Search Results
Overview
| Uniprot ID | P36957 |
|---|---|
| Protein Name | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial |
| Gene Name | DLST |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 154 | GAAPAKAKPAEAPAA |
| 203 | GKPVSAVKPTVAPPL |
| 217 | LAEPGAGKGLRSEHR |
| 239 | QRIAQRLKEAQNTCA |
| 267 | QEMRARHKEAFLKKH |
| 353 | TITELGEKARKNELA |
| 74 | KDDLVTVKTPAFAES |
Function
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 CO(2). 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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0160167 | oxoadipate dehydrogenase complex |
| Cellular Component | GO:0045252 | oxoglutarate dehydrogenase complex |
| Molecular Function | GO:0016746 | acyltransferase activity |
| Molecular Function | GO:0004149 | dihydrolipoyllysine-residue succinyltransferase activity |
| Biological Process | GO:0120551 | 2-oxoglutarate decarboxylation to succinyl-CoA |
| Biological Process | GO:0006103 | 2-oxoglutarate metabolic process |
| Biological Process | GO:0006091 | generation of precursor metabolites and energy |
| Biological Process | GO:0033512 | L-lysine catabolic process to acetyl-CoA via L-saccharopine |
| Biological Process | GO:0006104 | succinyl-CoA metabolic process |
| Biological Process | GO:0006099 | tricarboxylic acid cycle |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.