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Details on Person UniProt:P10515 DLAT
| Class:Id | ReferenceGeneProduct:60872 |
|---|---|
| _chainChangeLog | transit peptide:1-86 added on Sat February 7 2015;chain:87-647 added on Sat February 7 2015 |
| _displayName | UniProt:P10515 DLAT |
| _timestamp | 2026-02-20 22:46:50 |
| chain | transit peptide:1-86 chain:87-647 |
| checksum | DD93A8E666E377C2 |
| comment | FUNCTION The pyruvate dehydrogenase (PDH) complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3); (Probable). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acetyl groups from acetyl-lipoyl moiety generated by the pyruvate dehydrogenase, leading to acetyl-CoA formation (Probable).CATALYTIC ACTIVITY N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + acetyl-CoA = N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CoACOFACTOR Binds 2 lipoyl cofactors covalently.SUBUNIT Part of the pyruvate dehydrogenase (PDH) complex that is a multi-enzyme complex composed of multiple copies of three enzymes, pyruvate dehydrogenase (subunits PDH1A and PDHB, E1 component), dihydrolipoamide acetyltransferase (DLAT, E2 component), and dihydrolipoamide dehydrogenase (DLD, E3 component) to which is added an additional protein the E3-binding protein (PDHX, E3BP) (By similarity). In terms of structural architecture, the E2 and E3BP components assemble into a 60meric central core with icosahedral symmetry (PubMed:14638692, PubMed:20361979). The central core is decorated with E1 and E3 proteins (By similarity). Currently, two alternative models for the E2:E3BP stoichiometry are considered as being either 48:12 (E2(48)-E3BP(12)) or 40:20 (E2(40)-E3BP(20)) (PubMed:14638692, PubMed:20361979). Interacts with PDK2 and PDK3 (PubMed:15861126, PubMed:17532006, PubMed:17683942, PubMed:18387944). Interacts with SIRT4 (PubMed:25525879). Interacts with PDHB (PubMed:20160912).INTERACTION Delipoylated at Lys-132 and Lys-259 by SIRT4, delipoylation decreases the PHD complex activity.DISEASE Primary biliary cirrhosis is a chronic, progressive cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients' serum. It manifests with inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. Patients with primary biliary cirrhosis show autoantibodies against the E2 component of pyruvate dehydrogenase complex.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the 2-oxoacid dehydrogenase family.SEQUENCE CAUTION Contaminating sequence. Sequence of unknown origin in the N-terminal part. |
| description | recommendedName: fullName evidence="21"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial ecNumber evidence="22"2.3.1.12 alternativeName: fullName evidence="24"70 kDa mitochondrial autoantigen of primary biliary cirrhosis shortName: PBC alternativeName: fullName evidence="1"Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex alternativeName: fullName evidence="24"M2 antigen complex 70 kDa subunit alternativeName: Pyruvate dehydrogenase complex component E2 shortName evidence="20"PDC-E2 shortName: PDCE2 |
| geneName | DLAT DLTA |
| identifier | P10515 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Acyltransferase Carbohydrate metabolism Glucose metabolism Lipoyl Mitochondrion Phosphoprotein Proteomics identification Reference proteome Repeat Transferase Transit peptide Tricarboxylic acid cycle |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | DLAT |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8995584] ENSEMBL:ENSG00000150768 DLAT [Homo sapiens] |
| secondaryIdentifier | ODP2_HUMAN Q16783 Q53EP3 |
| sequenceLength | 647 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:69969] Lipo-K259-DLAT [mitochondrial matrix] [Homo sapiens] [EntityWithAccessionedSequence:6792585] DLAT [mitochondrial matrix] [Homo sapiens] [EntityWithAccessionedSequence:9861594] AcetyllipoH2-K132,K259-DLAT [mitochondrial matrix] [Homo sapiens] [EntityWithAccessionedSequence:9861664] LipoH2-K259-DLAT [mitochondrial matrix] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:1169150] N6-lipoyl-L-lysine at 132 [ModifiedResidue:1169151] N6-lipoyl-L-lysine at 259 [GroupModifiedResidue:9861614] N6-lipoyl-L-lysine ((R)-N6-(S8-acetyldihydrolipoyl)-L-lysine residue) at 259 [GroupModifiedResidue:9861636] N6-lipoyl-L-lysine ((R)-N6-dihydrolipoyl-L-lysine residue) at 259 |
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No pathways have been reviewed or authored by UniProt:P10515 DLAT (60872)
