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Showing Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 (HMDBP00159)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 8 metabolites
Identification
HMDB Protein ID HMDBP00159
Secondary Accession Numbers
  • 5391
  • HMDBP03482
Name NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
Synonyms
  1. CI-B8
  2. Complex I-B8
  3. NADH-ubiquinone oxidoreductase B8 subunit
Gene Name NDUFA2
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 Not Available
Cellular Location
  1. Peripheral membrane protein
  2. Mitochondrion inner membrane
  3. Matrix side
Gene Properties
Chromosome Location Chromosome:5
Locus 5q31
SNPs NDUFA2
Gene Sequence 
>300 bp
ATGGCGGCGGCCGCAGCAAGTCGAGGAGTCGGGGCAAAGCTGGGCCTGCGTGAGATTCGC
ATCCACTTATGTCAGCGCTCGCCCGGCAGCCAGGGCGTCAGGGACTTCATTGAGAAACGC
TACGTGGAGCTGAAGAAGGCGAATCCCGACCTACCCATCCTAATCCGCGAATGCTCCGAT
GTGCAGCCCAAGCTCTGGGCCCGCTACGCATTTGGCCAAGAGACGAATGTCCCTTTGAAC
AACTTCAGTGCTGATCAGGTAACCAGAGCCCTGGAGAACGTTCTAAGTGGTAAAGCCTGA
Protein Properties
Number of Residues 99
Molecular Weight 10921.4
Theoretical pI 10.11
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
MAAAAASRGVGAKLGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPILIRECSD
VQPKLWARYAFGQETNVPLNNFSADQVTRALENVLSGKA
GenBank ID Protein 12539408
UniProtKB/Swiss-Prot ID O43678
UniProtKB/Swiss-Prot Entry Name NDUA2_HUMAN
PDB IDs
GenBank Gene ID AB054976
GeneCard ID NDUFA2
GenAtlas ID NDUFA2
HGNC ID HGNC:7685
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. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
  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. 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 ]
  6. Ton C, Hwang DM, Dempsey AA, Liew CC: Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. Biochem Biophys Res Commun. 1997 Dec 18;241(2):589-94. [PubMed:9425316 ]
  7. Brockmann C, Diehl A, Rehbein K, Strauss H, Schmieder P, Korn B, Kuhne R, Oschkinat H: The oxidized subunit B8 from human complex I adopts a thioredoxin fold. Structure. 2004 Sep;12(9):1645-54. [PubMed:15341729 ]