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P00367

- DHE3_HUMAN

UniProt

P00367 - DHE3_HUMAN

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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).By similarity

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

Enzyme regulationi

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471SubstrateBy similarity
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei176 – 1761NADBy similarity
Active sitei183 – 1831
Binding sitei252 – 2521NADBy similarity
Binding sitei266 – 2661GTPBy similarity
Binding sitei270 – 2701GTPBy similarity
Binding sitei319 – 3191GTPBy similarity
Binding sitei322 – 3221GTPBy similarity
Binding sitei438 – 4381SubstrateBy similarity
Binding sitei444 – 4441NADBy similarity
Binding sitei450 – 4501ADPBy similarity
Binding sitei516 – 5161ADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi141 – 1433NADBy similarity

GO - Molecular functioni

  1. ADP binding Source: BHF-UCL
  2. ATP binding Source: UniProtKB-KW
  3. glutamate dehydrogenase (NAD+) activity Source: UniProtKB
  4. glutamate dehydrogenase [NAD(P)+] activity Source: BHF-UCL
  5. GTP binding Source: BHF-UCL
  6. identical protein binding Source: BHF-UCL
  7. leucine binding Source: BHF-UCL
  8. NAD+ binding Source: BHF-UCL

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. glutamate biosynthetic process Source: BHF-UCL
  4. glutamate catabolic process Source: UniProtKB
  5. glutamine metabolic process Source: UniProtKB
  6. positive regulation of insulin secretion Source: BHF-UCL
  7. small molecule metabolic process Source: Reactome
  8. substantia nigra development Source: UniProt
  9. tricarboxylic acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

ATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07548-MONOMER.
BRENDAi1.4.1.3. 2681.
ReactomeiREACT_238. Amino acid synthesis and interconversion (transamination).
SABIO-RKP00367.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
Gene namesi
Name:GLUD1
Synonyms:GLUD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:4335. GLUD1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Familial hyperinsulinemic hypoglycemia 6 (HHF6) [MIM:606762]: Familial 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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti270 – 2701S → C in HHF6; diminished sensitivity to GTP. 1 Publication
VAR_016760
Natural varianti274 – 2741R → C in HHF6; diminished sensitivity to GTP. 2 Publications
Corresponds to variant rs56275071 [ dbSNP | Ensembl ].
VAR_016761
Natural varianti318 – 3181R → K in HHF6. 1 Publication
VAR_009270
Natural varianti318 – 3181R → T in HHF6; diminished sensitivity to GTP. 1 Publication
VAR_016762
Natural varianti319 – 3191Y → C in HHF6. 1 Publication
VAR_016763
Natural varianti322 – 3221R → C in HHF6; diminished sensitivity to GTP. 1 Publication
VAR_016764
Natural varianti322 – 3221R → H in HHF6; diminished sensitivity to GTP. 2 Publications
VAR_016765
Natural varianti349 – 3491E → A in HHF6. 1 Publication
VAR_009271
Natural varianti498 – 4981S → L in HHF6. 1 Publication
VAR_008666
Natural varianti499 – 4991G → D in HHF6. 1 Publication
VAR_008667
Natural varianti499 – 4991G → S in HHF6. 1 Publication
VAR_008668
Natural varianti501 – 5011S → P in HHF6. 1 Publication
VAR_008669
Natural varianti507 – 5071H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 1 Publication
VAR_008670

