NDUB9_HUMAN
ID NDUB9_HUMAN Reviewed; 179 AA.
AC Q9Y6M9; B2R8M6; Q9UQE8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;
DE AltName: Full=Complex I-B22;
DE Short=CI-B22;
DE AltName: Full=LYR motif-containing protein 3;
DE AltName: Full=NADH-ubiquinone oxidoreductase B22 subunit;
GN Name=NDUFB9; Synonyms=LYRM3, UQOR22;
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].
RA Triepels R., Smeets R., Loeffen J., Ruitenbeek W., van den Heuvel L.,
RA Smeitink J.;
RT "B22 subunit of NADH:ubiquinone oxidoreductase (complex I).";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10077726; DOI=10.1159/000022848;
RA Lin X., Wells D.E., Kimberling W.J., Kumar S.;
RT "Human NDUFB9 gene: genomic organization and a possible candidate gene
RT associated with deafness disorder mapped to chromosome 8q13.";
RL Hum. Hered. 49:75-80(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Astrocytoma;
RX PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
RA Ye Z., Connor J.R.;
RT "cDNA cloning by amplification of circularized first strand cDNAs reveals
RT non-IRE-regulated iron-responsive mRNAs.";
RL Biochem. Biophys. Res. Commun. 275:223-227(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-146.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP PROTEIN SEQUENCE OF 2-15, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon adenocarcinoma;
RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
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 [12]
RP INVOLVEMENT IN MC1DN24, AND VARIANT MC1DN24 PRO-64.
RX PubMed=22200994; DOI=10.1136/jmedgenet-2011-100577;
RA Haack T.B., Madignier F., Herzer M., Lamantea E., Danhauser K.,
RA Invernizzi F., Koch J., Freitag M., Drost R., Hillier I., Haberberger B.,
RA Mayr J.A., Ahting U., Tiranti V., Roetig A., Iuso A., Horvath R.,
RA Tesarova M., Baric I., Uziel G., Rolinski B., Sperl W., Meitinger T.,
RA Zeviani M., Freisinger P., Prokisch H.;
RT "Mutation screening of 75 candidate genes in 152 complex I deficiency cases
RT identifies pathogenic variants in 16 genes including NDUFB9.";
RL J. Med. Genet. 49:83-89(2012).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
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 to be not
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: Mammalian complex I is composed of 45 different subunits.
CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC -!- INTERACTION:
CC Q9Y6M9; P42858: HTT; NbExp=10; IntAct=EBI-713654, EBI-466029;
CC Q9Y6M9; P43364: MAGEA11; NbExp=4; IntAct=EBI-713654, EBI-739552;
CC Q9Y6M9; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-713654, EBI-10178634;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Peripheral membrane protein
CC {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 24 (MC1DN24)
CC [MIM:618245]: 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. MC1DN24 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:22200994}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the complex I LYR family. {ECO:0000305}.
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DR EMBL; AF044956; AAD42057.1; -; mRNA.
DR EMBL; AF261090; AAF99683.1; -; mRNA.
DR EMBL; AF067168; AAD32452.1; -; mRNA.
DR EMBL; AK313432; BAG36223.1; -; mRNA.
DR EMBL; CH471060; EAW92068.1; -; Genomic_DNA.
DR EMBL; BC007672; AAH07672.1; -; mRNA.
DR CCDS; CCDS6352.1; -.
DR RefSeq; NP_001298097.1; NM_001311168.1.
DR RefSeq; NP_004996.1; NM_005005.2.
DR PDB; 5XTC; EM; 3.70 A; p=8-179.
DR PDB; 5XTD; EM; 3.70 A; p=8-179.
DR PDB; 5XTH; EM; 3.90 A; p=8-179.
DR PDB; 5XTI; EM; 17.40 A; Bp/p=8-179.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; Q9Y6M9; -.
DR SMR; Q9Y6M9; -.
DR BioGRID; 110795; 134.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; Q9Y6M9; -.
DR IntAct; Q9Y6M9; 41.
DR MINT; Q9Y6M9; -.
DR STRING; 9606.ENSP00000276689; -.
DR BindingDB; Q9Y6M9; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; Q9Y6M9; -.
DR GlyGen; Q9Y6M9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6M9; -.
DR PhosphoSitePlus; Q9Y6M9; -.
DR SwissPalm; Q9Y6M9; -.
DR BioMuta; NDUFB9; -.
DR DMDM; 8134589; -.
DR EPD; Q9Y6M9; -.
DR jPOST; Q9Y6M9; -.
DR MassIVE; Q9Y6M9; -.
DR MaxQB; Q9Y6M9; -.
DR PaxDb; Q9Y6M9; -.
DR PeptideAtlas; Q9Y6M9; -.
DR PRIDE; Q9Y6M9; -.
DR ProteomicsDB; 86739; -.
DR TopDownProteomics; Q9Y6M9; -.
DR Antibodypedia; 27088; 350 antibodies from 34 providers.
DR DNASU; 4715; -.
DR Ensembl; ENST00000276689.8; ENSP00000276689.3; ENSG00000147684.10.
DR Ensembl; ENST00000677021.1; ENSP00000504235.1; ENSG00000147684.10.
DR GeneID; 4715; -.
DR KEGG; hsa:4715; -.
DR MANE-Select; ENST00000276689.8; ENSP00000276689.3; NM_005005.3; NP_004996.1.
DR UCSC; uc003yrg.5; human.
DR CTD; 4715; -.
DR DisGeNET; 4715; -.
DR GeneCards; NDUFB9; -.
DR HGNC; HGNC:7704; NDUFB9.
DR HPA; ENSG00000147684; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; NDUFB9; -.
DR MIM; 601445; gene.
DR MIM; 618245; phenotype.
DR neXtProt; NX_Q9Y6M9; -.
DR OpenTargets; ENSG00000147684; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR PharmGKB; PA31515; -.
DR VEuPathDB; HostDB:ENSG00000147684; -.
DR eggNOG; KOG3466; Eukaryota.
DR GeneTree; ENSGT00390000005809; -.
DR HOGENOM; CLU_108081_0_0_1; -.
DR InParanoid; Q9Y6M9; -.
DR OMA; ESWCVFR; -.
DR OrthoDB; 1553121at2759; -.
DR PhylomeDB; Q9Y6M9; -.
DR TreeFam; TF315148; -.
DR BioCyc; MetaCyc:HS07466-MON; -.
DR PathwayCommons; Q9Y6M9; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; Q9Y6M9; -.
DR SIGNOR; Q9Y6M9; -.
DR BioGRID-ORCS; 4715; 419 hits in 1093 CRISPR screens.
DR ChiTaRS; NDUFB9; human.
DR GeneWiki; NDUFB9; -.
DR GenomeRNAi; 4715; -.
DR Pharos; Q9Y6M9; Tclin.
DR PRO; PR:Q9Y6M9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y6M9; protein.
DR Bgee; ENSG00000147684; Expressed in left ventricle myocardium and 188 other tissues.
DR ExpressionAtlas; Q9Y6M9; baseline and differential.
DR Genevisible; Q9Y6M9; 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:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:ProtInc.
DR GO; GO:0009060; P:aerobic respiration; IC: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; IC:ComplexPortal.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR CDD; cd20263; Complex1_LYR_NDUFB9_LYRM3; 1.
DR InterPro; IPR008011; Complex1_LYR_dom.
DR InterPro; IPR045292; Complex1_LYR_NDUFB9_LYRM3.
DR InterPro; IPR033034; NDUFB9.
DR PANTHER; PTHR12868; PTHR12868; 1.
DR Pfam; PF05347; Complex1_LYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Primary mitochondrial disease; Reference proteome;
KW Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:25944712"
FT CHAIN 2..179
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 9"
FT /id="PRO_0000174306"
FT REGION 136..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:25944712"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VARIANT 64
FT /note="L -> P (in MC1DN24; dbSNP:rs776388520)"
FT /evidence="ECO:0000269|PubMed:22200994"
FT /id="VAR_081460"
FT VARIANT 146
FT /note="P -> S (in dbSNP:rs10195)"
FT /evidence="ECO:0000269|PubMed:11042152"
FT /id="VAR_014484"
SQ SEQUENCE 179 AA; 21831 MW; 2287AE8757F85E68 CRC64;
MAFLASGPYL THQQKVLRLY KRALRHLESW CVQRDKYRYF ACLMRARFEE HKNEKDMAKA
TQLLKEAEEE FWYRQHPQPY IFPDSPGGTS YERYDCYKVP EWCLDDWHPS EKAMYPDYFA
KREQWKKLRR ESWEREVKQL QEETPPGGPL TEALPPARKE GDLPPLWWYI VTRPRERPM
