UniProtKB - P00367 (DHE3_HUMAN)
Protein
Glutamate dehydrogenase 1, mitochondrial
Gene
GLUD1
Organism
Homo sapiens (Human)
Status
Functioni
Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (PubMed:11032875, PubMed:16959573, PubMed:11254391, PubMed:16023112). Plays a role in insulin homeostasis (PubMed:9571255, PubMed:11297618). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).By similarity6 Publications
Catalytic activityi
Activity regulationi
Subject to allosteric regulation. Activated by ADP (PubMed:11903050). Inhibited by GTP and ATP (PubMed:11254391, PubMed:11032875, PubMed:9571255, PubMed:11903050, PubMed:11297618). ADP can occupy the NADH binding site and activate the enzyme (PubMed:16023112). Inhibited by SIRT4 (PubMed:16959573). Inhibited by HADH (By similarity).By similarity7 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 147 | SubstrateBy similarity | 1 | |
Binding sitei | 171 | SubstrateBy similarity | 1 | |
Binding sitei | 176 | NADBy similarity | 1 | |
Active sitei | 183 | PROSITE-ProRule annotation | 1 | |
Binding sitei | 252 | NADBy similarity | 1 | |
Binding sitei | 266 | GTPBy similarity | 1 | |
Binding sitei | 270 | GTPBy similarity | 1 | |
Binding sitei | 319 | GTPBy similarity | 1 | |
Binding sitei | 322 | GTPBy similarity | 1 | |
Binding sitei | 438 | SubstrateBy similarity | 1 | |
Binding sitei | 444 | NADBy similarity | 1 | |
Binding sitei | 450 | ADPBy similarity | 1 | |
Binding sitei | 516 | ADPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 141 – 143 | NADBy similarity | 3 |
GO - Molecular functioni
- ADP binding Source: BHF-UCL
- ATP binding Source: UniProtKB-KW
- glutamate dehydrogenase (NAD+) activity Source: UniProtKB
- glutamate dehydrogenase [NAD(P)+] activity Source: BHF-UCL
- GTP binding Source: BHF-UCL
- identical protein binding Source: BHF-UCL
- leucine binding Source: BHF-UCL
- NAD+ binding Source: BHF-UCL
GO - Biological processi
- cellular amino acid biosynthetic process Source: Reactome
- glutamate biosynthetic process Source: BHF-UCL
- glutamate catabolic process Source: UniProtKB
- glutamine metabolic process Source: UniProtKB
- positive regulation of insulin secretion Source: BHF-UCL
- substantia nigra development Source: UniProtKB
- tricarboxylic acid metabolic process Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Ligand | ATP-binding, GTP-binding, NADP, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:HS07548-MONOMER |
BRENDAi | 1.4.1.3, 2681 |
PathwayCommonsi | P00367 |
Reactomei | R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis R-HSA-8964539, Glutamate and glutamine metabolism |
SABIO-RKi | P00367 |
SIGNORi | P00367 |
Names & Taxonomyi
Protein namesi | Recommended name: Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.35 Publications)Short name: GDH 1 |
Gene namesi | Name:GLUD1 Synonyms:GLUD |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000148672.8 |
HGNCi | HGNC:4335, GLUD1 |
MIMi | 138130, gene |
neXtProti | NX_P00367 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum 1 Publication
Mitochondrion
- Mitochondrion 1 Publication
Note: Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum.1 Publication
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrion Source: UniProtKB
Other locations
- cytoplasm Source: BHF-UCL
Keywords - Cellular componenti
Endoplasmic reticulum, MitochondrionPathology & Biotechi
Involvement in diseasei
Familial hyperinsulinemic hypoglycemia 6 (HHF6)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionFamilial hyperinsulinemic hypoglycemia [MIM:256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_016760 | 270 | S → C in HHF6; diminished sensitivity to GTP. 1 Publication | 1 | |
Natural variantiVAR_016761 | 274 | R → C in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs56275071EnsemblClinVar. | 1 | |
Natural variantiVAR_009270 | 318 | R → K in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909736EnsemblClinVar. | 1 | |
Natural variantiVAR_016762 | 318 | R → T in HHF6; diminished sensitivity to GTP. 1 Publication | 1 | |
Natural variantiVAR_016763 | 319 | Y → C in HHF6. 1 PublicationCorresponds to variant dbSNP:rs1554906133EnsemblClinVar. | 1 | |
Natural variantiVAR_016764 | 322 | R → C in HHF6; diminished sensitivity to GTP. 1 Publication | 1 | |
Natural variantiVAR_016765 | 322 | R → H in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs121909737EnsemblClinVar. | 1 | |
Natural variantiVAR_009271 | 349 | E → A in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909735EnsemblClinVar. | 1 | |
Natural variantiVAR_008666 | 498 | S → L in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909731EnsemblClinVar. | 1 | |
Natural variantiVAR_008667 | 499 | G → D in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909734EnsemblClinVar. | 1 | |
Natural variantiVAR_008668 | 499 | G → S in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909733EnsemblClinVar. | 1 | |
Natural variantiVAR_008669 | 501 | S → P in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909732EnsemblClinVar. | 1 | |
Natural variantiVAR_008670 | 507 | H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP; Strongly reduces inhibition by GTP. 3 PublicationsCorresponds to variant dbSNP:rs121909730EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 501 | S → A: Reduces activity and inhibition by GTP. 1 Publication | 1 | |
Mutagenesisi | 516 | R → A: Abolishes activation by ADP. 1 Publication | 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNETi | 2746 |
GeneReviewsi | GLUD1 |
MalaCardsi | GLUD1 |
MIMi | 606762, phenotype |
OpenTargetsi | ENSG00000148672 |
Orphaneti | 35878, Hyperinsulinism-hyperammonemia syndrome |
PharmGKBi | PA28737 |
Miscellaneous databases
Pharosi | P00367, Tbio |
Chemistry databases
DrugBanki | DB11081, Aluminum chloride DB00142, Glutamic acid DB04137, Guanosine-5'-Triphosphate DB00756, Hexachlorophene DB00157, NADH |
DrugCentrali | P00367 |
Polymorphism and mutation databases
BioMutai | GLUD1 |
DMDMi | 118541 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 53 | MitochondrionCombined sources2 PublicationsAdd BLAST | 53 | |
ChainiPRO_0000007206 | 54 – 558 | Glutamate dehydrogenase 1, mitochondrialAdd BLAST | 505 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 68 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 79 | PhosphoserineBy similarity | 1 | |
Modified residuei | 84 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 84 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 110 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 110 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 128 | PhosphoserineBy similarity | 1 | |
Modified residuei | 135 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 162 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 162 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 171 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 172 | ADP-ribosylcysteine1 Publication | 1 | |
Modified residuei | 183 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 183 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 187 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 191 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 191 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 200 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 211 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 227 | PhosphoserineCombined sources | 1 | |
Modified residuei | 326 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 346 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 346 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 352 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 352 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 363 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 363 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 365 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 365 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 384 | PhosphoserineCombined sources | 1 | |
Modified residuei | 386 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 390 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 390 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 399 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 410 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 415 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 415 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 457 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 457 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 457 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 477 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 477 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 480 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 480 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 503 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 503 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 503 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 512 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 527 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 527 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 527 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 545 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 545 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 548 | N6-acetyllysineBy similarity | 1 |
Post-translational modificationi
ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity (PubMed:16959573). Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer (PubMed:16023112).2 Publications
Keywords - PTMi
Acetylation, ADP-ribosylation, PhosphoproteinProteomic databases
EPDi | P00367 |
jPOSTi | P00367 |
MassIVEi | P00367 |
MaxQBi | P00367 |
PaxDbi | P00367 |
PeptideAtlasi | P00367 |
PRIDEi | P00367 |
ProteomicsDBi | 3743 4147 51236 [P00367-1] |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00016801 |
SWISS-2DPAGEi | P00367 |
UCD-2DPAGEi | P00367 |
PTM databases
iPTMneti | P00367 |
MetOSitei | P00367 |
PhosphoSitePlusi | P00367 |
SwissPalmi | P00367 |
Expressioni
Gene expression databases
Bgeei | ENSG00000148672, Expressed in hypothalamus and 241 other tissues |
ExpressionAtlasi | P00367, baseline and differential |
Genevisiblei | P00367, HS |
Organism-specific databases
HPAi | ENSG00000148672, Tissue enhanced (liver) |
Interactioni
Subunit structurei
Homohexamer (By similarity).
Interacts with HADH; this interaction inhibits the activation of GLUD1 (By similarity).
By similarityGO - Molecular functioni
- identical protein binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 109008, 81 interactors |
IntActi | P00367, 59 interactors |
MINTi | P00367 |
STRINGi | 9606.ENSP00000277865 |
Miscellaneous databases
RNActi | P00367, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P00367 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P00367 |
Family & Domainsi
Sequence similaritiesi
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.Curated
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG2250, Eukaryota |
GeneTreei | ENSGT00390000000854 |
HOGENOMi | CLU_025763_1_0_1 |
InParanoidi | P00367 |
OMAi | PCFAAFP |
PhylomeDBi | P00367 |
TreeFami | TF313945 |
Family and domain databases
CDDi | cd01076, NAD_bind_1_Glu_DH, 1 hit |
InterProi | View protein in InterPro IPR006095, Glu/Leu/Phe/Val_DH IPR033524, Glu/Leu/Phe/Val_DH_AS IPR006096, Glu/Leu/Phe/Val_DH_C IPR006097, Glu/Leu/Phe/Val_DH_dimer_dom IPR036291, NAD(P)-bd_dom_sf IPR033922, NAD_bind_Glu_DH |
Pfami | View protein in Pfam PF00208, ELFV_dehydrog, 1 hit PF02812, ELFV_dehydrog_N, 1 hit |
PRINTSi | PR00082, GLFDHDRGNASE |
SMARTi | View protein in SMART SM00839, ELFV_dehydrog, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00074, GLFV_DEHYDROGENASE, 1 hit |
s (3)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketIsoform 1 (identifier: P00367-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR
60 70 80 90 100
RHYSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY
NEAGVTFT
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_016760 | 270 | S → C in HHF6; diminished sensitivity to GTP. 1 Publication | 1 | |
Natural variantiVAR_016761 | 274 | R → C in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs56275071EnsemblClinVar. | 1 | |
Natural variantiVAR_009270 | 318 | R → K in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909736EnsemblClinVar. | 1 | |
Natural variantiVAR_016762 | 318 | R → T in HHF6; diminished sensitivity to GTP. 1 Publication | 1 | |
Natural variantiVAR_016763 | 319 | Y → C in HHF6. 1 PublicationCorresponds to variant dbSNP:rs1554906133EnsemblClinVar. | 1 | |
Natural variantiVAR_016764 | 322 | R → C in HHF6; diminished sensitivity to GTP. 1 Publication | 1 | |
Natural variantiVAR_016765 | 322 | R → H in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs121909737EnsemblClinVar. | 1 | |
Natural variantiVAR_009271 | 349 | E → A in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909735EnsemblClinVar. | 1 | |
Natural variantiVAR_008666 | 498 | S → L in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909731EnsemblClinVar. | 1 | |
Natural variantiVAR_008667 | 499 | G → D in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909734EnsemblClinVar. | 1 | |
Natural variantiVAR_008668 | 499 | G → S in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909733EnsemblClinVar. | 1 | |
Natural variantiVAR_008669 | 501 | S → P in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909732EnsemblClinVar. | 1 | |
Natural variantiVAR_008670 | 507 | H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP; Strongly reduces inhibition by GTP. 3 PublicationsCorresponds to variant dbSNP:rs121909730EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_056244 | 1 – 167 | Missing in isoform 2. 1 PublicationAdd BLAST | 167 | |
Alternative sequenceiVSP_056523 | 1 – 16 | MYRYL…SRAGP → MTCPCDNASSVFLGFC in isoform 3. 1 PublicationAdd BLAST | 16 | |
Alternative sequenceiVSP_056524 | 17 – 149 | Missing in isoform 3. 1 PublicationAdd BLAST | 133 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000277865; ENSP00000277865; ENSG00000148672 [P00367-1] |
GeneIDi | 2746 |
KEGGi | hsa:2746 |
UCSCi | uc001keh.4, human [P00367-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
Wikipedia Glutamate dehydrogenase 1 entry |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1L1F | X-ray | 2.70 | A/B/C/D/E/F | 54-558 | [»] | |
1NR1 | X-ray | 3.30 | A/B/C/D/E/F | 63-558 | [»] | |
6DQG | X-ray | 2.70 | A/B/C/D/E/F | 63-558 | [»] | |
SMRi | P00367 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109008, 81 interactors |
IntActi | P00367, 59 interactors |
MINTi | P00367 |
STRINGi | 9606.ENSP00000277865 |
Chemistry databases
DrugBanki | DB11081, Aluminum chloride DB00142, Glutamic acid DB04137, Guanosine-5'-Triphosphate DB00756, Hexachlorophene DB00157, NADH |
DrugCentrali | P00367 |
PTM databases
iPTMneti | P00367 |
MetOSitei | P00367 |
PhosphoSitePlusi | P00367 |
SwissPalmi | P00367 |
Polymorphism and mutation databases
BioMutai | GLUD1 |
DMDMi | 118541 |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00016801 |
SWISS-2DPAGEi | P00367 |
UCD-2DPAGEi | P00367 |
Proteomic databases
EPDi | P00367 |
jPOSTi | P00367 |
MassIVEi | P00367 |
MaxQBi | P00367 |
PaxDbi | P00367 |
PeptideAtlasi | P00367 |
PRIDEi | P00367 |
ProteomicsDBi | 3743 4147 51236 [P00367-1] |
Protocols and materials databases
Antibodypediai | 16023, 240 antibodies |
Genome annotation databases
Ensembli | ENST00000277865; ENSP00000277865; ENSG00000148672 [P00367-1] |
GeneIDi | 2746 |
KEGGi | hsa:2746 |
UCSCi | uc001keh.4, human [P00367-1] |
Organism-specific databases
CTDi | 2746 |
DisGeNETi | 2746 |
EuPathDBi | HostDB:ENSG00000148672.8 |
GeneCardsi | GLUD1 |
GeneReviewsi | GLUD1 |
HGNCi | HGNC:4335, GLUD1 |
HPAi | ENSG00000148672, Tissue enhanced (liver) |
MalaCardsi | GLUD1 |
MIMi | 138130, gene 606762, phenotype |
neXtProti | NX_P00367 |
OpenTargetsi | ENSG00000148672 |
Orphaneti | 35878, Hyperinsulinism-hyperammonemia syndrome |
PharmGKBi | PA28737 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG2250, Eukaryota |
GeneTreei | ENSGT00390000000854 |
HOGENOMi | CLU_025763_1_0_1 |
InParanoidi | P00367 |
OMAi | PCFAAFP |
PhylomeDBi | P00367 |
TreeFami | TF313945 |
Enzyme and pathway databases
BioCyci | MetaCyc:HS07548-MONOMER |
BRENDAi | 1.4.1.3, 2681 |
PathwayCommonsi | P00367 |
Reactomei | R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis R-HSA-8964539, Glutamate and glutamine metabolism |
SABIO-RKi | P00367 |
SIGNORi | P00367 |
Miscellaneous databases
BioGRID-ORCSi | 2746, 7 hits in 844 CRISPR screens |
ChiTaRSi | GLUD1, human |
EvolutionaryTracei | P00367 |
GeneWikii | Glutamate_dehydrogenase_1 |
GenomeRNAii | 2746 |
Pharosi | P00367, Tbio |
PROi | PR:P00367 |
RNActi | P00367, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000148672, Expressed in hypothalamus and 241 other tissues |
ExpressionAtlasi | P00367, baseline and differential |
Genevisiblei | P00367, HS |
Family and domain databases
CDDi | cd01076, NAD_bind_1_Glu_DH, 1 hit |
InterProi | View protein in InterPro IPR006095, Glu/Leu/Phe/Val_DH IPR033524, Glu/Leu/Phe/Val_DH_AS IPR006096, Glu/Leu/Phe/Val_DH_C IPR006097, Glu/Leu/Phe/Val_DH_dimer_dom IPR036291, NAD(P)-bd_dom_sf IPR033922, NAD_bind_Glu_DH |
Pfami | View protein in Pfam PF00208, ELFV_dehydrog, 1 hit PF02812, ELFV_dehydrog_N, 1 hit |
PRINTSi | PR00082, GLFDHDRGNASE |
SMARTi | View protein in SMART SM00839, ELFV_dehydrog, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00074, GLFV_DEHYDROGENASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DHE3_HUMAN | |
Accessioni | P00367Primary (citable) accession number: P00367 Secondary accession number(s): B3KV55, B4DGN5, Q5TBU3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 1, 1990 | |
Last modified: | December 2, 2020 | |
This is version 226 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations