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Q64HZ8

- DHE4_PANTR

UniProt

Q64HZ8 - DHE4_PANTR

Protein

Glutamate dehydrogenase 2, mitochondrial

Gene

GLUD2

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (25 Oct 2004)
      Previous versions | rss
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    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

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

    GO - Biological processi

    1. cellular amino acid metabolic process Source: InterPro

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    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

    « Hide

    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: October 1, 2014
    This is version 71 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