NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

Details

Name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
Synonyms
  • CI-13kD-A
  • Complex I-13kD-A
  • NADH-ubiquinone oxidoreductase 13 kDa-A subunit
Gene Name
NDUFS6
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016013|NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
MAAAMTFCRLLNRCGEAARSLPLGARCFGVRVSPTGEKVTHTGQVYDDKDYRRIRFVGRQ
KEVNENFAIDLIAEQPVSEVETRVIACDGGGGALGHPKVYINLDKETKTGTCGYCGLQFR
QHHH
Number of residues
124
Molecular Weight
13711.535
Theoretical pI
8.38
GO Classification
Functions
electron carrier activity / NADH dehydrogenase (ubiquinone) activity
Processes
cardiovascular system development / cellular metabolic process / fatty acid metabolic process / mitochondrial electron transport, NADH to ubiquinone / mitochondrion morphogenesis / multicellular organism growth / multicellular organismal aging / muscle contraction / reproductive system development / respiratory electron transport chain / small molecule metabolic process
Components
mitochondrial inner membrane / mitochondrial respiratory chain complex I
General Function
Nadh dehydrogenase (ubiquinone) activity
Specific Function
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion inner membrane
Gene sequence
>lcl|BSEQ0016014|NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial (NDUFS6)
ATGGCGGCGGCGATGACCTTCTGCCGGCTGCTGAACCGGTGTGGCGAGGCGGCGCGGAGC
CTGCCCCTGGGCGCCAGGTGTTTCGGGGTGCGGGTCTCGCCGACCGGGGAGAAGGTCACG
CACACTGGCCAGGTTTATGATGATAAAGACTACAGGAGAATTCGGTTTGTAGGTCGTCAG
AAAGAGGTGAATGAAAACTTTGCCATTGATTTGATAGCAGAGCAGCCCGTGAGCGAGGTG
GAGACTCGGGTGATAGCGTGCGATGGCGGCGGGGGAGCTCTTGGCCACCCAAAAGTGTAT
ATAAACTTGGACAAAGAAACAAAAACCGGCACATGCGGTTACTGTGGGCTCCAGTTCAGA
CAGCACCACCACTAG
Chromosome Location
5
Locus
5p15.33
External Identifiers
ResourceLink
UniProtKB IDO75380
UniProtKB Entry NameNDUS6_HUMAN
GenBank Protein ID3348137
GenBank Gene IDAF044959
GenAtlas IDNDUFS6
HGNC IDHGNC:7713
General References
  1. Loeffen J, van den Heuvel L, Smeets R, Triepels R, Sengers R, Trijbels F, Smeitink J: cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed. Biochem Biophys Res Commun. 1998 Jun 29;247(3):751-8. [Article]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  3. Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA: The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. [Article]
  4. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  5. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  6. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00157NADHapproved, nutraceuticalunknownDetails