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UniProtKB/Swiss-Prot entry P49448


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

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Entry information
Entry name DHE4_HUMAN
Primary accession number P49448
Secondary accession number Q9UDQ4
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on April 27, 2001 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 69)
Name and origin of the protein
Protein name Glutamate dehydrogenase 2, mitochondrial [Precursor]
Synonyms GDH
EC 1.4.1.3
Gene name
Name: GLUD2
Synonyms: GLUDP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Retina;
PubMed=8207021 [NCBI, ExPASy, EBI, Israel, Japan]
Shashidharan P., Michaelidis T.M., Robakis N.K., Kresovali A., Papamatheakis J., Plaitakis A.;
"Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene.";
J. Biol. Chem. 269:16971-16976(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
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
X66310; CAA46995.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U08997; AAA20969.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006144; AAD05030.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050732; AAH50732.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A53719; A53719.
RefSeq NP_036216.2; -.
UniGene Hs.368538
3D structure databases
HSSP P00367; 1L1F. [HSSP ENTRY / PDB]
SMR P49448; 58-558.
ModBase P49448.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11465; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00027146; -.
Organism-specific databases
H-InvDB HIX0017030; -.
HGNC HGNC:4336; GLUD2.
GenAtlas GLUD2.
MIM 300144; gene. [NCBI / EBI]
PharmGKB PA28738; -.
GeneCards P49448.
Gene expression databases
ArrayExpress P49448; -.
GermOnline ENSG00000182890; Homo sapiens.
Ontologies
GO
GO:0004352; Molecular function: glutamate dehydrogenase activity (inferred from direct assay from UniProtKB).
GO:0006536; Biological process: glutamate metabolic process (inferred from direct assay from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from direct assay 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 P49448.
Proteomic databases
PeptideAtlas P49448; -.
Genome annotation databases
Ensembl ENSG00000182890; Homo sapiens. [Contig view]
GeneID 2747; -.
KEGG hsa:2747; -.
NMPDR fig|9606.3.peg.33334; -.
Phylogenomic databases
HOGENOM P49448; -.
HOVERGEN P49448; -.
Other
DrugBank DB00142; L-Glutamic Acid.
DB00157; NADH.
SOURCE GLUD2; Homo sapiens.
ProtoNet P49448.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Mitochondrion; NADP; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    53  53     Mitochondrion (By similarity). 
CHAIN   54   558  505     Glutamate dehydrogenase 2, mitochondrial. PRO_0000007208
ACT_SITE   183   183        By similarity. 
BINDING   84    84        Substrate (By similarity). 
CONFLICT   286   286        E -> Q (in Ref. 1; CAA46995/AAA20969). 
Sequence information
Length: 558 AA [This is the length of the unprocessed precursor] Molecular weight: 61434 Da [This is the MW of the unprocessed precursor] CRC64: F222B1B2CB74A6EA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MYRYLAKALL PSRAGPAALG SAANHSAALL GRGRGQPAAA SQPGLALAAR RHYSELVADR 

        70         80         90        100        110        120 
EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN RVRGILRIIK PCNHVLSLSF 

       130        140        150        160        170        180 
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG 

       190        200        210        220        230        240 
GAKAGVKINP KNYTENELEK ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY 

       250        260        270        280        290        300 
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR 

       310        320        330        340        350        360 
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG 

       370        380        390        400        410        420 
FPKAKPYEGS ILEVDCDILI PAATEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER 

       430        440        450        460        470        480 
NILVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLLSV QESLERKFGK 

       490        500        510        520        530        540 
HGGTIPIVPT AEFQDSISGA SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV 

       550 
NAIEKVFKVY SEAGVTFT 

P49448 in FASTA format

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