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Entry version 217 (07 Oct 2020)
Sequence version 4 (11 Jan 2011)
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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

DLST

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

Annotation score:5 out of 5

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

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

Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711, PubMed:30929736). 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 (PubMed:29211711).2 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 '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

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine degradation via saccharopine pathway

This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lysine ketoglutarate reductase (AASS), Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS), Lysine ketoglutarate reductase (AASS)
  2. Lysine ketoglutarate reductase (AASS), Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS), Lysine ketoglutarate reductase (AASS)
  3. no protein annotated in this organism
  4. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (AADAT)
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (E2k)
This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Pathwayi: tricarboxylic acid cycle

This protein is involved in the pathway tricarboxylic acid cycle, which is part of Carbohydrate metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei4241 Publication1
Active sitei428By similarity1

<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 functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS04324-MONOMER

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P36957

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-389661, Glyoxylate metabolism and glycine degradation
R-HSA-71064, Lysine catabolism
R-HSA-71403, Citric acid cycle (TCA cycle)

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P36957

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00223
UPA00868;UER00840

<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:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.611 Publication)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2K
<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:DLST
Synonyms:DLTS
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000119689.14

Human Gene Nomenclature Database

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HGNCi
HGNC:2911, DLST

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
126063, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P36957

<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, 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

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

Paragangliomas 7 (PGL7)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant tumor predisposition syndrome characterized by adult-onset development of paragangliomas, neural crest tumors usually derived from the chromoreceptor tissue of a paraganglion. PGL7 tumors are generally benign, tend to be abdominal, and often secrete normetanephrine.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_083034231R → Q in PGL7; unknown pathological significance; not changed dihydrolipoyllysine-residue succinyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs771616810Ensembl.1
Natural variantiVAR_083036374G → E in PGL7; decreased dihydrolipoyllysine-residue succinyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs1270341616EnsemblClinVar.1
Natural variantiVAR_083037422Y → C in PGL7; unknown pathological significance; not changed dihydrolipoyllysine-residue succinyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs778239022Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi224 – 226REK → AEA: Reduced nuclear localization of the 2-oxoglutarate dehydrogenase complex. Reduced histone succinylation. 1 Publication3
Mutagenesisi424H → A: Loss of dihydrolipoyllysine-residue succinyltransferase activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
1743

MalaCards human disease database

More...
MalaCardsi
DLST
MIMi618475, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000119689

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27367

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P36957, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
DLST

Domain mapping of disease mutations (DMDM)

More...
DMDMi
317373578

<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 – 67Mitochondrion1 PublicationAdd BLAST67
<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_000002047268 – 453Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST386

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 residuei81PhosphoserineBy similarity1
Modified residuei110N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei154N6-acetyllysineBy similarity1
Modified residuei267N6-acetyllysineBy similarity1
Modified residuei272N6-acetyllysineBy similarity1
Modified residuei273N6-acetyllysineBy similarity1
Modified residuei277N6-acetyllysineBy similarity1
Modified residuei307N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P36957

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P36957

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P36957

MaxQB - The MaxQuant DataBase

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MaxQBi
P36957

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

More...
PaxDbi
P36957

PeptideAtlas

More...
PeptideAtlasi
P36957

PRoteomics IDEntifications database

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PRIDEi
P36957

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
55248 [P36957-1]
6726

Consortium for Top Down Proteomics

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TopDownProteomicsi
P36957-1 [P36957-1]

2D gel databases

USC-OGP 2-DE database

More...
OGPi
P36957

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P36957

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P36957

MetOSite database of methionine sulfoxide sites

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MetOSitei
P36957

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

More...
PhosphoSitePlusi
P36957

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P36957

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000119689, Expressed in heart and 239 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P36957, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P36957, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000119689, Low tissue specificity

<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

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 (PubMed:29211711).

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
108087, 296 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P36957

Protein interaction database and analysis system

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IntActi
P36957, 285 interactors

Molecular INTeraction database

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MINTi
P36957

STRING: functional protein association networks

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STRINGi
9606.ENSP00000335304

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P36957, 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

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P36957

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini70 – 144Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST75

<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 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0559, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00930000151014

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_016733_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P36957

KEGG Orthology (KO)

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KOi
K00658

Identification of Orthologs from Complete Genome Data

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OMAi
MKVPSPG

Database for complete collections of gene phylogenies

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PhylomeDBi
P36957

TreeFam database of animal gene trees

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TreeFami
TF314164

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.559.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003016, 2-oxoA_DH_lipoyl-BS
IPR001078, 2-oxoacid_DH_actylTfrase
IPR000089, Biotin_lipoyl
IPR023213, CAT-like_dom_sf
IPR011053, Single_hybrid_motif
IPR006255, SucB

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00198, 2-oxoacid_dh, 1 hit
PF00364, Biotin_lipoyl, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51230, SSF51230, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01347, sucB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00189, LIPOYL, 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>Sequences (2+)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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P36957-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI
60 70 80 90 100
NNSVFSVRFF RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED
110 120 130 140 150
EVVCEIETDK TSVQVPSPAN GVIEALLVPD GGKVEGGTPL FTLRKTGAAP
160 170 180 190 200
AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI PTQMPPVPSP SQPPSGKPVS
210 220 230 240 250
AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE AQNTCAMLTT
260 270 280 290 300
FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA
310 320 330 340 350
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL
360 370 380 390 400
GEKARKNELA IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF
410 420 430 440 450
DRPVAIGGKV EVRPMMYVAL TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL

LDL
Length:453
Mass (Da):48,755
Last modified:January 11, 2011 - v4
<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:iA30E8CC959106B8F
GO
Isoform 2 (identifier: P36957-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MLSRSRCVSRAFSRSLSAFQKGN → MTWLQSKPQRLQNLSQREMSGGR
     24-109: Missing.

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Length:367
Mass (Da):39,553
Checksum:i3EEF7F48175530EC
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 are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q86SW4Q86SW4_HUMAN
Dihydrolipoamide acetyltransferase ...
DLST
279Annotation score:

Annotation score:2 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>
B7ZAZ8B7ZAZ8_HUMAN
Dihydrolipoyllysine-residue succiny...
DLST
67Annotation 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>
G3V3F0G3V3F0_HUMAN
Dihydrolipoyllysine-residue succiny...
DLST
104Annotation 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>
H0YJF9H0YJF9_HUMAN
Dihydrolipoyllysine-residue succiny...
DLST
74Annotation 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>
G3V5L9G3V5L9_HUMAN
Dihydrolipoyllysine-residue succiny...
DLST
110Annotation 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>
G3V5M3G3V5M3_HUMAN
Dihydrolipoyllysine-residue succiny...
DLST
83Annotation 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>
G3V498G3V498_HUMAN
Dihydrolipoyllysine-residue succiny...
DLST
37Annotation 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 conflicti14 – 15RS → AP in BAA03871 (PubMed:8268217).Curated2
Sequence conflicti14 – 15RS → AP in BAA05536 (PubMed:8076640).Curated2
Sequence conflicti14 – 15RS → AP in AAB59629 (Ref. 3) Curated2
Sequence conflicti132G → T in BAA03871 (PubMed:8268217).Curated1
Sequence conflicti212E → D in BAA03871 (PubMed:8268217).Curated1
Sequence conflicti212E → D in BAA05536 (PubMed:8076640).Curated1
Sequence conflicti312R → T in BAA05536 (PubMed:8076640).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004976213P → A2 Publications1
Natural variantiVAR_083034231R → Q in PGL7; unknown pathological significance; not changed dihydrolipoyllysine-residue succinyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs771616810Ensembl.1
Natural variantiVAR_083035304D → N Neutral polymorphism; not changed dihydrolipoyllysine-residue succinyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs373295097Ensembl.1
Natural variantiVAR_083036374G → E in PGL7; decreased dihydrolipoyllysine-residue succinyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs1270341616EnsemblClinVar.1
Natural variantiVAR_004977384P → T. 1
Natural variantiVAR_083037422Y → C in PGL7; unknown pathological significance; not changed dihydrolipoyllysine-residue succinyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs778239022Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0564391 – 23MLSRS…FQKGN → MTWLQSKPQRLQNLSQREMS GGR in isoform 2. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_05644024 – 109Missing in isoform 2. 1 PublicationAdd BLAST86

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

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DDBJi
Links Updated
D16373 mRNA Translation: BAA03871.1
D26535 Genomic DNA Translation: BAA05536.1
L37418 mRNA Translation: AAB59629.1
AK289414 mRNA Translation: BAF82103.1
AK299505 mRNA Translation: BAH13054.1
AC006530 Genomic DNA Translation: AAD30181.1
CH471061 Genomic DNA Translation: EAW81199.1
BC000302 mRNA Translation: AAH00302.1
BC001922 mRNA Translation: AAH01922.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS9833.1 [P36957-1]

Protein sequence database of the Protein Information Resource

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PIRi
S39786, PN0673

NCBI Reference Sequences

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RefSeqi
NP_001924.2, NM_001933.4 [P36957-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000334220; ENSP00000335304; ENSG00000119689 [P36957-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
1743

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1743

UCSC genome browser

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UCSCi
uc001xqv.3, human [P36957-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
D16373 mRNA Translation: BAA03871.1
D26535 Genomic DNA Translation: BAA05536.1
L37418 mRNA Translation: AAB59629.1
AK289414 mRNA Translation: BAF82103.1
AK299505 mRNA Translation: BAH13054.1
AC006530 Genomic DNA Translation: AAD30181.1
CH471061 Genomic DNA Translation: EAW81199.1
BC000302 mRNA Translation: AAH00302.1
BC001922 mRNA Translation: AAH01922.1
CCDSiCCDS9833.1 [P36957-1]
PIRiS39786, PN0673
RefSeqiNP_001924.2, NM_001933.4 [P36957-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6H05electron microscopy2.90A68-453[»]
SMRiP36957
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi108087, 296 interactors
CORUMiP36957
IntActiP36957, 285 interactors
MINTiP36957
STRINGi9606.ENSP00000335304

PTM databases

iPTMnetiP36957
MetOSiteiP36957
PhosphoSitePlusiP36957
SwissPalmiP36957

Polymorphism and mutation databases

BioMutaiDLST
DMDMi317373578

2D gel databases

OGPiP36957
UCD-2DPAGEiP36957

Proteomic databases

EPDiP36957
jPOSTiP36957
MassIVEiP36957
MaxQBiP36957
PaxDbiP36957
PeptideAtlasiP36957
PRIDEiP36957
ProteomicsDBi55248 [P36957-1]
6726
TopDownProteomicsiP36957-1 [P36957-1]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P36957, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

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Antibodypediai
45, 193 antibodies

The DNASU plasmid repository

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DNASUi
1743

Genome annotation databases

EnsembliENST00000334220; ENSP00000335304; ENSG00000119689 [P36957-1]
GeneIDi1743
KEGGihsa:1743
UCSCiuc001xqv.3, human [P36957-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1743
DisGeNETi1743
EuPathDBiHostDB:ENSG00000119689.14

GeneCards: human genes, protein and diseases

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GeneCardsi
DLST
HGNCiHGNC:2911, DLST
HPAiENSG00000119689, Low tissue specificity
MalaCardsiDLST
MIMi126063, gene
618475, phenotype
neXtProtiNX_P36957
OpenTargetsiENSG00000119689
PharmGKBiPA27367

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0559, Eukaryota
GeneTreeiENSGT00930000151014
HOGENOMiCLU_016733_0_0_1
InParanoidiP36957
KOiK00658
OMAiMKVPSPG
PhylomeDBiP36957
TreeFamiTF314164

Enzyme and pathway databases

UniPathwayiUPA00223
UPA00868;UER00840
BioCyciMetaCyc:HS04324-MONOMER
PathwayCommonsiP36957
ReactomeiR-HSA-389661, Glyoxylate metabolism and glycine degradation
R-HSA-71064, Lysine catabolism
R-HSA-71403, Citric acid cycle (TCA cycle)
SABIO-RKiP36957

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
1743, 189 hits in 876 CRISPR screens

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

More...
ChiTaRSi
DLST, human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
DLST

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

More...
GenomeRNAii
1743
PharosiP36957, Tbio

Protein Ontology

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PROi
PR:P36957
RNActiP36957, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000119689, Expressed in heart and 239 other tissues
ExpressionAtlasiP36957, baseline and differential
GenevisibleiP36957, HS

Family and domain databases

Gene3Di3.30.559.10, 1 hit
InterProiView protein in InterPro
IPR003016, 2-oxoA_DH_lipoyl-BS
IPR001078, 2-oxoacid_DH_actylTfrase
IPR000089, Biotin_lipoyl
IPR023213, CAT-like_dom_sf
IPR011053, Single_hybrid_motif
IPR006255, SucB
PfamiView protein in Pfam
PF00198, 2-oxoacid_dh, 1 hit
PF00364, Biotin_lipoyl, 1 hit
SUPFAMiSSF51230, SSF51230, 1 hit
TIGRFAMsiTIGR01347, sucB, 1 hit
PROSITEiView protein in PROSITE
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00189, LIPOYL, 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 nameiODO2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P36957
Secondary accession number(s): B7Z5W8
, E7ESY5, Q7LDY7, Q9BQ32
<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: June 1, 1994
Last sequence update: January 11, 2011
Last modified: October 7, 2020
This is version 217 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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