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Entry version 181 (02 Jun 2021)
Sequence version 1 (01 Aug 1992)
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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

Organism
Mus musculus (Mouse)
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 (PubMed:20670938).

Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (By similarity).

Plays a role in insulin homeostasis (PubMed:16959573).

May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).

By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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. Inhibited by SIRT4 (By similarity). Inhibited by HADH (PubMed:20670938).By similarity1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=107 µM for 2-oxoglutarate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei183PROSITE-ProRule annotation1
    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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

    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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.4.1.3, 3474

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-MMU-2151201, Transcriptional activation of mitochondrial biogenesis
    R-MMU-8964539, Glutamate and glutamine metabolism

    <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%5Fand%5Ftaxonomy%5Fsection">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:1.4.1.31 Publication)
    Short name:
    GDH 1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 14

    Organism-specific databases

    Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

    More...
    MGIi
    MGI:95753, Glud1

    <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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Mitochondrion

    <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 – 53MitochondrionBy similarityAdd BLAST53
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000721254 – 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-succinyllysineCombined sources1
    Modified residuei79PhosphoserineCombined sources1
    Modified residuei84N6-acetyllysine; alternateCombined sources1
    Modified residuei84N6-succinyllysine; alternateCombined sources1
    Modified residuei90N6-acetyllysineCombined sources1
    Modified residuei110N6-acetyllysine; alternateCombined sources1
    Modified residuei110N6-succinyllysine; alternateBy similarity1
    Modified residuei128PhosphoserineCombined sources1
    Modified residuei135PhosphotyrosineCombined sources1
    Modified residuei162N6-acetyllysine; alternateCombined sources1
    Modified residuei162N6-succinyllysine; alternateCombined sources1
    Modified residuei171N6-acetyllysineCombined sources1
    Modified residuei172ADP-ribosylcysteineBy similarity1
    Modified residuei183N6-acetyllysine; alternateBy similarity1
    Modified residuei183N6-succinyllysine; alternateCombined sources1
    Modified residuei187N6-acetyllysineCombined sources1
    Modified residuei191N6-acetyllysine; alternateCombined sources1
    Modified residuei191N6-succinyllysine; alternateCombined sources1
    Modified residuei200N6-succinyllysineCombined sources1
    Modified residuei211N6-acetyllysineCombined sources1
    Modified residuei227PhosphoserineBy similarity1
    Modified residuei326N6-acetyllysineCombined sources1
    Modified residuei346N6-acetyllysine; alternateCombined sources1
    Modified residuei346N6-succinyllysine; alternateCombined sources1
    Modified residuei352N6-acetyllysine; alternateCombined sources1
    Modified residuei352N6-succinyllysine; alternateCombined sources1
    Modified residuei363N6-acetyllysine; alternateCombined sources1
    Modified residuei363N6-succinyllysine; alternateCombined sources1
    Modified residuei365N6-acetyllysine; alternateCombined sources1
    Modified residuei365N6-succinyllysine; alternateCombined sources1
    Modified residuei384PhosphoserineBy similarity1
    Modified residuei386N6-acetyllysineBy similarity1
    Modified residuei390N6-acetyllysine; alternateCombined sources1
    Modified residuei390N6-succinyllysine; alternateCombined sources1
    Modified residuei399N6-acetyllysineCombined sources1
    Modified residuei410PhosphothreonineBy similarity1
    Modified residuei415N6-acetyllysine; alternateCombined sources1
    Modified residuei415N6-succinyllysine; alternateBy similarity1
    Modified residuei457N6-acetyllysine; alternateCombined sources1
    Modified residuei457N6-malonyllysine; alternateBy similarity1
    Modified residuei457N6-succinyllysine; alternateBy similarity1
    Modified residuei477N6-acetyllysine; alternateCombined sources1
    Modified residuei477N6-succinyllysine; alternateCombined sources1
    Modified residuei480N6-acetyllysine; alternateCombined sources1
    Modified residuei480N6-succinyllysine; alternateCombined sources1
    Modified residuei503N6-acetyllysine; alternateCombined sources1
    Modified residuei503N6-malonyllysine; alternateBy similarity1
    Modified residuei503N6-succinyllysine; alternateCombined sources1
    Modified residuei512PhosphotyrosineBy similarity1
    Modified residuei527N6-acetyllysine; alternateCombined sources1
    Modified residuei527N6-malonyllysine; alternateBy similarity1
    Modified residuei527N6-succinyllysine; alternateCombined sources1
    Modified residuei545N6-acetyllysine; alternateCombined sources1
    Modified residuei545N6-succinyllysine; alternateCombined sources1
    Modified residuei548N6-acetyllysineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

    Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.
    ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity (PubMed:16959573). Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer (By similarity).By similarity1 Publication

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    non-CPTAC-3785

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P26443

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P26443

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P26443

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

    More...
    PaxDbi
    P26443

    PeptideAtlas

    More...
    PeptideAtlasi
    P26443

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P26443

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    277333

    2D gel databases

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    P26443

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

    More...
    SWISS-2DPAGEi
    P26443

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    P26443

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P26443

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

    More...
    PhosphoSitePlusi
    P26443

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P26443

    <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

    More...
    Bgeei
    ENSMUSG00000021794, Expressed in liver and 339 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P26443, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P26443, MM

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homohexamer (By similarity).

    Interacts with HADH; this interaction inhibits the activation of GLUD1 (PubMed:20670938).

    By similarity1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    199956, 10 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P26443, 14 interactors

    Molecular INTeraction database

    More...
    MINTi
    P26443

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000022322

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P26443, protein

    <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

    3D structure databases

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

    More...
    SMRi
    P26443

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000000854

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_025763_1_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P26443

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    PCFAAFP

    Database of Orthologous Groups

    More...
    OrthoDBi
    692851at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P26443

    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

    More...
    PRINTSi
    PR00082, GLFDHDRGNASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00839, ELFV_dehydrog, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735, SSF51735, 1 hit

    PROSITE; a protein domain and family database

    More...
    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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    P26443-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR
    60 70 80 90 100
    RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK 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 HRFGAKCVGV GESDGSIWNP DGIDPKELED
    360 370 380 390 400
    FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI
    410 420 430 440 450
    IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS
    460 470 480 490 500
    YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA
    510 520 530 540 550
    SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY

    NEAGVTFT
    Length:558
    Mass (Da):61,337
    Last modified:August 1, 1992 - v1
    <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:i92738AA5A133838A
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    F7CFA5F7CFA5_MOUSE
    Glutamate dehydrogenase 1, mitochon...
    Glud1
    144Annotation score:

    Annotation score:1 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 Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti495D → G in BAC40767 (PubMed:16141072).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X57024 mRNA Translation: CAA40341.1
    AK089152 mRNA Translation: BAC40767.1
    BC052724 mRNA Translation: AAH52724.1
    BC057347 mRNA Translation: AAH57347.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS26935.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S16239

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_032159.1, NM_008133.4

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    14661

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:14661

    UCSC genome browser

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    UCSCi
    uc007tas.2, mouse

    <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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X57024 mRNA Translation: CAA40341.1
    AK089152 mRNA Translation: BAC40767.1
    BC052724 mRNA Translation: AAH52724.1
    BC057347 mRNA Translation: AAH57347.1
    CCDSiCCDS26935.1
    PIRiS16239
    RefSeqiNP_032159.1, NM_008133.4

    3D structure databases

    SMRiP26443
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi199956, 10 interactors
    IntActiP26443, 14 interactors
    MINTiP26443
    STRINGi10090.ENSMUSP00000022322

    PTM databases

    iPTMnetiP26443
    PhosphoSitePlusiP26443
    SwissPalmiP26443

    2D gel databases

    REPRODUCTION-2DPAGEiP26443
    SWISS-2DPAGEiP26443
    UCD-2DPAGEiP26443

    Proteomic databases

    CPTACinon-CPTAC-3785
    EPDiP26443
    jPOSTiP26443
    MaxQBiP26443
    PaxDbiP26443
    PeptideAtlasiP26443
    PRIDEiP26443
    ProteomicsDBi277333

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    14661

    Genome annotation databases

    EnsembliENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794
    GeneIDi14661
    KEGGimmu:14661
    UCSCiuc007tas.2, mouse

    Organism-specific databases

    Comparative Toxicogenomics Database

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    CTDi
    2746
    MGIiMGI:95753, Glud1

    Phylogenomic databases

    eggNOGiKOG2250, Eukaryota
    GeneTreeiENSGT00390000000854
    HOGENOMiCLU_025763_1_0_1
    InParanoidiP26443
    OMAiPCFAAFP
    OrthoDBi692851at2759
    PhylomeDBiP26443
    TreeFamiTF313945

    Enzyme and pathway databases

    BRENDAi1.4.1.3, 3474
    ReactomeiR-MMU-2151201, Transcriptional activation of mitochondrial biogenesis
    R-MMU-8964539, Glutamate and glutamine metabolism

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

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    BioGRID-ORCSi
    14661, 0 hits in 52 CRISPR screens

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

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    ChiTaRSi
    Glud1, mouse

    Protein Ontology

    More...
    PROi
    PR:P26443
    RNActiP26443, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000021794, Expressed in liver and 339 other tissues
    ExpressionAtlasiP26443, baseline and differential
    GenevisibleiP26443, MM

    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

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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_MOUSE
    <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: P26443
    Secondary accession number(s): Q8C273
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: June 2, 2021
    This is version 181 of the entry and version 1 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

    <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

    Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families
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