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Identification
HMDB Protein ID HMDBP00170
Secondary Accession Numbers
  • 5402
  • HMDBP03468
Name NADH dehydrogenase [ubiquinone] 1 subunit C2
Synonyms
  1. CI-B14.5b
  2. Complex I-B14.5b
  3. HLC-1
  4. Human lung cancer oncogene 1 protein
  5. NADH-ubiquinone oxidoreductase subunit B14.5b
Gene Name NDUFC2
Protein Type Enzyme
Biological Properties
General Function Involved in 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
membrane
cell part
organelle membrane
organelle inner membrane
mitochondrial inner membrane
Function
catalytic activity
nadh dehydrogenase activity
nadh dehydrogenase (quinone) activity
nadh dehydrogenase (ubiquinone) activity
oxidoreductase activity
oxidoreductase activity, acting on nadh or nadph
Process
metabolic process
generation of precursor metabolites and energy
electron transport chain
respiratory electron transport chain
cellular metabolic process
mitochondrial electron transport, nadh to ubiquinone
Cellular Location
  1. Single-pass membrane protein
  2. Mitochondrion inner membrane
  3. Matrix side
Gene Properties
Chromosome Location Chromosome:1
Locus 11q14.1
SNPs NDUFC2
Gene Sequence
>360 bp
ATGATCGCACGGCGGAACCCAGAACCCTTACGGTTTCTGCCGGATGAGGCCCGGAGCCTG
CCCCCGCCCAAGCTGACCGACCCGCGGCTCCTCTACATCGGCTTCTTGGGCTACTGCTCC
GGCCTGATTGATAACCTGATCCGGCGGAGGCCGATCGCGACGGCTGGTTTGCATCGCCAG
CTTCTATATATTACGGCCTTTTTTTTTGCTGGATATTATCTTGTAAAACGTGAAGACTAC
CTGTATGCTGTGAGGGACCGTGAAATGTTTGGATATATGAAATTACATCCAGAGGATTTT
CCTGAAGAAGATAAGAAAACATATGGTGAAATTTTTGAAAAATTCCATCCAATACGTTGA
Protein Properties
Number of Residues 119
Molecular Weight 14187.3
Theoretical pI 9.27
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • 56-75
Protein Sequence
>NADH dehydrogenase [ubiquinone] 1 subunit C2
MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQ
LLYITAFFFAGYYLVKREDYLYAVRDREMFGYMKLHPEDFPEEDKKTYGEIFEKFHPIR
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID O95298
UniProtKB/Swiss-Prot Entry Name NDUC2_HUMAN
PDB IDs Not Available
GenBank Gene ID AF087659
GeneCard ID NDUFC2
GenAtlas ID NDUFC2
HGNC ID HGNC:7706
References
General References
  1. 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. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed:11230166 ]
  4. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed:11042152 ]
  5. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed:9878551 ]
  6. 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. [PubMed:12611891 ]