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P00367

- DHE3_HUMAN

UniProt

P00367 - DHE3_HUMAN

Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei147 – 1471SubstrateBy similarity
    Binding sitei171 – 1711SubstrateBy similarity
    Binding sitei176 – 1761NADBy similarity
    Active sitei183 – 1831
    Binding sitei252 – 2521NADBy similarity
    Binding sitei266 – 2661GTPBy similarity
    Binding sitei270 – 2701GTPBy similarity
    Binding sitei319 – 3191GTPBy similarity
    Binding sitei322 – 3221GTPBy similarity
    Binding sitei438 – 4381SubstrateBy similarity
    Binding sitei444 – 4441NADBy similarity
    Binding sitei450 – 4501ADPBy similarity
    Binding sitei516 – 5161ADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi141 – 1433NADBy similarity

    GO - Molecular functioni

    1. ADP binding Source: BHF-UCL
    2. ATP binding Source: UniProtKB-KW
    3. glutamate dehydrogenase (NAD+) activity Source: UniProtKB
    4. glutamate dehydrogenase [NAD(P)+] activity Source: BHF-UCL
    5. GTP binding Source: BHF-UCL
    6. identical protein binding Source: BHF-UCL
    7. leucine binding Source: BHF-UCL
    8. NAD+ binding Source: BHF-UCL
    9. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular amino acid biosynthetic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. glutamate biosynthetic process Source: BHF-UCL
    4. glutamate catabolic process Source: UniProtKB
    5. glutamine metabolic process Source: UniProtKB
    6. positive regulation of insulin secretion Source: BHF-UCL
    7. small molecule metabolic process Source: Reactome
    8. tricarboxylic acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    ATP-binding, GTP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07548-MONOMER.
    BRENDAi1.4.1.3. 2681.
    ReactomeiREACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP00367.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH 1
    Gene namesi
    Name:GLUD1
    Synonyms:GLUD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:4335. GLUD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Familial hyperinsulinemic hypoglycemia 6 (HHF6) [MIM:606762]: Familial hyperinsulinemic hypoglycemia [MIM:256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti270 – 2701S → C in HHF6; diminished sensitivity to GTP. 1 Publication
    VAR_016760
    Natural varianti274 – 2741R → C in HHF6; diminished sensitivity to GTP. 2 Publications
    Corresponds to variant rs56275071 [ dbSNP | Ensembl ].
    VAR_016761
    Natural varianti318 – 3181R → K in HHF6. 1 Publication
    VAR_009270
    Natural varianti318 – 3181R → T in HHF6; diminished sensitivity to GTP. 1 Publication
    VAR_016762
    Natural varianti319 – 3191Y → C in HHF6. 1 Publication
    VAR_016763
    Natural varianti322 – 3221R → C in HHF6; diminished sensitivity to GTP. 1 Publication
    VAR_016764
    Natural varianti322 – 3221R → H in HHF6; diminished sensitivity to GTP. 2 Publications
    VAR_016765
    Natural varianti349 – 3491E → A in HHF6. 1 Publication
    VAR_009271
    Natural varianti498 – 4981S → L in HHF6. 1 Publication
    VAR_008666
    Natural varianti499 – 4991G → D in HHF6. 1 Publication
    VAR_008667
    Natural varianti499 – 4991G → S in HHF6. 1 Publication
    VAR_008668
    Natural varianti501 – 5011S → P in HHF6. 1 Publication
    VAR_008669
    Natural varianti507 – 5071H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 1 Publication
    VAR_008670

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi501 – 5011S → A: Reduces activity and inhibition by GTP. 1 Publication
    Mutagenesisi507 – 5071H → A: Strongly reduces inhibition by GTP.
    Mutagenesisi516 – 5161R → A: Abolishes activation by ADP. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi606762. phenotype.
    Orphaneti35878. Hyperinsulinism-hyperammonemia syndrome.
    PharmGKBiPA28737.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353Mitochondrion2 PublicationsAdd
    BLAST
    Chaini54 – 558505Glutamate dehydrogenase 1, mitochondrialPRO_0000007206Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681N6-succinyllysineBy similarity
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei84 – 841N6-acetyllysine; alternate1 Publication
    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-ribosylcysteine2 Publications
    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 residuei352 – 3521N6-acetyllysine; alternateBy similarity
    Modified residuei352 – 3521N6-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-malonyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-succinyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-acetyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-succinyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
    Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-acetyllysine; alternate1 Publication
    Modified residuei503 – 5031N6-malonyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-succinyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-acetyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-malonyllysine; 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

    ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity By similarity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein

    Proteomic databases

    MaxQBiP00367.
    PaxDbiP00367.
    PeptideAtlasiP00367.
    PRIDEiP00367.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00016801.
    SWISS-2DPAGEP00367.
    UCD-2DPAGEP00367.

    PTM databases

    PhosphoSiteiP00367.

    Expressioni

    Gene expression databases

    ArrayExpressiP00367.
    BgeeiP00367.
    CleanExiHS_GLUD1.
    GenevestigatoriP00367.

    Organism-specific databases

    HPAiHPA042492.
    HPA044839.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    BioGridi109008. 22 interactions.
    IntActiP00367. 18 interactions.
    MINTiMINT-5005913.
    STRINGi9606.ENSP00000277865.

    Structurei

    Secondary structure

    1
    558
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi66 – 9025
    Helixi91 – 933
    Helixi95 – 973
    Helixi99 – 1024
    Helixi104 – 1096
    Beta strandi113 – 12311
    Beta strandi125 – 1273
    Beta strandi129 – 13810
    Beta strandi142 – 15211
    Helixi158 – 17417
    Beta strandi180 – 1867
    Helixi190 – 1923
    Helixi195 – 21117
    Turni217 – 2193
    Beta strandi220 – 2234
    Helixi230 – 24213
    Turni243 – 2475
    Helixi251 – 2533
    Helixi260 – 2623
    Helixi271 – 28414
    Helixi287 – 2937
    Beta strandi298 – 3003
    Beta strandi303 – 3075
    Helixi311 – 32212
    Beta strandi326 – 3316
    Helixi345 – 35410
    Beta strandi355 – 3584
    Turni371 – 3733
    Beta strandi377 – 3815
    Beta strandi383 – 3864
    Turni390 – 3923
    Helixi393 – 3953
    Beta strandi399 – 4024
    Beta strandi405 – 4073
    Helixi411 – 4199
    Beta strandi423 – 4253
    Helixi427 – 4304
    Helixi433 – 44715
    Turni451 – 4555
    Helixi456 – 47520
    Turni476 – 4794
    Beta strandi481 – 4844
    Helixi491 – 4988
    Helixi502 – 52726
    Helixi534 – 55118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L1FX-ray2.70A/B/C/D/E/F54-558[»]
    1NR1X-ray3.30A/B/C/D/E/F63-558[»]
    ProteinModelPortaliP00367.
    SMRiP00367. Positions 63-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00367.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0334.
    HOGENOMiHOG000243801.
    HOVERGENiHBG005479.
    InParanoidiP00367.
    KOiK00261.
    OMAiTCIGVIE.
    OrthoDBiEOG73NG50.
    PhylomeDBiP00367.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00367-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR    50
    RHYSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN 100
    RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
    RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK 200
    ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN 250
    AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 300
    DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED 350
    FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI 400
    IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS 450
    YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA 500
    SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY 550
    NEAGVTFT 558
    Length:558
    Mass (Da):61,398
    Last modified:January 1, 1990 - v2
    Checksum:iA7319A840F57FBB2
    GO
    Isoform 2 (identifier: P00367-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-167: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:391
    Mass (Da):42,950
    Checksum:i8A493E2898605460
    GO
    Isoform 3 (identifier: P00367-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: MYRYLGEALLLSRAGP → MTCPCDNASSVFLGFC
         17-149: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:425
    Mass (Da):46,575
    Checksum:i2637B3023F58A7C4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti270 – 2701S → C in HHF6; diminished sensitivity to GTP. 1 Publication
    VAR_016760
    Natural varianti274 – 2741R → C in HHF6; diminished sensitivity to GTP. 2 Publications
    Corresponds to variant rs56275071 [ dbSNP | Ensembl ].
    VAR_016761
    Natural varianti318 – 3181R → K in HHF6. 1 Publication
    VAR_009270
    Natural varianti318 – 3181R → T in HHF6; diminished sensitivity to GTP. 1 Publication
    VAR_016762
    Natural varianti319 – 3191Y → C in HHF6. 1 Publication
    VAR_016763
    Natural varianti322 – 3221R → C in HHF6; diminished sensitivity to GTP. 1 Publication
    VAR_016764
    Natural varianti322 – 3221R → H in HHF6; diminished sensitivity to GTP. 2 Publications
    VAR_016765
    Natural varianti349 – 3491E → A in HHF6. 1 Publication
    VAR_009271
    Natural varianti498 – 4981S → L in HHF6. 1 Publication
    VAR_008666
    Natural varianti499 – 4991G → D in HHF6. 1 Publication
    VAR_008667
    Natural varianti499 – 4991G → S in HHF6. 1 Publication
    VAR_008668
    Natural varianti501 – 5011S → P in HHF6. 1 Publication
    VAR_008669
    Natural varianti507 – 5071H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 1 Publication
    VAR_008670

