ID   NDUB5_HUMAN             Reviewed;         189 AA.
AC   O43674; Q561V6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;
DE   AltName: Full=Complex I-SGDH;
DE            Short=CI-SGDH;
DE   AltName: Full=NADH-ubiquinone oxidoreductase SGDH subunit;
DE   Flags: Precursor;
GN   Name=NDUFB5;
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).
RC   TISSUE=Heart;
RX   PubMed=9425316; DOI=10.1006/bbrc.1997.7707;
RA   Ton C., Hwang D.M., Dempsey A.A., Liew C.-C.;
RT   "Identification and primary structure of five human NADH-ubiquinone
RT   oxidoreductase subunits.";
RL   Biochem. Biophys. Res. Commun. 241:589-594(1997).
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., 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, Skin, and Urinary bladder;
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   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   [8]
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   [9]
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       O43674; P57086: SCAND1; NbExp=3; IntAct=EBI-1246293, EBI-745846;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:12611891}; Single-pass membrane protein
CC       {ECO:0000305}; Matrix side {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O43674-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43674-2; Sequence=VSP_042516;
CC   -!- SIMILARITY: Belongs to the complex I NDUFB5 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF047181; AAC04266.1; -; mRNA.
DR   EMBL; AC090425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78393.1; -; Genomic_DNA.
DR   EMBL; BC005271; AAH05271.1; -; mRNA.
DR   EMBL; BC093071; AAH93071.1; -; mRNA.
DR   EMBL; BC009796; AAH09796.1; -; mRNA.
DR   CCDS; CCDS3234.1; -. [O43674-1]
DR   CCDS; CCDS56297.1; -. [O43674-2]
DR   PIR; JC5820; JC5820.
DR   RefSeq; NP_001186886.1; NM_001199957.1. [O43674-2]
DR   RefSeq; NP_001186887.1; NM_001199958.1.
DR   RefSeq; NP_002483.1; NM_002492.3. [O43674-1]
DR   PDB; 5XTC; EM; 3.70 A; a=52-189.
DR   PDB; 5XTD; EM; 3.70 A; a=52-189.
DR   PDB; 5XTH; EM; 3.90 A; a=52-189.
DR   PDB; 5XTI; EM; 17.40 A; Ba/a=52-189.
DR   PDBsum; 5XTC; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   AlphaFoldDB; O43674; -.
DR   SMR; O43674; -.
DR   BioGRID; 110791; 120.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; O43674; -.
DR   IntAct; O43674; 56.
DR   MINT; O43674; -.
DR   STRING; 9606.ENSP00000259037; -.
DR   BindingDB; O43674; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; O43674; -.
DR   GlyGen; O43674; 2 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; O43674; -.
DR   PhosphoSitePlus; O43674; -.
DR   BioMuta; NDUFB5; -.
DR   EPD; O43674; -.
DR   jPOST; O43674; -.
DR   MassIVE; O43674; -.
DR   MaxQB; O43674; -.
DR   PaxDb; 9606-ENSP00000259037; -.
DR   PeptideAtlas; O43674; -.
DR   ProteomicsDB; 49102; -. [O43674-1]
DR   ProteomicsDB; 49103; -. [O43674-2]
DR   Pumba; O43674; -.
DR   TopDownProteomics; O43674-1; -. [O43674-1]
DR   TopDownProteomics; O43674-2; -. [O43674-2]
DR   Antibodypedia; 1272; 174 antibodies from 31 providers.
DR   DNASU; 4711; -.
DR   Ensembl; ENST00000259037.8; ENSP00000259037.3; ENSG00000136521.13. [O43674-1]
DR   Ensembl; ENST00000493866.5; ENSP00000419656.1; ENSG00000136521.13. [O43674-2]
DR   GeneID; 4711; -.
DR   KEGG; hsa:4711; -.
DR   MANE-Select; ENST00000259037.8; ENSP00000259037.3; NM_002492.4; NP_002483.1.
DR   UCSC; uc003fkc.4; human. [O43674-1]
DR   AGR; HGNC:7700; -.
DR   CTD; 4711; -.
DR   DisGeNET; 4711; -.
DR   GeneCards; NDUFB5; -.
DR   HGNC; HGNC:7700; NDUFB5.
DR   HPA; ENSG00000136521; Low tissue specificity.
DR   MIM; 603841; gene.
DR   neXtProt; NX_O43674; -.
DR   OpenTargets; ENSG00000136521; -.
DR   PharmGKB; PA31511; -.
DR   VEuPathDB; HostDB:ENSG00000136521; -.
DR   eggNOG; KOG4632; Eukaryota.
DR   GeneTree; ENSGT00390000009980; -.
DR   HOGENOM; CLU_100260_2_0_1; -.
DR   InParanoid; O43674; -.
DR   OMA; HHHMTIK; -.
DR   OrthoDB; 2871720at2759; -.
DR   PhylomeDB; O43674; -.
DR   TreeFam; TF313997; -.
DR   BioCyc; MetaCyc:HS06175-MONOMER; -.
DR   PathwayCommons; O43674; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   SignaLink; O43674; -.
DR   SIGNOR; O43674; -.
DR   BioGRID-ORCS; 4711; 146 hits in 1169 CRISPR screens.
DR   ChiTaRS; NDUFB5; human.
DR   GenomeRNAi; 4711; -.
DR   Pharos; O43674; Tclin.
DR   PRO; PR:O43674; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O43674; Protein.
DR   Bgee; ENSG00000136521; Expressed in heart right ventricle and 208 other cell types or tissues.
DR   ExpressionAtlas; O43674; baseline and differential.
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; TAS:ProtInc.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; TAS:ProtInc.
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; NAS:ComplexPortal.
DR   InterPro; IPR019173; NADH_UbQ_OxRdtase_B5_su.
DR   PANTHER; PTHR13178:SF0; NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT 5, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13178; NADH-UBIQUINONE OXIDOREDUCTASE SGDH SUBUNIT; 1.
DR   Pfam; PF09781; NDUF_B5; 1.
DR   Genevisible; O43674; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Respiratory chain; Transit peptide; Transmembrane; Transmembrane helix;
KW   Transport.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           47..189
FT                   /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT                   subunit 5, mitochondrial"
FT                   /id="PRO_0000020052"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         42..93
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042516"
FT   VARIANT         133
FT                   /note="Y -> H (in dbSNP:rs4147793)"
FT                   /id="VAR_050590"
SQ   SEQUENCE   189 AA;  21750 MW;  66D288F7AB7FD5C5 CRC64;
     MAAMSLLRRV SVTAVAALSG RPLGTRLGFG GFLTRGFPKA AAPVRHSGDH GKRLFVIRPS
     RFYDRRFLKL LRFYIALTGI PVAIFITLVN VFIGQAELAE IPEGYVPEHW EYYKHPISRW
     IARNFYDSPE KIYERTMAVL QIEAEKAELR VKELEVRKLM HVRGDGPWYY YETIDKELID
     HSPKATPDN
//