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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei147SubstrateBy similarity1
Binding sitei171SubstrateBy similarity1
Binding sitei176NADBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1831
Binding sitei252NADBy similarity1
Binding sitei266GTPBy similarity1
Binding sitei270GTPBy similarity1
Binding sitei319GTPBy similarity1
Binding sitei322GTPBy similarity1
Binding sitei438SubstrateBy similarity1
Binding sitei444NADBy similarity1
Binding sitei450ADPBy similarity1
Binding sitei516ADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi141 – 143NADBy similarity3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS07548-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.4.1.3 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-70614 Amino acid synthesis and interconversion (transamination)

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P00367

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P00367

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GLUD1
Synonyms:GLUD
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000148672.8

Human Gene Nomenclature Database

More...
HGNCi
HGNC:4335 GLUD1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
138130 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P00367

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Familial hyperinsulinemic hypoglycemia 6 (HHF6)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionFamilial 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.
See also OMIM:606762
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016760270S → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016761274R → C in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs56275071EnsemblClinVar.1
Natural variantiVAR_009270318R → K in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909736EnsemblClinVar.1
Natural variantiVAR_016762318R → T in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016763319Y → C in HHF6. 1 Publication1
Natural variantiVAR_016764322R → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016765322R → H in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs121909737EnsemblClinVar.1
Natural variantiVAR_009271349E → A in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909735EnsemblClinVar.1
Natural variantiVAR_008666498S → L in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909731EnsemblClinVar.1
Natural variantiVAR_008667499G → D in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909734EnsemblClinVar.1
Natural variantiVAR_008668499G → S in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909733EnsemblClinVar.1
Natural variantiVAR_008669501S → P in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909732EnsemblClinVar.1
Natural variantiVAR_008670507H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 3 PublicationsCorresponds to variant dbSNP:rs121909730EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi501S → A: Reduces activity and inhibition by GTP. 1 Publication1
Mutagenesisi507H → A: Strongly reduces inhibition by GTP. 1
Mutagenesisi516R → A: Abolishes activation by ADP. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2746

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
GLUD1

MalaCards human disease database

More...
MalaCardsi
GLUD1
MIMi606762 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000148672

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
35878 Hyperinsulinism-hyperammonemia syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28737

Chemistry databases

Drug and drug target database

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DrugBanki
DB04137 Guanosine-5'-Triphosphate
DB00756 Hexachlorophene
DB00142 L-Glutamic Acid
DB00157 NADH

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
GLUD1

Domain mapping of disease mutations (DMDM)

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DMDMi
118541

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 53MitochondrionCombined sources2 PublicationsAdd BLAST53
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000720654 – 558Glutamate dehydrogenase 1, mitochondrialAdd BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei68N6-succinyllysineBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei84N6-acetyllysine; alternateCombined sources1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei110N6-acetyllysine; alternateBy similarity1
Modified residuei110N6-succinyllysine; alternateBy similarity1
Modified residuei128PhosphoserineBy similarity1
Modified residuei135PhosphotyrosineBy similarity1
Modified residuei162N6-acetyllysine; alternateBy similarity1
Modified residuei162N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei172ADP-ribosylcysteine1 Publication1
Modified residuei183N6-acetyllysine; alternateBy similarity1
Modified residuei183N6-succinyllysine; alternateBy similarity1
Modified residuei187N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei200N6-succinyllysineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1
Modified residuei227PhosphoserineCombined sources1
Modified residuei326N6-acetyllysineBy similarity1
Modified residuei346N6-acetyllysine; alternateBy similarity1
Modified residuei346N6-succinyllysine; alternateBy similarity1
Modified residuei352N6-acetyllysine; alternateBy similarity1
Modified residuei352N6-succinyllysine; alternateBy similarity1
Modified residuei363N6-acetyllysine; alternateBy similarity1
Modified residuei363N6-succinyllysine; alternateBy similarity1
Modified residuei365N6-acetyllysine; alternateBy similarity1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei384PhosphoserineCombined sources1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei390N6-acetyllysine; alternateBy similarity1
Modified residuei390N6-succinyllysine; alternateBy similarity1
Modified residuei399N6-acetyllysineBy similarity1
Modified residuei410PhosphothreonineBy similarity1
Modified residuei415N6-acetyllysine; alternateBy similarity1
Modified residuei415N6-succinyllysine; alternateBy similarity1
Modified residuei457N6-acetyllysine; alternateBy similarity1
Modified residuei457N6-malonyllysine; alternateBy similarity1
Modified residuei457N6-succinyllysine; alternateBy similarity1
Modified residuei477N6-acetyllysine; alternateBy similarity1
Modified residuei477N6-succinyllysine; alternateBy similarity1
Modified residuei480N6-acetyllysine; alternateCombined sources1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei503N6-acetyllysine; alternateCombined sources1
Modified residuei503N6-malonyllysine; alternateBy similarity1
Modified residuei503N6-succinyllysine; alternateBy similarity1
Modified residuei512PhosphotyrosineCombined sources1
Modified residuei527N6-acetyllysine; alternateBy similarity1
Modified residuei527N6-malonyllysine; alternateBy similarity1
Modified residuei527N6-succinyllysine; alternateBy similarity1
Modified residuei545N6-acetyllysine; alternateBy similarity1
Modified residuei545N6-succinyllysine; alternateBy similarity1
Modified residuei548N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P00367

