COX5B_HUMAN
ID COX5B_HUMAN Reviewed; 129 AA.
AC P10606; Q53YB7; Q96J18; Q99610;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Cytochrome c oxidase subunit 5B, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Vb;
DE Flags: Precursor;
GN Name=COX5B;
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=2840351; DOI=10.1016/0378-1119(88)90411-8;
RA Zeviani M., Sakoda S., Sherbany A., Nakase H., Rizzuto R., Samitt C.E.,
RA Dimauro S., Schon E.A.;
RT "Sequence of cDNAs encoding subunit Vb of human and bovine cytochrome c
RT oxidase.";
RL Gene 65:1-11(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1646156; DOI=10.1016/0888-7543(91)90476-u;
RA Lomax M.I., Hsieh C.L., Darras B.T., Francke U.;
RT "Structure of the human cytochrome c oxidase subunit Vb gene and
RT chromosomal mapping of the coding gene and of seven pseudogenes.";
RL Genomics 10:1-9(1991).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=8806766; DOI=10.1006/abbi.1996.0376;
RA Bachman N.J., Yang T.L., Dasen J.S., Ernst R.E., Lomax M.I.;
RT "Phylogenetic footprinting of the human cytochrome c oxidase subunit VB
RT promoter.";
RL Arch. Biochem. Biophys. 333:152-162(1996).
RN [7]
RP PROTEIN SEQUENCE OF 32-44.
RC TISSUE=Liver;
RX PubMed=8313870; DOI=10.1002/elps.11501401181;
RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C.,
RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.;
RT "Human liver protein map: update 1993.";
RL Electrophoresis 14:1216-1222(1993).
RN [8]
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 [9]
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 [10]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER MET-31, AND
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 STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), AND SUBUNIT.
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).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS).
RX PubMed=30030519; DOI=10.1038/s41422-018-0071-1;
RA Zong S., Wu M., Gu J., Liu T., Guo R., Yang M.;
RT "Structure of the intact 14-subunit human cytochrome c oxidase.";
RL Cell Res. 28:1026-1034(2018).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P04037}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P04037}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A1 (or COX6A2), COX6B1 (or COX6B2), COX6C,
CC COX7A2 (or COX7A1), COX7B, COX7C, COX8A and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:30030519). The complex exists as a
CC monomer or a dimer and forms supercomplexes (SCs) in the inner
CC mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I,
CC CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex,
CC complex III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:28844695).
CC {ECO:0000269|PubMed:28844695, ECO:0000269|PubMed:30030519}.
CC -!- INTERACTION:
CC P10606; Q03989: ARID5A; NbExp=3; IntAct=EBI-1053725, EBI-948603;
CC P10606; O14503: BHLHE40; NbExp=4; IntAct=EBI-1053725, EBI-711810;
CC P10606; O14613: CDC42EP2; NbExp=3; IntAct=EBI-1053725, EBI-3438291;
CC P10606; Q01850: CDR2; NbExp=7; IntAct=EBI-1053725, EBI-1181367;
CC P10606; Q86X02: CDR2L; NbExp=3; IntAct=EBI-1053725, EBI-11063830;
CC P10606; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-1053725, EBI-10694655;
CC P10606; Q86W67: FAM228A; NbExp=3; IntAct=EBI-1053725, EBI-12958227;
CC P10606; O75955: FLOT1; NbExp=3; IntAct=EBI-1053725, EBI-603643;
CC P10606; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1053725, EBI-618309;
CC P10606; P42858: HTT; NbExp=7; IntAct=EBI-1053725, EBI-466029;
CC P10606; Q8IYA8: IHO1; NbExp=4; IntAct=EBI-1053725, EBI-8638439;
CC P10606; P19012: KRT15; NbExp=3; IntAct=EBI-1053725, EBI-739566;
CC P10606; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1053725, EBI-3044087;
CC P10606; Q15323: KRT31; NbExp=3; IntAct=EBI-1053725, EBI-948001;
CC P10606; Q14525: KRT33B; NbExp=3; IntAct=EBI-1053725, EBI-1049638;
CC P10606; P59942: MCCD1; NbExp=3; IntAct=EBI-1053725, EBI-11987923;
CC P10606; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1053725, EBI-10172526;
CC P10606; Q9UKK9: NUDT5; NbExp=3; IntAct=EBI-1053725, EBI-721623;
CC P10606; O43482: OIP5; NbExp=3; IntAct=EBI-1053725, EBI-536879;
CC P10606; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1053725, EBI-742388;
CC P10606; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-1053725, EBI-302345;
CC P10606; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-1053725, EBI-12000762;
CC P10606; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-1053725, EBI-11320284;
CC P10606; P31321: PRKAR1B; NbExp=5; IntAct=EBI-1053725, EBI-2805516;
CC P10606; Q5RL73: RBM48; NbExp=3; IntAct=EBI-1053725, EBI-473821;
CC P10606; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-1053725, EBI-10269374;
CC P10606; Q5VWN6: TASOR2; NbExp=4; IntAct=EBI-1053725, EBI-745958;
CC P10606; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-1053725, EBI-12090309;
CC P10606; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-1053725, EBI-1105213;
CC P10606; Q13077: TRAF1; NbExp=3; IntAct=EBI-1053725, EBI-359224;
CC P10606; P36406: TRIM23; NbExp=5; IntAct=EBI-1053725, EBI-740098;
CC P10606; P14373: TRIM27; NbExp=3; IntAct=EBI-1053725, EBI-719493;
CC P10606; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-1053725, EBI-12146727;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:30030519}; Peripheral membrane protein
CC {ECO:0000269|PubMed:30030519}; Matrix side
CC {ECO:0000269|PubMed:30030519}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B family.
CC {ECO:0000305}.
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DR EMBL; M19961; AAA52061.1; -; mRNA.
DR EMBL; M59250; AAA52060.1; -; Genomic_DNA.
DR EMBL; BT006742; AAP35388.1; -; mRNA.
DR EMBL; AC017099; AAY24279.1; -; Genomic_DNA.
DR EMBL; BC006229; AAH06229.1; -; mRNA.
DR EMBL; U41284; AAB19185.1; -; Genomic_DNA.
DR CCDS; CCDS2032.1; -.
DR PIR; JT0324; OTHU5B.
DR RefSeq; NP_001853.2; NM_001862.2.
DR PDB; 5Z62; EM; 3.60 A; F=32-129.
DR PDBsum; 5Z62; -.
DR AlphaFoldDB; P10606; -.
DR SMR; P10606; -.
DR BioGRID; 107722; 149.
DR ComplexPortal; CPX-6123; Mitochondrial respiratory chain complex IV.
DR IntAct; P10606; 76.
DR MINT; P10606; -.
DR STRING; 9606.ENSP00000258424; -.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB04464; N-Formylmethionine.
DR TCDB; 3.D.4.11.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR iPTMnet; P10606; -.
DR PhosphoSitePlus; P10606; -.
DR SwissPalm; P10606; -.
DR BioMuta; COX5B; -.
DR DMDM; 20141332; -.
DR SWISS-2DPAGE; P10606; -.
DR EPD; P10606; -.
DR jPOST; P10606; -.
DR MassIVE; P10606; -.
DR PaxDb; P10606; -.
DR PeptideAtlas; P10606; -.
DR PRIDE; P10606; -.
DR ProteomicsDB; 52618; -.
DR TopDownProteomics; P10606; -.
DR Antibodypedia; 32635; 383 antibodies from 35 providers.
DR DNASU; 1329; -.
DR Ensembl; ENST00000258424.3; ENSP00000258424.2; ENSG00000135940.7.
DR GeneID; 1329; -.
DR KEGG; hsa:1329; -.
DR MANE-Select; ENST00000258424.3; ENSP00000258424.2; NM_001862.3; NP_001853.2.
DR UCSC; uc002sya.4; human.
DR CTD; 1329; -.
DR DisGeNET; 1329; -.
DR GeneCards; COX5B; -.
DR HGNC; HGNC:2269; COX5B.
DR HPA; ENSG00000135940; Tissue enhanced (skeletal).
DR MIM; 123866; gene.
DR neXtProt; NX_P10606; -.
DR OpenTargets; ENSG00000135940; -.
DR PharmGKB; PA26786; -.
DR VEuPathDB; HostDB:ENSG00000135940; -.
DR eggNOG; KOG3352; Eukaryota.
DR GeneTree; ENSGT00390000011010; -.
DR HOGENOM; CLU_127178_0_0_1; -.
DR InParanoid; P10606; -.
DR OMA; DSHDTIY; -.
DR OrthoDB; 1345924at2759; -.
DR PhylomeDB; P10606; -.
DR TreeFam; TF105063; -.
DR BioCyc; MetaCyc:HS06090-MON; -.
DR PathwayCommons; P10606; -.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; P10606; -.
DR SIGNOR; P10606; -.
DR UniPathway; UPA00705; -.
DR BioGRID-ORCS; 1329; 326 hits in 1081 CRISPR screens.
DR ChiTaRS; COX5B; human.
DR GeneWiki; COX5B; -.
DR GenomeRNAi; 1329; -.
DR Pharos; P10606; Tbio.
DR PRO; PR:P10606; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P10606; protein.
DR Bgee; ENSG00000135940; Expressed in heart right ventricle and 208 other tissues.
DR ExpressionAtlas; P10606; baseline and differential.
DR Genevisible; P10606; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:ComplexPortal.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:ProtInc.
DR CDD; cd00924; Cyt_c_Oxidase_Vb; 1.
DR Gene3D; 2.60.11.10; -; 1.
DR InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR PANTHER; PTHR10122; PTHR10122; 1.
DR Pfam; PF01215; COX5B; 1.
DR PROSITE; PS00848; COX5B_1; 1.
DR PROSITE; PS51359; COX5B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8313870,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 32..129
FT /note="Cytochrome c oxidase subunit 5B, mitochondrial"
FT /id="PRO_0000006109"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P00428"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT CONFLICT 36..37
FT /note="GV -> TR (in Ref. 6; AAB19185)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="E -> Q (in Ref. 1; AAA52061/AAA52060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 13696 MW; 877BF4CD334AC931 CRC64;
MASRLLRGAG TLAAQALRAR GPSGAAAMRS MASGGGVPTD EEQATGLERE IMLAAKKGLD
PYNVLAPKGA SGTREDPNLV PSISNKRIVG CICEEDNTSV VWFWLHKGEA QRCPRCGAHY
KLVPQQLAH
