NDUB7_HUMAN
ID NDUB7_HUMAN Reviewed; 137 AA.
AC P17568; Q6ICN9; Q9UI16;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;
DE AltName: Full=Cell adhesion protein SQM1;
DE AltName: Full=Complex I-B18;
DE Short=CI-B18;
DE AltName: Full=NADH-ubiquinone oxidoreductase B18 subunit;
GN Name=NDUFB7;
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=2302251; DOI=10.1016/0006-291x(90)90908-6;
RA Wong Y.-C., Tsao S.-W., Kakefuda M., Bernal S.D.;
RT "cDNA cloning of a novel cell adhesion protein expressed in human squamous
RT carcinoma cells.";
RL Biochem. Biophys. Res. Commun. 166:984-992(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10830904; DOI=10.1007/s004390000278;
RA Triepels R., Smeitink J., Loeffen J., Smeets R., Trijbels F.,
RA van den Heuvel L.;
RT "Characterization of the human complex I NDUFB7 and 17.2-kDa cDNAs and
RT mutational analysis of 19 genes of the HP fraction in complex I-deficient-
RT patients.";
RL Hum. Genet. 106:385-391(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA Ghosh S.S., Capaldi R.A.;
RT "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT one-step immunopurification.";
RL J. Biol. Chem. 278:13619-13622(2003).
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 SUBCELLULAR LOCATION, DOMAIN, AND MOTIF.
RX PubMed=21310150; DOI=10.1016/j.febslet.2011.01.046;
RA Szklarczyk R., Wanschers B.F., Nabuurs S.B., Nouws J., Nijtmans L.G.,
RA Huynen M.A.;
RT "NDUFB7 and NDUFA8 are located at the intermembrane surface of complex I.";
RL FEBS Lett. 585:737-743(2011).
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 FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
RX PubMed=27626371; DOI=10.1038/nature19754;
RA Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
RA Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
RA Salim A., Ryan M.T.;
RT "Accessory subunits are integral for assembly and function of human
RT mitochondrial complex I.";
RL Nature 538:123-126(2016).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC -!- INTERACTION:
CC P17568; Q5U5Z8-3: AGBL2; NbExp=3; IntAct=EBI-1246238, EBI-12226473;
CC P17568; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-1246238, EBI-12170453;
CC P17568; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-1246238, EBI-12006308;
CC P17568; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-1246238, EBI-8643161;
CC P17568; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-1246238, EBI-1104933;
CC P17568; P24863: CCNC; NbExp=3; IntAct=EBI-1246238, EBI-395261;
CC P17568; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-1246238, EBI-5278764;
CC P17568; P55273: CDKN2D; NbExp=3; IntAct=EBI-1246238, EBI-745859;
CC P17568; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-1246238, EBI-741528;
CC P17568; Q9BW66: CINP; NbExp=3; IntAct=EBI-1246238, EBI-739784;
CC P17568; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-1246238, EBI-11980535;
CC P17568; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-1246238, EBI-11962928;
CC P17568; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-1246238, EBI-744099;
CC P17568; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-1246238, EBI-7225287;
CC P17568; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-1246238, EBI-6658203;
CC P17568; P55040: GEM; NbExp=3; IntAct=EBI-1246238, EBI-744104;
CC P17568; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-1246238, EBI-11959863;
CC P17568; P13807: GYS1; NbExp=3; IntAct=EBI-1246238, EBI-740553;
CC P17568; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-1246238, EBI-11955579;
CC P17568; P25791-3: LMO2; NbExp=3; IntAct=EBI-1246238, EBI-11959475;
CC P17568; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-1246238, EBI-746778;
CC P17568; O14770-4: MEIS2; NbExp=3; IntAct=EBI-1246238, EBI-8025850;
CC P17568; Q13064: MKRN3; NbExp=3; IntAct=EBI-1246238, EBI-2340269;
CC P17568; Q15653: NFKBIB; NbExp=3; IntAct=EBI-1246238, EBI-352889;
CC P17568; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-1246238, EBI-10271199;
CC P17568; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-1246238, EBI-1504830;
CC P17568; Q6P9E2: RECK; NbExp=3; IntAct=EBI-1246238, EBI-10253121;
CC P17568; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-1246238, EBI-10226430;
CC P17568; Q5TAB7: RIPPLY2; NbExp=3; IntAct=EBI-1246238, EBI-10246897;
CC P17568; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-1246238, EBI-748391;
CC P17568; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1246238, EBI-5235340;
CC P17568; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-1246238, EBI-7082156;
CC P17568; Q9BX79-6: STRA6; NbExp=3; IntAct=EBI-1246238, EBI-12140683;
CC P17568; Q01664: TFAP4; NbExp=3; IntAct=EBI-1246238, EBI-2514218;
CC P17568; Q08117-2: TLE5; NbExp=3; IntAct=EBI-1246238, EBI-11741437;
CC P17568; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=3; IntAct=EBI-1246238, EBI-12369705;
CC P17568; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-1246238, EBI-373456;
CC P17568; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1246238, EBI-740727;
CC P17568; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-1246238, EBI-10273713;
CC P17568; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-1246238, EBI-6427977;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21310150}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21310150}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:21310150}.
CC -!- DOMAIN: Contains two C-X9-C motifs that are predicted to form a helix-
CC coil-helix structure, permitting the formation of intramolecular
CC disulfide bonds. {ECO:0000269|PubMed:21310150}.
CC -!- SIMILARITY: Belongs to the complex I NDUFB7 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35675.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M33374; AAA35675.1; ALT_FRAME; mRNA.
DR EMBL; AF217091; AAF91223.1; -; mRNA.
DR EMBL; AF112200; AAF17188.1; -; mRNA.
DR EMBL; CR450354; CAG29350.1; -; mRNA.
DR EMBL; CH471106; EAW84436.1; -; Genomic_DNA.
DR EMBL; BC002595; AAH02595.1; -; mRNA.
DR CCDS; CCDS12314.1; -.
DR PIR; A34653; A34653.
DR RefSeq; NP_004137.2; NM_004146.5.
DR PDB; 5XTC; EM; 3.70 A; v=3-124.
DR PDB; 5XTD; EM; 3.70 A; v=1-137.
DR PDB; 5XTH; EM; 3.90 A; v=3-124.
DR PDB; 5XTI; EM; 17.40 A; Bv/v=3-124.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P17568; -.
DR SMR; P17568; -.
DR BioGRID; 110793; 99.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; P17568; -.
DR IntAct; P17568; 62.
DR MINT; P17568; -.
DR STRING; 9606.ENSP00000215565; -.
DR BindingDB; P17568; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; P17568; -.
DR GlyGen; P17568; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P17568; -.
DR PhosphoSitePlus; P17568; -.
DR BioMuta; NDUFB7; -.
DR DMDM; 12644140; -.
DR EPD; P17568; -.
DR jPOST; P17568; -.
DR MassIVE; P17568; -.
DR MaxQB; P17568; -.
DR PaxDb; P17568; -.
DR PeptideAtlas; P17568; -.
DR PRIDE; P17568; -.
DR ProteomicsDB; 53493; -.
DR Antibodypedia; 1259; 154 antibodies from 29 providers.
DR DNASU; 4713; -.
DR Ensembl; ENST00000215565.3; ENSP00000215565.1; ENSG00000099795.7.
DR GeneID; 4713; -.
DR KEGG; hsa:4713; -.
DR MANE-Select; ENST00000215565.3; ENSP00000215565.1; NM_004146.6; NP_004137.2.
DR UCSC; uc002mzg.4; human.
DR CTD; 4713; -.
DR DisGeNET; 4713; -.
DR GeneCards; NDUFB7; -.
DR HGNC; HGNC:7702; NDUFB7.
DR HPA; ENSG00000099795; Low tissue specificity.
DR MIM; 603842; gene.
DR neXtProt; NX_P17568; -.
DR OpenTargets; ENSG00000099795; -.
DR PharmGKB; PA31513; -.
DR VEuPathDB; HostDB:ENSG00000099795; -.
DR eggNOG; KOG3468; Eukaryota.
DR GeneTree; ENSGT00390000018759; -.
DR HOGENOM; CLU_154847_1_0_1; -.
DR InParanoid; P17568; -.
DR OMA; FVYQCAH; -.
DR OrthoDB; 1570033at2759; -.
DR PhylomeDB; P17568; -.
DR TreeFam; TF315152; -.
DR BioCyc; MetaCyc:HS01908-MON; -.
DR PathwayCommons; P17568; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; P17568; -.
DR SIGNOR; P17568; -.
DR BioGRID-ORCS; 4713; 328 hits in 1079 CRISPR screens.
DR ChiTaRS; NDUFB7; human.
DR GeneWiki; NDUFB7; -.
DR GenomeRNAi; 4713; -.
DR Pharos; P17568; Tclin.
DR PRO; PR:P17568; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P17568; protein.
DR Bgee; ENSG00000099795; Expressed in apex of heart and 199 other tissues.
DR ExpressionAtlas; P17568; baseline and differential.
DR Genevisible; P17568; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR InterPro; IPR008698; NDUB7.
DR PANTHER; PTHR20900; PTHR20900; 1.
DR Pfam; PF05676; NDUF_B7; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Lipoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Myristate; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..137
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 7"
FT /id="PRO_0000118811"
FT DOMAIN 56..98
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 59..69
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 80..90
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CR61"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT DISULFID 59..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 69..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT VARIANT 106
FT /note="R -> G (in dbSNP:rs3752220)"
FT /id="VAR_050591"
SQ SEQUENCE 137 AA; 16402 MW; 2743716544288776 CRC64;
MGAHLVRRYL GDASVEPDPL QMPTFPPDYG FPERKEREMV ATQQEMMDAQ LRLQLRDYCA
HHLIRLLKCK RDSFPNFLAC KQERHDWDYC EHRDYVMRMK EFERERRLLQ RKKRREKKAA
ELAKGQGPGE VDPKVAL
