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Q64HZ8

- DHE4_PANTR

UniProt

Q64HZ8 - DHE4_PANTR

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Protein

Glutamate dehydrogenase 2, mitochondrial

Gene
GLUD2
Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Substrate By similarity
Active sitei183 – 1831 By similarity

GO - Molecular functioni

  1. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase 2, mitochondrial (EC:1.4.1.3)
Short name:
GDH 2
Gene namesi
Name:GLUD2
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
ProteomesiUP000002277: Unplaced

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Mitochondrion By similarityAdd
BLAST
Chaini54 – 558505Glutamate dehydrogenase 2, mitochondrialPRO_0000007210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681N6-succinyllysine By similarity
Modified residuei79 – 791Phosphoserine By similarity
Modified residuei84 – 841N6-acetyllysine; alternate By similarity
Modified residuei84 – 841N6-succinyllysine; alternate By similarity
Modified residuei110 – 1101N6-acetyllysine; alternate By similarity
Modified residuei110 – 1101N6-succinyllysine; alternate By similarity
Modified residuei128 – 1281Phosphoserine By similarity
Modified residuei135 – 1351Phosphotyrosine By similarity
Modified residuei162 – 1621N6-acetyllysine; alternate By similarity
Modified residuei162 – 1621N6-succinyllysine; alternate By similarity
Modified residuei171 – 1711N6-acetyllysine By similarity
Modified residuei172 – 1721ADP-ribosylcysteine By similarity
Modified residuei183 – 1831N6-acetyllysine; alternate By similarity
Modified residuei183 – 1831N6-succinyllysine; alternate By similarity
Modified residuei187 – 1871N6-acetyllysine By similarity
Modified residuei191 – 1911N6-acetyllysine; alternate By similarity
Modified residuei191 – 1911N6-succinyllysine; alternate By similarity
Modified residuei200 – 2001N6-succinyllysine By similarity
Modified residuei211 – 2111N6-acetyllysine By similarity
Modified residuei326 – 3261N6-acetyllysine By similarity
Modified residuei346 – 3461N6-acetyllysine; alternate By similarity
Modified residuei346 – 3461N6-succinyllysine; alternate By similarity
Modified residuei363 – 3631N6-acetyllysine; alternate By similarity
Modified residuei363 – 3631N6-succinyllysine; alternate By similarity
Modified residuei365 – 3651N6-acetyllysine; alternate By similarity
Modified residuei365 – 3651N6-succinyllysine; alternate By similarity
Modified residuei386 – 3861N6-acetyllysine By similarity
Modified residuei390 – 3901N6-acetyllysine; alternate By similarity
Modified residuei390 – 3901N6-succinyllysine; alternate By similarity
Modified residuei399 – 3991N6-acetyllysine By similarity
Modified residuei415 – 4151N6-acetyllysine; alternate By similarity
Modified residuei415 – 4151N6-succinyllysine; alternate By similarity
Modified residuei457 – 4571N6-acetyllysine; alternate By similarity
Modified residuei457 – 4571N6-succinyllysine; alternate By similarity
Modified residuei477 – 4771N6-acetyllysine; alternate By similarity
Modified residuei477 – 4771N6-succinyllysine; alternate By similarity
Modified residuei480 – 4801N6-acetyllysine; alternate By similarity
Modified residuei480 – 4801N6-succinyllysine; alternate By similarity
Modified residuei503 – 5031N6-acetyllysine; alternate By similarity
Modified residuei503 – 5031N6-succinyllysine; alternate By similarity
Modified residuei527 – 5271N6-acetyllysine; alternate By similarity
Modified residuei527 – 5271N6-succinyllysine; alternate By similarity
Modified residuei545 – 5451N6-acetyllysine; alternate By similarity
Modified residuei545 – 5451N6-succinyllysine; alternate By similarity
Modified residuei548 – 5481N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

PRIDEiQ64HZ8.

Interactioni

Subunit structurei

Homohexamer By similarity.

Protein-protein interaction databases

STRINGi9598.ENSPTRP00000004733.

Structurei

3D structure databases

ProteinModelPortaliQ64HZ8.
SMRiQ64HZ8. Positions 63-558.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243801.
HOVERGENiHBG005479.
InParanoidiQ64HZ8.
KOiK00261.

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.

Q64HZ8-1 [UniParc]FASTAAdd to Basket

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MYRYLAKALL TSRAGPAALG SAANHSAALL GRGPGQPAAA SQPGLALAAR    50
RHYSELVADR EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN 100
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTENELEK 200
ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY ASTIGHYDIN 250
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR 300
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED 350
FRLQHGSLLG FPKAKPYEGS ILEIDCDILI PAATEKQLTK SNAPRVKAKI 400
IAEGANGPTT PEADKIFLER NILVIPDLYL NAGGVTVSYF EWLKNLNHVS 450
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDSISGA 500
SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV NAIEKVFKVY 550
SEAGVTFT 558
Length:558
Mass (Da):61,439
Last modified:October 25, 2004 - v1
Checksum:i9180BC7CB62C251D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY588274 Genomic DNA. Translation: AAU03136.1.
RefSeqiNP_001009004.1. NM_001009004.1.
UniGeneiPtr.6132.

Genome annotation databases

GeneIDi449581.
KEGGiptr:449581.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY588274 Genomic DNA. Translation: AAU03136.1 .
RefSeqi NP_001009004.1. NM_001009004.1.
UniGenei Ptr.6132.

3D structure databases

ProteinModelPortali Q64HZ8.
SMRi Q64HZ8. Positions 63-558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9598.ENSPTRP00000004733.

Proteomic databases

PRIDEi Q64HZ8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 449581.
KEGGi ptr:449581.

Organism-specific databases

CTDi 2747.

Phylogenomic databases

eggNOGi COG0334.
HOGENOMi HOG000243801.
HOVERGENi HBG005479.
InParanoidi Q64HZ8.
KOi K00261.

Miscellaneous databases

NextBioi 20832694.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006095. 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 ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux."
    Burki F., Kaessmann H.
    Nat. Genet. 36:1061-1063(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDHE4_PANTR
AccessioniPrimary (citable) accession number: Q64HZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 25, 2004
Last modified: March 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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