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Glutamate dehydrogenase 1, mitochondrial (GDH 1) (EC 1.4.1.3)

 DHE3_HUMAN              Reviewed;         558 AA.
P00367; B3KV55; B4DGN5; Q5TBU3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
07-NOV-2018, entry version 211.
RecName: Full=Glutamate dehydrogenase 1, mitochondrial;
Short=GDH 1;
EC=1.4.1.3;
Flags: Precursor;
Name=GLUD1; Synonyms=GLUD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Liver;
PubMed=3426581; DOI=10.1016/0006-291X(87)90381-0;
Nakatani Y., Banner C., von Herrat M., Schneider M.E., Smith H.H.,
Freese E.;
"Comparison of human brain and liver glutamate dehydrogenase cDNAs.";
Biochem. Biophys. Res. Commun. 149:405-410(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=3377777; DOI=10.1016/S0006-291X(88)80440-6;
Amuro N., Yamaura M., Goto Y., Okazaki T.;
"Molecular cloning and nucleotide sequence of the cDNA for human liver
glutamate dehydrogenase precursor.";
Biochem. Biophys. Res. Commun. 152:1395-1400(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3399399; DOI=10.1093/nar/16.13.6237;
Nakatani Y., Schneider M.E., Banner C., Freese E.;
"Complete nucleotide sequence of human glutamate dehydrogenase cDNA.";
Nucleic Acids Res. 16:6237-6237(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=3368458; DOI=10.1073/pnas.85.10.3494;
Mavrothalassitis G., Tzimagiorgis G., Mitsialis A., Zannis V.,
Plaitakis A., Papamatheakis J., Moschonas N.;
"Isolation and characterization of cDNA clones encoding human liver
glutamate dehydrogenase: evidence for a small gene family.";
Proc. Natl. Acad. Sci. U.S.A. 85:3494-3498(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8486350; DOI=10.1006/geno.1993.1152;
Michaelidis T.M., Tzimagiorgis G., Moschonas N.K., Papamatheakis J.;
"The human glutamate dehydrogenase gene family: gene organization and
structural characterization.";
Genomics 16:150-160(1993).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, and Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Duodenum, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 54-558.
TISSUE=Liver;
PubMed=429360;
Julliard J.H., Smith E.L.;
"Partial amino acid sequence of the glutamate dehydrogenase of human
liver and a revision of the sequence of the bovine enzyme.";
J. Biol. Chem. 254:3427-3438(1979).
[11]
PROTEIN SEQUENCE OF 54-69.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
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.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 301-558 (ISOFORM 1).
TISSUE=Brain;
PubMed=3585334; DOI=10.1111/j.1471-4159.1987.tb03422.x;
Banner C., Silverman S., Thomas J.W., Lampel K.A., Vitkovic L.,
Huie D., Wenthold R.J.;
"Isolation of a human brain cDNA for glutamate dehydrogenase.";
J. Neurochem. 49:246-252(1987).
[13]
PROTEIN SEQUENCE OF 481-496, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 540-558.
PubMed=8314555; DOI=10.1007/BF00217767;
Tzimagiorgis G., Leversha M.A., Chroniary K., Goulielmos G.,
Sargent C.A., Ferguson-Smith M., Moschonas N.K.;
"Structure and expression analysis of a member of the human glutamate
dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2.";
Hum. Genet. 91:433-438(1993).
[15]
ADP-RIBOSYLATION AT CYS-172.
PubMed=16023112; DOI=10.1016/j.febslet.2005.06.041;
Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W.;
"Identification of ADP-ribosylation site in human glutamate
dehydrogenase isozymes.";
FEBS Lett. 579:4125-4130(2005).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-480 AND LYS-503, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-384 AND
TYR-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER TYR-53, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
CHARACTERIZATION OF VARIANT TYR-507, AND ALLOSTERIC REGULATION.
PubMed=11254391; DOI=10.1006/jmbi.2001.4499;
Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A.;
"Structures of bovine glutamate dehydrogenase complexes elucidate the
mechanism of purine regulation.";
J. Mol. Biol. 307:707-720(2001).
[21]
MUTAGENESIS OF SER-501 AND ARG-516, CHARACTERIZATION OF VARIANT
TYR-507, AND ALLOSTERIC REGULATION.
PubMed=11903050; DOI=10.1042/0264-6021:3630081;
Fang J., Hsu B.Y.L., MacMullen C.M., Poncz M., Smith T.J.,
Stanley C.A.;
"Expression, purification and characterization of human glutamate
dehydrogenase (GDH) allosteric regulatory mutations.";
Biochem. J. 363:81-87(2002).
[22]
ADP-RIBOSYLATION.
PubMed=16959573; DOI=10.1016/j.cell.2006.06.057;
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.;
"SIRT4 inhibits glutamate dehydrogenase and opposes the effects of
calorie restriction in pancreatic beta cells.";
Cell 126:941-954(2006).
[23]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-558.
PubMed=12054821; DOI=10.1016/S0022-2836(02)00161-4;
Smith T.J., Schmidt T., Fang J., Wu J., Siuzdak G., Stanley C.A.;
"The structure of apo human glutamate dehydrogenase details subunit
communication and allostery.";
J. Mol. Biol. 318:765-777(2002).
[24]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 63-558 OF MUTANT ALA-516, AND
ALLOSTERIC REGULATION.
PubMed=12653548; DOI=10.1021/bi0206917;
Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J.;
"Structural studies on ADP activation of mammalian glutamate
dehydrogenase and the evolution of regulation.";
Biochemistry 42:3446-3456(2003).
[25]
REVIEW ON VARIANTS.
PubMed=10338089;
DOI=10.1002/(SICI)1098-1004(1999)13:5<351::AID-HUMU3>3.0.CO;2-R;
Meissner T., Beinbrech B., Mayatepek E.;
"Congenital hyperinsulinism: molecular basis of a heterogeneous
disease.";
Hum. Mutat. 13:351-361(1999).
[26]
VARIANTS HHF6 LEU-498; SER-499; ASP-499; PRO-501 AND TYR-507.
PubMed=9571255; DOI=10.1056/NEJM199805073381904;
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.;
"Hyperinsulinism and hyperammonemia in infants with regulatory
mutations of the glutamate dehydrogenase gene.";
N. Engl. J. Med. 338:1352-1357(1998).
[27]
VARIANTS HHF6 LYS-318 AND ALA-349.
PubMed=10636977; DOI=10.1016/S0022-3476(00)90052-0;
Miki Y., Taki T., Ohura T., Kato H., Yanagisawa M., Hayashi Y.;
"Novel missense mutations in the glutamate dehydrogenase gene in the
congenital hyperinsulinism-hyperammonemia syndrome.";
J. Pediatr. 136:69-72(2000).
[28]
VARIANTS HHF6 CYS-274 AND HIS-322.
PubMed=11214910; DOI=10.1007/s004390000432;
Santer R., Kinner M., Passarge M., Superti-Furga A., Mayatepek E.,
Meissner T., Schneppenheim R., Schaub J.;
"Novel missense mutations outside the allosteric domain of glutamate
dehydrogenase are prevalent in European patients with the congenital
hyperinsulinism-hyperammonemia syndrome.";
Hum. Genet. 108:66-71(2001).
[29]
VARIANTS HHF6 CYS-270; CYS-274; THR-318; CYS-319; CYS-322 AND HIS-322.
PubMed=11297618; DOI=10.1210/jcem.86.4.7414;
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.;
"Hyperinsulinism/hyperammonemia syndrome in children with regulatory
mutations in the inhibitory guanosine triphosphate-binding domain of
glutamate dehydrogenase.";
J. Clin. Endocrinol. Metab. 86:1782-1787(2001).
-!- 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).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2-
oxoglutarate + NH(3) + NAD(P)H. {ECO:0000255|PROSITE-
ProRule:PRU10011}.
-!- ACTIVITY 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: Homohexamer.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P00367-1; Sequence=Displayed;
Name=2;
IsoId=P00367-2; Sequence=VSP_056244;
Note=No experimental confirmation available.;
Name=3;
IsoId=P00367-3; Sequence=VSP_056523, VSP_056524;
Note=No experimental confirmation available.;
-!- PTM: 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. {ECO:0000250}.
-!- 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. {ECO:0000269|PubMed:10636977,
ECO:0000269|PubMed:11214910, ECO:0000269|PubMed:11297618,
ECO:0000269|PubMed:9571255}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Glutamate dehydrogenase 1
entry;
URL="https://en.wikipedia.org/wiki/Glutamate_dehydrogenase_1";
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EMBL; X07674; CAA30521.1; -; mRNA.
EMBL; M20867; AAA52526.1; -; mRNA.
EMBL; M37154; AAA52525.1; -; mRNA.
EMBL; X07769; CAA30598.1; -; mRNA.
EMBL; J03248; AAA52523.1; -; mRNA.
EMBL; X66300; CAA46994.2; -; Genomic_DNA.
EMBL; X66301; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66302; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66303; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66304; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66305; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66306; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66307; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66308; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66309; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66311; CAA46994.2; JOINED; Genomic_DNA.
EMBL; X66312; CAA46994.2; JOINED; Genomic_DNA.
EMBL; AK122685; BAG53667.1; -; mRNA.
EMBL; AK294685; BAG57846.1; -; mRNA.
EMBL; AL136982; CAI17120.1; -; Genomic_DNA.
EMBL; CH471142; EAW80300.1; -; Genomic_DNA.
EMBL; CH471142; EAW80302.1; -; Genomic_DNA.
EMBL; BC040132; AAH40132.1; -; mRNA.
EMBL; BC112946; AAI12947.1; -; mRNA.
EMBL; X67491; CAA47830.1; -; Genomic_DNA.
CCDS; CCDS7382.1; -. [P00367-1]
PIR; A28208; DEHUE.
PIR; I37424; I37424.
PIR; S29331; S29331.
PIR; S60192; S60192.
RefSeq; NP_001305829.1; NM_001318900.1. [P00367-3]
RefSeq; NP_001305830.1; NM_001318901.1. [P00367-2]
RefSeq; NP_001305831.1; NM_001318902.1. [P00367-2]
RefSeq; NP_001305833.1; NM_001318904.1. [P00367-2]
RefSeq; NP_001305834.1; NM_001318905.1. [P00367-2]
RefSeq; NP_001305835.1; NM_001318906.1. [P00367-2]
RefSeq; NP_005262.1; NM_005271.4. [P00367-1]
UniGene; Hs.500409; -.
UniGene; Hs.731740; -.
PDB; 1L1F; X-ray; 2.70 A; A/B/C/D/E/F=54-558.
PDB; 1NR1; X-ray; 3.30 A; A/B/C/D/E/F=63-558.
PDB; 6DQG; X-ray; 2.70 A; A/B/C/D/E/F=63-558.
PDBsum; 1L1F; -.
PDBsum; 1NR1; -.
PDBsum; 6DQG; -.
ProteinModelPortal; P00367; -.
SMR; P00367; -.
BioGrid; 109008; 43.
IntAct; P00367; 44.
MINT; P00367; -.
STRING; 9606.ENSP00000277865; -.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
DrugBank; DB00756; Hexachlorophene.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00157; NADH.
iPTMnet; P00367; -.
PhosphoSitePlus; P00367; -.
SwissPalm; P00367; -.
BioMuta; GLUD1; -.
DMDM; 118541; -.
REPRODUCTION-2DPAGE; IPI00016801; -.
SWISS-2DPAGE; P00367; -.
UCD-2DPAGE; P00367; -.
EPD; P00367; -.
MaxQB; P00367; -.
PaxDb; P00367; -.
PeptideAtlas; P00367; -.
PRIDE; P00367; -.
ProteomicsDB; 51236; -.
