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Showing Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 (HMDBP00190)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 8 metabolites
Identification
HMDB Protein ID HMDBP00190
Secondary Accession Numbers
  • 5422
  • HMDBP03483
Name NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
Synonyms
  1. CI-B16.6
  2. Cell death regulatory protein GRIM-19
  3. Complex I-B16.6
  4. GRIM-19
  5. Gene associated with retinoic and IFN-induced mortality 19 protein
  6. Gene associated with retinoic and interferon-induced mortality 19 protein
  7. NADH-ubiquinone oxidoreductase B16.6 subunit
Gene Name NDUFA13
Protein Type Enzyme
Biological Properties
General Function Involved in ATP binding
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. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Nucleus
  2. Single-pass membrane protein
  3. Mitochondrion inner membrane
  4. Matrix side
Gene Properties
Chromosome Location Chromosome:1
Locus 19p13.2
SNPs NDUFA13
Gene Sequence 
>435 bp
ATGGCGGCGTCAAAGGTGAAGCAGGACATGCCTCCGCCGGGGGGCTATGGGCCCATCGAC
TACAAACGGAACTTGCCGCGTCGAGGACTGTCGGGCTACAGCATGCTGGCCATAGGGATT
GGAACCCTGATCTACGGGCACTGGAGCATAATGAAGTGGAACCGTGAGCGCAGGCGCCTA
CAAATCGAGGACTTCGAGGCTCGCATCGCGCTGTTGCCACTGTTACAGGCAGAAACCGAC
CGGAGGACCTTGCAGATGCTTCGGGAGAACCTGGAGGAGGAGGCCATCATCATGAAGGAC
GTGCCCGACTGGAAGGTGGGGGAGTCTGTGTTCCACACAACCCGCTGGGTGCCCCCCTTG
ATCGGGGAGCTGTACGGGCTGCGCACCACAGAGGAGGCTCTCCATGCCAGCCACGGCTTC
ATGTGGTACACGTAG
Protein Properties
Number of Residues 144
Molecular Weight 16698.2
Theoretical pI 8.84
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • 30-51
Protein Sequence 
>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLIYGHWSIMKWNRERRRL
QIEDFEARIALLPLLQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVPPL
IGELYGLRTTEEALHASHGFMWYT
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9P0J0
UniProtKB/Swiss-Prot Entry Name NDUAD_HUMAN
PDB IDs Not Available
GenBank Gene ID AF286697
GeneCard ID NDUFA13
GenAtlas ID NDUFA13
HGNC ID HGNC:17194
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. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed:10931946 ]
  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. [PubMed:12611891 ]
  4. Angell JE, Lindner DJ, Shapiro PS, Hofmann ER, Kalvakolanu DV: Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-beta and retinoic acid combination, using a genetic approach. J Biol Chem. 2000 Oct 27;275(43):33416-26. [PubMed:10924506 ]
  5. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed:10810093 ]
  6. Seo T, Lee D, Shim YS, Angell JE, Chidambaram NV, Kalvakolanu DV, Choe J: Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated herpesvirus interacts with a cell death regulator, GRIM19, and inhibits interferon/retinoic acid-induced cell death. J Virol. 2002 Sep;76(17):8797-807. [PubMed:12163600 ]
  7. Lufei C, Ma J, Huang G, Zhang T, Novotny-Diermayr V, Ong CT, Cao X: GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 2003 Mar 17;22(6):1325-35. [PubMed:12628925 ]
  8. Zhang J, Yang J, Roy SK, Tininini S, Hu J, Bromberg JF, Poli V, Stark GR, Kalvakolanu DV: The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9342-7. Epub 2003 Jul 16. [PubMed:12867595 ]
  9. Huang G, Lu H, Hao A, Ng DC, Ponniah S, Guo K, Lufei C, Zeng Q, Cao X: GRIM-19, a cell death regulatory protein, is essential for assembly and function of mitochondrial complex I. Mol Cell Biol. 2004 Oct;24(19):8447-56. [PubMed:15367666 ]
  10. Zhang X, Huang Q, Yang Z, Li Y, Li CY: GW112, a novel antiapoptotic protein that promotes tumor growth. Cancer Res. 2004 Apr 1;64(7):2474-81. [PubMed:15059901 ]
  11. Barnich N, Hisamatsu T, Aguirre JE, Xavier R, Reinecker HC, Podolsky DK: GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. J Biol Chem. 2005 May 13;280(19):19021-6. Epub 2005 Mar 7. [PubMed:15753091 ]
  12. Maximo V, Botelho T, Capela J, Soares P, Lima J, Taveira A, Amaro T, Barbosa AP, Preto A, Harach HR, Williams D, Sobrinho-Simoes M: Somatic and germline mutation in GRIM-19, a dual function gene involved in mitochondrial metabolism and cell death, is linked to mitochondrion-rich (Hurthle cell) tumours of the thyroid. Br J Cancer. 2005 May 23;92(10):1892-8. [PubMed:15841082 ]