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P00367 (DHE3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate dehydrogenase 1, mitochondrial

Short name=GDH 1
EC=1.4.1.3
Gene names
Name:GLUD1
Synonyms:GLUD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Enzyme regulation

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

Subunit structure

Homohexamer.

Subcellular location

Mitochondrion matrix.

Post-translational modification

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.24 Ref.25

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DiseaseDisease mutation
   DomainTransit peptide
   LigandATP-binding
GTP-binding
NADP
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMAcetylation
ADP-ribosylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular amino acid biosynthetic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

glutamate biosynthetic process

Inferred from direct assay PubMed 11032875. Source: BHF-UCL

glutamate catabolic process

Inferred from direct assay PubMed 6121377. Source: UniProtKB

glutamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion

Inferred from mutant phenotype PubMed 11502802. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

tricarboxylic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18688271. Source: BHF-UCL

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 15578726. Source: UniProtKB

   Molecular_functionADP binding

Inferred from direct assay PubMed 12742085. Source: BHF-UCL

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from direct assay PubMed 11032875. Source: BHF-UCL

NAD+ binding

Inferred from direct assay PubMed 12193607. Source: BHF-UCL

glutamate dehydrogenase (NAD+) activity

Inferred from direct assay PubMed 15578726. Source: UniProtKB

glutamate dehydrogenase [NAD(P)+] activity

Inferred from direct assay PubMed 11032875. Source: BHF-UCL

identical protein binding

Traceable author statement Ref.17. Source: BHF-UCL

leucine binding

Inferred from direct assay PubMed 12742085. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.18. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion Ref.8 Ref.9
Chain54 – 558505Glutamate dehydrogenase 1, mitochondrial
PRO_0000007206

Regions

Nucleotide binding141 – 1433NAD By similarity

Sites

Active site1831
Binding site1471Substrate By similarity
Binding site1711Substrate By similarity
Binding site1761NAD By similarity
Binding site2521NAD By similarity
Binding site2661GTP By similarity
Binding site2701GTP By similarity
Binding site3191GTP By similarity
Binding site3221GTP By similarity
Binding site4381Substrate By similarity
Binding site4441NAD By similarity
Binding site4501ADP By similarity
Binding site5161ADP By similarity

Amino acid modifications

Modified residue681N6-succinyllysine By similarity
Modified residue791Phosphoserine By similarity
Modified residue841N6-acetyllysine; alternate Ref.14
Modified residue841N6-succinyllysine; alternate By similarity
Modified residue1101N6-acetyllysine; alternate By similarity
Modified residue1101N6-succinyllysine; alternate By similarity
Modified residue1281Phosphoserine By similarity
Modified residue1351Phosphotyrosine By similarity
Modified residue1621N6-acetyllysine; alternate By similarity
Modified residue1621N6-succinyllysine; alternate By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue1721ADP-ribosylcysteine
Modified residue1831N6-acetyllysine; alternate By similarity
Modified residue1831N6-succinyllysine; alternate By similarity
Modified residue1871N6-acetyllysine By similarity
Modified residue1911N6-acetyllysine; alternate By similarity
Modified residue1911N6-succinyllysine; alternate By similarity
Modified residue2001N6-succinyllysine By similarity
Modified residue2111N6-acetyllysine By similarity
Modified residue3261N6-acetyllysine By similarity
Modified residue3461N6-acetyllysine; alternate By similarity
Modified residue3461N6-succinyllysine; alternate By similarity
Modified residue3521N6-acetyllysine; alternate By similarity
Modified residue3521N6-succinyllysine; alternate By similarity
Modified residue3631N6-acetyllysine; alternate By similarity
Modified residue3631N6-succinyllysine; alternate By similarity
Modified residue3651N6-acetyllysine; alternate By similarity
Modified residue3651N6-succinyllysine; alternate By similarity
Modified residue3861N6-acetyllysine By similarity
Modified residue3901N6-acetyllysine; alternate By similarity
Modified residue3901N6-succinyllysine; alternate By similarity
Modified residue3991N6-acetyllysine By similarity
Modified residue4151N6-acetyllysine; alternate By similarity
Modified residue4151N6-succinyllysine; alternate By similarity
Modified residue4571N6-acetyllysine; alternate By similarity
Modified residue4571N6-malonyllysine; alternate By similarity
Modified residue4571N6-succinyllysine; alternate By similarity
Modified residue4771N6-acetyllysine; alternate By similarity
Modified residue4771N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine; alternate Ref.14
Modified residue4801N6-succinyllysine; alternate By similarity
Modified residue5031N6-acetyllysine; alternate Ref.14
Modified residue5031N6-malonyllysine; alternate By similarity
Modified residue5031N6-succinyllysine; alternate By similarity
Modified residue5271N6-acetyllysine; alternate By similarity
Modified residue5271N6-malonyllysine; alternate By similarity
Modified residue5271N6-succinyllysine; alternate By similarity
Modified residue5451N6-acetyllysine; alternate By similarity
Modified residue5451N6-succinyllysine; alternate By similarity
Modified residue5481N6-acetyllysine By similarity

