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   28-JAN-2026, entry version 200.
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_004548.3. [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   PDB; 9CWT; EM; 3.44 A; d=1-172.
DR   PDBsum; 5XTC; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   PDBsum; 9CWT; -.
DR   AlphaFoldDB; O96000; -.
DR   EMDB; EMD-45974; -.
DR   SMR; O96000; -.
DR   BioGRID; 110796; 165.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; O96000; -.
DR   DIP; DIP-38298N; -.
DR   FunCoup; O96000; 823.
DR   IntAct; O96000; 74.
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   jPOST; O96000; -.
DR   MassIVE; O96000; -.
DR   PaxDb; 9606-ENSP00000268668; -.
DR   PeptideAtlas; O96000; -.
DR   ProteomicsDB; 51179; -. [O96000-1]
DR   ProteomicsDB; 76829; -.
DR   Pumba; O96000; -.
DR   TopDownProteomics; O96000-1; -. [O96000-1]
DR   Antibodypedia; 23340; 349 antibodies from 32 providers.
DR   DNASU; 4716; -.
DR   Ensembl; ENST00000268668.11; ENSP00000268668.6; ENSG00000140990.16. [O96000-1]
DR   Ensembl; ENST00000543683.6; ENSP00000445086.2; ENSG00000140990.16. [O96000-2]
DR   Ensembl; ENST00000709233.1; ENSP00000517571.1; ENSG00000291930.1. [O96000-1]
DR   Ensembl; ENST00000709234.1; ENSP00000517572.1; ENSG00000291930.1. [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   AGR; HGNC:7696; -.
DR   ClinPGx; PA31502; -.
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   OpenTargets; ENSG00000140990; -.
DR   Orphanet; 2609; Isolated complex I deficiency.
DR   VEuPathDB; HostDB:ENSG00000140990; -.
DR   eggNOG; KOG4009; Eukaryota.
DR   GeneTree; ENSGT00390000006348; -.
DR   HOGENOM; CLU_112615_1_0_1; -.
DR   InParanoid; O96000; -.
DR   OMA; CKPILEQ; -.
DR   OrthoDB; 6017729at2759; -.
DR   PAN-GO; O96000; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; O96000; -.
DR   BioCyc; MetaCyc:HS06786-MONOMER; -.
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   Agora; ENSG00000140990; -.
DR   BioGRID-ORCS; 4716; 378 hits in 1183 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
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 181 other cell types or tissues.
DR   ExpressionAtlas; O96000; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0045271; C:respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   InterPro; IPR019377; NADH_UbQ_OxRdtase_su10.
DR   InterPro; IPR039993; NDUFB10.
DR   PANTHER; PTHR13094:SF1; NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT 10; 1.
DR   PANTHER; PTHR13094; NADH-UBIQUINONE OXIDOREDUCTASE PDSW SUBUNIT; 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; Proteomics identification;
KW   Reference proteome; Respiratory chain; 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
//