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Protein

Glutamate dehydrogenase 2, mitochondrial

Gene

GLUD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841SubstrateBy similarity
Active sitei183 – 1831PROSITE-ProRule annotation

GO - Molecular functioni

  • ADP binding Source: BHF-UCL
  • glutamate dehydrogenase (NAD+) activity Source: UniProtKB
  • glutamate dehydrogenase [NAD(P)+] activity Source: BHF-UCL
  • GTP binding Source: BHF-UCL
  • leucine binding Source: BHF-UCL

GO - Biological processi

  • glutamate biosynthetic process Source: BHF-UCL
  • glutamate catabolic process Source: BHF-UCL
  • glutamate metabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS00018-MONOMER.
BRENDAi1.4.1.3. 2681.
SABIO-RKP49448.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 2, mitochondrial (EC:1.4.1.3)
Short name:
GDH 2
Gene namesi
Name:GLUD2
Synonyms:GLUDP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:4336. GLUD2.

Subcellular locationi

  • Mitochondrion matrix 1 Publication

GO - Cellular componenti

  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28738.

Polymorphism and mutation databases

BioMutaiGLUD2.
DMDMi13432152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Mitochondrion1 PublicationAdd
BLAST
Chaini54 – 558505Glutamate dehydrogenase 2, mitochondrialPRO_0000007208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721ADP-ribosylcysteine1 Publication

Post-translational modificationi

Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.

Keywords - PTMi

ADP-ribosylation

Proteomic databases

MaxQBiP49448.
PaxDbiP49448.
PeptideAtlasiP49448.
PRIDEiP49448.

2D gel databases

REPRODUCTION-2DPAGEIPI00027146.

PTM databases

PhosphoSiteiP49448.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP49448.
GenevisibleiP49448. HS.

Organism-specific databases

HPAiHPA042492.
HPA044839.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

BioGridi109009. 8 interactions.
IntActiP49448. 4 interactions.
MINTiMINT-1411373.
STRINGi9606.ENSP00000327589.

Structurei

3D structure databases

ProteinModelPortaliP49448.
SMRiP49448. Positions 63-558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP49448.
KOiK00261.
OMAiYINAIQK.
OrthoDBiEOG73NG50.
PhylomeDBiP49448.
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.

P49448-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRYLAKALL PSRAGPAALG SAANHSAALL GRGRGQPAAA SQPGLALAAR
60 70 80 90 100
RHYSELVADR EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTENELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGSILG FPKAKPYEGS ILEVDCDILI PAATEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NILVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLLSV QESLERKFGK HGGTIPIVPT AEFQDSISGA
510 520 530 540 550
SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV NAIEKVFKVY

SEAGVTFT
Length:558
Mass (Da):61,434
Last modified:April 27, 2001 - v2
Checksum:iF222B1B2CB74A6EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti286 – 2861E → Q in CAA46995 (PubMed:8207021).Curated
Sequence conflicti286 – 2861E → Q in AAA20969 (PubMed:8207021).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti498 – 4981S → A.
Corresponds to variant rs9697983 [ dbSNP | Ensembl ].
VAR_048867

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14603.1.
PIRiA53719.
RefSeqiNP_036216.2. NM_012084.3.
UniGeneiHs.368538.

Genome annotation databases

EnsembliENST00000328078; ENSP00000327589; ENSG00000182890.
GeneIDi2747.
KEGGihsa:2747.
UCSCiuc004eto.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14603.1.
PIRiA53719.
RefSeqiNP_036216.2. NM_012084.3.
UniGeneiHs.368538.

3D structure databases

ProteinModelPortaliP49448.
SMRiP49448. Positions 63-558.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109009. 8 interactions.
IntActiP49448. 4 interactions.
MINTiMINT-1411373.
STRINGi9606.ENSP00000327589.

PTM databases

PhosphoSiteiP49448.

Polymorphism and mutation databases

BioMutaiGLUD2.
DMDMi13432152.

2D gel databases

REPRODUCTION-2DPAGEIPI00027146.

Proteomic databases

MaxQBiP49448.
PaxDbiP49448.
PeptideAtlasiP49448.
PRIDEiP49448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328078; ENSP00000327589; ENSG00000182890.
GeneIDi2747.
KEGGihsa:2747.
UCSCiuc004eto.3. human.

Organism-specific databases

CTDi2747.
GeneCardsiGC0XP120181.
HGNCiHGNC:4336. GLUD2.
HPAiHPA042492.
HPA044839.
MIMi300144. gene.
neXtProtiNX_P49448.
PharmGKBiPA28738.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0334.
GeneTreeiENSGT00390000000854.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiP49448.
KOiK00261.
OMAiYINAIQK.
OrthoDBiEOG73NG50.
PhylomeDBiP49448.
TreeFamiTF313945.

Enzyme and pathway databases

BioCyciMetaCyc:HS00018-MONOMER.
BRENDAi1.4.1.3. 2681.
SABIO-RKP49448.

Miscellaneous databases

GeneWikiiGLUD2.
GenomeRNAii2747.
NextBioi10828.
PROiP49448.
SOURCEiSearch...

Gene expression databases

BgeeiP49448.
GenevisibleiP49448. HS.

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]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiDHE4_HUMAN
AccessioniPrimary (citable) accession number: P49448
Secondary accession number(s): B2R8G0, Q9UDQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 27, 2001
Last modified: June 24, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.