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UniProtKB/Swiss-Prot entry P26443


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHE3_MOUSE
Primary accession number P26443
Secondary accession number Q8C273
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 81)
Name and origin of the protein
Protein name Glutamate dehydrogenase 1, mitochondrial [Precursor]
Synonyms GDH
EC 1.4.1.3
Gene name
Name: Glud1
Synonyms: Glud
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Brain;
DOI=10.1016/0167-4781(91)90017-G; PubMed=1711373 [NCBI, ExPASy, EBI, Israel, Japan]
Tzimagiorgis G., Moschonas N.K.;
"Molecular cloning, structure and expression analysis of a full-length mouse brain glutamate dehydrogenase cDNA.";
Biochim. Biophys. Acta 1089:250-253(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Olfactory bulb;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
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;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 108-123; 303-318; 400-420 AND 481-496, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-503 AND LYS-527, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135 AND TYR-512, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X57024; CAA40341.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK089152; BAC40767.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052724; AAH52724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC057347; AAH57347.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S16239; S16239.
RefSeq NP_032159.1; -.
UniGene Mm.10600
3D structure databases
HSSP P00367; 1L1F. [HSSP ENTRY / PDB]
SMR P26443; 58-558.
ModBase P26443.
Protein-protein interaction databases
IntAct P26443; -.
PTM databases
PhosphoSite P26443; -.
2D gel databases
SWISS-2DPAGE P26443; -.
REPRODUCTION-2DPAGE P26443; -.
Organism-specific databases
MGI MGI:95753; Glud1.
Gene expression databases
ArrayExpress P26443; -.
CleanEx MM_GLUD1; -.
GermOnline ENSMUSG00000021794; Mus musculus.
Ontologies
GO
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
GO:0004353; Molecular function: glutamate dehydrogenase [NAD(P)+] activity (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0046676; Biological process: negative regulation of insulin secretion (inferred from genetic interaction from MGI).
GO:0007169; Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11606:SF2; GLFV_DH; 1.
Pfam PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00082; GLFDHDRGNASE.
PROSITE PS00074; GLFV_DEHYDROGENASE; 1.
BLOCKS P26443.
Genome annotation databases
Ensembl ENSMUSG00000021794; Mus musculus. [Contig view]
GeneID 14661; -.
KEGG mmu:14661; -.
NMPDR fig|10090.3.peg.28839; -.
Phylogenomic databases
HOGENOM P26443; -.
HOVERGEN P26443; -.
Other
SOURCE Glud1; Mus musculus.
ProtoNet P26443.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Direct protein sequencing; GTP-binding; Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase; Phosphoprotein; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    53  53     Mitochondrion. 
CHAIN   54   558  505     Glutamate dehydrogenase 1, mitochondrial. PRO_0000007212
NP_BIND   141   143  3     NAD (By similarity). 
ACT_SITE   183   183        By similarity. 
BINDING   147   147        Substrate (By similarity). 
BINDING   171   171        Substrate (By similarity). 
BINDING   176   176        NAD (By similarity). 
BINDING   252   252        NAD (By similarity). 
BINDING   266   266        GTP (By similarity). 
BINDING   270   270        GTP (By similarity). 
BINDING   319   319        GTP (By similarity). 
BINDING   322   322        GTP (By similarity). 
BINDING   438   438        Substrate (By similarity). 
BINDING   444   444        NAD (By similarity). 
BINDING   450   450        ADP (By similarity). 
BINDING   516   516        ADP (By similarity). 
MOD_RES   84    84        N6-acetyllysine. 
MOD_RES   135   135        Phosphotyrosine. 
MOD_RES   227   227        Phosphoserine. 
MOD_RES   503   503        N6-acetyllysine. 
MOD_RES   512   512        Phosphotyrosine. 
MOD_RES   527   527        N6-acetyllysine. 
CONFLICT   495   495        D -> G (in Ref. 2; BAC40767). 
Sequence information
Length: 558 AA [This is the length of the unprocessed precursor] Molecular weight: 61337 Da [This is the MW of the unprocessed precursor] CRC64: 92738AA5A133838A [This is a checksum on the sequence]
        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 

P26443 in FASTA format

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