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi501 – 5011S → A: Reduces activity and inhibition by GTP. 1 Publication
Mutagenesisi507 – 5071H → A: Strongly reduces inhibition by GTP.
Mutagenesisi516 – 5161R → A: Abolishes activation by ADP. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi606762. phenotype.
Orphaneti35878. Hyperinsulinism-hyperammonemia syndrome.
PharmGKBiPA28737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Mitochondrion2 PublicationsAdd
BLAST
Chaini54 – 558505Glutamate dehydrogenase 1, mitochondrialPRO_0000007206Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-succinyllysineBy similarity
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei84 – 841N6-acetyllysine; alternate1 Publication
Modified residuei84 – 841N6-succinyllysine; alternateBy similarity
Modified residuei110 – 1101N6-acetyllysine; alternateBy similarity
Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei135 – 1351PhosphotyrosineBy similarity
Modified residuei162 – 1621N6-acetyllysine; alternateBy similarity
Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
Modified residuei171 – 1711N6-acetyllysineBy similarity
Modified residuei172 – 1721ADP-ribosylcysteine1 Publication
Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
Modified residuei183 – 1831N6-succinyllysine; alternateBy similarity
Modified residuei187 – 1871N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
Modified residuei200 – 2001N6-succinyllysineBy similarity
Modified residuei211 – 2111N6-acetyllysineBy similarity
Modified residuei326 – 3261N6-acetyllysineBy similarity
Modified residuei346 – 3461N6-acetyllysine; alternateBy similarity
Modified residuei346 – 3461N6-succinyllysine; alternateBy similarity
Modified residuei352 – 3521N6-acetyllysine; alternateBy similarity
Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
Modified residuei363 – 3631N6-acetyllysine; alternateBy similarity
Modified residuei363 – 3631N6-succinyllysine; alternateBy similarity
Modified residuei365 – 3651N6-acetyllysine; alternateBy similarity
Modified residuei365 – 3651N6-succinyllysine; alternateBy similarity
Modified residuei386 – 3861N6-acetyllysineBy similarity
Modified residuei390 – 3901N6-acetyllysine; alternateBy similarity
Modified residuei390 – 3901N6-succinyllysine; alternateBy similarity
Modified residuei399 – 3991N6-acetyllysineBy similarity
Modified residuei415 – 4151N6-acetyllysine; alternateBy similarity
Modified residuei415 – 4151N6-succinyllysine; alternateBy similarity
Modified residuei457 – 4571N6-acetyllysine; alternateBy similarity
Modified residuei457 – 4571N6-malonyllysine; alternateBy similarity
Modified residuei457 – 4571N6-succinyllysine; alternateBy similarity
Modified residuei477 – 4771N6-acetyllysine; alternateBy similarity
Modified residuei477 – 4771N6-succinyllysine; alternateBy similarity
Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
Modified residuei503 – 5031N6-acetyllysine; alternate1 Publication
Modified residuei503 – 5031N6-malonyllysine; alternateBy similarity
Modified residuei503 – 5031N6-succinyllysine; alternateBy similarity
Modified residuei527 – 5271N6-acetyllysine; alternateBy similarity
Modified residuei527 – 5271N6-malonyllysine; alternateBy similarity
Modified residuei527 – 5271N6-succinyllysine; alternateBy similarity
Modified residuei545 – 5451N6-acetyllysine; alternateBy similarity
Modified residuei545 – 5451N6-succinyllysine; alternateBy similarity
Modified residuei548 – 5481N6-acetyllysineBy similarity

Post-translational modificationi

ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity (By similarity). Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

MaxQBiP00367.
PaxDbiP00367.
PeptideAtlasiP00367.
PRIDEiP00367.

2D gel databases

REPRODUCTION-2DPAGEIPI00016801.
SWISS-2DPAGEP00367.
UCD-2DPAGEP00367.

PTM databases

PhosphoSiteiP00367.

Expressioni

Gene expression databases

BgeeiP00367.
CleanExiHS_GLUD1.
ExpressionAtlasiP00367. baseline and differential.
GenevestigatoriP00367.

Organism-specific databases

HPAiHPA042492.
HPA044839.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi109008. 24 interactions.
IntActiP00367. 18 interactions.
MINTiMINT-5005913.
STRINGi9606.ENSP00000277865.

Structurei

Secondary structure

1
558
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 9025Combined sources
Helixi91 – 933Combined sources
Helixi95 – 973Combined sources
Helixi99 – 1024Combined sources
Helixi104 – 1096Combined sources
Beta strandi113 – 12311Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 13810Combined sources
Beta strandi142 – 15211Combined sources
Helixi158 – 17417Combined sources
Beta strandi180 – 1867Combined sources
Helixi190 – 1923Combined sources
Helixi195 – 21117Combined sources
Turni217 – 2193Combined sources
Beta strandi220 – 2234Combined sources
Helixi230 – 24213Combined sources
Turni243 – 2475Combined sources
Helixi251 – 2533Combined sources
Helixi260 – 2623Combined sources
Helixi271 – 28414Combined sources
Helixi287 – 2937Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi303 – 3075Combined sources
Helixi311 – 32212Combined sources
Beta strandi326 – 3316Combined sources
Helixi345 – 35410Combined sources
Beta strandi355 – 3584Combined sources
Turni371 – 3733Combined sources
Beta strandi377 – 3815Combined sources
Beta strandi383 – 3864Combined sources
Turni390 – 3923Combined sources
Helixi393 – 3953Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi405 – 4073Combined sources
Helixi411 – 4199Combined sources
Beta strandi423 – 4253Combined sources
Helixi427 – 4304Combined sources
Helixi433 – 44715Combined sources
Turni451 – 4555Combined sources
Helixi456 – 47520Combined sources
Turni476 – 4794Combined sources
Beta strandi481 – 4844Combined sources
Helixi491 – 4988Combined sources
Helixi502 – 52726Combined sources
Helixi534 – 55118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1FX-ray2.70A/B/C/D/E/F54-558[»]
1NR1X-ray3.30A/B/C/D/E/F63-558[»]
ProteinModelPortaliP00367.
SMRiP00367. Positions 63-558.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00367.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP00367.
KOiK00261.
OMAiTCIGVIE.
OrthoDBiEOG73NG50.
PhylomeDBiP00367.
TreeFamiTF313945.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000185. Glu_DH. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P00367-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Length:558
Mass (Da):61,398
Last modified:January 1, 1990 - v2
Checksum:iA7319A840F57FBB2
GO
Isoform 2 (identifier: P00367-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-167: Missing.

Note: No experimental confirmation available.

Show »
Length:391
Mass (Da):42,950
Checksum:i8A493E2898605460
GO
Isoform 3 (identifier: P00367-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MYRYLGEALLLSRAGP → MTCPCDNASSVFLGFC
     17-149: Missing.

Note: No experimental confirmation available.

Show »
Length:425
Mass (Da):46,575
Checksum:i2637B3023F58A7C4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti270 – 2701S → C in HHF6; diminished sensitivity to GTP. 1 Publication
VAR_016760
Natural varianti274 – 2741R → C in HHF6; diminished sensitivity to GTP. 2 Publications
Corresponds to variant rs56275071 [ dbSNP | Ensembl ].
VAR_016761
Natural varianti318 – 3181R → K in HHF6. 1 Publication
VAR_009270
Natural varianti318 – 3181R → T in HHF6; diminished sensitivity to GTP. 1 Publication
VAR_016762
Natural varianti319 – 3191Y → C in HHF6. 1 Publication
VAR_016763
Natural varianti322 – 3221R → C in HHF6; diminished sensitivity to GTP. 1 Publication
VAR_016764
Natural varianti322 – 3221R → H in HHF6; diminished sensitivity to GTP. 2 Publications
VAR_016765
Natural varianti349 – 3491E → A in HHF6. 1 Publication
VAR_009271
Natural varianti498 – 4981S → L in HHF6. 1 Publication
VAR_008666
Natural varianti499 – 4991G → D in HHF6. 1 Publication
VAR_008667
Natural varianti499 – 4991G → S in HHF6. 1 Publication
VAR_008668
Natural varianti501 – 5011S → P in HHF6. 1 Publication
VAR_008669
Natural varianti507 – 5071H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 1 Publication
VAR_008670

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 167167Missing in isoform 2. 1 PublicationVSP_056244Add
BLAST
Alternative sequencei1 – 1616MYRYL…SRAGP → MTCPCDNASSVFLGFC in isoform 3. 1 PublicationVSP_056523Add
BLAST
Alternative sequencei17 – 149133Missing in isoform 3. 1 PublicationVSP_056524Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07674 mRNA. Translation: CAA30521.1.
M20867 mRNA. Translation: AAA52526.1.
M37154 mRNA. Translation: AAA52525.1.
X07769 mRNA. Translation: CAA30598.1.
J03248 mRNA. Translation: AAA52523.1.
X66300
, X66301, X66302, X66303, X66304, X66305, X66306, X66307, X66308, X66309, X66311, X66312 Genomic DNA. Translation: CAA46994.2.
AK122685 mRNA. Translation: BAG53667.1.
AK294685 mRNA. Translation: BAG57846.1.
AL136982 Genomic DNA. Translation: CAI17120.1.
CH471142 Genomic DNA. Translation: EAW80300.1.
CH471142 Genomic DNA. Translation: EAW80302.1.
BC040132 mRNA. Translation: AAH40132.1.
BC112946 mRNA. Translation: AAI12947.1.
X67491 Genomic DNA. Translation: CAA47830.1.
CCDSiCCDS7382.1. [P00367-1]
PIRiA28208. DEHUE.
I37424.
S29331.
S60192.
RefSeqiNP_005262.1. NM_005271.3. [P00367-1]
UniGeneiHs.500409.

Genome annotation databases

EnsembliENST00000277865; ENSP00000277865; ENSG00000148672. [P00367-1]
GeneIDi2746.
KEGGihsa:2746.
UCSCiuc001keg.3. human. [P00367-1]

Polymorphism databases

DMDMi118541.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Glutamate dehydrogenase 1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07674 mRNA. Translation: CAA30521.1 .
M20867 mRNA. Translation: AAA52526.1 .
M37154 mRNA. Translation: AAA52525.1 .
X07769 mRNA. Translation: CAA30598.1 .
J03248 mRNA. Translation: AAA52523.1 .
X66300
, X66301 , X66302 , X66303 , X66304 , X66305 , X66306 , X66307 , X66308 , X66309 , X66311 , X66312 Genomic DNA. Translation: CAA46994.2 .
AK122685 mRNA. Translation: BAG53667.1 .
AK294685 mRNA. Translation: BAG57846.1 .
AL136982 Genomic DNA. Translation: CAI17120.1 .
CH471142 Genomic DNA. Translation: EAW80300.1 .
CH471142 Genomic DNA. Translation: EAW80302.1 .
BC040132 mRNA. Translation: AAH40132.1 .
BC112946 mRNA. Translation: AAI12947.1 .
X67491 Genomic DNA. Translation: CAA47830.1 .
CCDSi CCDS7382.1. [P00367-1 ]
PIRi A28208. DEHUE.
I37424.
S29331.
S60192.
RefSeqi NP_005262.1. NM_005271.3. [P00367-1 ]
UniGenei Hs.500409.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P00367.
SMRi P00367. Positions 63-558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109008. 24 interactions.
IntActi P00367. 18 interactions.
MINTi MINT-5005913.
STRINGi 9606.ENSP00000277865.

Chemistry

DrugBanki DB00756. Hexachlorophene.

PTM databases

PhosphoSitei P00367.

Polymorphism databases

DMDMi 118541.

2D gel databases

REPRODUCTION-2DPAGE IPI00016801.
SWISS-2DPAGE P00367.
UCD-2DPAGE P00367.

Proteomic databases

MaxQBi P00367.
PaxDbi P00367.
PeptideAtlasi P00367.
PRIDEi P00367.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000277865 ; ENSP00000277865 ; ENSG00000148672 . [P00367-1 ]
GeneIDi 2746.
KEGGi hsa:2746.
UCSCi uc001keg.3. human. [P00367-1 ]

Organism-specific databases

CTDi 2746.
GeneCardsi GC10M088809.
GeneReviewsi GLUD1.
HGNCi HGNC:4335. GLUD1.
HPAi HPA042492.
HPA044839.
MIMi 138130. gene.
606762. phenotype.
neXtProti NX_P00367.
Orphaneti 35878. Hyperinsulinism-hyperammonemia syndrome.
PharmGKBi PA28737.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0334.
GeneTreei ENSGT00390000000854.
HOGENOMi HOG000243801.
HOVERGENi HBG005479.
InParanoidi P00367.
KOi K00261.
OMAi TCIGVIE.
OrthoDBi EOG73NG50.
PhylomeDBi P00367.
TreeFami TF313945.

Enzyme and pathway databases

BioCyci MetaCyc:HS07548-MONOMER.
BRENDAi 1.4.1.3. 2681.
Reactomei REACT_238. Amino acid synthesis and interconversion (transamination).
SABIO-RK P00367.

Miscellaneous databases

ChiTaRSi GLUD1. human.
EvolutionaryTracei P00367.
GeneWikii Glutamate_dehydrogenase_1.
GenomeRNAii 2746.
NextBioi 10824.
PROi P00367.
SOURCEi Search...

Gene expression databases

Bgeei P00367.
CleanExi HS_GLUD1.
ExpressionAtlasi P00367. baseline and differential.
Genevestigatori P00367.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000185. Glu_DH. 1 hit.
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain and Liver.
  2. "Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor."
    Amuro N., Yamaura M., Goto Y., Okazaki T.
    Biochem. Biophys. Res. Commun. 152:1395-1400(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Complete nucleotide sequence of human glutamate dehydrogenase cDNA."
    Nakatani Y., Schneider M.E., Banner C., Freese E.
    Nucleic Acids Res. 16:6237-6237(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family."
    Mavrothalassitis G., Tzimagiorgis G., Mitsialis A., Zannis V., Plaitakis A., Papamatheakis J., Moschonas N.
    Proc. Natl. Acad. Sci. U.S.A. 85:3494-3498(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. "The human glutamate dehydrogenase gene family: gene organization and structural characterization."
    Michaelidis T.M., Tzimagiorgis G., Moschonas N.K., Papamatheakis J.
    Genomics 16:150-160(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain and Brain cortex.
  7. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Duodenum and Eye.
  10. "Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme."
    Julliard J.H., Smith E.L.
    J. Biol. Chem. 254:3427-3438(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-558.
    Tissue: Liver.
  11. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-69.
    Tissue: Liver.
  12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 301-558 (ISOFORM 1).
    Tissue: Brain.
  13. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 481-496, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  14. "Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2."
    Tzimagiorgis G., Leversha M.A., Chroniary K., Goulielmos G., Sargent C.A., Ferguson-Smith M., Moschonas N.K.
    Hum. Genet. 91:433-438(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 540-558.
  15. "Identification of ADP-ribosylation site in human glutamate dehydrogenase isozymes."
    Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W.
    FEBS Lett. 579:4125-4130(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION AT CYS-172.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-480 AND LYS-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation."
    Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A.
    J. Mol. Biol. 307:707-720(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT TYR-507, ALLOSTERIC REGULATION.
  19. "Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations."
    Fang J., Hsu B.Y.L., MacMullen C.M., Poncz M., Smith T.J., Stanley C.A.
    Biochem. J. 363:81-87(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-501 AND ARG-516, CHARACTERIZATION OF VARIANT TYR-507, ALLOSTERIC REGULATION.
  20. "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells."
    Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., Christodoulou D.C., Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Karow M., Blander G., Wolberger C., Prolla T.A., Weindruch R., Alt F.W., Guarente L.
    Cell 126:941-954(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION.
  21. "The structure of apo human glutamate dehydrogenase details subunit communication and allostery."
    Smith T.J., Schmidt T., Fang J., Wu J., Siuzdak G., Stanley C.A.
    J. Mol. Biol. 318:765-777(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-558.
  22. "Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation."
    Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J.
    Biochemistry 42:3446-3456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 63-558 OF MUTANT ALA-516, ALLOSTERIC REGULATION.
  23. "Congenital hyperinsulinism: molecular basis of a heterogeneous disease."
    Meissner T., Beinbrech B., Mayatepek E.
    Hum. Mutat. 13:351-361(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  24. "Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene."
    Stanley C.A., Lieu Y.K., Hsu B.Y.L., Burlina A.B., Greenberg C.R., Hopwood N.J., Perlman K., Rich B.H., Zammarchi E., Poncz M.
    N. Engl. J. Med. 338:1352-1357(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HHF6 LEU-498; SER-499; ASP-499; PRO-501 AND TYR-507.
  25. "Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome."
    Miki Y., Taki T., Ohura T., Kato H., Yanagisawa M., Hayashi Y.
    J. Pediatr. 136:69-72(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HHF6 LYS-318 AND ALA-349.
  26. "Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome."
    Santer R., Kinner M., Passarge M., Superti-Furga A., Mayatepek E., Meissner T., Schneppenheim R., Schaub J.
    Hum. Genet. 108:66-71(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HHF6 CYS-274 AND HIS-322.
  27. "Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase."
    MacMullen C., Fang J., Hsu B.Y.L., Kelly A., de Lonlay-Debeney P., Saudubray J.-M., Ganguly A., Smith T.J., Stanley C.A., Brown R., Buist N., Dasouki M., Fefferman R., Grange D., Karaviti L., Luedke C., Marriage B., McLaughlin J.
    , Perlman K., Seashore M., van Vliet G.
    J. Clin. Endocrinol. Metab. 86:1782-1787(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HHF6 CYS-270; CYS-274; THR-318; CYS-319; CYS-322 AND HIS-322.

Entry informationi

Entry nameiDHE3_HUMAN
AccessioniPrimary (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: November 26, 2014
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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