NDUB4_HUMAN
ID NDUB4_HUMAN Reviewed; 129 AA.
AC O95168; B2RUY3; B9EJC7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;
DE AltName: Full=Complex I-B15;
DE Short=CI-B15;
DE AltName: Full=NADH-ubiquinone oxidoreductase B15 subunit;
GN Name=NDUFB4;
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] (ISOFORM 1).
RX PubMed=9878551; DOI=10.1006/bbrc.1998.9786;
RA Loeffen J.L.C.M., Triepels R.H., van den Heuvel L.P., Schuelke M.,
RA Buskens C.A.F., Smeets R.J.P., Trijbels J.M.F., Smeitink J.A.M.;
RT "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase:
RT human complex I cDNA characterization completed.";
RL Biochem. Biophys. Res. Commun. 253:415-422(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Cervix;
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 [5]
RP IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
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 [10]
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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Single-pass membrane protein
CC {ECO:0000255}; Matrix side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95168-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95168-2; Sequence=VSP_042719;
CC -!- SIMILARITY: Belongs to the complex I NDUFB4 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF044957; AAD05421.1; -; mRNA.
DR EMBL; AC126182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79525.1; -; Genomic_DNA.
DR EMBL; BC000855; AAH00855.1; -; mRNA.
DR EMBL; BC070285; AAH70285.1; -; mRNA.
DR EMBL; BC146885; AAI46886.1; -; mRNA.
DR EMBL; BC146887; AAI46888.1; -; mRNA.
DR EMBL; BC146927; AAI46928.1; -; mRNA.
DR EMBL; BC146932; AAI46933.1; -; mRNA.
DR CCDS; CCDS2999.1; -. [O95168-1]
DR CCDS; CCDS54630.1; -. [O95168-2]
DR PIR; JE0383; JE0383.
DR RefSeq; NP_001161803.1; NM_001168331.1. [O95168-2]
DR RefSeq; NP_004538.2; NM_004547.5. [O95168-1]
DR PDB; 5XTC; EM; 3.70 A; o=2-129.
DR PDB; 5XTD; EM; 3.70 A; o=2-129.
DR PDB; 5XTH; EM; 3.90 A; o=2-129.
DR PDB; 5XTI; EM; 17.40 A; Bo/o=2-129.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O95168; -.
DR SMR; O95168; -.
DR BioGRID; 110790; 74.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O95168; -.
DR IntAct; O95168; 34.
DR MINT; O95168; -.
DR STRING; 9606.ENSP00000184266; -.
DR BindingDB; O95168; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O95168; -.
DR iPTMnet; O95168; -.
DR PhosphoSitePlus; O95168; -.
DR SwissPalm; O95168; -.
DR BioMuta; NDUFB4; -.
DR EPD; O95168; -.
DR jPOST; O95168; -.
DR MassIVE; O95168; -.
DR MaxQB; O95168; -.
DR PaxDb; O95168; -.
DR PeptideAtlas; O95168; -.
DR PRIDE; O95168; -.
DR ProteomicsDB; 50681; -. [O95168-1]
DR ProteomicsDB; 50682; -. [O95168-2]
DR TopDownProteomics; O95168-1; -. [O95168-1]
DR Antibodypedia; 32798; 82 antibodies from 24 providers.
DR DNASU; 4710; -.
DR Ensembl; ENST00000184266.3; ENSP00000184266.2; ENSG00000065518.8. [O95168-1]
DR Ensembl; ENST00000485064.1; ENSP00000419578.1; ENSG00000065518.8. [O95168-2]
DR GeneID; 4710; -.
DR KEGG; hsa:4710; -.
DR MANE-Select; ENST00000184266.3; ENSP00000184266.2; NM_004547.6; NP_004538.2.
DR UCSC; uc003edt.4; human. [O95168-1]
DR CTD; 4710; -.
DR GeneCards; NDUFB4; -.
DR HGNC; HGNC:7699; NDUFB4.
DR HPA; ENSG00000065518; Tissue enhanced (skeletal).
DR MIM; 603840; gene.
DR neXtProt; NX_O95168; -.
DR OpenTargets; ENSG00000065518; -.
DR PharmGKB; PA31510; -.
DR VEuPathDB; HostDB:ENSG00000065518; -.
DR eggNOG; ENOG502S2HF; Eukaryota.
DR GeneTree; ENSGT00390000007133; -.
DR HOGENOM; CLU_123402_0_0_1; -.
DR InParanoid; O95168; -.
DR OMA; PLFFWFY; -.
DR OrthoDB; 1434967at2759; -.
DR PhylomeDB; O95168; -.
DR TreeFam; TF328761; -.
DR BioCyc; MetaCyc:HS00843-MON; -.
DR PathwayCommons; O95168; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O95168; -.
DR SIGNOR; O95168; -.
DR BioGRID-ORCS; 4710; 393 hits in 1086 CRISPR screens.
DR ChiTaRS; NDUFB4; human.
DR GenomeRNAi; 4710; -.
DR Pharos; O95168; Tclin.
DR PRO; PR:O95168; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O95168; protein.
DR Bgee; ENSG00000065518; Expressed in heart right ventricle and 206 other tissues.
DR ExpressionAtlas; O95168; baseline and differential.
DR Genevisible; O95168; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR InterPro; IPR009866; NADH_UbQ_OxRdtase_NDUFB4_su.
DR PANTHER; PTHR15469; PTHR15469; 1.
DR Pfam; PF07225; NDUF_B4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..129
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 4"
FT /id="PRO_0000118800"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 110..129
FT /note="DRKEKLIQEGKLDRTFHLSY -> VSIQTRCLVFE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042719"
SQ SEQUENCE 129 AA; 15209 MW; E5060D0BF46FFF28 CRC64;
MSFPKYKPSS LRTLPETLDP AEYNISPETR RAQAERLAIR AQLKREYLLQ YNDPNRRGLI
ENPALLRWAY ARTINVYPNF RPTPKNSLMG ALCGFGPLIF IYYIIKTERD RKEKLIQEGK
LDRTFHLSY
