HUMAN:DHE3

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Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
Gene Name(s)	GLUD1 ( synonyms: GLUD )
Protein Name(s)	Glutamate dehydrogenase 1, mitochondrial GDH 1
External Links
UniProt Identifier	DHE3_HUMAN
UniProt Accessions	P00367, Q5TBU3,
EMBL	X07674, M20867, M37154, X07769, J03248, X66300, X66301, X66302, X66303, X66304, X66305, X66306, X66307, X66308, X66309, X66311, X66312, AL136982, BC040132, BC112946, X67491,
PIR	A28208, I37424, S29331, S60192,
RefSeq	NP_005262.1,
PDB	1L1F, 1NR1,
IntAct	P00367,
Ensembl	ENST00000277865,
Pfam	PF00208, PF02812,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0005759	mitochondrial matrix		IEA: Inferred from Electronic Annotation		C	Source: UniProtKB-SubCell
	GO:0043531	ADP binding		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0005524	ATP binding		IEA: Inferred from Electronic Annotation		F	Source: UniProtKB-KW
	GO:0004353	glutamate dehydrogenase [NAD(P)+] activity		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0004352	glutamate dehydrogenase activity		IDA: Inferred from Direct Assay		F	Source: UniProtKB
	GO:0005525	GTP binding		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0042802	identical protein binding		TAS: Traceable Author Statement		F	Source: BHF-UCL
	GO:0070728	leucine binding		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0070403	NAD binding		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0006537	glutamate biosynthetic process		IDA: Inferred from Direct Assay		P	Source: BHF-UCL
	GO:0019459	glutamate deamidation		IDA: Inferred from Direct Assay		P	Source: BHF-UCL
	GO:0055114	oxidation reduction		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
	GO:0032024	positive regulation of insulin secretion		IMP: Inferred from Mutant Phenotype		P	Source: BHF-UCL
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F
	GO:0004352	glutamate dehydrogenase activity	PMID:11903050^[1]	IDA: Inferred from Direct Assay		F
	GO:0004352	glutamate dehydrogenase activity	PMID:15578726^[2]	IDA: Inferred from Direct Assay		F
	GO:0004353	glutamate dehydrogenase (NAD(P)+) activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:1.4.1.3	F
	GO:0004353	glutamate dehydrogenase (NAD(P)+) activity	PMID:11032875^[3]	IDA: Inferred from Direct Assay		F
	GO:0004353	glutamate dehydrogenase (NAD(P)+) activity	Reactome:REACT_1896	EXP: Inferred from Experiment		F
	GO:0004353	glutamate dehydrogenase (NAD(P)+) activity	Reactome:REACT_710	EXP: Inferred from Experiment		F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016040	F
	GO:0005515	protein binding	PMID:16959573^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y6E7	F
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F
	GO:0005525	GTP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0342	F
	GO:0005525	GTP binding	PMID:11032875^[3]	IDA: Inferred from Direct Assay		F
	GO:0005737	cytoplasm	PMID:18688271^[5]	IDA: Inferred from Direct Assay		C
	GO:0005739	mitochondrion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0496	C
	GO:0005739	mitochondrion	PMID:15578726^[2]	IDA: Inferred from Direct Assay		C
	GO:0005759	mitochondrial matrix	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0170	C
	GO:0005759	mitochondrial matrix	Reactome:REACT_1896	TAS: Traceable Author Statement		C
	GO:0005759	mitochondrial matrix	Reactome:REACT_710	TAS: Traceable Author Statement		C
	GO:0006520	cellular amino acid metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006095	P
	GO:0006520	cellular amino acid metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006096	P
	GO:0006520	cellular amino acid metabolic process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006097	P
	GO:0006537	glutamate biosynthetic process	PMID:11032875^[3]	IDA: Inferred from Direct Assay		P
	GO:0006538	glutamate catabolic process	PMID:11032875^[3]	IDA: Inferred from Direct Assay		P
	GO:0006538	glutamate catabolic process	PMID:6121377^[6]	IDA: Inferred from Direct Assay		P
	GO:0008652	cellular amino acid biosynthetic process	Reactome:REACT_238	TAS: Traceable Author Statement		P
	GO:0016491	oxidoreductase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006095	F
	GO:0016491	oxidoreductase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006096	F
	GO:0016491	oxidoreductase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006097	F
	GO:0016491	oxidoreductase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0560	F
	GO:0032024	positive regulation of insulin secretion	PMID:11502802^[7]	IMP: Inferred from Mutant Phenotype		P
	GO:0034641	cellular nitrogen compound metabolic process	Reactome:REACT_13	TAS: Traceable Author Statement		P
	GO:0042802	identical protein binding	PMID:11903050^[1]	TAS: Traceable Author Statement		F
	GO:0043531	ADP binding	PMID:12742085^[8]	IDA: Inferred from Direct Assay		F
	GO:0055114	oxidation-reduction process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006095	P
	GO:0055114	oxidation-reduction process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006096	P
	GO:0055114	oxidation-reduction process	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR006097	P
	GO:0055114	oxidation-reduction process	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0560	P
	GO:0070403	NAD+ binding	PMID:12193607^[9]	IDA: Inferred from Direct Assay		F
	GO:0070728	leucine binding	PMID:12742085^[8]	IDA: Inferred from Direct Assay		F
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Fang J et al. (2002) Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J 363: 81-7 PubMed GONUTS page
↑ ^2.0 ^2.1 Mastorodemos V et al. (2005) Molecular basis of human glutamate dehydrogenase regulation under changing energy demands. J Neurosci Res 79: 65-73 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Plaitakis A et al. (2000) Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biologic function. J Neurochem 75: 1862-9 PubMed GONUTS page
↑ Haigis MC et al. (2006) SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126: 941-54 PubMed GONUTS page
↑ Rosso L et al. (2008) Mitochondrial targeting adaptation of the hominoid-specific glutamate dehydrogenase driven by positive Darwinian selection. PLoS Genet 4: e1000150 PubMed GONUTS page
↑ Plaitakis A et al. (1982) Abnormal glutamate metabolism in an adult-onset degenerative neurological disorder. Science 216: 193-6 PubMed GONUTS page
↑ Kelly A et al. (2001) Acute insulin responses to leucine in children with the hyperinsulinism/hyperammonemia syndrome. J Clin Endocrinol Metab 86: 3724-8 PubMed GONUTS page
↑ ^8.0 ^8.1 Plaitakis A et al. (2003) Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme. Neurochem Int 43: 401-10 PubMed GONUTS page
↑ Yoon HY et al. (2002) Importance of glutamate 279 for the coenzyme binding of human glutamate dehydrogenase. J Biol Chem 277: 41448-54 PubMed GONUTS page

