE-7 AND PRO-87.
RX PubMed=1757091; DOI=10.1007/bf00206061;
RA Marzuki S., Noer A.S., Lertrit P., Thyagarajan D., Kapsa R.,
RA Utthanaphol P., Byrne E.;
RT "Normal variants of human mitochondrial DNA and translation products: the
RT building of a reference data base.";
RL Hum. Genet. 88:139-145(1991).
RN [12]
RP VARIANTS LHON ASN-171 AND MET-356.
RX PubMed=1732158; DOI=10.1093/genetics/130.1.163;
RA Brown M.D., Voljavec A.S., Lott M.T., Torroni A., Yang C.C., Wallace D.C.;
RT "Mitochondrial DNA complex I and III mutations associated with Leber's
RT hereditary optic neuropathy.";
RL Genetics 130:163-173(1992).
RN [13]
RP VARIANT EXERCISE INTOLERANCE ASP-290.
RX PubMed=8910895; DOI=10.1006/mcpr.1996.0053;
RA Dumoulin R., Sagnol I., Ferlin T., Bozon D., Stepien G., Mousson B.;
RT "A novel gly290asp mitochondrial cytochrome b mutation linked to a complex
RT III deficiency in progressive exercise intolerance.";
RL Mol. Cell. Probes 10:389-391(1996).
RN [14]
RP VARIANT MM GLU-339.
RX PubMed=9818877; DOI=10.1212/wnl.51.5.1444;
RA Andreu A.L., Bruno C., Shanske S., Shtilbans A., Hirano M., Krishna S.,
RA Hayward L., Systrom D.S., Brown R.H. Jr., Dimauro S.;
RT "Missense mutation in the mtDNA cytochrome b gene in a patient with
RT myopathy.";
RL Neurology 51:1444-1447(1998).
RN [15]
RP VARIANTS COLORECTAL CANCER HIS-80 AND LEU-276.
RX PubMed=9806551; DOI=10.1038/3108;
RA Polyak K., Li Y., Zhu H., Lengauer C., Willson J.K.V., Markowitz S.D.,
RA Trush M.A., Kinzler K.W., Vogelstein B.;
RT "Somatic mutations of the mitochondrial genome in human colorectal
RT tumours.";
RL Nat. Genet. 20:291-293(1998).
RN [16]
RP VARIANT HCM GLU-166, AND VARIANTS ILE-7; SER-8; LEU-18; ALA-194; ILE-236
RP AND THR-316.
RX PubMed=10453733; DOI=10.1007/s004390050988;
RA Valnot I., Kassis J., Chretien D., de Lonlay P., Parfait B., Munnich A.,
RA Kachaner J., Rustin P., Roetig A.;
RT "A mitochondrial cytochrome b mutation but no mutations of nuclearly
RT encoded subunits in ubiquinol cytochrome c reductase (complex III)
RT deficiency.";
RL Hum. Genet. 104:460-466(1999).
RN [17]
RP VARIANTS MM SER-34 AND 251-GLY--LEU-258 DEL.
RX PubMed=10502593; DOI=10.1056/nejm199909303411404;
RA Andreu A.L., Hanna M.G., Reichmann H., Bruno C., Penn A.S., Tanji K.,
RA Pallotti F., Iwata S., Bonilla E., Lach B., Morgan-Hughes J., DiMauro S.;
RT "Exercise intolerance due to mutations in the cytochrome b gene of
RT mitochondrial DNA.";
RL N. Engl. J. Med. 341:1037-1044(1999).
RN [18]
RP VARIANT CMIH ASP-251.
RX PubMed=10960495; DOI=10.1203/00006450-200009000-00008;
RA Andreu A.L., Checcarelli N., Iwata S., Shanske S., DiMauro S.;
RT "A missense mutation in the mitochondrial cytochrome b gene in a revisited
RT case with histiocytoid cardiomyopathy.";
RL Pediatr. Res. 48:311-314(2000).
RN [19]
RP VARIANT MULTISYSTEM DISORDER CYS-278.
RX PubMed=11601507; DOI=10.1002/ana.1224;
RA Wibrand F., Ravn K., Schwartz M., Rosenberg T., Horn N., Vissing J.;
RT "Multisystem disorder associated with a missense mutation in the
RT mitochondrial cytochrome b gene.";
RL Ann. Neurol. 50:540-543(2001).
RN [20]
RP VARIANT EXERCISE INTOLERANCE PRO-151.
RX PubMed=11464242; DOI=10.1038/sj.ejhg.5200678;
RA Legros F., Chatzoglou E., Frachon P., de Baulny H.O., Laforet P.,
RA Jardel C., Godinot C., Lombes A.;
RT "Functional characterization of novel mutations in the human cytochrome b
RT gene.";
RL Eur. J. Hum. Genet. 9:510-518(2001).
RN [21]
RP VARIANT EXERCICE INTOLERANCE PRO-35.
RX PubMed=11891837; DOI=10.1002/ana.10151;
RA Schuelke M., Krude H., Finckh B., Mayatepek E., Janssen A., Schmelz M.,
RA Trefz F., Trijbels F., Smeitink J.;
RT "Septo-optic dysplasia associated with a new mitochondrial cytochrome b
RT mutation.";
RL Ann. Neurol. 51:388-392(2002).
RN [22]
RP VARIANT SER-251.
RX PubMed=12905068; DOI=10.1007/s00439-003-0983-8;
RA Okura T., Koda M., Ando F., Niino N., Tanaka M., Shimokata H.;
RT "Association of the mitochondrial DNA 15497G/A polymorphism with obesity in
RT a middle-aged and elderly Japanese population.";
RL Hum. Genet. 113:432-436(2003).
RN [23]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-7, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex) that is part of the
CC mitochondrial respiratory chain. The b-c1 complex mediates electron
CC transfer from ubiquinol to cytochrome c. Contributes to the generation
CC of a proton gradient across the mitochondrial membrane that is then
CC used for ATP synthesis. {ECO:0000250|UniProtKB:P00157}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00157};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00157};
CC -!- SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory
CC subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and
CC UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7,
CC UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of
CC UQCRFS1). This cytochrome bc1 complex then forms a dimer.
CC {ECO:0000250|UniProtKB:P00157}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00157}.
CC -!- DISEASE: Note=Defects in MT-CYB are a rare cause of mitochondrial
CC dysfunction underlying different myopathies. They include mitochondrial
CC encephalomyopathy, hypertrophic cardiomyopathy (HCM), and sporadic
CC mitochondrial myopathy (MM). In mitochondrial myopathy, exercise
CC intolerance is the predominant symptom. Additional features include
CC lactic acidosis, muscle weakness and/or myoglobinuria. Defects in MTCYB
CC are also found in cases of exercise intolerance accompanied by
CC deafness, intellectual disability, retinitis pigmentosa, cataract,
CC growth retardation, epilepsy (multisystem disorder).
CC {ECO:0000269|PubMed:11047755, ECO:0000269|PubMed:11601507}.
CC -!- DISEASE: Cardiomyopathy, infantile histiocytoid (CMIH) [MIM:500000]: A
CC heart disease characterized by the presence of pale granular foamy
CC histiocyte-like cells within the myocardium. It usually affects
CC children younger than 2 years of age, with a clear predominance of
CC females over males. Infants present with dysrhythmia or cardiac arrest.
CC The clinical course is usually fulminant, sometimes simulating sudden
CC infant death syndrome. {ECO:0000269|PubMed:10960495}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A
CC maternally inherited form of Leber hereditary optic neuropathy, a
CC mitochondrial disease resulting in bilateral painless loss of central
CC vision due to selective degeneration of the retinal ganglion cells and
CC their axons. The disorder shows incomplete penetrance and male
CC predominance. Cardiac conduction defects and neurological defects have
CC also been described in some LHON patients. LHON results from primary
CC mitochondrial DNA mutations affecting the respiratory chain complexes.
CC {ECO:0000269|PubMed:1732158}. Note=The disease is caused by variants
CC affecting distinct genetic loci, including the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC at about 566 nm. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC -!- CAUTION: The full-length protein contains only eight transmembrane
CC helices, not nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00157}.
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DR EMBL; V00662; CAA24038.1; -; Genomic_DNA.
DR EMBL; J01415; AAB58955.3; -; Genomic_DNA.
DR EMBL; U09500; AAA19775.1; -; Genomic_DNA.
DR EMBL; D38112; BAA77674.1; -; Genomic_DNA.
DR EMBL; AF346963; AAK17219.1; -; Genomic_DNA.
DR EMBL; AF346964; AAK17232.2; -; Genomic_DNA.
DR EMBL; AF346965; AAK17245.2; -; Genomic_DNA.
DR EMBL; AF346966; AAK17258.1; -; Genomic_DNA.
DR EMBL; AF346967; AAK17271.2; -; Genomic_DNA.
DR EMBL; AF346968; AAK17284.2; -; Genomic_DNA.
DR EMBL; AF346969; AAK17297.2; -; Genomic_DNA.
DR EMBL; AF346970; AAK17310.2; -; Genomic_DNA.
DR EMBL; AF346971; AAK17323.2; -; Genomic_DNA.
DR EMBL; AF346972; AAK17336.2; -; Genomic_DNA.
DR EMBL; AF346973; AAK17349.2; -; Genomic_DNA.
DR EMBL; AF346974; AAK17362.2; -; Genomic_DNA.
DR EMBL; AF346975; AAK17375.2; -; Genomic_DNA.
DR EMBL; AF346976; AAK17388.1; -; Genomic_DNA.
DR EMBL; AF346977; AAK17401.1; -; Genomic_DNA.
DR EMBL; AF346978; AAK17414.1; -; Genomic_DNA.
DR EMBL; AF346979; AAK17427.1; -; Genomic_DNA.
DR EMBL; AF346980; AAK17440.2; -; Genomic_DNA.
DR EMBL; AF346981; AAK17453.2; -; Genomic_DNA.
DR EMBL; AF346982; AAK17466.1; -; Genomic_DNA.
DR EMBL; AF346983; AAK17479.1; -; Genomic_DNA.
DR EMBL; AF346984; AAK17492.2; -; Genomic_DNA.
DR EMBL; AF346985; AAK17505.2; -; Genomic_DNA.
DR EMBL; AF346986; AAK17518.2; -; Genomic_DNA.
DR EMBL; AF346987; AAK17531.2; -; Genomic_DNA.
DR EMBL; AF346988; AAK17544.1; -; Genomic_DNA.
DR EMBL; AF346989; AAK17557.2; -; Genomic_DNA.
DR EMBL; AF346990; AAK17570.1; -; Genomic_DNA.
DR EMBL; AF346991; AAK17583.2; -; Genomic_DNA.
DR EMBL; AF346992; AAK17596.2; -; Genomic_DNA.
DR EMBL; AF346993; AAK17609.2; -; Genomic_DNA.
DR EMBL; AF346994; AAK17622.2; -; Genomic_DNA.
DR EMBL; AF346995; AAK17635.2; -; Genomic_DNA.
DR EMBL; AF346996; AAK17648.2; -; Genomic_DNA.
DR EMBL; AF346997; AAK17661.2; -; Genomic_DNA.
DR EMBL; AF346998; AAK17674.2; -; Genomic_DNA.
DR EMBL; AF346999; AAK17687.2; -; Genomic_DNA.
DR EMBL; AF347000; AAK17700.1; -; Genomic_DNA.
DR EMBL; AF347001; AAK17713.2; -; Genomic_DNA.
DR EMBL; AF347002; AAK17726.2; -; Genomic_DNA.
DR EMBL; AF347003; AAK17739.2; -; Genomic_DNA.
DR EMBL; AF347004; AAK17752.2; -; Genomic_DNA.
DR EMBL; AF347005; AAK17765.2; -; Genomic_DNA.
DR EMBL; AF347006; AAK17778.2; -; Genomic_DNA.
DR EMBL; AF347007; AAK17791.2; -; Genomic_DNA.
DR EMBL; AF347008; AAK17804.2; -; Genomic_DNA.
DR EMBL; AF347009; AAK17817.2; -; Genomic_DNA.
DR EMBL; AF347010; AAK17830.2; -; Genomic_DNA.
DR EMBL; AF347011; AAK17843.2; -; Genomic_DNA.
DR EMBL; AF347012; AAK17856.2; -; Genomic_DNA.
DR EMBL; AF347013; AAK17869.2; -; Genomic_DNA.
DR EMBL; AF347014; AAK17882.2; -; Genomic_DNA.
DR EMBL; AF347015; AAK17895.2; -; Genomic_DNA.
DR EMBL; AF381981; AAL54394.1; -; Genomic_DNA.
DR EMBL; AF381982; AAL54409.1; -; Genomic_DNA.
DR EMBL; AF381983; AAL54422.1; -; Genomic_DNA.
DR EMBL; AF381984; AAL54435.1; -; Genomic_DNA.
DR EMBL; AF381985; AAL54448.1; -; Genomic_DNA.
DR EMBL; AF381986; AAL54461.1; -; Genomic_DNA.
DR EMBL; AF381987; AAL54474.1; -; Genomic_DNA.
DR EMBL; AF381988; AAL54487.1; -; Genomic_DNA.
DR EMBL; AF381989; AAL54500.1; -; Genomic_DNA.
DR EMBL; AF381990; AAL54513.1; -; Genomic_DNA.
DR EMBL; AF381991; AAL54526.1; -; Genomic_DNA.
DR EMBL; AF381992; AAL54539.1; -; Genomic_DNA.
DR EMBL; AF381993; AAL54552.1; -; Genomic_DNA.
DR EMBL; AF381994; AAL54565.1; -; Genomic_DNA.
DR EMBL; AF381995; AAL54578.1; -; Genomic_DNA.
DR EMBL; AF381996; AAL54591.1; -; Genomic_DNA.
DR EMBL; AF381997; AAL54604.1; -; Genomic_DNA.
DR EMBL; AF381998; AAL54617.1; -; Genomic_DNA.
DR EMBL; AF381999; AAL54630.1; -; Genomic_DNA.
DR EMBL; AF382000; AAL54643.1; -; Genomic_DNA.
DR EMBL; AF382001; AAL54656.1; -; Genomic_DNA.
DR EMBL; AF382002; AAL54669.1; -; Genomic_DNA.
DR EMBL; AF382003; AAL54682.1; -; Genomic_DNA.
DR EMBL; AF382004; AAL54695.1; -; Genomic_DNA.
DR EMBL; AF382005; AAL54708.1; -; Genomic_DNA.
DR EMBL; AF382006; AAL54721.1; -; Genomic_DNA.
DR EMBL; AF382007; AAL54734.1; -; Genomic_DNA.
DR EMBL; AF382008; AAL54747.1; -; Genomic_DNA.
DR EMBL; AF382009; AAL54760.1; -; Genomic_DNA.
DR EMBL; AF382010; AAL54773.1; -; Genomic_DNA.
DR EMBL; AF382011; AAL54786.1; -; Genomic_DNA.
DR EMBL; AF382012; AAL54799.1; -; Genomic_DNA.
DR EMBL; AF382013; AAL54812.1; -; Genomic_DNA.
DR EMBL; AF465942; AAN14559.1; -; Genomic_DNA.
DR EMBL; AF465945; AAN14592.1; -; Genomic_DNA.
DR EMBL; AF465946; AAN14603.1; -; Genomic_DNA.
DR EMBL; AF465947; AAN14614.1; -; Genomic_DNA.
DR EMBL; AF465948; AAN14625.1; -; Genomic_DNA.
DR EMBL; AF465949; AAN14636.1; -; Genomic_DNA.
DR EMBL; AF465953; AAN14680.1; -; Genomic_DNA.
DR EMBL; AF465956; AAN14713.1; -; Genomic_DNA.
DR EMBL; AF465968; AAN14845.1; -; Genomic_DNA.
DR EMBL; AF465971; AAN14878.1; -; Genomic_DNA.
DR EMBL; AF465972; AAN14889.1; -; Genomic_DNA.
DR EMBL; AF465973; AAN14900.1; -; Genomic_DNA.
DR EMBL; AF465974; AAN14911.1; -; Genomic_DNA.
DR EMBL; AF465975; AAN14922.1; -; Genomic_DNA.
DR EMBL; AF465977; AAN14944.1; -; Genomic_DNA.
DR EMBL; M28016; AAA31851.1; -; mRNA.
DR PIR; A00151; CBHU.
DR RefSeq; YP_003024038.1; NC_012920.1.
DR PDB; 5XTE; EM; 3.40 A; J/V=2-379.
DR PDB; 5XTH; EM; 3.90 A; AJ/AV=2-379.
DR PDB; 5XTI; EM; 17.40 A; AJ/AV=2-379.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P00156; -.
DR SMR; P00156; -.
DR BioGRID; 110619; 21.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; P00156; 10.
DR MINT; P00156; -.
DR STRING; 9606.ENSP00000354554; -.
DR BindingDB; P00156; -.
DR DrugBank; DB07763; (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE.
DR DrugBank; DB07778; (S)-famoxadone.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB07636; 5-Heptyl-6-hydroxy-1,3-benzothiazole-4,7-dione.
DR DrugBank; DB04799; 6-Hydroxy-5-undecyl-4,7-benzothiazoledione.
DR DrugBank; DB07401; Azoxystrobin.
DR DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DR DrugBank; DB08690; Ubiquinone Q2.
DR iPTMnet; P00156; -.
DR PhosphoSitePlus; P00156; -.
DR SwissPalm; P00156; -.
DR BioMuta; MT-CYB; -.
DR DMDM; 408360043; -.
DR EPD; P00156; -.
DR jPOST; P00156; -.
DR MassIVE; P00156; -.
DR PaxDb; P00156; -.
DR PeptideAtlas; P00156; -.
DR PRIDE; P00156; -.
DR ProteomicsDB; 51225; -.
DR TopDownProteomics; P00156; -.
DR Antibodypedia; 35365; 181 antibodies from 28 providers.
DR DNASU; 4519; -.
DR Ensembl; ENST00000361789.2; ENSP00000354554.2; ENSG00000198727.2.
DR GeneID; 4519; -.
DR KEGG; hsa:4519; -.
DR CTD; 4519; -.
DR DisGeNET; 4519; -.
DR GeneCards; MT-CYB; -.
DR GeneReviews; MT-CYB; -.
DR HGNC; HGNC:7427; MT-CYB.
DR HPA; ENSG00000198727; Tissue enhanced (heart).
DR MalaCards; MT-CYB; -.
DR MIM; 500000; phenotype.
DR MIM; 516020; gene.
DR MIM; 535000; phenotype.
DR neXtProt; NX_P00156; -.
DR OpenTargets; ENSG00000198727; -.
DR Orphanet; 137675; Histiocytoid cardiomyopathy.
DR Orphanet; 1460; Isolated complex III deficiency.
DR Orphanet; 104; Leber hereditary optic neuropathy.
DR PharmGKB; PA31234; -.
DR VEuPathDB; HostDB:ENSG00000198727; -.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P00156; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 1125966at2759; -.
DR PhylomeDB; P00156; -.
DR TreeFam; TF353088; -.
DR BioCyc; MetaCyc:HS00029-MON; -.
DR PathwayCommons; P00156; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; P00156; -.
DR SIGNOR; P00156; -.
DR BioGRID-ORCS; 4519; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CYTB; human.
DR GeneWiki; MT-CYB; -.
DR GenomeRNAi; 4519; -.
DR Pharos; P00156; Tbio.
DR PRO; PR:P00156; -.
DR Proteomes; UP000005640; Mitochondrion.
DR RNAct; P00156; protein.
DR Bgee; ENSG00000198727; Expressed in apex of heart and 93 other tissues.
DR ExpressionAtlas; P00156; baseline and differential.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; NAS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; NAS:UniProtKB.
DR CDD; cd00290; cytochrome_b_C; 1.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR030689; Cytochrome_b.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PIRSF; PIRSF038885; COB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cardiomyopathy; Cataract; Deafness; Disease variant;
KW Electron transport; Heme; Iron; Leber hereditary optic neuropathy;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..380
FT /note="Cytochrome b"
FT /id="PRO_0000061045"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 83
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 97
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 182
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 196
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 201
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT VARIANT 7
FT /note="T -> I (in dbSNP:rs193302980)"
FT /evidence="ECO:0000269|PubMed:10453733,
FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319,
FT ECO:0000269|PubMed:12022039, ECO:0000269|PubMed:1757091,
FT ECO:0000269|PubMed:7530363, ECO:0000269|PubMed:7623448,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_008585"
FT VARIANT 8
FT /note="N -> S (in dbSNP:rs28357679)"
FT /evidence="ECO:0000269|PubMed:10453733,
FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319"
FT /id="VAR_013643"
FT VARIANT 18
FT /note="F -> L (in dbSNP:rs28357681)"
FT /evidence="ECO:0000269|PubMed:10453733,
FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319"
FT /id="VAR_013644"
FT VARIANT 34
FT /note="G -> S (in mitochondrial myopathy; sporadic;
FT dbSNP:rs207459998)"
FT /evidence="ECO:0000269|PubMed:10502593"
FT /id="VAR_013645"
FT VARIANT 35
FT /note="S -> P (in exercice intolerance; with cardiomyopathy
FT and septo-optic dysplasia; dbSNP:rs207460004)"
FT /evidence="ECO:0000269|PubMed:11891837"
FT /id="VAR_033058"
FT VARIANT 39
FT /note="A -> T (in dbSNP:rs2853505)"
FT /evidence="ECO:0000269|PubMed:12022039"
FT /id="VAR_015571"
FT VARIANT 39
FT /note="A -> V (in dbSNP:rs1603224933)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013646"
FT VARIANT 78
FT /note="I -> T (in dbSNP:rs200786872)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013647"
FT VARIANT 78
FT /note="I -> V (in dbSNP:rs199997767)"
FT /evidence="ECO:0000269|PubMed:12022039"
FT /id="VAR_015572"
FT VARIANT 80
FT /note="R -> H (in colorectal cancer; dbSNP:rs207459995)"
FT /evidence="ECO:0000269|PubMed:9806551"
FT /id="VAR_008388"
FT VARIANT 87
FT /note="A -> P (in dbSNP:rs1603225017)"
FT /evidence="ECO:0000269|PubMed:1757091"
FT /id="VAR_008586"
FT VARIANT 122
FT /note="A -> T (in dbSNP:rs28357685)"
FT /evidence="ECO:0000269|PubMed:11130070,
FT ECO:0000269|PubMed:11553319"
FT /id="VAR_013648"
FT VARIANT 123
FT /note="T -> A (in dbSNP:rs1603225089)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013649"
FT VARIANT 151
FT /note="S -> P (in exercise intolerance; dbSNP:rs207460001)"
FT /evidence="ECO:0000269|PubMed:11464242"
FT /id="VAR_013650"
FT VARIANT 153
FT /note="I -> T (in dbSNP:rs28357687)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013651"
FT VARIANT 164
FT /note="I -> V (in dbSNP:rs201250154)"
FT /evidence="ECO:0000269|PubMed:11553319"
FT /id="VAR_013652"
FT VARIANT 166
FT /note="G -> E (in hyperthrophic cardiomyopathy;
FT dbSNP:rs1603225167)"
FT /evidence="ECO:0000269|PubMed:10453733"
FT /id="VAR_013653"
FT VARIANT 171
FT /note="D -> N (in LHON; secondary mutation; does not seem
FT to directly cause the disease; dbSNP:rs41518645)"
FT /evidence="ECO:0000269|PubMed:1732158"
FT /id="VAR_002197"
FT VARIANT 189..190
FT /note="IA -> VT"
FT /id="VAR_013654"
FT VARIANT 191
FT /note="A -> T (in dbSNP:rs2853507)"
FT /evidence="ECO:0000269|PubMed:12022039,
FT ECO:0000269|PubMed:7530363"
FT /id="VAR_011339"
FT VARIANT 194
FT /note="T -> A (in dbSNP:rs2853508)"
FT /evidence="ECO:0000269|PubMed:10453733,
FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319,
FT ECO:0000269|PubMed:12022039, ECO:0000269|PubMed:7530363"
FT /id="VAR_011340"
FT VARIANT 229
FT /note="A -> T (in dbSNP:rs193302993)"
FT /evidence="ECO:0000269|PubMed:11130070,
FT ECO:0000269|PubMed:11553319, ECO:0000269|PubMed:7530363"
FT /id="VAR_011341"
FT VARIANT 236
FT /note="L -> I (in dbSNP:rs193302994)"
FT /evidence="ECO:0000269|PubMed:10453733,
FT ECO:0000269|PubMed:11130070, ECO:0000269|PubMed:11553319"
FT /id="VAR_013655"
FT VARIANT 251..258
FT /note="Missing (in mitochondrial myopathy; sporadic)"
FT /evidence="ECO:0000269|PubMed:10502593"
FT /id="VAR_013657"
FT VARIANT 251
FT /note="G -> D (in CMIH; dbSNP:rs207460003)"
FT /evidence="ECO:0000269|PubMed:10960495"
FT /id="VAR_013656"
FT VARIANT 251
FT /note="G -> S (associated with susceptibility to obesity;
FT dbSNP:rs199951903)"
FT /evidence="ECO:0000269|PubMed:12905068"
FT /id="VAR_033059"
FT VARIANT 255
FT /note="N -> H (in cardiomyopathy; fatal; post-partum)"
FT /evidence="ECO:0000269|PubMed:7623448"
FT /id="VAR_013658"
FT VARIANT 260
FT /note="N -> D (in dbSNP:rs1603225331)"
FT /evidence="ECO:0000269|PubMed:12022039"
FT /id="VAR_015573"
FT VARIANT 276
FT /note="F -> L (in colorectal cancer; dbSNP:rs207459996)"
FT /evidence="ECO:0000269|PubMed:9806551"
FT /id="VAR_008389"
FT VARIANT 278
FT /note="Y -> C (in multisystem disorder; dbSNP:rs207460002)"
FT /evidence="ECO:0000269|PubMed:11601507"
FT /id="VAR_013659"
FT VARIANT 290
FT /note="G -> D (in exercise intolerance; dbSNP:rs207459997)"
FT /evidence="ECO:0000269|PubMed:8910895"
FT /id="VAR_013660"
FT VARIANT 306
FT /note="I -> T (in dbSNP:rs369851331)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013661"
FT VARIANT 316
FT /note="M -> T (in dbSNP:rs200975632)"
FT /evidence="ECO:0000269|PubMed:10453733"
FT /id="VAR_013662"
FT VARIANT 329
FT /note="A -> T (in dbSNP:rs1556424652)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013663"
FT VARIANT 330
FT /note="A -> T (in dbSNP:rs386829259)"
FT /evidence="ECO:0000269|PubMed:11553319"
FT /id="VAR_013664"
FT VARIANT 334
FT /note="I -> V (in dbSNP:rs386829260)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013665"
FT VARIANT 339
FT /note="G -> E (in mitochondrial myopathy)"
FT /evidence="ECO:0000269|PubMed:9818877"
FT /id="VAR_002198"
FT VARIANT 353
FT /note="V -> M (in dbSNP:rs1603225508)"
FT /evidence="ECO:0000269|PubMed:11130070"
FT /id="VAR_013666"
FT VARIANT 356
FT /note="V -> M (in LHON; secondary mutation; does not seem
FT to directly cause the disease; dbSNP:rs200336777)"
FT /evidence="ECO:0000269|PubMed:11130070,
FT ECO:0000269|PubMed:1732158"
FT /id="VAR_002199"
FT VARIANT 360
FT /note="T -> A (in dbSNP:rs28357376)"
FT /evidence="ECO:0000269|PubMed:11553319"
FT /id="VAR_013667"
FT VARIANT 368
FT /note="T -> I (in dbSNP:rs202225494)"
FT /evidence="ECO:0000269|PubMed:11130070,
FT ECO:0000269|PubMed:11553319"
FT /id="VAR_013668"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 32..52
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 110..131
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 172..200
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 220..244
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 319..339
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 345..363
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:5XTE"
SQ SEQUENCE 380 AA; 42718 MW; 600E520C262E5498 CRC64;
MTPMRKTNPL MKLINHSFID LPTPSNISAW WNFGSLLGAC LILQITTGLF LAMHYSPDAS
TAFSSIAHIT RDVNYGWIIR YLHANGASMF FICLFLHIGR GLYYGSFLYS ETWNIGIILL
LATMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGYSV DSPTLTRFFT
FHFILPFIIA ALATLHLLFL HETGSNNPLG ITSHSDKITF HPYYTIKDAL GLLLFLLSLM
TLTLFSPDLL GDPDNYTLAN PLNTPPHIKP EWYFLFAYTI LRSVPNKLGG VLALLLSILI
LAMIPILHMS KQQSMMFRPL SQSLYWLLAA DLLILTWIGG QPVSYPFTII GQVASVLYFT
TILILMPTIS LIENKMLKWA
