IDH3G

General Information

Full gene name:isocitrate dehydrogenase 3 (NAD+) gamma
Entrez Gene ID:3421
Location:Xq28
Synonyms:H-IDHG
Type:protein-coding

User SNPs

SNPs given by the user that are near or inside this gene:

SNP Distance (bp) Direction
rs3020789 158234 downstream

NCBI Summary

Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the gamma subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. This gene is a candidate gene for periventricular heterotopia. Several alternatively spliced transcript variants of this gene have been described, but only some of their full length natures have been determined. [provided by RefSeq, Jul 2008]

OMIM

OMIM ID:`OMIM ID 300089 `_

NCBI Phenotypes

No phenotypes found linked to this gene.

Gene Ontology

  • nucleolus
  • magnesium ion binding
  • NAD binding
  • negative regulation of growth
  • isocitrate dehydrogenase (NAD+) activity
  • carbohydrate metabolic process
  • mitochondrial matrix
  • small molecule metabolic process
  • 2-oxoglutarate metabolic process
  • mitochondrion
  • isocitrate metabolic process
  • nucleus
  • ATP binding
  • NADH metabolic process
  • tricarboxylic acid cycle

GeneRIFs

  • active sites of the human NAD-IDH are shared between alpha and gamma subunits and between alpha and beta subunits [PMID 16737955]
  • Affinity Capture-MS [PMID 17314511]
  • Aspartate-190 is a determinant of IDH gamma subunit affinity for the manganese (MnII) ion, as well as for nicotinamide-adenine dinucleotide (NAD), but is not directly required for the catalytic reaction. [PMID 17432878]

PubMed Articles

Recent articles:

  • Barbe L et al. “Toward a confocal subcellular atlas of the human proteome.” Mol Cell Proteomics. 2008 Mar;7(3):499-508. PMID 18029348
  • Bzymek KP et al. “Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase.” Biochemistry. 2007 May 8;46(18):5391-7. PMID 17432878
  • Koch HB et al. “Large-scale identification of c-MYC-associated proteins using a combined TAP/MudPIT approach.” Cell Cycle. 2007 Jan 15;6(2):205-17. PMID 17314511
  • Soundar S et al. “Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase.” J Biol Chem. 2006 Jul 28;281(30):21073-81. PMID 16737955
  • Mehrle A et al. “The LIFEdb database in 2006.” Nucleic Acids Res. 2006 Jan 1;34(Database issue):D415-8. PMID 16381901
  • Gerhard DS et al. “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. PMID 15489334
  • Wiemann S et al. “From ORFeome to biology: a functional genomics pipeline.” Genome Res. 2004 Oct;14(10B):2136-44. PMID 15489336
  • Soundar S et al. “Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase.” J Biol Chem. 2003 Dec 26;278(52):52146-53. PMID 14555658
  • Strausberg RL et al. “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.” Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. PMID 12477932
  • Simpson JC et al. “Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.” EMBO Rep. 2000 Sep;1(3):287-92. PMID 11256614

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