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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

Dld

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

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).By similarity1 Publication

Miscellaneous

The active site is a redox-active disulfide bond.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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

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 sitei89FADBy similarity1
Binding sitei154FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei243NADBy similarity1
Binding sitei278NAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei314NAD; via amide nitrogenBy similarity1
Binding sitei355FADBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei448Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy similarity1
Sitei473Important for interaction with PDHX and activity of pyruvate dehydrogenase complexBy 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 sitei487Proton acceptorBy 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 bindingi71 – 80FADBy similarity10
Nucleotide bindingi183 – 185FADBy similarity3
Nucleotide bindingi220 – 227NADBy similarity8
Nucleotide bindingi361 – 364FADBy similarity4

<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
LigandFAD, Flavoprotein, NAD

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-MMU-389661 Glyoxylate metabolism and glycine degradation
R-MMU-5362517 Signaling by Retinoic Acid
R-MMU-6783984 Glycine degradation
R-MMU-70268 Pyruvate metabolism
R-MMU-70895 Branched-chain amino acid catabolism
R-MMU-71064 Lysine catabolism
R-MMU-71403 Citric acid cycle (TCA cycle)

<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:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4By similarity)
Alternative name(s):
Dihydrolipoamide dehydrogenase
<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:Dld
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 12

Organism-specific databases

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

More...
MGIi
MGI:107450 Dld

<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

Cell projection, Cilium, Cytoplasmic vesicle, Flagellum, Mitochondrion, Nucleus

<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
CHEMBL2176826

<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 – 35MitochondrionBy similarityAdd BLAST35
<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_000003029736 – 509Dihydrolipoyl dehydrogenase, mitochondrialAdd BLAST474

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 residuei66N6-acetyllysine; alternateCombined sources1
Modified residuei66N6-succinyllysine; alternateCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi80 ↔ 85Redox-activeBy similarity
Modified residuei104N6-acetyllysine; alternateCombined sources1
Modified residuei104N6-succinyllysine; alternateCombined sources1
Modified residuei122N6-acetyllysine; alternateCombined sources1
Modified residuei122N6-succinyllysine; alternateCombined sources1
Modified residuei132N6-acetyllysine; alternateCombined sources1
Modified residuei132N6-succinyllysine; alternateCombined sources1
Modified residuei143N6-acetyllysine; alternateCombined sources1
Modified residuei143N6-succinyllysine; alternateCombined sources1
Modified residuei159N6-succinyllysineCombined sources1
Modified residuei166N6-succinyllysineCombined sources1
Modified residuei273N6-succinyllysineCombined sources1
Modified residuei277N6-succinyllysineCombined sources1
Modified residuei285PhosphoserineCombined sources1
Modified residuei297PhosphoserineBy similarity1
Modified residuei334N6-acetyllysine; alternateCombined sources1
Modified residuei334N6-succinyllysine; alternateCombined sources1
Modified residuei346N6-acetyllysineCombined sources1
Modified residuei410N6-acetyllysine; alternateCombined sources1
Modified residuei410N6-succinyllysine; alternateCombined sources1
Modified residuei417N6-acetyllysineBy similarity1
Modified residuei420N6-acetyllysineCombined sources1
Modified residuei430N6-succinyllysineCombined sources1
Modified residuei505N6-acetyllysine; alternateCombined sources1
Modified residuei505N6-succinyllysine; alternateCombined sources1

<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

Tyrosine phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O08749

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O08749

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O08749

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

More...
PaxDbi
O08749

PeptideAtlas

More...
PeptideAtlasi
O08749

PRoteomics IDEntifications database

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PRIDEi
O08749

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
O08749

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

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SWISS-2DPAGEi
O08749

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O08749

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

More...
PhosphoSitePlusi
O08749

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O08749

<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

Expressed in liver (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000020664 Expressed in 330 organ(s), highest expression level in brown adipose tissue

CleanEx database of gene expression profiles

More...
CleanExi
MM_DLD

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O08749 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_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

Homodimer. Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDHA (PDHA1 or PDHA2) and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds). The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A. Interacts with PDHX.By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
NfkbieO549104EBI-773199,EBI-6688774

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199227, 6 interactors

Protein interaction database and analysis system

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IntActi
O08749, 36 interactors

Molecular INTeraction database

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MINTi
O08749

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000106481

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O08749

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

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SMRi
O08749

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...

<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

Redox-active center, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1335 Eukaryota
COG1249 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00550000074844

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000276708

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG002290

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O08749

KEGG Orthology (KO)

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KOi
K00382

Identification of Orthologs from Complete Genome Data

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OMAi
TMSEAVM

Database of Orthologous Groups

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OrthoDBi
581771at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O08749

TreeFam database of animal gene trees

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TreeFami
TF300414

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.390.30, 1 hit
3.50.50.60, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006258 Lipoamide_DH
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000350 Mercury_reductase_MerA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01350 lipoamide_DH, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 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>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.

O08749-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG
60 70 80 90 100
PGGYVAAIKS AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM
110 120 130 140 150
AHGKDFASRG IEIPEVRLNL EKMMEQKHSA VKALTGGIAH LFKQNKVVHV
160 170 180 190 200
NGFGKITGKN QVTATKADGS TQVIDTKNIL VATGSEVTPF PGITIDEDTI
210 220 230 240 250
VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT AVEFLGHVGG
260 270 280 290 300
IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK
310 320 330 340 350
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI
360 370 380 390 400
YAIGDVVAGP MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA
410 420 430 440 450
WVGKSEEQLK EEGIEFKIGK FPFAANSRAK TNADTDGMVK ILGHKSTDRV
460 470 480 490 500
LGAHILGPGA GEMVNEAALA LEYGASCEDI ARVCHAHPTL SEAFREANLA

AAFGKPINF
Length:509
Mass (Da):54,272
Last modified:November 28, 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:i2C381852BAAD0441
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 conflicti54Y → C in AAC53170 (PubMed:9169128).Curated1
Sequence conflicti144Q → T in BAE22867 (PubMed:16141072).Curated1
Sequence conflicti149H → L in BAE31961 (PubMed:16141072).Curated1
Sequence conflicti283K → E in BAE40693 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U73445 mRNA Translation: AAC53170.1
AK117104 mRNA Translation: BAE43405.1
AK136193 mRNA Translation: BAE22867.1
AK153399 mRNA Translation: BAE31961.1
AK168875 mRNA Translation: BAE40693.1
BC003368 mRNA Translation: AAH03368.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS36428.1

NCBI Reference Sequences

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RefSeqi
NP_031887.2, NM_007861.5

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.3131
Mm.471230

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664

Database of genes from NCBI RefSeq genomes

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GeneIDi
13382

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13382

UCSC genome browser

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UCSCi
uc007nhg.3 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
U73445 mRNA Translation: AAC53170.1
AK117104 mRNA Translation: BAE43405.1
AK136193 mRNA Translation: BAE22867.1
AK153399 mRNA Translation: BAE31961.1
AK168875 mRNA Translation: BAE40693.1
BC003368 mRNA Translation: AAH03368.1
CCDSiCCDS36428.1
RefSeqiNP_031887.2, NM_007861.5
UniGeneiMm.3131
Mm.471230

3D structure databases

ProteinModelPortaliO08749
SMRiO08749
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199227, 6 interactors
IntActiO08749, 36 interactors
MINTiO08749
STRINGi10090.ENSMUSP00000106481

Chemistry databases

ChEMBLiCHEMBL2176826

PTM databases

iPTMnetiO08749
PhosphoSitePlusiO08749
SwissPalmiO08749

2D gel databases

REPRODUCTION-2DPAGEiO08749
SWISS-2DPAGEiO08749

Proteomic databases

EPDiO08749
jPOSTiO08749
MaxQBiO08749
PaxDbiO08749
PeptideAtlasiO08749
PRIDEiO08749

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664
GeneIDi13382
KEGGimmu:13382
UCSCiuc007nhg.3 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1738
MGIiMGI:107450 Dld

Phylogenomic databases

eggNOGiKOG1335 Eukaryota
COG1249 LUCA
GeneTreeiENSGT00550000074844
HOGENOMiHOG000276708
HOVERGENiHBG002290
InParanoidiO08749
KOiK00382
OMAiTMSEAVM
OrthoDBi581771at2759
PhylomeDBiO08749
TreeFamiTF300414

Enzyme and pathway databases

ReactomeiR-MMU-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-MMU-389661 Glyoxylate metabolism and glycine degradation
R-MMU-5362517 Signaling by Retinoic Acid
R-MMU-6783984 Glycine degradation
R-MMU-70268 Pyruvate metabolism
R-MMU-70895 Branched-chain amino acid catabolism
R-MMU-71064 Lysine catabolism
R-MMU-71403 Citric acid cycle (TCA cycle)

Miscellaneous databases

Protein Ontology

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PROi
PR:O08749

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000020664 Expressed in 330 organ(s), highest expression level in brown adipose tissue
CleanExiMM_DLD
GenevisibleiO08749 MM

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006258 Lipoamide_DH
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit
PIRSFiPIRSF000350 Mercury_reductase_MerA, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit
TIGRFAMsiTIGR01350 lipoamide_DH, 1 hit
PROSITEiView protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiDLDH_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: O08749
Secondary accession number(s): Q3TG55
, Q3U5W5, Q3UWP7, Q99LD3
<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 15, 1999
Last sequence update: November 28, 2006
Last modified: January 16, 2019
This is version 170 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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