NDUBB_HUMAN
ID NDUBB_HUMAN Reviewed; 153 AA.
AC Q9NX14; Q5JRR3; Q5JRR4; Q6IAB6; Q8WZ96; Q9BXX9;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;
DE AltName: Full=Complex I-ESSS;
DE Short=CI-ESSS;
DE AltName: Full=NADH-ubiquinone oxidoreductase ESSS subunit;
DE AltName: Full=Neuronal protein 17.3;
DE Short=Np17.3;
DE Short=p17.3;
DE Flags: Precursor;
GN Name=NDUFB11; ORFNames=UNQ111/PRO1064;
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=Fetal brain;
RX PubMed=10544803; DOI=10.1023/a:1018734605214;
RA Cui Y., Yu L., Gong R., Zhang M., Fan Y., Yue P., Zhao S.;
RT "Cloning and tissue expressional characterization of a full-length cDNA
RT encoding human neuronal protein P17.3.";
RL Biochem. Genet. 37:175-185(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S.,
RA Tang R., Chen X., Wu C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye;
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 IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [9]
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 [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 INVOLVEMENT IN LSDMCA3.
RX PubMed=25772934; DOI=10.1016/j.ajhg.2015.02.002;
RA van Rahden V.A., Fernandez-Vizarra E., Alawi M., Brand K., Fellmann F.,
RA Horn D., Zeviani M., Kutsche K.;
RT "Mutations in NDUFB11, encoding a complex I component of the mitochondrial
RT respiratory chain, cause microphthalmia with linear skin defects
RT syndrome.";
RL Am. J. Hum. Genet. 96:640-650(2015).
RN [12]
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 [13]
RP VARIANTS 85-TRP--GLU-153 DEL AND 108-TYR--GLU-153 DEL.
RX PubMed=25921236; DOI=10.1002/ajmg.a.37138;
RA Shehata B.M., Cundiff C.A., Lee K., Sabharwal A., Lalwani M.K., Davis A.K.,
RA Agrawal V., Sivasubbu S., Iannucci G.J., Gibson G.;
RT "Exome sequencing of patients with histiocytoid cardiomyopathy reveals a de
RT novo NDUFB11 mutation that plays a role in the pathogenesis of histiocytoid
RT cardiomyopathy.";
RL Am. J. Med. Genet. A 167A:2114-2121(2015).
RN [14]
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 [15]
RP INTERACTION WITH BCAP31, AND SUBCELLULAR LOCATION.
RX PubMed=31206022; DOI=10.1126/sciadv.aaw1386;
RA Namba T.;
RT "BAP31 regulates mitochondrial function via interaction with Tom40 within
RT ER-mitochondria contact sites.";
RL Sci. Adv. 5:eaaw1386-eaaw1386(2019).
RN [16]
RP INVOLVEMENT IN MC1DN30, AND VARIANT MC1DN30 LYS-121.
RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679;
RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y.,
RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H.,
RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y.,
RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K.,
RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M.,
RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K.,
RA Ohtake A., Okazaki Y.;
RT "A comprehensive genomic analysis reveals the genetic landscape of
RT mitochondrial respiratory chain complex deficiencies.";
RL PLoS Genet. 12:E1005679-E1005679(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 (PubMed:12611891, PubMed:27626371). Interacts with BCAP31
CC (PubMed:31206022). {ECO:0000269|PubMed:12611891,
CC ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:31206022}.
CC -!- INTERACTION:
CC Q9NX14; O95471: CLDN7; NbExp=3; IntAct=EBI-1246182, EBI-740744;
CC Q9NX14; Q15125: EBP; NbExp=3; IntAct=EBI-1246182, EBI-3915253;
CC Q9NX14; Q969F0: FATE1; NbExp=6; IntAct=EBI-1246182, EBI-743099;
CC Q9NX14; P08034: GJB1; NbExp=3; IntAct=EBI-1246182, EBI-17565645;
CC Q9NX14; Q96P66: GPR101; NbExp=3; IntAct=EBI-1246182, EBI-17935713;
CC Q9NX14; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-1246182, EBI-13345167;
CC Q9NX14; O15529: GPR42; NbExp=3; IntAct=EBI-1246182, EBI-18076404;
CC Q9NX14; P31937: HIBADH; NbExp=3; IntAct=EBI-1246182, EBI-11427100;
CC Q9NX14; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-1246182, EBI-6268651;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:31206022, ECO:0000305|PubMed:12611891}; Single-pass
CC membrane protein {ECO:0000305}. Note=The interaction with BCAP31
CC mediates mitochondria localization. {ECO:0000269|PubMed:31206022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NX14-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NX14-2; Sequence=VSP_018251;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Linear skin defects with multiple congenital anomalies 3
CC (LSDMCA3) [MIM:300952]: A disorder characterized by dermal, ocular,
CC neurological and cardiac abnormalities. LSDMCA3 clinical features
CC include linear skin defects on face and neck at birth, lacrimal duct
CC atresia, myopia, nystagmus, strabismus, cardiomyopathy, axial
CC hypotonia, seizures, corpus callosum agenesis, and dilation of lateral
CC ventricles. {ECO:0000269|PubMed:25772934}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 30 (MC1DN30)
CC [MIM:301021]: 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. {ECO:0000269|PubMed:26741492}. Note=The disease may
CC be caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the complex I NDUFB11 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF044213; AAL32064.1; -; mRNA.
DR EMBL; AF251063; AAK34953.1; -; mRNA.
DR EMBL; AK000501; BAA91208.1; -; mRNA.
DR EMBL; AY359056; AAQ89415.1; -; mRNA.
DR EMBL; CR457239; CAG33520.1; -; mRNA.
DR EMBL; AL513366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010665; AAH10665.1; -; mRNA.