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 167167Missing in isoform 2. 1 PublicationVSP_056244Add
    BLAST
    Alternative sequencei1 – 1616MYRYL…SRAGP → MTCPCDNASSVFLGFC in isoform 3. 1 PublicationVSP_056523Add
    BLAST
    Alternative sequencei17 – 149133Missing in isoform 3. 1 PublicationVSP_056524Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07674 mRNA. Translation: CAA30521.1.
    M20867 mRNA. Translation: AAA52526.1.
    M37154 mRNA. Translation: AAA52525.1.
    X07769 mRNA. Translation: CAA30598.1.
    J03248 mRNA. Translation: AAA52523.1.
    X66300
    , X66301, X66302, X66303, X66304, X66305, X66306, X66307, X66308, X66309, X66311, X66312 Genomic DNA. Translation: CAA46994.2.
    AK122685 mRNA. Translation: BAG53667.1.
    AK294685 mRNA. Translation: BAG57846.1.
    AL136982 Genomic DNA. Translation: CAI17120.1.
    CH471142 Genomic DNA. Translation: EAW80300.1.
    CH471142 Genomic DNA. Translation: EAW80302.1.
    BC040132 mRNA. Translation: AAH40132.1.
    BC112946 mRNA. Translation: AAI12947.1.
    X67491 Genomic DNA. Translation: CAA47830.1.
    CCDSiCCDS7382.1.
    PIRiA28208. DEHUE.
    I37424.
    S29331.
    S60192.
    RefSeqiNP_005262.1. NM_005271.3.
    UniGeneiHs.500409.

    Genome annotation databases

    EnsembliENST00000277865; ENSP00000277865; ENSG00000148672.
    ENST00000537649; ENSP00000439291; ENSG00000148672.
    ENST00000544149; ENSP00000444732; ENSG00000148672.
    GeneIDi2746.
    KEGGihsa:2746.
    UCSCiuc001keg.3. human.

    Polymorphism databases

    DMDMi118541.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Glutamate dehydrogenase 1 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07674 mRNA. Translation: CAA30521.1 .
    M20867 mRNA. Translation: AAA52526.1 .
    M37154 mRNA. Translation: AAA52525.1 .
    X07769 mRNA. Translation: CAA30598.1 .
    J03248 mRNA. Translation: AAA52523.1 .
    X66300
    , X66301 , X66302 , X66303 , X66304 , X66305 , X66306 , X66307 , X66308 , X66309 , X66311 , X66312 Genomic DNA. Translation: CAA46994.2 .
    AK122685 mRNA. Translation: BAG53667.1 .
    AK294685 mRNA. Translation: BAG57846.1 .
    AL136982 Genomic DNA. Translation: CAI17120.1 .
    CH471142 Genomic DNA. Translation: EAW80300.1 .
    CH471142 Genomic DNA. Translation: EAW80302.1 .
    BC040132 mRNA. Translation: AAH40132.1 .
    BC112946 mRNA. Translation: AAI12947.1 .
    X67491 Genomic DNA. Translation: CAA47830.1 .
    CCDSi CCDS7382.1.
    PIRi A28208. DEHUE.
    I37424.
    S29331.
    S60192.
    RefSeqi NP_005262.1. NM_005271.3.
    UniGenei Hs.500409.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L1F X-ray 2.70 A/B/C/D/E/F 54-558 [» ]
    1NR1 X-ray 3.30 A/B/C/D/E/F 63-558 [» ]
    ProteinModelPortali P00367.
    SMRi P00367. Positions 63-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109008. 22 interactions.
    IntActi P00367. 18 interactions.
    MINTi MINT-5005913.
    STRINGi 9606.ENSP00000277865.

    Chemistry

    DrugBanki DB00142. L-Glutamic Acid.
    DB00157. NADH.

    PTM databases

    PhosphoSitei P00367.

    Polymorphism databases

    DMDMi 118541.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00016801.
    SWISS-2DPAGE P00367.
    UCD-2DPAGE P00367.

    Proteomic databases

    MaxQBi P00367.
    PaxDbi P00367.
    PeptideAtlasi P00367.
    PRIDEi P00367.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000277865 ; ENSP00000277865 ; ENSG00000148672 .
    ENST00000537649 ; ENSP00000439291 ; ENSG00000148672 .
    ENST00000544149 ; ENSP00000444732 ; ENSG00000148672 .
    GeneIDi 2746.
    KEGGi hsa:2746.
    UCSCi uc001keg.3. human.

    Organism-specific databases

    CTDi 2746.
    GeneCardsi GC10M088809.
    GeneReviewsi GLUD1.
    HGNCi HGNC:4335. GLUD1.
    HPAi HPA042492.
    HPA044839.
    MIMi 138130. gene.
    606762. phenotype.
    neXtProti NX_P00367.
    Orphaneti 35878. Hyperinsulinism-hyperammonemia syndrome.
    PharmGKBi PA28737.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0334.
    HOGENOMi HOG000243801.
    HOVERGENi HBG005479.
    InParanoidi P00367.
    KOi K00261.
    OMAi TCIGVIE.
    OrthoDBi EOG73NG50.
    PhylomeDBi P00367.
    TreeFami TF313945.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07548-MONOMER.
    BRENDAi 1.4.1.3. 2681.
    Reactomei REACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RK P00367.

    Miscellaneous databases

    EvolutionaryTracei P00367.
    GeneWikii Glutamate_dehydrogenase_1.
    GenomeRNAii 2746.
    NextBioi 10824.
    PROi P00367.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00367.
    Bgeei P00367.
    CleanExi HS_GLUD1.
    Genevestigatori P00367.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain and Liver.
    2. "Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor."
      Amuro N., Yamaura M., Goto Y., Okazaki T.
      Biochem. Biophys. Res. Commun. 152:1395-1400(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Complete nucleotide sequence of human glutamate dehydrogenase cDNA."
      Nakatani Y., Schneider M.E., Banner C., Freese E.
      Nucleic Acids Res. 16:6237-6237(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family."
      Mavrothalassitis G., Tzimagiorgis G., Mitsialis A., Zannis V., Plaitakis A., Papamatheakis J., Moschonas N.
      Proc. Natl. Acad. Sci. U.S.A. 85:3494-3498(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    5. "The human glutamate dehydrogenase gene family: gene organization and structural characterization."
      Michaelidis T.M., Tzimagiorgis G., Moschonas N.K., Papamatheakis J.
      Genomics 16:150-160(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    6. "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] (ISOFORMS 2 AND 3).
      Tissue: Brain and Brain cortex.
    7. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1).
      Tissue: Duodenum and Eye.
    10. "Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme."
      Julliard J.H., Smith E.L.
      J. Biol. Chem. 254:3427-3438(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 54-558.
      Tissue: Liver.
    11. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 54-69.
      Tissue: Liver.
    12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 301-558 (ISOFORM 1).
      Tissue: Brain.
    13. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 481-496, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    14. "Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2."
      Tzimagiorgis G., Leversha M.A., Chroniary K., Goulielmos G., Sargent C.A., Ferguson-Smith M., Moschonas N.K.
      Hum. Genet. 91:433-438(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 540-558.
    15. "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.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-480 AND LYS-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation."
      Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A.
      J. Mol. Biol. 307:707-720(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT TYR-507, ALLOSTERIC REGULATION.
    19. "Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations."
      Fang J., Hsu B.Y.L., MacMullen C.M., Poncz M., Smith T.J., Stanley C.A.
      Biochem. J. 363:81-87(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-501 AND ARG-516, CHARACTERIZATION OF VARIANT TYR-507, ALLOSTERIC REGULATION.
    20. "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells."
      Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., Christodoulou D.C., Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Karow M., Blander G., Wolberger C., Prolla T.A., Weindruch R., Alt F.W., Guarente L.
      Cell 126:941-954(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION.
    21. "The structure of apo human glutamate dehydrogenase details subunit communication and allostery."
      Smith T.J., Schmidt T., Fang J., Wu J., Siuzdak G., Stanley C.A.
      J. Mol. Biol. 318:765-777(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 54-558.
    22. "Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation."
      Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J.
      Biochemistry 42:3446-3456(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 63-558 OF MUTANT ALA-516, ALLOSTERIC REGULATION.
    23. "Congenital hyperinsulinism: molecular basis of a heterogeneous disease."
      Meissner T., Beinbrech B., Mayatepek E.
      Hum. Mutat. 13:351-361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    24. "Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene."
      Stanley C.A., Lieu Y.K., Hsu B.Y.L., Burlina A.B., Greenberg C.R., Hopwood N.J., Perlman K., Rich B.H., Zammarchi E., Poncz M.
      N. Engl. J. Med. 338:1352-1357(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HHF6 LEU-498; SER-499; ASP-499; PRO-501 AND TYR-507.
    25. "Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome."
      Miki Y., Taki T., Ohura T., Kato H., Yanagisawa M., Hayashi Y.
      J. Pediatr. 136:69-72(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HHF6 LYS-318 AND ALA-349.
    26. "Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome."
      Santer R., Kinner M., Passarge M., Superti-Furga A., Mayatepek E., Meissner T., Schneppenheim R., Schaub J.
      Hum. Genet. 108:66-71(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HHF6 CYS-274 AND HIS-322.
    27. "Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase."
      MacMullen C., Fang J., Hsu B.Y.L., Kelly A., de Lonlay-Debeney P., Saudubray J.-M., Ganguly A., Smith T.J., Stanley C.A., Brown R., Buist N., Dasouki M., Fefferman R., Grange D., Karaviti L., Luedke C., Marriage B., McLaughlin J.
      , Perlman K., Seashore M., van Vliet G.
      J. Clin. Endocrinol. Metab. 86:1782-1787(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HHF6 CYS-270; CYS-274; THR-318; CYS-319; CYS-322 AND HIS-322.

    Entry informationi

    Entry nameiDHE3_HUMAN
    AccessioniPrimary (citable) accession number: P00367
    Secondary accession number(s): B3KV55, B4DGN5, Q5TBU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 171 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3