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HUMAN:DHE3

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) GLUD1 (synonyms: GLUD)
Protein Name(s) Glutamate dehydrogenase 1, mitochondrial

GDH 1

External Links
UniProt P00367
EMBL X07674
M20867
M37154
X07769
J03248
X66300
X66301
X66302
X66303
X66304
X66305
X66306
X66307
X66308
X66309
X66311
X66312
AK122685
AK294685
AL136982
CH471142
CH471142
BC040132
BC112946
X67491
CCDS CCDS7382.1
PIR A28208
I37424
S29331
S60192
RefSeq NP_005262.1
UniGene Hs.500409
PDB 1L1F
1NR1
PDBsum 1L1F
1NR1
ProteinModelPortal P00367
SMR P00367
BioGrid 109008
IntAct P00367
MINT MINT-5005913
STRING 9606.ENSP00000277865
DrugBank DB00756
PhosphoSite P00367
DMDM 118541
REPRODUCTION-2DPAGE IPI00016801
SWISS-2DPAGE P00367
UCD-2DPAGE P00367
MaxQB P00367
PaxDb P00367
PeptideAtlas P00367
PRIDE P00367
Ensembl ENST00000277865
GeneID 2746
KEGG hsa:2746
UCSC uc001keg.3
CTD 2746
GeneCards GC10M088809
GeneReviews GLUD1
HGNC HGNC:4335
HPA HPA042492
HPA044839
MIM 138130
606762
neXtProt NX_P00367
Orphanet 35878
PharmGKB PA28737
eggNOG COG0334
GeneTree ENSGT00390000000854
HOGENOM HOG000243801
HOVERGEN HBG005479
InParanoid P00367
KO K00261
OMA FINEANY
OrthoDB EOG73NG50
PhylomeDB P00367
TreeFam TF313945
BioCyc MetaCyc:HS07548-MONOMER
BRENDA 1.4.1.3
Reactome REACT_238
SABIO-RK P00367
ChiTaRS GLUD1
EvolutionaryTrace P00367
GeneWiki Glutamate_dehydrogenase_1
GenomeRNAi 2746
NextBio 10824
PRO PR:P00367
Proteomes UP000005640
Bgee P00367
CleanEx HS_GLUD1
ExpressionAtlas P00367
Genevestigator P00367
GO GO:0005737
GO:0005759
GO:0005739
GO:0043531
GO:0005524
GO:0004352
GO:0004353
GO:0005525
GO:0042802
GO:0070728
GO:0070403
GO:0008652
GO:0034641
GO:0006537
GO:0006538
GO:0006541
GO:0032024
GO:0044281
GO:0021762
GO:0072350
Gene3D 3.40.50.720
InterPro IPR006095
IPR006096
IPR006097
IPR016040
Pfam PF00208
PF02812
PRINTS PR00082
SMART SM00839
PROSITE PS00074

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0021762

substantia nigra development

PMID:22926577[1]

ECO:0007007

high throughput expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0070728

leucine binding

PMID:12742085[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:12193607[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043531

ADP binding

PMID:12742085[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0032024

positive regulation of insulin secretion

PMID:11502802[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006538

glutamate catabolic process

PMID:11032875[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006537

glutamate biosynthetic process

PMID:11032875[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:18688271[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

PMID:11032875[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004353

glutamate dehydrogenase [NAD(P)+] activity

PMID:11032875[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004352

glutamate dehydrogenase (NAD+) activity

PMID:11903050[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0072350

tricarboxylic acid metabolic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P26443

P

Seeded From UniProt

complete

involved_in

GO:0006541

glutamine metabolic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P26443

P

Seeded From UniProt

complete

involved_in

GO:0006538

glutamate catabolic process

PMID:6121377[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:15578726[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004352

glutamate dehydrogenase (NAD+) activity

PMID:15578726[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006520

cellular amino acid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006095
InterPro:IPR006096
InterPro:IPR006097

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006095
InterPro:IPR006096
InterPro:IPR006097

F

Seeded From UniProt

complete

enables

GO:0016639

oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033922

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006095
InterPro:IPR006096
InterPro:IPR006097

P

Seeded From UniProt

complete

enables

GO:0004353

glutamate dehydrogenase [NAD(P)+] activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.4.1.3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:11903050[7]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

Reactome:R-HSA-70614

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

Reactome:R-HSA-70600
Reactome:R-HSA-70589
Reactome:R-HSA-5688289
Reactome:R-HSA-5688276

ECO:0000304

author statement supported by traceable reference used in manual assertion




C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0342

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0170

C

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ Chen, S et al. (2012) Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis. Neurochem. Res. 37 2805-13 PubMed GONUTS page
  2. ↑ 2.0 2.1 Plaitakis, A et al. () 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 5.0 5.1 5.2 5.3 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
  6. ↑ 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
  7. ↑ 7.0 7.1 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
  8. ↑ Plaitakis, A et al. (1982) Abnormal glutamate metabolism in an adult-onset degenerative neurological disorder. Science 216 193-6 PubMed GONUTS page
  9. ↑ 9.0 9.1 Mastorodemos, V et al. () Molecular basis of human glutamate dehydrogenase regulation under changing energy demands. J. Neurosci. Res. 79 65-73 PubMed GONUTS page
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