P00367 (DHE3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate dehydrogenase 1, mitochondrial
Short name=GDH 1
EC=1.4.1.3

Gene names

Name:	GLUD1
Synonyms:	GLUD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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	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.21 Ref.22 Ref.23 Ref.24
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
Cellular component	Mitochondrion
Disease	Disease mutation
Domain	Transit peptide
Ligand	ATP-binding GTP-binding NADP Nucleotide-binding
Molecular function	Oxidoreductase
PTM	ADP-ribosylation Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 positive regulation of insulin secretion Inferred from mutant phenotype PubMed 11502802. Source: BHF-UCL
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	ADP 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 53

53

Mitochondrion Ref.8 Ref.9

Chain

54 – 558

505

Glutamate dehydrogenase 1, mitochondrial

PRO_0000007206

Regions

Nucleotide binding

141 – 143

3

NAD By similarity

Sites

Active site

183

1

Binding site

147

1

Substrate By similarity

Binding site

171

1

Substrate By similarity

Binding site

176

1

NAD By similarity

Binding site

252

1

NAD By similarity

Binding site

266

1

GTP By similarity

Binding site

270

1

GTP By similarity

Binding site

319

1

GTP By similarity

Binding site

322

1

GTP By similarity

Binding site

438

1

Substrate By similarity

Binding site

444

1

NAD By similarity

Binding site

450

1

ADP By similarity

Binding site

516

1

ADP By similarity

Amino acid modifications

Modified residue

84

1

N6-acetyllysine Ref.14

Modified residue

84

1

N6-succinyllysine; alternate By similarity

Modified residue

110

1

N6-acetyllysine; alternate By similarity

Modified residue

110

1

N6-succinyllysine; alternate By similarity

Modified residue

135

1

Phosphotyrosine By similarity

Modified residue

162

1

N6-acetyllysine; alternate By similarity

Modified residue

162

1

N6-succinyllysine; alternate By similarity

Modified residue

172

1

ADP-ribosylcysteine

Modified residue

183

1

N6-acetyllysine By similarity

Modified residue

191

1

N6-acetyllysine By similarity

Modified residue

227

1

Phosphoserine By similarity

Modified residue

363

1

N6-acetyllysine; alternate By similarity

Modified residue

363

1

N6-succinyllysine; alternate By similarity

Modified residue

365

1

N6-acetyllysine By similarity

Modified residue

386

1

N6-acetyllysine By similarity

Modified residue

399

1

N6-acetyllysine By similarity

Modified residue

415

1

N6-acetyllysine; alternate By similarity

Modified residue

415

1

N6-succinyllysine; alternate By similarity

Modified residue

450

1

Phosphoserine By similarity

Modified residue

457

1

N6-acetyllysine; alternate By similarity

Modified residue

457

1

N6-malonyllysine; alternate By similarity

Modified residue

457

1

N6-succinyllysine; alternate By similarity

Modified residue

480

1

N6-acetyllysine Ref.14

Modified residue

503

1

N6-acetyllysine Ref.14

Modified residue

503

1

N6-malonyllysine; alternate By similarity

Modified residue

503

1

N6-succinyllysine; alternate By similarity

Modified residue

512

1

Phosphotyrosine By similarity

Modified residue

527

1

N6-acetyllysine; alternate By similarity

Modified residue

527

1

N6-malonyllysine; alternate By similarity

Modified residue

527

1

N6-succinyllysine; alternate By similarity

Modified residue

545

1

N6-acetyllysine; alternate By similarity

Modified residue

545

1

N6-succinyllysine; alternate By similarity

Natural variations

Natural variant

270

1

S → C in HHF6; diminished sensitivity to GTP. Ref.24

VAR_016760

Natural variant

274

1

R → C in HHF6; diminished sensitivity to GTP. Ref.23 Ref.24
Corresponds to variant rs56275071 [ dbSNP | Ensembl ].

VAR_016761

Natural variant

318

1

R → K in HHF6. Ref.22

VAR_009270

Natural variant

318

1

R → T in HHF6; diminished sensitivity to GTP. Ref.24

VAR_016762

Natural variant

319

1

Y → C in HHF6. Ref.24

VAR_016763

Natural variant

322

1

R → C in HHF6; diminished sensitivity to GTP. Ref.24

VAR_016764

Natural variant

322

1

R → H in HHF6; diminished sensitivity to GTP. Ref.23 Ref.24

VAR_016765

Natural variant

349

1

E → A in HHF6. Ref.22

VAR_009271

Natural variant

498

1

S → L in HHF6. Ref.21

VAR_008666

Natural variant

499

1

G → D in HHF6. Ref.21

VAR_008667

Natural variant

499

1

G → S in HHF6. Ref.21

VAR_008668

Natural variant

501

1

S → P in HHF6. Ref.21

VAR_008669

Natural variant

507

1

H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. Ref.16 Ref.17 Ref.21

VAR_008670

Experimental info

Mutagenesis

501

1

S → A: Reduces activity and inhibition by GTP. Ref.17

Mutagenesis

507

1

H → A: Strongly reduces inhibition by GTP.

Mutagenesis

516

1

R → A: Abolishes activation by ADP. Ref.17

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

558

Helix Strand Turn

Details...

Helix

66 – 90

25

Helix

91 – 93

3

Helix

95 – 97

3

Helix

99 – 102

4

Helix

104 – 109

6

Beta strand

113 – 123

11

Beta strand

125 – 127

3

Beta strand

129 – 138

10

Beta strand

142 – 152

11

Helix

158 – 174

17

Beta strand

180 – 186

7

Helix

190 – 192

3

Helix

195 – 211

17

Turn

217 – 219

3

Beta strand

220 – 223

4

Helix

230 – 242

13

Turn

243 – 247

5

Helix

251 – 253

3

Helix

260 – 262

3

Helix

271 – 284

14

Helix

287 – 293

7

Beta strand

298 – 300

3

Beta strand

303 – 307

5

Helix

311 – 322

12

Beta strand

326 – 331

6

Helix

345 – 354

10

Beta strand

355 – 358

4

Turn

371 – 373

3

Beta strand

377 – 381

5

Beta strand

383 – 386

4

Turn

390 – 392

3

Helix

393 – 395

3

Beta strand

399 – 402

4

Beta strand

405 – 407

3

Helix

411 – 419

9

Beta strand

423 – 425

3

Helix

427 – 430

4

Helix

433 – 447

15

Turn

451 – 455

5

Helix

456 – 475

20

Turn

476 – 479

4

Beta strand

481 – 484

4

Helix

491 – 498

8

Helix

502 – 527

26

Helix

534 – 551

18

Sequences

	Sequence		Length	Mass (Da)
	P00367 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: A7319A840F57FBB2	FASTA	558	61,398
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY.
[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]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
+	Additional computationally mapped references.

Web resources

GeneReviews

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 , 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.

IPI

IPI00016801.

PIR

DEHUE. A28208.
I37424.
S29331.
S60192.

RefSeq

NP_005262.1. NM_005271.3.

UniGene

Hs.500409.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00367.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00367. 16 interactions.

MINT

MINT-5005913.

STRING

9606.ENSP00000277865.

PTM databases

PhosphoSite

P00367.

Polymorphism databases

DMDM

118541.

2D gel databases

REPRODUCTION-2DPAGE

IPI00016801.

SWISS-2DPAGE

P00367.

UCD-2DPAGE

P00367.

Proteomic databases

PaxDb

P00367.

PeptideAtlas

P00367.

PRIDE

P00367.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000277865; ENSP00000277865; ENSG00000148672.

GeneID

2746.

KEGG

hsa:2746.

UCSC

uc001keg.3. human.

Organism-specific databases

CTD

2746.

GeneCards

GC10M088800.

HGNC

HGNC:4335. GLUD1.

HPA

HPA042492.
HPA044839.

MIM

138130. gene.
606762. phenotype.

neXtProt

NX_P00367.

Orphanet

35878. Hyperinsulinism-hyperammonemia syndrome.

PharmGKB

PA28737.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0334.

HOGENOM

HOG000243801.

HOVERGEN

HBG005479.

InParanoid

P00367.

KO

K00261.

OMA

TCIGVIE.

OrthoDB

EOG4H72B7.

PhylomeDB

P00367.

Enzyme and pathway databases

BioCyc

MetaCyc:HS07548-MONOMER.

BRENDA

1.4.1.3. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P00367.

Gene expression databases

ArrayExpress

P00367.

Bgee

P00367.

CleanEx

HS_GLUD1.

Genevestigator

P00367.

GermOnline

ENSG00000148672. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR006095. 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]

Pfam

PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]

PRINTS

PR00082. GLFDHDRGNASE.

SMART

SM00839. ELFV_dehydrog. 1 hit.
[Graphical view]

PROSITE

PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00142. L-Glutamic Acid.
DB00157. NADH.

EvolutionaryTrace

P00367.

GenomeRNAi

2746.

NextBio

10824.

SOURCE

Search...

Entry information

Entry name

DHE3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 157 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.