NDUBA_HUMAN
ID NDUBA_HUMAN Reviewed; 172 AA.
AC O96000; Q96II6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;
DE AltName: Full=Complex I-PDSW;
DE Short=CI-PDSW;
DE AltName: Full=NADH-ubiquinone oxidoreductase PDSW subunit;
GN Name=NDUFB10;
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 [GENOMIC DNA].
RA Wang L., Zhang J., Smith D.I.;
RT "One subunit of human NADH-ubiquinone oxidoreductase, hPDSW, located at
RT 16p13.3 and down-regulated in a prostate cell line.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary, and 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 [7]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, 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 [10]
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 [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 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).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHCHD4, DISULFIDE BOND,
RP INVOLVEMENT IN MC1DN35, VARIANT MC1DN35 SER-107, AND CHARACTERIZATION OF
RP VARIANT MC1DN35 SER-107.
RX PubMed=28040730; DOI=10.1093/hmg/ddw431;
RA Friederich M.W., Erdogan A.J., Coughlin C.R. II, Elos M.T., Jiang H.,
RA O'Rourke C.P., Lovell M.A., Wartchow E., Gowan K., Chatfield K.C.,
RA Chick W.S., Spector E.B., Van Hove J.L.K., Riemer J.;
RT "Mutations in the accessory subunit NDUFB10 result in isolated complex I
RT deficiency and illustrate the critical role of intermembrane space import
RT for complex I holoenzyme assembly.";
RL Hum. Mol. Genet. 26:702-716(2017).
CC -!- FUNCTION: Accessory subunit that is involved in the functional assembly
CC of the mitochondrial respiratory chain complex I. Complex I has an NADH
CC dehydrogenase activity with ubiquinone as an immediate electron
CC acceptor and mediates the transfer of electrons from NADH to the
CC respiratory chain. {ECO:0000269|PubMed:27626371,
CC ECO:0000269|PubMed:28040730}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits
CC (PubMed:12611891, PubMed:27626371, PubMed:28040730). Interacts with
CC CHCHD4; assists NDUFB10 oxidation, folding and import into
CC mitochondrion (PubMed:28040730). {ECO:0000269|PubMed:12611891,
CC ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:28040730}.
CC -!- INTERACTION:
CC O96000; Q8IZU0: FAM9B; NbExp=6; IntAct=EBI-1246371, EBI-10175124;
CC O96000; O14964: HGS; NbExp=3; IntAct=EBI-1246371, EBI-740220;
CC O96000; P42858: HTT; NbExp=13; IntAct=EBI-1246371, EBI-466029;
CC O96000; O15160: POLR1C; NbExp=3; IntAct=EBI-1246371, EBI-1055079;
CC O96000; P05455: SSB; NbExp=3; IntAct=EBI-1246371, EBI-358037;
CC O96000; Q8NFB2: TMEM185A; NbExp=3; IntAct=EBI-1246371, EBI-21757569;
CC O96000-2; P42858: HTT; NbExp=3; IntAct=EBI-25930682, EBI-466029;
CC O96000-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25930682, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:28040730, ECO:0000305|PubMed:12611891}; Peripheral
CC membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O96000-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O96000-2; Sequence=VSP_056555;
CC -!- PTM: The formation of intramolecular disulfide bonds is assisted by
CC CHCHD4 and ensures folding, import into the mitochondrion and is
CC required for the function in mitochondrial respiratory chain complex I
CC assembly. {ECO:0000269|PubMed:28040730}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 35 (MC1DN35)
CC [MIM:619003]: A form of mitochondrial complex I deficiency, the most
CC common biochemical signature of mitochondrial disorders, a group of
CC highly heterogeneous conditions characterized by defective oxidative
CC phosphorylation, which collectively affects 1 in 5-10000 live births.
CC Clinical disorders have variable severity, ranging from lethal neonatal
CC disease to adult-onset neurodegenerative disorders. Phenotypes include
CC macrocephaly with progressive leukodystrophy, non-specific
CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC syndrome, Leber hereditary optic neuropathy, and some forms of
CC Parkinson disease. MC1DN35 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:28040730}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the complex I NDUFB10 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF044954; AAD05419.1; -; mRNA.
DR EMBL; AF088995; AAD16091.1; -; Genomic_DNA.
DR EMBL; AF088992; AAD16091.1; JOINED; Genomic_DNA.
DR EMBL; AF088993; AAD16091.1; JOINED; Genomic_DNA.
DR EMBL; AF088994; AAD16091.1; JOINED; Genomic_DNA.
DR EMBL; AF088991; AAD08677.1; -; mRNA.
DR EMBL; AF067169; AAD32453.1; -; mRNA.
DR EMBL; AC005363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85597.1; -; Genomic_DNA.
DR EMBL; BC007509; AAH07509.1; -; mRNA.
DR EMBL; BC005829; AAH05829.1; -; mRNA.
DR CCDS; CCDS10451.1; -. [O96000-1]
DR PIR; JE0381; JE0381.
DR RefSeq; NP_004539.1; NM_004548.2. [O96000-1]
DR PDB; 5XTC; EM; 3.70 A; d=1-171.
DR PDB; 5XTD; EM; 3.70 A; d=1-171.
DR PDB; 5XTH; EM; 3.90 A; d=1-171.
DR PDB; 5XTI; EM; 17.40 A; Bd/d=1-171.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O96000; -.
DR SMR; O96000; -.
DR BioGRID; 110796; 124.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O96000; -.
DR DIP; DIP-38298N; -.
DR IntAct; O96000; 43.
DR MINT; O96000; -.
DR STRING; 9606.ENSP00000268668; -.
DR BindingDB; O96000; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O96000; -.
DR GlyGen; O96000; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O96000; -.
DR PhosphoSitePlus; O96000; -.
DR SwissPalm; O96000; -.
DR BioMuta; NDUFB10; -.
DR UCD-2DPAGE; O96000; -.
DR EPD; O96000; -.
DR jPOST; O96000; -.
DR MassIVE; O96000; -.
DR MaxQB; O96000; -.
DR PaxDb; O96000; -.
DR PeptideAtlas; O96000; -.
DR PRIDE; O96000; -.
DR ProteomicsDB; 51179; -. [O96000-1]
DR ProteomicsDB; 76829; -.
DR TopDownProteomics; O96000-1; -. [O96000-1]
DR Antibodypedia; 23340; 346 antibodies from 31 providers.
DR DNASU; 4716; -.
DR Ensembl; ENST00000268668.11; ENSP00000268668.6; ENSG00000140990.15. [O96000-1]
DR Ensembl; ENST00000543683.6; ENSP00000445086.2; ENSG00000140990.15. [O96000-2]
DR GeneID; 4716; -.
DR KEGG; hsa:4716; -.
DR MANE-Select; ENST00000268668.11; ENSP00000268668.6; NM_004548.3; NP_004539.1.
DR UCSC; uc002cni.3; human. [O96000-1]
DR CTD; 4716; -.
DR DisGeNET; 4716; -.
DR GeneCards; NDUFB10; -.
DR HGNC; HGNC:7696; NDUFB10.
DR HPA; ENSG00000140990; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; NDUFB10; -.
DR MIM; 603843; gene.
DR MIM; 619003; phenotype.
DR neXtProt; NX_O96000; -.
DR OpenTargets; ENSG00000140990; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR PharmGKB; PA31502; -.
DR VEuPathDB; HostDB:ENSG00000140990; -.
DR eggNOG; KOG4009; Eukaryota.
DR GeneTree; ENSGT00390000006348; -.
DR HOGENOM; CLU_112615_1_0_1; -.
DR InParanoid; O96000; -.
DR OMA; ERMKACQ; -.
DR PhylomeDB; O96000; -.
DR TreeFam; TF105792; -.
DR BioCyc; MetaCyc:HS06786-MON; -.
DR PathwayCommons; O96000; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O96000; -.
DR SIGNOR; O96000; -.
DR BioGRID-ORCS; 4716; 353 hits in 1093 CRISPR screens.
DR ChiTaRS; NDUFB10; human.
DR GeneWiki; NDUFB10; -.
DR GenomeRNAi; 4716; -.
DR Pharos; O96000; Tclin.
DR PRO; PR:O96000; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O96000; protein.
DR Bgee; ENSG00000140990; Expressed in left ventricle myocardium and 179 other tissues.
DR ExpressionAtlas; O96000; baseline and differential.
DR Genevisible; O96000; 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: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; IPR019377; NADH_UbQ_OxRdtase_su10.
DR InterPro; IPR039993; NDUFB10.
DR PANTHER; PTHR13094; PTHR13094; 1.
DR Pfam; PF10249; NDUFB10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..172
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 10"
FT /id="PRO_0000118830"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 137..172
FT /note="YQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS -> CACPTHPQPPTI
FT LLRPGGQNHCKSSLPSLVLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056555"
FT VARIANT 107
FT /note="C -> S (in MC1DN35; decreased protein abundance;
FT decreased CHCHD4-mediated oxidation; loss of mitochondrial
FT localization; retained in the cytosol; loss of function in
FT mitochondrial respiratory chain complex I assembly)"
FT /evidence="ECO:0000269|PubMed:28040730"
FT /id="VAR_084767"
SQ SEQUENCE 172 AA; 20777 MW; A5E6561402F4486A CRC64;
MPDSWDKDVY PEPPRRTPVQ PNPIVYMMKA FDLIVDRPVT LVREFIERQH AKNRYYYYHR
QYRRVPDITE CKEEDIMCMY EAEMQWKRDY KVDQEIINIM QDRLKACQQR EGQNYQQNCI
KEVEQFTQVA KAYQDRYQDL GAYSSARKCL AKQRQRMLQE RKAAKEAAAA TS
