Reviewed, UniProtKB/Swiss-Prot P49448 (DHE4_HUMAN)

Names and origin

Protein names

Recommended name:
    Glutamate dehydrogenase 2, mitochondrial
      Short name=GDH
    EC=1.4.1.3

Gene names

Name:	GLUD2
Synonyms:	GLUDP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.
Catalytic activity	L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H.
Subunit structure	Homohexamer By similarity.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Expressed in retina, testis and, at a lower level, brain.
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	glutamate metabolic process Ref.1 Inferred from direct assay. Source: UniProtKB oxidation reduction Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro glutamate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: EC glutamate dehydrogenase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 53	53	Mitochondrion By similarity
	Chain	54 – 558	505	Glutamate dehydrogenase 2, mitochondrial		PRO_0000007208
Sites
	Active site	183	1	By similarity
	Binding site	84	1	Substrate By similarity
Experimental info
	Sequence conflict	286	1	E → Q in CAA46995 and AAA20969. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49448-1 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: F222B1B2CB74A6EA	FASTA	558	61,434
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene." Shashidharan P., Michaelidis T.M., Robakis N.K., Kresovali A., Papamatheakis J., Plaitakis A. J. Biol. Chem. 269:16971-16976(1994) [PubMed: 8207021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Retina.
[2]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X66310 Genomic DNA. Translation: CAA46995.1. U08997 Genomic DNA. Translation: AAA20969.1. AC006144 Genomic DNA. Translation: AAD05030.1. BC050732 mRNA. Translation: AAH50732.1.
PIR	A53719.
RefSeq	NP_036216.2.
UniGene	Hs.368538
3D structure databases
HSSP	HSSP built from PDB template 1L1F based on UniProtKB P00367.
SMR	P49448. Positions 58-558.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49448.
PTM databases
PhosphoSite	P49448.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00027146.
Proteomic databases
PeptideAtlas	P49448.
Genome annotation databases
Ensembl	ENSG00000182890. Homo sapiens. [Contig view]
GeneID	2747.
KEGG	hsa:2747.
NMPDR	fig|9606.3.peg.33334.
Organism-specific databases
H-InvDB	HIX0017030.
HGNC	HGNC:4336. GLUD2.
MIM	300144. gene.
PharmGKB	PA28738.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P49448.
HOVERGEN	P49448.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-11465.
Gene expression databases
ArrayExpress	P49448.
GermOnline	ENSG00000182890. Homo sapiens.
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11606:SF2. GLFV_DH. 1 hit.
Pfam	PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view]
PRINTS	PR00082. GLFDHDRGNASE.
PROSITE	PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00142. L-Glutamic Acid. DB00157. NADH.
NextBio	10828.
SOURCE	Search...

Entry information

Entry name

DHE4_HUMAN

Accession

Primary (citable) accession number: P49448
Secondary accession number(s): Q9UDQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	April 27, 2001
Last modified:	November 25, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)