Search Results

Overview

Uniprot IDQ96CM8
Protein NameMedium-chain acyl-CoA ligase ACSF2, mitochondrial
Gene NameACSF2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
179 CKALVFPKQFKTQQY
182 LVFPKQFKTQQYYNV
340 SPIFNGKKALEAISR
599 YPLTISGKIQKFKLR
66 SYVQGCTKKHLNSKT
72 TKKHLNSKTVGQCLE

Function

Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA (PubMed:17762044). Has some preference toward medium-chain substrates (PubMed:17762044). Plays a role in adipocyte differentiation (PubMed:16380219)

Protein Sequence

10 MAVYVGMLRL 20 GRLCAGSSGV 30 LGARAALSRS 40 WQEARLQGVR 50 FLSSREVDRM 60 VSTPIGGLSY 70 VQGCTKKHLN 80 SKTVGQCLET 90 TAQRVPEREA 100 LVVLHEDVRL 110 TFAQLKEEVD 120 KAASGLLSIG 130 LCKGDRLGMW 140 GPNSYAWVLM 150 QLATAQAGII 160 LVSVNPAYQA 170 MELEYVLKKV 180 GCKALVFPKQ 190 FKTQQYYNVL 200 KQICPEVENA 210 QPGALKSQRL 220 PDLTTVISVD 230 APLPGTLLLD 240 EVVAAGSTRQ 250 HLDQLQYNQQ 260 FLSCHDPINI 270 QFTSGTTGSP 280 KGATLSHYNI 290 VNNSNILGER 300 LKLHEKTPEQ 310 LRMILPNPLY 320 HCLGSVAGTM 330 MCLMYGATLI 340 LASPIFNGKK 350 ALEAISRERG 360 TFLYGTPTMF 370 VDILNQPDFS 380 SYDISTMCGG 390 VIAGSPAPPE 400 LIRAIINKIN 410 MKDLVVAYGT 420 TENSPVTFAH 430 FPEDTVEQKA 440 ESVGRIMPHT 450 EARIMNMEAG 460 TLAKLNTPGE 470 LCIRGYCVML 480 GYWGEPQKTE 490 EAVDQDKWYW 500 TGDVATMNEQ 510 GFCKIVGRSK 520 DMIIRGGENI 530 YPAELEDFFH 540 THPKVQEVQV 550 VGVKDDRMGE 560 EICACIRLKD 570 GEETTVEEIK 580 AFCKGKISHF 590 KIPKYIVFVT 600 NYPLTISGKI 610 QKFKLREQME RHLNL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0004467 long-chain fatty acid-CoA ligase activity
Molecular Function GO:0031956 medium-chain fatty acid-CoA ligase activity
Biological Process GO:0006637 acyl-CoA metabolic process
Biological Process GO:0006631 fatty acid metabolic process

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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.