NDUB8_HUMAN
ID NDUB8_HUMAN Reviewed; 186 AA.
AC O95169; A8K0L4; Q5W143; Q5W144; Q5W145; Q9UG53; Q9UJR4; Q9UQF3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;
DE AltName: Full=Complex I-ASHI;
DE Short=CI-ASHI;
DE AltName: Full=NADH-ubiquinone oxidoreductase ASHI subunit;
DE Flags: Precursor;
GN Name=NDUFB8;
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 [MRNA] (ISOFORM 1).
RA Ge H.P., Yu L., Jin L., Fu Q., Wang X.K., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to Bos taurus CI-
RT ASHI mRNA.";
RL Submitted (JUL-2003) 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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
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 MRNA] (ISOFORMS 1 AND 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-71.
RC TISSUE=Blood;
RX PubMed=10570959; DOI=10.1016/s0378-1119(99)00330-3;
RA Emahazion T., Jobs M., Howell W.M., Siegfried M., Wyoni P.I., Prince J.A.,
RA Brookes J.A.;
RT "Identification of 167 polymorphisms in 88 genes from candidate
RT neurodegeneration pathways.";
RL Gene 238:315-324(1999).
RN [11]
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 [12]
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 [13]
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 [14]
RP INVOLVEMENT IN MC1DN32, AND VARIANTS MC1DN32 HIS-62; GLN-76;
RP 105-MET--VAL-156 DEL AND TRP-144.
RX PubMed=29429571; DOI=10.1016/j.ajhg.2018.01.008;
RA Piekutowska-Abramczuk D., Assouline Z., Matakovic L., Feichtinger R.G.,
RA Konarikova E., Jurkiewicz E., Stawinski P., Gusic M., Koller A., Pollak A.,
RA Gasperowicz P., Trubicka J., Ciara E., Iwanicka-Pronicka K., Rokicki D.,
RA Hanein S., Wortmann S.B., Sperl W., Roetig A., Prokisch H., Pronicka E.,
RA Ploski R., Barcia G., Mayr J.A.;
RT "NDUFB8 Mutations Cause Mitochondrial Complex I Deficiency in Individuals
RT with Leigh-like Encephalomyopathy.";
RL Am. J. Hum. Genet. 102:460-467(2018).
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=3;
CC Name=1;
CC IsoId=O95169-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95169-2; Sequence=VSP_054843, VSP_054844;
CC Name=3;
CC IsoId=O95169-3; Sequence=VSP_054842;
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 32 (MC1DN32)
CC [MIM:618252]: 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. MC1DN32 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:29429571}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the complex I NDUFB8 subunit family.
CC {ECO:0000305}.
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DR EMBL; AF044958; AAD05422.1; -; mRNA.
DR EMBL; AF115968; AAP97239.1; -; mRNA.
DR EMBL; AF077028; AAD27761.1; -; mRNA.
DR EMBL; AL080056; CAB45691.1; -; mRNA.
DR EMBL; CR533490; CAG38521.1; -; mRNA.
DR EMBL; AK289579; BAF82268.1; -; mRNA.
DR EMBL; AK295867; BAG58666.1; -; mRNA.
DR EMBL; AL133352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49819.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49820.1; -; Genomic_DNA.
DR EMBL; BC000466; AAH00466.1; -; mRNA.
DR EMBL; BC019276; AAH19276.1; -; mRNA.
DR EMBL; BI602529; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Y18944; CAB46274.1; -; Genomic_DNA.
DR CCDS; CCDS65916.1; -. [O95169-3]
DR CCDS; CCDS65917.1; -. [O95169-2]
DR CCDS; CCDS7497.1; -. [O95169-1]
DR PIR; JE0382; JE0382.
DR RefSeq; NP_001271296.1; NM_001284367.1. [O95169-2]
DR RefSeq; NP_001271297.1; NM_001284368.1. [O95169-3]
DR RefSeq; NP_004995.1; NM_005004.3. [O95169-1]
DR PDB; 5XTC; EM; 3.70 A; c=34-186.
DR PDB; 5XTD; EM; 3.70 A; c=34-186.
DR PDB; 5XTH; EM; 3.90 A; c=34-186.
DR PDB; 5XTI; EM; 17.40 A; Bc/c=34-186.
DR PDBsum; 5XTC; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O95169; -.
DR SMR; O95169; -.
DR BioGRID; 110794; 132.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O95169; -.
DR IntAct; O95169; 46.
DR MINT; O95169; -.
DR STRING; 9606.ENSP00000299166; -.
DR BindingDB; O95169; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O95169; -.
DR GlyGen; O95169; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95169; -.
DR MetOSite; O95169; -.
DR PhosphoSitePlus; O95169; -.
DR SwissPalm; O95169; -.
DR BioMuta; NDUFB8; -.
DR EPD; O95169; -.
DR jPOST; O95169; -.
DR MassIVE; O95169; -.
DR MaxQB; O95169; -.
DR PaxDb; O95169; -.
DR PeptideAtlas; O95169; -.
DR PRIDE; O95169; -.
DR ProteomicsDB; 50683; -. [O95169-1]
DR ProteomicsDB; 65796; -.
DR ProteomicsDB; 65797; -.
DR TopDownProteomics; O95169-1; -. [O95169-1]
DR Antibodypedia; 1271; 105 antibodies from 25 providers.
DR DNASU; 4714; -.
DR Ensembl; ENST00000299166.9; ENSP00000299166.4; ENSG00000166136.16. [O95169-1]
DR Ensembl; ENST00000370320.4; ENSP00000359344.4; ENSG00000166136.16. [O95169-2]
DR Ensembl; ENST00000370322.5; ENSP00000359346.1; ENSG00000166136.16. [O95169-3]
DR GeneID; 4714; -.
DR KEGG; hsa:4714; -.
DR MANE-Select; ENST00000299166.9; ENSP00000299166.4; NM_005004.4; NP_004995.1.
DR UCSC; uc001kri.3; human. [O95169-1]
DR CTD; 4714; -.
DR DisGeNET; 4714; -.
DR GeneCards; NDUFB8; -.
DR HGNC; HGNC:7703; NDUFB8.
DR HPA; ENSG00000166136; Low tissue specificity.
DR MalaCards; NDUFB8; -.
DR MIM; 602140; gene.
DR MIM; 618252; phenotype.
DR neXtProt; NX_O95169; -.
DR OpenTargets; ENSG00000166136; -.
DR Orphanet; 70474; Leigh syndrome with cardiomyopathy.
DR PharmGKB; PA31514; -.
DR VEuPathDB; HostDB:ENSG00000166136; -.
DR eggNOG; KOG4040; Eukaryota.
DR GeneTree; ENSGT00390000000628; -.
DR HOGENOM; CLU_108654_1_0_1; -.
DR InParanoid; O95169; -.
DR OMA; ATRTAHY; -.
DR OrthoDB; 1427659at2759; -.
DR PhylomeDB; O95169; -.
DR TreeFam; TF317319; -.
DR BioCyc; MetaCyc:HS09335-MON; -.
DR PathwayCommons; O95169; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O95169; -.
DR SIGNOR; O95169; -.
DR BioGRID-ORCS; 4714; 287 hits in 1084 CRISPR screens.
DR ChiTaRS; NDUFB8; human.
DR GeneWiki; NDUFB8; -.
DR GenomeRNAi; 4714; -.
DR Pharos; O95169; Tclin.
DR PRO; PR:O95169; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95169; protein.
DR Bgee; ENSG00000166136; Expressed in endothelial cell and 215 other tissues.
DR ExpressionAtlas; O95169; baseline and differential.
DR Genevisible; O95169; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
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; NAS:UniProtKB.
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; IPR008699; NDUFB8.
DR InterPro; IPR016551; Ndufb8_metazoa.
DR PANTHER; PTHR12840; PTHR12840; 1.
DR Pfam; PF05821; NDUF_B8; 1.
DR PIRSF; PIRSF009288; NDUB8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 29..186
FT /note="NADH dehydrogenase [ubiquinone] 1 beta subcomplex
FT subunit 8, mitochondrial"
FT /id="PRO_0000020046"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054842"
FT VAR_SEQ 157..172
FT /note="GPKQYPYNNLYLERGG -> CRHHFSYNLGFLSALG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054843"
FT VAR_SEQ 173..186
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054844"
FT VARIANT 62
FT /note="Y -> H (in MC1DN32; dbSNP:rs1554843434)"
FT /evidence="ECO:0000269|PubMed:29429571"
FT /id="VAR_081466"
FT VARIANT 76
FT /note="P -> Q (in MC1DN32; dbSNP:rs1239013578)"
FT /evidence="ECO:0000269|PubMed:29429571"
FT /id="VAR_081467"
FT VARIANT 105..156
FT /note="Missing (in MC1DN32; due to a nucleotide
FT substitution that results in exon 4 skipping or in missense
FT variant W-144; patient cells contain both type of
FT transcripts; transcript lacking exon 4 is the most
FT abundant)"
FT /evidence="ECO:0000269|PubMed:29429571"
FT /id="VAR_081468"
FT VARIANT 144
FT /note="C -> W (in MC1DN32; due to a nucleotide substitution
FT that results in exon 4 skipping or missense variant W-144;
FT patient cells contain both type of transcripts; transcript
FT with the missense variant is the less abundant;
FT dbSNP:rs1554843251)"
FT /evidence="ECO:0000269|PubMed:29429571"
FT /id="VAR_081469"
FT CONFLICT 44
FT /note="T -> I (in Ref. 4; CAB45691 and 5; CAG38521)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="G -> S (in Ref. 3; AAD27761)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="Y -> N (in Ref. 4; CAB45691 and 5; CAG38521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 21766 MW; 518459D44965D202 CRC64;
MAVARAGVLG VQWLQRASRN VMPLGARTAS HMTKDMFPGP YPRTPEERAA AAKKYNMRVE
DYEPYPDDGM GYGDYPKLPD RSQHERDPWY SWDQPGLRLN WGEPMHWHLD MYNRNRVDTS
PTPVSWHVMC MQLFGFLAFM IFMCWVGDVY PVYQPVGPKQ YPYNNLYLER GGDPSKEPER
VVHYEI