Ensembl; ENST00000277865; ENSP00000277865; ENSG00000148672. [P00367-1]
GeneID; 2746; -.
KEGG; hsa:2746; -.
UCSC; uc001keh.4; human. [P00367-1]
CTD; 2746; -.
DisGeNET; 2746; -.
EuPathDB; HostDB:ENSG00000148672.8; -.
GeneCards; GLUD1; -.
GeneReviews; GLUD1; -.
HGNC; HGNC:4335; GLUD1.
HPA; HPA042492; -.
HPA; HPA044839; -.
HPA; HPA061369; -.
MalaCards; GLUD1; -.
MIM; 138130; gene.
MIM; 606762; phenotype.
neXtProt; NX_P00367; -.
OpenTargets; ENSG00000148672; -.
Orphanet; 35878; Hyperinsulinism-hyperammonemia syndrome.
PharmGKB; PA28737; -.
eggNOG; KOG2250; Eukaryota.
eggNOG; COG0334; LUCA.
GeneTree; ENSGT00390000000854; -.
HOGENOM; HOG000243801; -.
HOVERGEN; HBG005479; -.
InParanoid; P00367; -.
KO; K00261; -.
OMA; PCFAAFP; -.
OrthoDB; EOG091G0KMT; -.
PhylomeDB; P00367; -.
TreeFam; TF313945; -.
BioCyc; MetaCyc:HS07548-MONOMER; -.
BRENDA; 1.4.1.3; 2681.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-70614; Amino acid synthesis and interconversion (transamination).
SABIO-RK; P00367; -.
SIGNOR; P00367; -.
ChiTaRS; GLUD1; human.
EvolutionaryTrace; P00367; -.
GeneWiki; Glutamate_dehydrogenase_1; -.
GenomeRNAi; 2746; -.
PRO; PR:P00367; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148672; Expressed in 228 organ(s), highest expression level in hypothalamus.
CleanEx; HS_GLUD1; -.
ExpressionAtlas; P00367; baseline and differential.
Genevisible; P00367; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043531; F:ADP binding; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:UniProtKB.
GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:BHF-UCL.
GO; GO:0005525; F:GTP binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; TAS:BHF-UCL.
GO; GO:0070728; F:leucine binding; IDA:BHF-UCL.
GO; GO:0070403; F:NAD+ binding; IDA:BHF-UCL.
GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
GO; GO:0006537; P:glutamate biosynthetic process; IDA:BHF-UCL.
GO; GO:0006538; P:glutamate catabolic process; IDA:UniProtKB.
GO; GO:0006541; P:glutamine metabolic process; ISS:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
GO; GO:0072350; P:tricarboxylic acid metabolic process; ISS:UniProtKB.
CDD; cd01076; NAD_bind_1_Glu_DH; 1.
InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR033922; NAD_bind_Glu_DH.
Pfam; PF00208; ELFV_dehydrog; 1.
Pfam; PF02812; ELFV_dehydrog_N; 1.
PRINTS; PR00082; GLFDHDRGNASE.
SMART; SM00839; ELFV_dehydrog; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
ATP-binding; Complete proteome; Direct protein sequencing;
Disease mutation; GTP-binding; Mitochondrion; NADP;
Nucleotide-binding; Oxidoreductase; Phosphoprotein;
Reference proteome; Transit peptide.
TRANSIT 1 53 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:429360}.
CHAIN 54 558 Glutamate dehydrogenase 1, mitochondrial.
/FTId=PRO_0000007206.
NP_BIND 141 143 NAD. {ECO:0000250}.
ACT_SITE 183 183
BINDING 147 147 Substrate. {ECO:0000250}.
BINDING 171 171 Substrate. {ECO:0000250}.
BINDING 176 176 NAD. {ECO:0000250}.
BINDING 252 252 NAD. {ECO:0000250}.
BINDING 266 266 GTP. {ECO:0000250}.
BINDING 270 270 GTP. {ECO:0000250}.
BINDING 319 319 GTP. {ECO:0000250}.
BINDING 322 322 GTP. {ECO:0000250}.