DR EMBL; BC107805; AAI07806.1; -; mRNA.
DR CCDS; CCDS14273.1; -. [Q9NX14-2]
DR CCDS; CCDS48100.1; -. [Q9NX14-1]
DR RefSeq; NP_001129470.1; NM_001135998.2. [Q9NX14-1]
DR RefSeq; NP_061929.2; NM_019056.6. [Q9NX14-2]
DR PDB; 5XTC; EM; 3.70 A; e=54-150.
DR PDB; 5XTD; EM; 3.70 A; e=54-150.
DR PDB; 5XTH; EM; 3.90 A; e=54-150.
DR PDB; 5XTI; EM; 17.40 A; Be/e=54-150.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; Q9NX14; -.
DR SMR; Q9NX14; -.
DR BioGRID; 120026; 105.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; Q9NX14; -.
DR IntAct; Q9NX14; 66.
DR MINT; Q9NX14; -.
DR STRING; 9606.ENSP00000276062; -.
DR BindingDB; Q9NX14; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugCentral; Q9NX14; -.
DR CarbonylDB; Q9NX14; -.
DR GlyGen; Q9NX14; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX14; -.
DR PhosphoSitePlus; Q9NX14; -.
DR BioMuta; NDUFB11; -.
DR DMDM; 32469787; -.
DR EPD; Q9NX14; -.
DR jPOST; Q9NX14; -.
DR MassIVE; Q9NX14; -.
DR MaxQB; Q9NX14; -.
DR PeptideAtlas; Q9NX14; -.
DR PRIDE; Q9NX14; -.
DR ProteomicsDB; 83021; -. [Q9NX14-1]
DR ProteomicsDB; 83022; -. [Q9NX14-2]
DR TopDownProteomics; Q9NX14-1; -. [Q9NX14-1]
DR TopDownProteomics; Q9NX14-2; -. [Q9NX14-2]
DR Antibodypedia; 25274; 180 antibodies from 24 providers.
DR DNASU; 54539; -.
DR Ensembl; ENST00000377811.4; ENSP00000367042.3; ENSG00000147123.12. [Q9NX14-1]
DR Ensembl; ENST00000687244.1; ENSP00000509334.1; ENSG00000147123.12. [Q9NX14-2]
DR GeneID; 54539; -.
DR KEGG; hsa:54539; -.
DR MANE-Select; ENST00000377811.4; ENSP00000367042.3; NM_001135998.3; NP_001129470.1.
DR UCSC; uc004dhc.4; human. [Q9NX14-1]
DR CTD; 54539; -.
DR DisGeNET; 54539; -.
DR GeneCards; NDUFB11; -.
DR GeneReviews; NDUFB11; -.
DR HGNC; HGNC:20372; NDUFB11.
DR HPA; ENSG00000147123; Tissue enhanced (skeletal).
DR MalaCards; NDUFB11; -.
DR MIM; 300403; gene.
DR MIM; 300952; phenotype.
DR MIM; 301021; phenotype.
DR neXtProt; NX_Q9NX14; -.
DR OpenTargets; ENSG00000147123; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR Orphanet; 2556; Microphthalmia with linear skin defects syndrome.
DR PharmGKB; PA134924203; -.
DR VEuPathDB; HostDB:ENSG00000147123; -.
DR eggNOG; KOG4808; Eukaryota.
DR GeneTree; ENSGT00390000003022; -.
DR HOGENOM; CLU_109862_0_0_1; -.
DR InParanoid; Q9NX14; -.
DR OMA; CAQSHFR; -.
DR OrthoDB; 1609364at2759; -.
DR PhylomeDB; Q9NX14; -.
DR TreeFam; TF314671; -.
DR BioCyc; MetaCyc:HS14193-MON; -.
DR PathwayCommons; Q9NX14; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; Q9NX14; -.
DR SIGNOR; Q9NX14; -.
DR BioGRID-ORCS; 54539; 64 hits in 710 CRISPR screens.
DR ChiTaRS; NDUFB11; human.
DR GeneWiki; NDUFB11; -.
DR GenomeRNAi; 54539; -.
DR Pharos; Q9NX14; Tclin.
DR PRO; PR:Q9NX14; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NX14; protein.
DR Bgee; ENSG00000147123; Expressed in apex of heart and 201 other tissues.
DR Genevisible; Q9NX14; 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:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
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; IPR019329; NADH_UbQ_OxRdtase_ESSS_su.
DR PANTHER; PTHR13327; PTHR13327; 1.
DR Pfam; PF10183; ESSS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cardiomyopathy; Disease variant;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..153
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 11, mitochondrial"
FT /id="PRO_0000020057"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 40..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 113
FT /note="R -> RCTGCPRAWDG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_018251"
FT VARIANT 85..153
FT /note="Missing (found in a patient with histiocytoid
FT cardiomyopathy; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25921236"
FT /id="VAR_078941"
FT VARIANT 108..153
FT /note="Missing (found in a patient with histiocytoid
FT cardiomyopathy; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25921236"
FT /id="VAR_078942"
FT VARIANT 121
FT /note="E -> K (in MC1DN30; dbSNP:rs1057519073)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076277"
FT CONFLICT 13
FT /note="L -> P (in Ref. 1; AAL32064)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> D (in Ref. 5; CAG33520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 17317 MW; 2AF8FDD248A86C41 CRC64;
MAAGLFGLSA RRLLAAAATR GLPAARVRWE SSFSRTVVAP SAVAGKRPPE PTTPWQEDPE
PEDENLYEKN PDSHGYDKDP VLDVWNMRLV FFFGVSIILV LGSTFVAYLP DYRMKEWSRR
EAERLVKYRE ANGLPIMESN CFDPSKIQLP EDE