Natural variations

Natural variant2701S → C in HHF6; diminished sensitivity to GTP. Ref.25
VAR_016760
Natural variant2741R → C in HHF6; diminished sensitivity to GTP. Ref.24 Ref.25
Corresponds to variant rs56275071 [ dbSNP | Ensembl ].
VAR_016761
Natural variant3181R → K in HHF6. Ref.23
VAR_009270
Natural variant3181R → T in HHF6; diminished sensitivity to GTP. Ref.25
VAR_016762
Natural variant3191Y → C in HHF6. Ref.25
VAR_016763
Natural variant3221R → C in HHF6; diminished sensitivity to GTP. Ref.25
VAR_016764
Natural variant3221R → H in HHF6; diminished sensitivity to GTP. Ref.24 Ref.25
VAR_016765
Natural variant3491E → A in HHF6. Ref.23
VAR_009271
Natural variant4981S → L in HHF6. Ref.22
VAR_008666
Natural variant4991G → D in HHF6. Ref.22
VAR_008667
Natural variant4991G → S in HHF6. Ref.22
VAR_008668
Natural variant5011S → P in HHF6. Ref.22
VAR_008669
Natural variant5071H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. Ref.16 Ref.17 Ref.22
VAR_008670

Experimental info

Mutagenesis5011S → A: Reduces activity and inhibition by GTP. Ref.17
Mutagenesis5071H → A: Strongly reduces inhibition by GTP.
Mutagenesis5161R → A: Abolishes activation by ADP. Ref.17

Secondary structure

.................................................................................... 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00367 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: A7319A840F57FBB2

FASTA55861,398
        10         20         30         40         50         60 
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR RHYSEAVADR 

        70         80         90        100        110        120 
EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF 

       130        140        150        160        170        180 
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG 

       190        200        210        220        230        240 
GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY 

       250        260        270        280        290        300 
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 

       310        320        330        340        350        360 
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG 

       370        380        390        400        410        420 
FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER 

       430        440        450        460        470        480 
NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK 

       490        500        510        520        530        540 
HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV 

       550 
NAIEKVFKVY NEAGVTFT 

« Hide

References

« Hide 'large scale' references
[1]"Comparison of human brain and liver glutamate dehydrogenase cDNAs."
Nakatani Y., Banner C., von Herrat M., Schneider M.E., Smith H.H., Freese E.
Biochem. Biophys. Res. Commun. 149:405-410(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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].
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].
[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].
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]"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. expand/collapse author list , 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].
[7]"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].
Tissue: Duodenum and Eye.
[8]"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.
[9]"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.
[10]"Isolation of a human brain cDNA for glutamate dehydrogenase."
Banner C., Silverman S., Thomas J.W., Lampel K.A., Vitkovic L., Huie D., Wenthold R.J.
J. Neurochem. 49:246-252(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 301-558.
Tissue: Brain.
[11]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.
[12]"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.
[13]"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.
[14]"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].
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Wikipedia

Glutamate dehydrogenase 1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , X66301, X66302, X66303, X66304, X66305, X66306, X66307, X66308, X66309, X66311, X66312 Genomic DNA. Translation: CAA46994.2.
AL136982 Genomic DNA. Translation: CAI17120.1.
BC040132 mRNA. Translation: AAH40132.1.
BC112946 mRNA. Translation: AAI12947.1.
X67491 Genomic DNA. Translation: CAA47830.1.
CCDSCCDS7382.1.
PIRDEHUE. A28208.
I37424.
S29331.
S60192.
RefSeqNP_005262.1. NM_005271.3.
UniGeneHs.500409.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1FX-ray2.70A/B/C/D/E/F54-558[»]
1NR1X-ray3.30A/B/C/D/E/F63-558[»]
ProteinModelPortalP00367.
SMRP00367. Positions 63-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109008. 19 interactions.
IntActP00367. 18 interactions.
MINTMINT-5005913.
STRING9606.ENSP00000277865.

Chemistry

DrugBankDB00142. L-Glutamic Acid.
DB00157. NADH.

PTM databases

PhosphoSiteP00367.

Polymorphism databases

DMDM118541.

2D gel databases

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

Proteomic databases

MaxQBP00367.
PaxDbP00367.
PeptideAtlasP00367.
PRIDEP00367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000277865; ENSP00000277865; ENSG00000148672.
GeneID2746.
KEGGhsa:2746.
UCSCuc001keg.3. human.

Organism-specific databases

CTD2746.
GeneCardsGC10M088809.
GeneReviewsGLUD1.
HGNCHGNC:4335. GLUD1.
HPAHPA042492.
HPA044839.
MIM138130. gene.
606762. phenotype.
neXtProtNX_P00367.
Orphanet35878. Hyperinsulinism-hyperammonemia syndrome.
PharmGKBPA28737.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0334.
HOGENOMHOG000243801.
HOVERGENHBG005479.
InParanoidP00367.
KOK00261.
OMATCIGVIE.
OrthoDBEOG73NG50.
PhylomeDBP00367.
TreeFamTF313945.

Enzyme and pathway databases

BioCycMetaCyc:HS07548-MONOMER.
BRENDA1.4.1.3. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00367.

Gene expression databases

ArrayExpressP00367.
BgeeP00367.
CleanExHS_GLUD1.
GenevestigatorP00367.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PRINTSPR00082. GLFDHDRGNASE.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00367.
GeneWikiGlutamate_dehydrogenase_1.
GenomeRNAi2746.
NextBio10824.
PROP00367.
SOURCESearch...

Entry information

Entry nameDHE3_HUMAN
AccessionPrimary (citable) accession number: P00367
Secondary accession number(s): Q5TBU3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM