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P49448 (DHE4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 2, mitochondrial

Short name=GDH 2
EC=1.4.1.3
Gene names
Name:GLUD2
Synonyms:GLUDP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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

Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.

Catalytic activity

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

Subunit structure

Homohexamer By similarity.

Subcellular location

Mitochondrion matrix Ref.7.

Tissue specificity

Expressed in retina, testis and, at a lower level, brain.

Post-translational modification

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 2, mitochondrial
PRO_0000007208

Sites

Active site1831 By similarity
Binding site841Substrate By similarity

Amino acid modifications

Modified residue681N6-succinyllysine By similarity
Modified residue791Phosphoserine By similarity
Modified residue841N6-acetyllysine; alternate By similarity
Modified residue841N6-succinyllysine; alternate By similarity
Modified residue1101N6-acetyllysine; alternate By similarity
Modified residue1101N6-succinyllysine; alternate By similarity
Modified residue1281Phosphoserine By similarity
Modified residue1351Phosphotyrosine By similarity
Modified residue1621N6-acetyllysine; alternate By similarity
Modified residue1621N6-succinyllysine; alternate By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue1721ADP-ribosylcysteine
Modified residue1831N6-acetyllysine; alternate By similarity
Modified residue1831N6-succinyllysine; alternate By similarity
Modified residue1871N6-acetyllysine By similarity
Modified residue1911N6-acetyllysine; alternate By similarity
Modified residue1911N6-succinyllysine; alternate By similarity
Modified residue2001N6-succinyllysine By similarity
Modified residue2111N6-acetyllysine By similarity
Modified residue3261N6-acetyllysine By similarity
Modified residue3461N6-acetyllysine; alternate By similarity
Modified residue3461N6-succinyllysine; alternate By similarity
Modified residue3521N6-acetyllysine; alternate By similarity
Modified residue3521N6-succinyllysine; alternate By similarity
Modified residue3631N6-acetyllysine; alternate By similarity
Modified residue3631N6-succinyllysine; alternate By similarity
Modified residue3651N6-acetyllysine; alternate By similarity
Modified residue3651N6-succinyllysine; alternate By similarity
Modified residue3861N6-acetyllysine By similarity
Modified residue3901N6-acetyllysine; alternate By similarity
Modified residue3901N6-succinyllysine; alternate By similarity
Modified residue3991N6-acetyllysine By similarity
Modified residue4151N6-acetyllysine; alternate By similarity
Modified residue4151N6-succinyllysine; alternate By similarity
Modified residue4571N6-acetyllysine; alternate By similarity
Modified residue4571N6-succinyllysine; alternate By similarity
Modified residue4771N6-acetyllysine; alternate By similarity
Modified residue4771N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine; alternate By similarity
Modified residue4801N6-succinyllysine; alternate By similarity
Modified residue5031N6-acetyllysine; alternate By similarity
Modified residue5031N6-succinyllysine; alternate By similarity
Modified residue5271N6-acetyllysine; alternate By similarity
Modified residue5271N6-succinyllysine; alternate By similarity
Modified residue5451N6-acetyllysine; alternate By similarity
Modified residue5451N6-succinyllysine; alternate By similarity
Modified residue5481N6-acetyllysine By similarity

Natural variations

Natural variant4981S → A.
Corresponds to variant rs9697983 [ dbSNP | Ensembl ].
VAR_048867

Experimental info

Sequence conflict2861E → Q in CAA46995. Ref.1
Sequence conflict2861E → Q in AAA20969. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49448 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: F222B1B2CB74A6EA

FASTA55861,434
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Retina.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Skin.
[5]"Identification of ADP-ribosylation site in human glutamate dehydrogenase isozymes."
Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W.
FEBS Lett. 579:4125-4130(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ADP-RIBOSYLATION AT CYS-172.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Alpha helical structures in the leader sequence of human GLUD2 glutamate dehydrogenase responsible for mitochondrial import."
Kotzamani D., Plaitakis A.
Neurochem. Int. 61:463-469(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSIT PEPTIDE CLEAVAGE SITE, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66310 Genomic DNA. Translation: CAA46995.1.
U08997 Genomic DNA. Translation: AAA20969.1.
AK313356 mRNA. Translation: BAG36157.1.
AC006144 Genomic DNA. Translation: AAD05030.1.
BC050732 mRNA. Translation: AAH50732.1.
PIRA53719.
RefSeqNP_036216.2. NM_012084.3.
UniGeneHs.368538.

3D structure databases

ProteinModelPortalP49448.
SMRP49448. Positions 63-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109009. 3 interactions.
IntActP49448. 4 interactions.
MINTMINT-1411373.
STRING9606.ENSP00000327589.

Chemistry

DrugBankDB00142. L-Glutamic Acid.
DB00157. NADH.

PTM databases

PhosphoSiteP49448.

Polymorphism databases

DMDM13432152.

2D gel databases

REPRODUCTION-2DPAGEIPI00027146.

Proteomic databases

PaxDbP49448.
PeptideAtlasP49448.
PRIDEP49448.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328078; ENSP00000327589; ENSG00000182890.
GeneID2747.
KEGGhsa:2747.
UCSCuc004eto.3. human.

Organism-specific databases

CTD2747.
GeneCardsGC0XP120181.
HGNCHGNC:4336. GLUD2.
HPAHPA042492.
HPA044839.
MIM300144. gene.
neXtProtNX_P49448.
PharmGKBPA28738.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0334.
HOGENOMHOG000243801.
HOVERGENHBG005479.
InParanoidP49448.
KOK00261.
OMAEDIYNQH.
OrthoDBEOG73NG50.
PhylomeDBP49448.
TreeFamTF313945.

Enzyme and pathway databases

BioCycMetaCyc:HS00018-MONOMER.
BRENDA1.4.1.3. 2681.
SABIO-RKP49448.

Gene expression databases

ArrayExpressP49448.
BgeeP49448.
GenevestigatorP49448.

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

GeneWikiGLUD2.
GenomeRNAi2747.
NextBio10828.
PROP49448.
SOURCESearch...

Entry information

Entry nameDHE4_HUMAN
AccessionPrimary (citable) accession number: P49448
Secondary accession number(s): B2R8G0, Q9UDQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 27, 2001
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM