QCR6_HUMAN
ID QCR6_HUMAN Reviewed; 91 AA.
AC P07919; B2R4V9; D3DQ18; Q5TDF6; Q6LDB8; Q9BQ91;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Cytochrome b-c1 complex subunit 6, mitochondrial;
DE AltName: Full=Complex III subunit 6;
DE AltName: Full=Complex III subunit VIII;
DE AltName: Full=Cytochrome c1 non-heme 11 kDa protein;
DE AltName: Full=Mitochondrial hinge protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 11 kDa protein;
DE Flags: Precursor;
GN Name=UQCRH;
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 [MRNA].
RX PubMed=2826252; DOI=10.1016/0014-5793(87)80573-2;
RA Ohta S., Goto K., Arai H., Kagawa Y.;
RT "An extremely acidic amino-terminal presequence of the precursor for the
RT human mitochondrial hinge protein.";
RL FEBS Lett. 226:171-175(1987).
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].
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Pancreas, and Placenta;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=7684318;
RA Liu A.Y., Bradner R.C.;
RT "Elevated expression of the human mitochondrial hinge protein gene in
RT cancer.";
RL Cancer Res. 53:2460-2465(1993).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
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 [11]
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 [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 17-91.
RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA Guo R., Zong S., Wu M., Gu J., Yang M.;
RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL Cell 170:1247-1257(2017).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. {ECO:0000250|UniProtKB:P00127}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (PubMed:28844695). {ECO:0000250|UniProtKB:P00126,
CC ECO:0000269|PubMed:28844695}.
CC -!- INTERACTION:
CC P07919; Q96BM9: ARL8A; NbExp=6; IntAct=EBI-1224427, EBI-4401082;
CC P07919; Q96H71: FAM189B; NbExp=3; IntAct=EBI-1224427, EBI-10195448;
CC P07919; Q9BT67: NDFIP1; NbExp=3; IntAct=EBI-1224427, EBI-11732799;
CC P07919; Q9NV92: NDFIP2; NbExp=3; IntAct=EBI-1224427, EBI-2933200;
CC P07919; O14668: PRRG1; NbExp=3; IntAct=EBI-1224427, EBI-12111452;
CC P07919; Q9Y225: RNF24; NbExp=3; IntAct=EBI-1224427, EBI-10195462;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00127}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00127}; Intermembrane side
CC {ECO:0000250|UniProtKB:P00127}.
CC -!- SIMILARITY: Belongs to the UQCRH/QCR6 family. {ECO:0000305}.
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DR EMBL; M36647; AAA36317.1; -; mRNA.
DR EMBL; Y00764; CAA68733.1; -; mRNA.
DR EMBL; BT007070; AAP35733.1; -; mRNA.
DR EMBL; AK311967; BAG34906.1; -; mRNA.
DR EMBL; AL122001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06922.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06924.1; -; Genomic_DNA.
DR EMBL; BC001426; AAH01426.1; -; mRNA.
DR EMBL; BC001934; AAH01934.1; -; mRNA.
DR EMBL; BC015177; AAH15177.1; -; mRNA.
DR EMBL; BC107703; AAI07704.1; -; mRNA.
DR EMBL; S61826; AAD13930.1; -; Genomic_DNA.
DR CCDS; CCDS30704.1; -.
DR PIR; S00219; S00219.
DR RefSeq; NP_005995.2; NM_006004.3.
DR PDB; 5XTE; EM; 3.40 A; E/R=17-91.
DR PDB; 5XTH; EM; 3.90 A; AE/AR=18-91.
DR PDB; 5XTI; EM; 17.40 A; AE/AR=18-91.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P07919; -.
DR SMR; P07919; -.
DR BioGRID; 113234; 140.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; P07919; 52.
DR MINT; P07919; -.
DR STRING; 9606.ENSP00000309565; -.
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; 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; P07919; -.
DR PhosphoSitePlus; P07919; -.
DR BioMuta; UQCRH; -.
DR DMDM; 20455515; -.
DR EPD; P07919; -.
DR jPOST; P07919; -.
DR MassIVE; P07919; -.
DR MaxQB; P07919; -.
DR PaxDb; P07919; -.
DR PeptideAtlas; P07919; -.
DR PRIDE; P07919; -.
DR ProteomicsDB; 52042; -.
DR TopDownProteomics; P07919; -.
DR Antibodypedia; 32789; 39 antibodies from 16 providers.
DR DNASU; 7388; -.
DR Ensembl; ENST00000311672.10; ENSP00000309565.5; ENSG00000173660.12.
DR GeneID; 7388; -.
DR KEGG; hsa:7388; -.
DR MANE-Select; ENST00000311672.10; ENSP00000309565.5; NM_006004.4; NP_005995.2.
DR UCSC; uc001cpp.4; human.
DR CTD; 7388; -.
DR DisGeNET; 7388; -.
DR GeneCards; UQCRH; -.
DR HGNC; HGNC:12590; UQCRH.
DR HPA; ENSG00000173660; Low tissue specificity.
DR MIM; 613844; gene.
DR neXtProt; NX_P07919; -.
DR OpenTargets; ENSG00000173660; -.
DR PharmGKB; PA37220; -.
DR VEuPathDB; HostDB:ENSG00000173660; -.
DR eggNOG; KOG4763; Eukaryota.
DR GeneTree; ENSGT00390000003860; -.
DR HOGENOM; CLU_115913_3_0_1; -.
DR InParanoid; P07919; -.
DR OMA; CQSKGHI; -.
DR OrthoDB; 1621720at2759; -.
DR PhylomeDB; P07919; -.
DR TreeFam; TF105036; -.
DR BioCyc; MetaCyc:HS10708-MON; -.
DR PathwayCommons; P07919; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; P07919; -.
DR SIGNOR; P07919; -.
DR BioGRID-ORCS; 7388; 514 hits in 1072 CRISPR screens.
DR ChiTaRS; UQCRH; human.
DR GeneWiki; UQCRH; -.
DR GenomeRNAi; 7388; -.
DR Pharos; P07919; Tbio.
DR PRO; PR:P07919; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P07919; protein.
DR Bgee; ENSG00000173660; Expressed in cerebellar vermis and 104 other tissues.
DR ExpressionAtlas; P07919; baseline and differential.
DR Genevisible; P07919; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005746; C:mitochondrial respirasome; TAS:ProtInc.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; TAS:ProtInc.
DR GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc.
DR Gene3D; 1.10.287.20; -; 1.
DR InterPro; IPR003422; Cyt_b-c1_6.
DR InterPro; IPR023184; Ubol_cytC_Rdtase_hinge_dom.
DR InterPro; IPR036811; Ubol_cytC_Rdtase_hinge_dom_sf.
DR PANTHER; PTHR15336; PTHR15336; 1.
DR Pfam; PF02320; UCR_hinge; 1.
DR PIRSF; PIRSF000019; Bc1_11K; 1.
DR SUPFAM; SSF81531; SSF81531; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disulfide bond; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P99028"
FT CHAIN 14..91
FT /note="Cytochrome b-c1 complex subunit 6, mitochondrial"
FT /id="PRO_0000035990"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99028"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99028"
FT DISULFID 37..81
FT /evidence="ECO:0000250|UniProtKB:P00126"
FT DISULFID 53..67
FT /evidence="ECO:0000250|UniProtKB:P00126"
FT VARIANT 51
FT /note="E -> Q (in dbSNP:rs34813470)"
FT /id="VAR_034579"
FT CONFLICT 57
FT /note="V -> D (in Ref. 1; AAA36317/CAA68733)"
FT /evidence="ECO:0000305"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5XTE"
SQ SEQUENCE 91 AA; 10739 MW; 499B5D069E738F4C CRC64;
MGLEDEQKML TESGDPEEEE EEEEELVDPL TTVREQCEQL EKCVKARERL ELCDERVSSR
SHTEEDCTEE LFDFLHARDH CVAHKLFNNL K