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00367

MaxQB - The MaxQuant DataBase

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MaxQBi
P00367

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P00367

PeptideAtlas

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PeptideAtlasi
P00367

PRoteomics IDEntifications database

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PRIDEi
P00367

ProteomicsDB human proteome resource

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ProteomicsDBi
51236

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00016801

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P00367

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P00367

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00367

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P00367

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P00367

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000148672 Expressed in 228 organ(s), highest expression level in hypothalamus

CleanEx database of gene expression profiles

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CleanExi
HS_GLUD1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00367 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P00367 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA042492
HPA044839
HPA061369

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109008, 52 interactors

Protein interaction database and analysis system

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IntActi
P00367, 44 interactors

Molecular INTeraction database

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MINTi
P00367

STRING: functional protein association networks

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STRINGi
9606.ENSP00000277865

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L1FX-ray2.70A/B/C/D/E/F54-558[»]
1NR1X-ray3.30A/B/C/D/E/F63-558[»]
6DQGX-ray2.70A/B/C/D/E/F63-558[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00367

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P00367

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00367

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2250 Eukaryota
COG0334 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000000854

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000243801

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005479

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00367

KEGG Orthology (KO)

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KOi
K00261

Identification of Orthologs from Complete Genome Data

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OMAi
PCFAAFP

Database of Orthologous Groups

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OrthoDBi
692851at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P00367

TreeFam database of animal gene trees

More...
TreeFami
TF313945

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01076 NAD_bind_1_Glu_DH, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006095 Glu/Leu/Phe/Val_DH
IPR033524 Glu/Leu/Phe/Val_DH_AS
IPR006096 Glu/Leu/Phe/Val_DH_C
IPR006097 Glu/Leu/Phe/Val_DH_dimer_dom
IPR036291 NAD(P)-bd_dom_sf
IPR033922 NAD_bind_Glu_DH

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00208 ELFV_dehydrog, 1 hit
PF02812 ELFV_dehydrog_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00082 GLFDHDRGNASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00839 ELFV_dehydrog, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00074 GLFV_DEHYDROGENASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
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.

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MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR
60 70 80 90 100
RHYSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY

NEAGVTFT
Length:558
Mass (Da):61,398
Last modified:January 1, 1990 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_016760270S → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016761274R → C in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs56275071EnsemblClinVar.1
Natural variantiVAR_009270318R → K in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909736EnsemblClinVar.1
Natural variantiVAR_016762318R → T in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016763319Y → C in HHF6. 1 Publication1
Natural variantiVAR_016764322R → C in HHF6; diminished sensitivity to GTP. 1 Publication1
Natural variantiVAR_016765322R → H in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs121909737EnsemblClinVar.1
Natural variantiVAR_009271349E → A in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909735EnsemblClinVar.1
Natural variantiVAR_008666498S → L in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909731EnsemblClinVar.1
Natural variantiVAR_008667499G → D in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909734EnsemblClinVar.1
Natural variantiVAR_008668499G → S in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909733EnsemblClinVar.1
Natural variantiVAR_008669501S → P in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909732EnsemblClinVar.1
Natural variantiVAR_008670507H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 3 PublicationsCorresponds to variant dbSNP:rs121909730EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0562441 – 167Missing in isoform 2. 1 PublicationAdd BLAST167
Alternative sequenceiVSP_0565231 – 16MYRYL…SRAGP → MTCPCDNASSVFLGFC in isoform 3. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_05652417 – 149Missing in isoform 3. 1 PublicationAdd BLAST133

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7382.1 [P00367-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A28208 DEHUE
I37424
S29331
S60192

NCBI Reference Sequences

More...
RefSeqi
NP_001305829.1, NM_001318900.1 [P00367-3]
NP_001305830.1, NM_001318901.1 [P00367-2]
NP_001305831.1, NM_001318902.1 [P00367-2]
NP_001305833.1, NM_001318904.1 [P00367-2]
NP_001305834.1, NM_001318905.1 [P00367-2]
NP_001305835.1, NM_001318906.1 [P00367-2]
NP_005262.1, NM_005271.4 [P00367-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.500409
Hs.731740

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000277865; ENSP00000277865; ENSG00000148672 [P00367-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2746

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2746

UCSC genome browser

More...
UCSCi
uc001keh.4 human [P00367-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Glutamate dehydrogenase 1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 [P00367-1]
PIRiA28208 DEHUE
I37424
S29331
S60192
RefSeqiNP_001305829.1, NM_001318900.1 [P00367-3]
NP_001305830.1, NM_001318901.1 [P00367-2]
NP_001305831.1, NM_001318902.1 [P00367-2]
NP_001305833.1, NM_001318904.1 [P00367-2]
NP_001305834.1, NM_001318905.1 [P00367-2]
NP_001305835.1, NM_001318906.1 [P00367-2]
NP_005262.1, NM_005271.4 [P00367-1]
UniGeneiHs.500409
Hs.731740

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L1FX-ray2.70A/B/C/D/E/F54-558[»]
1NR1X-ray3.30A/B/C/D/E/F63-558[»]
6DQGX-ray2.70A/B/C/D/E/F63-558[»]
ProteinModelPortaliP00367
SMRiP00367
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109008, 52 interactors
IntActiP00367, 44 interactors
MINTiP00367
STRINGi9606.ENSP00000277865

Chemistry databases

DrugBankiDB04137 Guanosine-5'-Triphosphate
DB00756 Hexachlorophene
DB00142 L-Glutamic Acid
DB00157 NADH

PTM databases

iPTMnetiP00367
PhosphoSitePlusiP00367
SwissPalmiP00367

Polymorphism and mutation databases

BioMutaiGLUD1
DMDMi118541

2D gel databases

REPRODUCTION-2DPAGEiIPI00016801
SWISS-2DPAGEiP00367
UCD-2DPAGEiP00367

Proteomic databases

EPDiP00367
jPOSTiP00367
MaxQBiP00367
PaxDbiP00367
PeptideAtlasiP00367
PRIDEiP00367
ProteomicsDBi51236

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000277865; ENSP00000277865; ENSG00000148672 [P00367-1]
GeneIDi2746
KEGGihsa:2746
UCSCiuc001keh.4 human [P00367-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2746
DisGeNETi2746
EuPathDBiHostDB:ENSG00000148672.8

GeneCards: human genes, protein and diseases

More...
GeneCardsi
GLUD1
GeneReviewsiGLUD1
HGNCiHGNC:4335 GLUD1
HPAiHPA042492
HPA044839
HPA061369
MalaCardsiGLUD1
MIMi138130 gene
606762 phenotype
neXtProtiNX_P00367
OpenTargetsiENSG00000148672
Orphaneti35878 Hyperinsulinism-hyperammonemia syndrome
PharmGKBiPA28737

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2250 Eukaryota
COG0334 LUCA
GeneTreeiENSGT00390000000854
HOGENOMiHOG000243801
HOVERGENiHBG005479
InParanoidiP00367
KOiK00261
OMAiPCFAAFP
OrthoDBi692851at2759
PhylomeDBiP00367
TreeFamiTF313945

Enzyme and pathway databases

BioCyciMetaCyc:HS07548-MONOMER
BRENDAi1.4.1.3 2681
ReactomeiR-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-70614 Amino acid synthesis and interconversion (transamination)
SABIO-RKiP00367
SIGNORiP00367

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
GLUD1 human
EvolutionaryTraceiP00367

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Glutamate_dehydrogenase_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2746

Protein Ontology

More...
PROi
PR:P00367

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000148672 Expressed in 228 organ(s), highest expression level in hypothalamus
CleanExiHS_GLUD1
ExpressionAtlasiP00367 baseline and differential
GenevisibleiP00367 HS

Family and domain databases

CDDicd01076 NAD_bind_1_Glu_DH, 1 hit
InterProiView protein in InterPro
IPR006095 Glu/Leu/Phe/Val_DH
IPR033524 Glu/Leu/Phe/Val_DH_AS
IPR006096 Glu/Leu/Phe/Val_DH_C
IPR006097 Glu/Leu/Phe/Val_DH_dimer_dom
IPR036291 NAD(P)-bd_dom_sf
IPR033922 NAD_bind_Glu_DH
PfamiView protein in Pfam
PF00208 ELFV_dehydrog, 1 hit
PF02812 ELFV_dehydrog_N, 1 hit
PRINTSiPR00082 GLFDHDRGNASE
SMARTiView protein in SMART
SM00839 ELFV_dehydrog, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00074 GLFV_DEHYDROGENASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDHE3_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00367
Secondary accession number(s): B3KV55, B4DGN5, Q5TBU3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: January 16, 2019
This is version 213 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
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