Search Results

Overview

Uniprot IDP10515
Protein NameDihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Gene NameDLAT
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
362 VFVSPLAKKLAVEKG
368 AKKLAVEKGIDLTQV
376 GIDLTQVKGTGPDGR
387 PDGRITKKDIDSFVP
440 AQRLMQSKQTIPHYY
466 LVRKELNKILEGRSK
473 KILEGRSKISVNDFI
547 DVVSLATKAREGKLQ

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)

Protein Sequence

10 MWRVCARRAQ 20 NVAPWAGLEA 30 RWTALQEVPG 40 TPRVTSRSGP 50 APARRNSVTT 60 GYGGVRALCG 70 WTPSSGATPR 80 NRLLLQLLGS 90 PGRRYYSLPP 100 HQKVPLPSLS 110 PTMQAGTIAR 120 WEKKEGDKIN 130 EGDLIAEVET 140 DKATVGFESL 150 EECYMAKILV 160 AEGTRDVPIG 170 AIICITVGKP 180 EDIEAFKNYT 190 LDSSAAPTPQ 200 AAPAPTPAAT 210 ASPPTPSAQA 220 PGSSYPPHMQ 230 VLLPALSPTM 240 TMGTVQRWEK 250 KVGEKLSEGD 260 LLAEIETDKA 270 TIGFEVQEEG 280 YLAKILVPEG 290 TRDVPLGTPL 300 CIIVEKEADI 310 SAFADYRPTE 320 VTDLKPQVPP 330 PTPPPVAAVP 340 PTPQPLAPTP 350 SAPCPATPAG 360 PKGRVFVSPL 370 AKKLAVEKGI 380 DLTQVKGTGP 390 DGRITKKDID 400 SFVPSKVAPA 410 PAAVVPPTGP 420 GMAPVPTGVF 430 TDIPISNIRR 440 VIAQRLMQSK 450 QTIPHYYLSI 460 DVNMGEVLLV 470 RKELNKILEG 480 RSKISVNDFI 490 IKASALACLK 500 VPEANSSWMD 510 TVIRQNHVVD 520 VSVAVSTPAG 530 LITPIVFNAH 540 IKGVETIAND 550 VVSLATKARE 560 GKLQPHEFQG 570 GTFTISNLGM 580 FGIKNFSAII 590 NPPQACILAI 600 GASEDKLVPA 610 DNEKGFDVAS 620 MMSVTLSCDH 630 RVVDGAVGAQ 640 WLAEFRKYLE KPITMLL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0045254 pyruvate dehydrogenase complex
Molecular Function GO:0004742 dihydrolipoyllysine-residue acetyltransferase activity
Molecular Function GO:0042802 identical protein binding
Biological Process GO:0006006 glucose metabolic process
Biological Process GO:0042867 pyruvate catabolic process
Biological Process GO:0006086 pyruvate decarboxylation to acetyl-CoA
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.

[4] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.