BINDING 438 438 Substrate. {ECO:0000250}.
BINDING 444 444 NAD. {ECO:0000250}.
BINDING 450 450 ADP. {ECO:0000250}.
BINDING 516 516 ADP. {ECO:0000250}.
MOD_RES 68 68 N6-succinyllysine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 84 84 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 84 84 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 110 110 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 110 110 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 135 135 Phosphotyrosine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 162 162 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 162 162 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 172 172 ADP-ribosylcysteine.
{ECO:0000269|PubMed:16023112}.
MOD_RES 183 183 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 183 183 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 187 187 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 191 191 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 191 191 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 200 200 N6-succinyllysine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 211 211 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 326 326 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 346 346 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 346 346 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 352 352 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 352 352 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 363 363 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 363 363 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 365 365 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 365 365 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 386 386 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 390 390 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 390 390 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 399 399 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 410 410 Phosphothreonine.
{ECO:0000250|UniProtKB:P10860}.
MOD_RES 415 415 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 415 415 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 457 457 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 457 457 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 457 457 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 477 477 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 477 477 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 480 480 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 480 480 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26443}.
MOD_RES 503 503 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 503 503 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 503 503 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 512 512 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 527 527 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 527 527 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 527 527 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 545 545 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 545 545 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P00366}.
MOD_RES 548 548 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26443}.
VAR_SEQ 1 167 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056244.
VAR_SEQ 1 16 MYRYLGEALLLSRAGP -> MTCPCDNASSVFLGFC (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056523.
VAR_SEQ 17 149 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056524.
VARIANT 270 270 S -> C (in HHF6; diminished sensitivity
to GTP). {ECO:0000269|PubMed:11297618}.
/FTId=VAR_016760.
VARIANT 274 274 R -> C (in HHF6; diminished sensitivity
to GTP; dbSNP:rs56275071).
{ECO:0000269|PubMed:11214910,
ECO:0000269|PubMed:11297618}.
/FTId=VAR_016761.
VARIANT 318 318 R -> K (in HHF6; dbSNP:rs121909736).
{ECO:0000269|PubMed:10636977}.
/FTId=VAR_009270.
VARIANT 318 318 R -> T (in HHF6; diminished sensitivity
to GTP). {ECO:0000269|PubMed:11297618}.
/FTId=VAR_016762.
VARIANT 319 319 Y -> C (in HHF6).
{ECO:0000269|PubMed:11297618}.
/FTId=VAR_016763.
VARIANT 322 322 R -> C (in HHF6; diminished sensitivity
to GTP). {ECO:0000269|PubMed:11297618}.
/FTId=VAR_016764.
VARIANT 322 322 R -> H (in HHF6; diminished sensitivity
to GTP; dbSNP:rs121909737).
{ECO:0000269|PubMed:11214910,
ECO:0000269|PubMed:11297618}.
/FTId=VAR_016765.
VARIANT 349 349 E -> A (in HHF6; dbSNP:rs121909735).
{ECO:0000269|PubMed:10636977}.
/FTId=VAR_009271.
VARIANT 498 498 S -> L (in HHF6; dbSNP:rs121909731).
{ECO:0000269|PubMed:9571255}.
/FTId=VAR_008666.
VARIANT 499 499 G -> D (in HHF6; dbSNP:rs121909734).
{ECO:0000269|PubMed:9571255}.
/FTId=VAR_008667.
VARIANT 499 499 G -> S (in HHF6; dbSNP:rs121909733).
{ECO:0000269|PubMed:9571255}.
/FTId=VAR_008668.
VARIANT 501 501 S -> P (in HHF6; dbSNP:rs121909732).
{ECO:0000269|PubMed:9571255}.
/FTId=VAR_008669.
VARIANT 507 507 H -> Y (in HHF6; abolishes inhibition by
ATP; no effect on activation by ADP;
dbSNP:rs121909730).
{ECO:0000269|PubMed:11254391,
ECO:0000269|PubMed:11903050,
ECO:0000269|PubMed:9571255}.
/FTId=VAR_008670.
MUTAGEN 501 501 S->A: Reduces activity and inhibition by
GTP. {ECO:0000269|PubMed:11903050}.
MUTAGEN 507 507 H->A: Strongly reduces inhibition by GTP.
MUTAGEN 516 516 R->A: Abolishes activation by ADP.
{ECO:0000269|PubMed:11903050}.
HELIX 66 90 {ECO:0000244|PDB:1L1F}.
HELIX 91 93 {ECO:0000244|PDB:1L1F}.
HELIX 95 97 {ECO:0000244|PDB:1L1F}.
HELIX 99 102 {ECO:0000244|PDB:1L1F}.
HELIX 104 109 {ECO:0000244|PDB:1L1F}.
STRAND 113 123 {ECO:0000244|PDB:1L1F}.
STRAND 125 127 {ECO:0000244|PDB:1L1F}.
STRAND 129 138 {ECO:0000244|PDB:1L1F}.
STRAND 142 152 {ECO:0000244|PDB:1L1F}.
HELIX 158 174 {ECO:0000244|PDB:1L1F}.
STRAND 180 186 {ECO:0000244|PDB:1L1F}.
HELIX 190 192 {ECO:0000244|PDB:1L1F}.
HELIX 195 211 {ECO:0000244|PDB:1L1F}.
TURN 217 219 {ECO:0000244|PDB:1L1F}.
STRAND 220 223 {ECO:0000244|PDB:1L1F}.
HELIX 230 242 {ECO:0000244|PDB:1L1F}.
TURN 243 247 {ECO:0000244|PDB:1L1F}.
HELIX 251 253 {ECO:0000244|PDB:1L1F}.
HELIX 260 262 {ECO:0000244|PDB:1L1F}.
HELIX 271 284 {ECO:0000244|PDB:1L1F}.
HELIX 287 293 {ECO:0000244|PDB:1L1F}.
STRAND 298 300 {ECO:0000244|PDB:1L1F}.
STRAND 303 307 {ECO:0000244|PDB:1L1F}.
HELIX 311 322 {ECO:0000244|PDB:1L1F}.
STRAND 326 331 {ECO:0000244|PDB:1L1F}.
STRAND 336 338 {ECO:0000244|PDB:6DQG}.
HELIX 345 354 {ECO:0000244|PDB:1L1F}.
STRAND 355 358 {ECO:0000244|PDB:1L1F}.
STRAND 364 366 {ECO:0000244|PDB:6DQG}.
TURN 371 373 {ECO:0000244|PDB:1L1F}.
STRAND 377 381 {ECO:0000244|PDB:1L1F}.
STRAND 383 386 {ECO:0000244|PDB:1L1F}.
TURN 390 392 {ECO:0000244|PDB:1L1F}.
HELIX 393 395 {ECO:0000244|PDB:1L1F}.
STRAND 399 402 {ECO:0000244|PDB:1L1F}.
STRAND 405 407 {ECO:0000244|PDB:1L1F}.
HELIX 411 419 {ECO:0000244|PDB:1L1F}.
STRAND 423 425 {ECO:0000244|PDB:1L1F}.
HELIX 427 430 {ECO:0000244|PDB:1L1F}.
HELIX 433 447 {ECO:0000244|PDB:1L1F}.
TURN 451 455 {ECO:0000244|PDB:1L1F}.
HELIX 456 475 {ECO:0000244|PDB:1L1F}.
TURN 476 479 {ECO:0000244|PDB:1L1F}.
STRAND 481 483 {ECO:0000244|PDB:6DQG}.
HELIX 491 498 {ECO:0000244|PDB:1L1F}.
HELIX 502 527 {ECO:0000244|PDB:1L1F}.
HELIX 534 551 {ECO:0000244|PDB:1L1F}.
SEQUENCE 558 AA; 61398 MW; A7319A840F57FBB2 CRC64;
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR RHYSEAVADR
EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG
FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK
HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV
NAIEKVFKVY NEAGVTFT


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