NDUB1_HUMAN
ID NDUB1_HUMAN Reviewed; 58 AA.
AC O75438; A0AV68;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;
DE AltName: Full=Complex I-MNLL;
DE Short=CI-MNLL;
DE AltName: Full=NADH-ubiquinone oxidoreductase MNLL subunit;
GN Name=NDUFB1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Triepels R.H., Smeets R.J.P., Loeffen J.L.C.M., Ruitenbeek W.,
RA Smeitink J.A.M., van den Heuvel L.;
RT "MNLL subunit of NADH-ubiquinone oxidoreductase.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP 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 [11]
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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Single-pass membrane protein
CC {ECO:0000255}; Matrix side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75438-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75438-2; Sequence=VSP_037859;
CC -!- SIMILARITY: Belongs to the complex I NDUFB1 subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD42054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF054181; AAC39914.1; -; mRNA.
DR EMBL; AK316557; BAG48175.1; -; Transcribed_RNA.
DR EMBL; AL121773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81479.1; -; Genomic_DNA.
DR EMBL; BC009691; AAH09691.2; -; mRNA.
DR EMBL; BC126232; AAI26233.1; -; mRNA.
DR EMBL; BC126234; AAI26235.1; -; mRNA.
DR EMBL; AF050638; AAD42054.1; ALT_INIT; mRNA.
DR CCDS; CCDS9901.1; -. [O75438-1]
DR RefSeq; NP_004536.2; NM_004545.3. [O75438-1]
DR PDB; 5XTC; EM; 3.70 A; n=3-58.
DR PDB; 5XTD; EM; 3.70 A; n=3-58.
DR PDB; 5XTH; EM; 3.90 A; n=3-58.
DR PDB; 5XTI; EM; 17.40 A; Bn/n=3-58.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O75438; -.
DR SMR; O75438; -.
DR BioGRID; 110787; 87.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O75438; -.
DR IntAct; O75438; 19.
DR MINT; O75438; -.
DR STRING; 9606.ENSP00000330787; -.
DR BindingDB; O75438; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O75438; -.
DR iPTMnet; O75438; -.
DR PhosphoSitePlus; O75438; -.
DR SwissPalm; O75438; -.
DR BioMuta; NDUFB1; -.
DR EPD; O75438; -.
DR jPOST; O75438; -.
DR MassIVE; O75438; -.
DR MaxQB; O75438; -.
DR PaxDb; O75438; -.
DR PeptideAtlas; O75438; -.
DR PRIDE; O75438; -.
DR ProteomicsDB; 50005; -. [O75438-1]
DR ProteomicsDB; 50006; -. [O75438-2]
DR TopDownProteomics; O75438-1; -. [O75438-1]
DR TopDownProteomics; O75438-2; -. [O75438-2]
DR Antibodypedia; 26722; 94 antibodies from 24 providers.
DR DNASU; 4707; -.
DR Ensembl; ENST00000329559.8; ENSP00000330787.4; ENSG00000183648.11. [O75438-1]
DR Ensembl; ENST00000553514.5; ENSP00000451090.2; ENSG00000183648.11. [O75438-1]
DR Ensembl; ENST00000555441.5; ENSP00000450776.1; ENSG00000183648.11. [O75438-1]
DR Ensembl; ENST00000605997.6; ENSP00000475170.1; ENSG00000183648.11. [O75438-1]
DR Ensembl; ENST00000617122.1; ENSP00000483888.1; ENSG00000183648.11. [O75438-2]
DR GeneID; 4707; -.
DR KEGG; hsa:4707; -.
DR MANE-Select; ENST00000605997.6; ENSP00000475170.1; NM_004545.4; NP_004536.3.
DR UCSC; uc001yaf.4; human. [O75438-1]
DR CTD; 4707; -.
DR GeneCards; NDUFB1; -.
DR HGNC; HGNC:7695; NDUFB1.
DR HPA; ENSG00000183648; Low tissue specificity.
DR MIM; 603837; gene.
DR neXtProt; NX_O75438; -.
DR OpenTargets; ENSG00000183648; -.
DR PharmGKB; PA31501; -.
DR VEuPathDB; HostDB:ENSG00000183648; -.
DR eggNOG; ENOG502S6X0; Eukaryota.
DR GeneTree; ENSGT00390000005052; -.
DR HOGENOM; CLU_208707_0_0_1; -.
DR InParanoid; O75438; -.
DR OMA; AREHWVN; -.
DR OrthoDB; 1624835at2759; -.
DR PhylomeDB; O75438; -.
DR TreeFam; TF324446; -.
DR BioCyc; MetaCyc:HS09306-MON; -.
DR PathwayCommons; O75438; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O75438; -.
DR SIGNOR; O75438; -.
DR BioGRID-ORCS; 4707; 94 hits in 1086 CRISPR screens.
DR ChiTaRS; NDUFB1; human.
DR GeneWiki; NDUFB1; -.
DR GenomeRNAi; 4707; -.
DR Pharos; O75438; Tclin.
DR PRO; PR:O75438; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O75438; protein.
DR Bgee; ENSG00000183648; Expressed in heart left ventricle and 199 other tissues.
DR ExpressionAtlas; O75438; baseline and differential.
DR Genevisible; O75438; 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:0016607; C:nuclear speck; 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; 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; IPR012575; NDUB1.
DR PANTHER; PTHR15222; PTHR15222; 1.
DR Pfam; PF08040; NADH_oxidored; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..58
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 1"
FT /id="PRO_0000118827"
FT TRANSMEM 11..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MICWRHPSAPCGRGEWQVPRSQLPLARVEFPVALGLGVAVGAEAAAI
FT M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037859"
SQ SEQUENCE 58 AA; 6961 MW; 2281D89AAE61EA52 CRC64;
MVNLLQIVRD HWVHVLVPMG FVIGCYLDRK SDERLTAFRN KSMLFKRELQ PSEEVTWK
