ID NDUB6_HUMAN Reviewed; 128 AA.
AC O95139; A8K0Y7; Q5VYT2; Q6IB84;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 190.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;
DE AltName: Full=Complex I-B17;
DE Short=CI-B17;
DE AltName: Full=NADH-ubiquinone oxidoreductase B17 subunit;
GN Name=NDUFB6;
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=9760212; DOI=10.1007/s004390050813;
RA Smeitink J., Loeffen J., Smeets R., Triepels R., Ruitenbeek W.,
RA Trijbels F., van den Heuvel L.;
RT "Molecular characterization and mutational analysis of the human B17
RT subunit of the mitochondrial respiratory chain complex I.";
RL Hum. Genet. 103:245-250(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Hypothalamus, 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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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 [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).
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 -!- INTERACTION:
CC O95139; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1053340, EBI-781551;
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=O95139-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95139-2; Sequence=VSP_045233;
CC -!- SIMILARITY: Belongs to the complex I NDUFB6 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF035840; AAC68838.1; -; mRNA.
DR EMBL; AF067167; AAD32451.1; -; mRNA.
DR EMBL; CR456920; CAG33201.1; -; mRNA.
DR EMBL; AK289702; BAF82391.1; -; mRNA.
DR EMBL; AL353671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58541.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58542.1; -; Genomic_DNA.
DR EMBL; BC009801; AAH09801.1; -; mRNA.
DR EMBL; BC029247; AAH29247.1; -; mRNA.
DR EMBL; BI669356; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS6528.1; -. [O95139-1]
DR CCDS; CCDS6529.1; -. [O95139-2]
DR RefSeq; NP_002484.1; NM_002493.4. [O95139-1]
DR RefSeq; NP_877416.1; NM_182739.2. [O95139-2]
DR PDB; 5XTC; EM; 3.70 A; b=1-128.
DR PDB; 5XTD; EM; 3.70 A; b=1-128.
DR PDB; 5XTH; EM; 3.90 A; b=3-126.
DR PDB; 5XTI; EM; 17.40 A; Bb/b=3-126.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O95139; -.
DR SMR; O95139; -.
DR BioGRID; 110792; 50.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O95139; -.
DR IntAct; O95139; 21.
DR MINT; O95139; -.
DR STRING; 9606.ENSP00000369176; -.
DR BindingDB; O95139; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O95139; -.
DR GlyGen; O95139; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95139; -.
DR PhosphoSitePlus; O95139; -.
DR BioMuta; NDUFB6; -.
DR EPD; O95139; -.
DR jPOST; O95139; -.
DR MassIVE; O95139; -.
DR MaxQB; O95139; -.
DR PaxDb; 9606-ENSP00000369176; -.
DR PeptideAtlas; O95139; -.
DR ProteomicsDB; 50658; -. [O95139-1]
DR ProteomicsDB; 65650; -.
DR Pumba; O95139; -.
DR TopDownProteomics; O95139-1; -. [O95139-1]
DR TopDownProteomics; O95139-2; -. [O95139-2]
DR Antibodypedia; 25071; 128 antibodies from 22 providers.
DR DNASU; 4712; -.
DR Ensembl; ENST00000350021.2; ENSP00000297983.3; ENSG00000165264.11. [O95139-2]
DR Ensembl; ENST00000379847.8; ENSP00000369176.3; ENSG00000165264.11. [O95139-1]
DR GeneID; 4712; -.
DR KEGG; hsa:4712; -.
DR MANE-Select; ENST00000379847.8; ENSP00000369176.3; NM_002493.5; NP_002484.1.
DR UCSC; uc003zre.3; human. [O95139-1]
DR AGR; HGNC:7701; -.
DR CTD; 4712; -.
DR DisGeNET; 4712; -.
DR GeneCards; NDUFB6; -.
DR HGNC; HGNC:7701; NDUFB6.
DR HPA; ENSG00000165264; Low tissue specificity.
DR MIM; 603322; gene.
DR neXtProt; NX_O95139; -.
DR OpenTargets; ENSG00000165264; -.
DR PharmGKB; PA31512; -.
DR VEuPathDB; HostDB:ENSG00000165264; -.
DR eggNOG; KOG4633; Eukaryota.
DR GeneTree; ENSGT00390000007535; -.
DR InParanoid; O95139; -.
DR OMA; KYHVNTK; -.
DR OrthoDB; 5382809at2759; -.
DR PhylomeDB; O95139; -.
DR TreeFam; TF328587; -.
DR BioCyc; MetaCyc:HS09208-MONOMER; -.
DR PathwayCommons; O95139; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O95139; -.
DR SIGNOR; O95139; -.
DR BioGRID-ORCS; 4712; 327 hits in 1167 CRISPR screens.
DR ChiTaRS; NDUFB6; human.
DR GeneWiki; NDUFB6; -.
DR GenomeRNAi; 4712; -.
DR Pharos; O95139; Tclin.
DR PRO; PR:O95139; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O95139; Protein.
DR Bgee; ENSG00000165264; Expressed in heart right ventricle and 209 other cell types or tissues.
DR ExpressionAtlas; O95139; baseline and differential.
DR Genevisible; O95139; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:ProtInc.
DR GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:CAFA.
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; NAS:ComplexPortal.
DR InterPro; IPR019174; NADH_DH_b-subcmplx_su6.
DR PANTHER; PTHR15083; NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT 6; 1.
DR PANTHER; PTHR15083:SF0; NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT 6; 1.
DR Pfam; PF09782; NDUF_B6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Electron transport;
KW Membrane; 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:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..128
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 6"
FT /id="PRO_0000118807"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIU2"
FT VAR_SEQ 92..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045233"
SQ SEQUENCE 128 AA; 15489 MW; E8F419F5EB154D0B CRC64;
MTGYTPDEKL RLQQLRELRR RWLKDQELSP REPVLPPQKM GPMEKFWNKF LENKSPWRKM
VHGVYKKSIF VFTHVLVPVW IIHYYMKYHV SEKPYGIVEK KSRIFPGDTI LETGEVIPPM
KEFPDQHH
//