[PMID:11903050-0] 1.0 ^1.1 Fang J et al. (2002) Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J 363: 81-7 PubMed GONUTS page

[PMID:15578726-1] 2.0 ^2.1 Mastorodemos V et al. (2005) Molecular basis of human glutamate dehydrogenase regulation under changing energy demands. J Neurosci Res 79: 65-73 PubMed GONUTS page

[PMID:11032875-2] 3.0 ^3.1 ^3.2 ^3.3 Plaitakis A et al. (2000) Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biologic function. J Neurochem 75: 1862-9 PubMed GONUTS page

[PMID:16959573-3] Haigis MC et al. (2006) SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126: 941-54 PubMed GONUTS page

[PMID:18688271-4] Rosso L et al. (2008) Mitochondrial targeting adaptation of the hominoid-specific glutamate dehydrogenase driven by positive Darwinian selection. PLoS Genet 4: e1000150 PubMed GONUTS page

[PMID:6121377-5] Plaitakis A et al. (1982) Abnormal glutamate metabolism in an adult-onset degenerative neurological disorder. Science 216: 193-6 PubMed GONUTS page

[PMID:11502802-6] Kelly A et al. (2001) Acute insulin responses to leucine in children with the hyperinsulinism/hyperammonemia syndrome. J Clin Endocrinol Metab 86: 3724-8 PubMed GONUTS page

[PMID:12742085-7] 8.0 ^8.1 Plaitakis A et al. (2003) Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme. Neurochem Int 43: 401-10 PubMed GONUTS page

[PMID:12193607-8] Yoon HY et al. (2002) Importance of glutamate 279 for the coenzyme binding of human glutamate dehydrogenase. J Biol Chem 277: 41448-54 PubMed GONUTS page

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HUMAN:DHE3

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