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P26443

- DHE3_MOUSE

UniProt

P26443 - DHE3_MOUSE

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Protein
Glutamate dehydrogenase 1, mitochondrial
Gene
Glud1, Glud
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.1 Publication

Catalytic activityi

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

Enzyme regulationi

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

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GTP binding Source: UniProtKB-KW
  3. glutamate dehydrogenase (NAD+) activity Source: Ensembl
  4. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB
  5. protein binding Source: MGI

GO - Biological processi

  1. glutamine metabolic process Source: UniProtKB
  2. long-term memory Source: Ensembl
  3. positive regulation of insulin secretion Source: MGI
  4. response to aluminum ion Source: Ensembl
  5. tricarboxylic acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
Gene namesi
Name:Glud1
Synonyms:Glud
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:95753. Glud1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Mitochondrion
Add
BLAST
Chaini54 – 558505Glutamate dehydrogenase 1, mitochondrial
PRO_0000007212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-succinyllysine1 Publication
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei84 – 841N6-acetyllysine; alternate2 Publications
Modified residuei84 – 841N6-succinyllysine; alternate1 Publication
Modified residuei90 – 901N6-acetyllysine1 Publication
Modified residuei110 – 1101N6-acetyllysine; alternate1 Publication
Modified residuei110 – 1101N6-succinyllysine; alternate By similarity
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei135 – 1351Phosphotyrosine1 Publication
Modified residuei162 – 1621N6-acetyllysine; alternate1 Publication
Modified residuei162 – 1621N6-succinyllysine; alternate1 Publication
Modified residuei171 – 1711N6-acetyllysine1 Publication
Modified residuei172 – 1721ADP-ribosylcysteine By similarity
Modified residuei183 – 1831N6-acetyllysine; alternate By similarity
Modified residuei183 – 1831N6-succinyllysine; alternate1 Publication
Modified residuei187 – 1871N6-acetyllysine1 Publication
Modified residuei191 – 1911N6-acetyllysine; alternate1 Publication
Modified residuei191 – 1911N6-succinyllysine; alternate1 Publication
Modified residuei200 – 2001N6-succinyllysine1 Publication
Modified residuei211 – 2111N6-acetyllysine1 Publication
Modified residuei326 – 3261N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-acetyllysine; alternate1 Publication
Modified residuei346 – 3461N6-succinyllysine; alternate1 Publication
Modified residuei352 – 3521N6-acetyllysine; alternate1 Publication
Modified residuei352 – 3521N6-succinyllysine; alternate1 Publication
Modified residuei363 – 3631N6-acetyllysine; alternate1 Publication
Modified residuei363 – 3631N6-succinyllysine; alternate1 Publication
Modified residuei365 – 3651N6-acetyllysine; alternate1 Publication
Modified residuei365 – 3651N6-succinyllysine; alternate1 Publication
Modified residuei386 – 3861N6-acetyllysine By similarity
Modified residuei390 – 3901N6-acetyllysine; alternate1 Publication
Modified residuei390 – 3901N6-succinyllysine; alternate1 Publication
Modified residuei399 – 3991N6-acetyllysine1 Publication
Modified residuei415 – 4151N6-acetyllysine; alternate1 Publication
Modified residuei415 – 4151N6-succinyllysine; alternate By similarity
Modified residuei457 – 4571N6-acetyllysine; alternate1 Publication
Modified residuei457 – 4571N6-malonyllysine; alternate By similarity
Modified residuei457 – 4571N6-succinyllysine; alternate By similarity
Modified residuei477 – 4771N6-acetyllysine; alternate1 Publication
Modified residuei477 – 4771N6-succinyllysine; alternate1 Publication
Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
Modified residuei480 – 4801N6-succinyllysine; alternate1 Publication
Modified residuei503 – 5031N6-acetyllysine; alternate2 Publications
Modified residuei503 – 5031N6-malonyllysine; alternate By similarity
Modified residuei503 – 5031N6-succinyllysine; alternate1 Publication
Modified residuei527 – 5271N6-acetyllysine; alternate2 Publications
Modified residuei527 – 5271N6-malonyllysine; alternate By similarity
Modified residuei527 – 5271N6-succinyllysine; alternate1 Publication
Modified residuei545 – 5451N6-acetyllysine; alternate2 Publications
Modified residuei545 – 5451N6-succinyllysine; alternate1 Publication
Modified residuei548 – 5481N6-acetyllysine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

MaxQBiP26443.
PaxDbiP26443.
PRIDEiP26443.

2D gel databases

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

PTM databases

PhosphoSiteiP26443.

Expressioni

Gene expression databases

ArrayExpressiP26443.
BgeeiP26443.
GenevestigatoriP26443.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi199956. 4 interactions.
IntActiP26443. 9 interactions.
MINTiMINT-1839447.

Structurei

3D structure databases

ProteinModelPortaliP26443.
SMRiP26443. Positions 63-558.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP26443.
KOiK00261.
OMAiTCIGVIE.
OrthoDBiEOG73NG50.
PhylomeDBiP26443.
TreeFamiTF313945.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P26443-1 [UniParc]FASTAAdd to Basket

« Hide

MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR    50
RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN 100
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK 200
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN 250
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 300
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED 350
FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI 400
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS 450
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA 500
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY 550
NEAGVTFT 558
Length:558
Mass (Da):61,337
Last modified:August 1, 1992 - v1
Checksum:i92738AA5A133838A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti495 – 4951D → G in BAC40767. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57024 mRNA. Translation: CAA40341.1.
AK089152 mRNA. Translation: BAC40767.1.
BC052724 mRNA. Translation: AAH52724.1.
BC057347 mRNA. Translation: AAH57347.1.
CCDSiCCDS26935.1.
PIRiS16239.
RefSeqiNP_032159.1. NM_008133.4.
UniGeneiMm.10600.

Genome annotation databases

EnsembliENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794.
GeneIDi14661.
KEGGimmu:14661.
UCSCiuc007tas.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57024 mRNA. Translation: CAA40341.1 .
AK089152 mRNA. Translation: BAC40767.1 .
BC052724 mRNA. Translation: AAH52724.1 .
BC057347 mRNA. Translation: AAH57347.1 .
CCDSi CCDS26935.1.
PIRi S16239.
RefSeqi NP_032159.1. NM_008133.4.
UniGenei Mm.10600.

3D structure databases

ProteinModelPortali P26443.
SMRi P26443. Positions 63-558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199956. 4 interactions.
IntActi P26443. 9 interactions.
MINTi MINT-1839447.

PTM databases

PhosphoSitei P26443.

2D gel databases

REPRODUCTION-2DPAGE P26443.
SWISS-2DPAGE P26443.
UCD-2DPAGE P26443.

Proteomic databases

MaxQBi P26443.
PaxDbi P26443.
PRIDEi P26443.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022322 ; ENSMUSP00000022322 ; ENSMUSG00000021794 .
GeneIDi 14661.
KEGGi mmu:14661.
UCSCi uc007tas.2. mouse.

Organism-specific databases

CTDi 2746.
MGIi MGI:95753. Glud1.

Phylogenomic databases

eggNOGi COG0334.
GeneTreei ENSGT00390000000854.
HOGENOMi HOG000243801.
HOVERGENi HBG005479.
InParanoidi P26443.
KOi K00261.
OMAi TCIGVIE.
OrthoDBi EOG73NG50.
PhylomeDBi P26443.
TreeFami TF313945.

Miscellaneous databases

ChiTaRSi GLUD1. mouse.
NextBioi 286534.
PROi P26443.
SOURCEi Search...

Gene expression databases

ArrayExpressi P26443.
Bgeei P26443.
Genevestigatori P26443.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
    , 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
    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. 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. 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.

Entry informationi

Entry nameiDHE3_MOUSE
AccessioniPrimary (citable) accession number: P26443
Secondary accession number(s): Q8C273
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi