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P26443 (DHE3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.8

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 By similarity.

Subunit structure

Homohexamer.

Subcellular location

Mitochondrion matrix.

Post-translational modification

Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Mitochondrion
Chain54 – 558505Glutamate dehydrogenase 1, mitochondrial
PRO_0000007212

Regions

Nucleotide binding141 – 1433NAD By similarity

Sites

Active site1831 By similarity
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 Ref.9
Modified residue791Phosphoserine Ref.6
Modified residue841N6-acetyllysine; alternate Ref.9 Ref.10
Modified residue841N6-succinyllysine; alternate Ref.9
Modified residue901N6-acetyllysine Ref.10
Modified residue1101N6-acetyllysine; alternate Ref.10
Modified residue1101N6-succinyllysine; alternate By similarity
Modified residue1281Phosphoserine Ref.6
Modified residue1351Phosphotyrosine Ref.7
Modified residue1621N6-acetyllysine; alternate Ref.10
Modified residue1621N6-succinyllysine; alternate Ref.9
Modified residue1711N6-acetyllysine Ref.10
Modified residue1721ADP-ribosylcysteine By similarity
Modified residue1831N6-acetyllysine; alternate By similarity
Modified residue1831N6-succinyllysine; alternate Ref.9
Modified residue1871N6-acetyllysine Ref.10
Modified residue1911N6-acetyllysine; alternate Ref.10
Modified residue1911N6-succinyllysine; alternate Ref.9
Modified residue2001N6-succinyllysine Ref.9
Modified residue2111N6-acetyllysine Ref.10
Modified residue3261N6-acetyllysine Ref.10
Modified residue3461N6-acetyllysine; alternate Ref.10
Modified residue3461N6-succinyllysine; alternate Ref.9
Modified residue3521N6-acetyllysine; alternate Ref.10
Modified residue3521N6-succinyllysine; alternate Ref.9
Modified residue3631N6-acetyllysine; alternate Ref.10
Modified residue3631N6-succinyllysine; alternate Ref.9
Modified residue3651N6-acetyllysine; alternate Ref.10
Modified residue3651N6-succinyllysine; alternate Ref.9
Modified residue3861N6-acetyllysine By similarity
Modified residue3901N6-acetyllysine; alternate Ref.10
Modified residue3901N6-succinyllysine; alternate Ref.9
Modified residue3991N6-acetyllysine Ref.10
Modified residue4151N6-acetyllysine; alternate Ref.10
Modified residue4151N6-succinyllysine; alternate By similarity
Modified residue4571N6-acetyllysine; alternate Ref.10
Modified residue4571N6-malonyllysine; alternate By similarity
Modified residue4571N6-succinyllysine; alternate By similarity
Modified residue4771N6-acetyllysine; alternate Ref.10
Modified residue4771N6-succinyllysine; alternate Ref.9
Modified residue4801N6-acetyllysine; alternate Ref.10
Modified residue4801N6-succinyllysine; alternate Ref.9
Modified residue5031N6-acetyllysine; alternate Ref.9 Ref.10
Modified residue5031N6-malonyllysine; alternate By similarity
Modified residue5031N6-succinyllysine; alternate Ref.9
Modified residue5271N6-acetyllysine; alternate Ref.9 Ref.10
Modified residue5271N6-malonyllysine; alternate By similarity
Modified residue5271N6-succinyllysine; alternate Ref.9
Modified residue5451N6-acetyllysine; alternate Ref.9 Ref.10
Modified residue5451N6-succinyllysine; alternate Ref.9
Modified residue5481N6-acetyllysine Ref.10

Experimental info

Sequence conflict4951D → G in BAC40767. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26443 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 92738AA5A133838A

FASTA55861,337
        10         20         30         40         50         60 
MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR RHYSEAAADR 

        70         80         90        100        110        120 
EDDPNFFKMV EGFFDRGASI VEDKLVEDLK 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 HRFGAKCVGV GESDGSIWNP DGIDPKELED FKLQHGSILG 

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

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

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

       550 
NAIEKVFKVY NEAGVTFT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, structure and expression analysis of a full-length mouse brain glutamate dehydrogenase cDNA."
Tzimagiorgis G., Moschonas N.K.
Biochim. Biophys. Acta 1089:250-253(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Olfactory bulb.
[3]"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].
Strain: C57BL/6.
Tissue: Brain.
[4]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-76; 108-123; 125-136; 152-183; 192-200; 212-231; 275-318; 327-346; 353-363; 366-386; 400-420; 461-476; 481-496; 504-516; 528-545 AND 549-558.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"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.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"The mTORC1 pathway stimulates glutamine metabolism and cell proliferation by repressing SIRT4."
Csibi A., Fendt S.M., Li C., Poulogiannis G., Choo A.Y., Chapski D.J., Jeong S.M., Dempsey J.M., Parkhitko A., Morrison T., Henske E.P., Haigis M.C., Cantley L.C., Stephanopoulos G., Yu J., Blenis J.
Cell 153:840-854(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ADP-RIBOSYLATION.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-503; LYS-527 AND LYS-545, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-84; LYS-162; LYS-183; LYS-191; LYS-200; LYS-346; LYS-352; LYS-363; LYS-365; LYS-390; LYS-477; LYS-480; LYS-503; LYS-527 AND LYS-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[10]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-90; LYS-110; LYS-162; LYS-171; LYS-187; LYS-191; LYS-211; LYS-326; LYS-346; LYS-352; LYS-363; LYS-365; LYS-390; LYS-399; LYS-415; LYS-457; LYS-477; LYS-480; LYS-503; LYS-527; LYS-545 AND LYS-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57024 mRNA. Translation: CAA40341.1.
AK089152 mRNA. Translation: BAC40767.1.
BC052724 mRNA. Translation: AAH52724.1.
BC057347 mRNA. Translation: AAH57347.1.
CCDSCCDS26935.1.
PIRS16239.
RefSeqNP_032159.1. NM_008133.4.
UniGeneMm.10600.

3D structure databases

ProteinModelPortalP26443.
SMRP26443. Positions 63-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199956. 4 interactions.
IntActP26443. 9 interactions.
MINTMINT-1839447.

PTM databases

PhosphoSiteP26443.

2D gel databases

REPRODUCTION-2DPAGEP26443.
SWISS-2DPAGEP26443.
UCD-2DPAGEP26443.

Proteomic databases

MaxQBP26443.
PaxDbP26443.
PRIDEP26443.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794.
GeneID14661.
KEGGmmu:14661.
UCSCuc007tas.2. mouse.

Organism-specific databases

CTD2746.
MGIMGI:95753. Glud1.

Phylogenomic databases

eggNOGCOG0334.
GeneTreeENSGT00390000000854.
HOGENOMHOG000243801.
HOVERGENHBG005479.
InParanoidP26443.
KOK00261.
OMATCIGVIE.
OrthoDBEOG73NG50.
PhylomeDBP26443.
TreeFamTF313945.

Gene expression databases

ArrayExpressP26443.
BgeeP26443.
GenevestigatorP26443.

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

ChiTaRSGLUD1. mouse.
NextBio286534.
PROP26443.
SOURCESearch...

Entry information

Entry nameDHE3_MOUSE
AccessionPrimary (citable) accession number: P26443
Secondary accession number(s): Q8C273
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot