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UniProtKB - P10860 (DHE3_RAT)

Entry version 171 (11 Dec 2019)
Sequence version 2 (04 Apr 2006)
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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

Organism
Rattus norvegicus (Rat)
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 (By similarity). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.By similarity1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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 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 <a href="http://www.uniprot.org/help/function_section">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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 5301

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P10860

<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
Alternative name(s):
Memory-related gene 2 protein
Short name:
MRG-2
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 16

Organism-specific databases

Rat genome database

More...RGDi		2708 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2176833

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000721354 – 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 residuei79PhosphoserineCombined sources1
Modified residuei84N6-acetyllysine; alternateBy similarity1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei90N6-acetyllysineBy similarity1
Modified residuei110N6-acetyllysine; alternateBy similarity1
Modified residuei110N6-succinyllysine; alternateBy similarity1
Modified residuei128PhosphoserineCombined sources1
Modified residuei135PhosphotyrosineBy similarity1
Modified residuei162N6-acetyllysine; alternateBy similarity1
Modified residuei162N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei172ADP-ribosylcysteineBy similarity1
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 residuei227PhosphoserineBy similarity1
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 residuei384PhosphoserineBy similarity1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei390N6-acetyllysine; alternateBy similarity1
Modified residuei390N6-succinyllysine; alternateBy similarity1
Modified residuei399N6-acetyllysineBy similarity1
Modified residuei410PhosphothreonineCombined sources1
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; alternateBy similarity1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei503N6-acetyllysine; alternateBy similarity1
Modified residuei503N6-malonyllysine; alternateBy similarity1
Modified residuei503N6-succinyllysine; alternateBy similarity1
Modified residuei512PhosphotyrosineBy similarity1
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. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer (By similarity).By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P10860

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

More...PaxDbi		P10860

PRoteomics IDEntifications database

More...PRIDEi		P10860

2D gel databases

The World-2DPAGE database

More...World-2DPAGEi		0004:P10860

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P10860

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P10860

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

More...PhosphoSitePlusi		P10860

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed throughout the hippocampus. After induction by training, highly expressed in the dentate gyrus, pyrimidal layer and lacunosum moleculare.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By water maze training in the hippocampus and in other regions of the brain including the laterodorsal nucleus of the thalamus and the cingulate cortex.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000057367 Expressed in 10 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P10860 RN

<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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		246566, 2 interactors

Protein interaction database and analysis system

More...IntActi		P10860, 6 interactors

Molecular INTeraction database

More...MINTi		P10860

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000013789

<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		P10860

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

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2250 Eukaryota
COG0334 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000000854

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000243801

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P10860

KEGG Orthology (KO)

More...KOi		K00261

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		P10860

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_length">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>Sequencei

<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.

P10860-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYRRLGEVLL LSRAGPAALG SAAADSAALL GWARGQPSAV PQPGLTPVAR 
        60         70         80         90        100
RHYSEAATDR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRENEEQKRN 
       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 SILGMTPGLG 
       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):61,416
Last modified:April 4, 2006 - 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:i388B8B5490C10F31
GO

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 conflicti56 – 57AA → GP in CAA32441 (PubMed:2704625).Curated2

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
X14223 mRNA Translation: CAA32441.1
X14044 mRNA Translation: CAA32202.1
BC081841 mRNA Translation: AAH81841.1
X64365 Genomic DNA Translation: CAA45717.1
U95148 mRNA Translation: AAB70012.1

Protein sequence database of the Protein Information Resource

More...PIRi		S03707

NCBI Reference Sequences

More...RefSeqi		NP_036702.1, NM_012570.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000083446; ENSRNOP00000075032; ENSRNOG00000057367

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24399

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24399

UCSC genome browser

More...UCSCi		RGD:2708 rat

<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
X14223 mRNA Translation: CAA32441.1
X14044 mRNA Translation: CAA32202.1
BC081841 mRNA Translation: AAH81841.1
X64365 Genomic DNA Translation: CAA45717.1
U95148 mRNA Translation: AAB70012.1
PIRiS03707
RefSeqiNP_036702.1, NM_012570.2

3D structure databases

SMRiP10860
ModBaseiSearch...

Protein-protein interaction databases

BioGridi246566, 2 interactors
IntActiP10860, 6 interactors
MINTiP10860
STRINGi10116.ENSRNOP00000013789

Chemistry databases

ChEMBLiCHEMBL2176833

PTM databases

CarbonylDBiP10860
iPTMnetiP10860
PhosphoSitePlusiP10860

2D gel databases

World-2DPAGEi0004:P10860

Proteomic databases

jPOSTiP10860
PaxDbiP10860
PRIDEiP10860

Genome annotation databases

EnsembliENSRNOT00000083446; ENSRNOP00000075032; ENSRNOG00000057367
GeneIDi24399
KEGGirno:24399
UCSCiRGD:2708 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2746
RGDi2708 Glud1

Phylogenomic databases

eggNOGiKOG2250 Eukaryota
COG0334 LUCA
GeneTreeiENSGT00390000000854
HOGENOMiHOG000243801
InParanoidiP10860
KOiK00261
OMAiPCFAAFP
OrthoDBi692851at2759
PhylomeDBiP10860
TreeFamiTF313945

Enzyme and pathway databases

BRENDAi1.4.1.3 5301
ReactomeiR-RNO-2151201 Transcriptional activation of mitochondrial biogenesis
R-RNO-8964539 Glutamate and glutamine metabolism
SABIO-RKiP10860

Miscellaneous databases

Protein Ontology

More...PROi		PR:P10860

Gene expression databases

BgeeiENSRNOG00000057367 Expressed in 10 organ(s), highest expression level in liver
GenevisibleiP10860 RN

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...

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_RAT
<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: P10860
Secondary accession number(s): Q66HI8, Q6LC16
<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 1, 1989
Last sequence update: April 4, 2006
Last modified: December 11, 2019
This is version 171 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

<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. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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