View source for IDH3G

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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Isocitrate dehydrogenase 3 (NAD+) gamma
 | HGNCid = 5386
 | Symbol = IDH3G
 | AltSymbols =; H-IDHG
 | OMIM = 300089
 | ECnumber =  
 | Homologene = 55803
 | MGIid = 1099463
 | GeneAtlas_image1 = PBB_GE_IDH3G_202471_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_IDH3G_214333_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004449 |text = isocitrate dehydrogenase (NAD+) activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016652 |text = oxidoreductase activity, acting on NADH or NADPH, NAD or NADP as acceptor}} 
 | Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} 
 | Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006099 |text = tricarboxylic acid cycle}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3421
    | Hs_Ensembl = ENSG00000067829
    | Hs_RefseqProtein = NP_004126
    | Hs_RefseqmRNA = NM_004135
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 152704415
    | Hs_GenLoc_end = 152713172
    | Hs_Uniprot = P51553
    | Mm_EntrezGene = 15929
    | Mm_Ensembl = ENSMUSG00000002010
    | Mm_RefseqmRNA = NM_008323
    | Mm_RefseqProtein = NP_032349
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 70031683
    | Mm_GenLoc_end = 70039617
    | Mm_Uniprot = Q3TGZ3
  }}
}}
'''Isocitrate dehydrogenase 3 (NAD+) gamma''', also known as '''IDH3G''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IDH3G isocitrate dehydrogenase 3 (NAD+) gamma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3421| accessdate = }}</ref>

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{{PBB_Summary
| section_title = 
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: IDH3G isocitrate dehydrogenase 3 (NAD+) gamma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3421| accessdate = }}</ref>
}}

==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Sandoval N, Bauer D, Brenner V, ''et al.'' |title=The genomic organization of a human creatine transporter (CRTR) gene located in Xq28. |journal=Genomics |volume=35 |issue= 2 |pages= 383-5 |year= 1996 |pmid= 8661155 |doi= 10.1006/geno.1996.0373 }}
*{{cite journal  | author=Brenner V, Nyakatura G, Rosenthal A, Platzer M |title=Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse. |journal=Genomics |volume=44 |issue= 1 |pages= 8-14 |year= 1997 |pmid= 9286695 |doi= 10.1006/geno.1997.4822 }}
*{{cite journal  | author=Kim YO, Koh HJ, Kim SH, ''et al.'' |title=Identification and functional characterization of a novel, tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta subunit isoform. |journal=J. Biol. Chem. |volume=274 |issue= 52 |pages= 36866-75 |year= 2000 |pmid= 10601238 |doi=  }}
*{{cite journal  | author=Weiss C, Zeng Y, Huang J, ''et al.'' |title=Bovine NAD+-dependent isocitrate dehydrogenase: alternative splicing and tissue-dependent expression of subunit 1. |journal=Biochemistry |volume=39 |issue= 7 |pages= 1807-16 |year= 2000 |pmid= 10677231 |doi=  }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
*{{cite journal  | author=Soundar S, O'hagan M, Fomulu KS, Colman RF |title=Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase. |journal=J. Biol. Chem. |volume=281 |issue= 30 |pages= 21073-81 |year= 2006 |pmid= 16737955 |doi= 10.1074/jbc.M602956200 }}
*{{cite journal  | author=Bzymek KP, Colman RF |title=Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase. |journal=Biochemistry |volume=46 |issue= 18 |pages= 5391-7 |year= 2007 |pmid= 17432878 |doi= 10.1021/bi700061t }}
}}
{{refend}}

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