Search Results

Overview

Uniprot ID	Q9P2J5
Protein Name	Leucine--tRNA ligase, cytoplasmic
Gene Name	LARS1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
1133	RRVPVLGKEYTEKTP
173	LSDEEIVKFSEAEHW
39	VNASNLEKQTSKGKY
43	NLEKQTSKGKYFVTF
970	NGKLPDNKVIASELG

Function

Aminoacyl-tRNA synthetase that catalyzes the specific attachment of leucine to its cognate tRNA (tRNA(Leu)) (PubMed:25051973, PubMed:32232361). It performs tRNA aminoacylation in a two-step reaction: Leu is initially activated by ATP to form a leucyl-adenylate (Leu-AMP) intermediate; then the leucyl moiety is transferred to the acceptor 3' end of the tRNA to yield leucyl-tRNA (PubMed:25051973). To improve the fidelity of catalytic reactions, it is also able to hydrolyze misactivated aminoacyl-adenylate intermediates (pre-transfer editing) and mischarged aminoacyl-tRNAs (post-transfer editing) (PubMed:25051973)

Protein Sequence

10 MAERKGTAKV 20 DFLKKIEKEI 30 QQKWDTERVF 40 EVNASNLEKQ 50 TSKGKYFVTF 60 PYPYMNGRLH 70 LGHTFSLSKC 80 EFAVGYQRLK 90 GKCCLFPFGL 100 HCTGMPIKAC 110 ADKLKREIEL 120 YGCPPDFPDE 130 EEEEEETSVK 140 TEDIIIKDKA 150 KGKKSKAAAK 160 AGSSKYQWGI 170 MKSLGLSDEE 180 IVKFSEAEHW 190 LDYFPPLAIQ 200 DLKRMGLKVD 210 WRRSFITTDV 220 NPYYDSFVRW 230 QFLTLRERNK 240 IKFGKRYTIY 250 SPKDGQPCMD 260 HDRQTGEGVG 270 PQEYTLLKLK 280 VLEPYPSKLS 290 GLKGKNIFLV 300 AATLRPETMF 310 GQTNCWVRPD 320 MKYIGFETVN 330 GDIFICTQKA 340 ARNMSYQGFT 350 KDNGVVPVVK 360 ELMGEEILGA 370 SLSAPLTSYK 380 VIYVLPMLTI 390 KEDKGTGVVT 400 SVPSDSPDDI 410 AALRDLKKKQ 420 ALRAKYGIRD 430 DMVLPFEPVP 440 VIEIPGFGNL 450 SAVTICDELK 460 IQSQNDREKL 470 AEAKEKIYLK 480 GFYEGIMLVD 490 GFKGQKVQDV 500 KKTIQKKMID 510 AGDALIYMEP 520 EKQVMSRSSD 530 ECVVALCDQW 540 YLDYGEENWK 550 KQTSQCLKNL 560 ETFCEETRRN 570 FEATLGWLQE 580 HACSRTYGLG 590 THLPWDEQWL 600 IESLSDSTIY 610 MAFYTVAHLL 620 QGGNLHGQAE 630 SPLGIRPQQM 640 TKEVWDYVFF 650 KEAPFPKTQI 660 AKEKLDQLKQ 670 EFEFWYPVDL 680 RVSGKDLVPN 690 HLSYYLYNHV 700 AMWPEQSDKW 710 PTAVRANGHL 720 LLNSEKMSKS 730 TGNFLTLTQA 740 IDKFSADGMR 750 LALADAGDTV 760 EDANFVEAMA 770 DAGILRLYTW 780 VEWVKEMVAN 790 WDSLRSGPAS 800 TFNDRVFASE 810 LNAGIIKTDQ 820 NYEKMMFKEA 830 LKTGFFEFQA 840 AKDKYRELAV 850 EGMHRELVFR 860 FIEVQTLLLA 870 PFCPHLCEHI 880 WTLLGKPDSI 890 MNASWPVAGP 900 VNEVLIHSSQ 910 YLMEVTHDLR 920 LRLKNYMMPA 930 KGKKTDKQPL 940 QKPSHCTIYV 950 AKNYPPWQHT 960 TLSVLRKHFE 970 ANNGKLPDNK 980 VIASELGSMP 990 ELKKYMKKVM 1000 PFVAMIKENL 1010 EKMGPRILDL 1020 QLEFDEKAVL 1030 MENIVYLTNS 1040 LELEHIEVKF 1050 ASEAEDKIRE 1060 DCCPGKPLNV 1070 FRIEPGVSVS 1080 LVNPQPSNGH 1090 FSTKIEIRQG 1100 DNCDSIIRRL 1110 MKMNRGIKDL 1120 SKVKLMRFDD 1130 PLLGPRRVPV 1140 LGKEYTEKTP 1150 ISEHAVFNVD 1160 LMSKKIHLTE 1170 NGIRVDIGDT IIYLVH

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0017101	aminoacyl-tRNA synthetase multienzyme complex
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0012505	endomembrane system
Cellular Component	GO:0005783	endoplasmic reticulum
Cellular Component	GO:0005764	lysosome
Molecular Function	GO:0002161	aminoacyl-tRNA deacylase activity
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0004819	glutamine-tRNA ligase activity
Molecular Function	GO:0005096	GTPase activator activity
Molecular Function	GO:0004823	leucine-tRNA ligase activity
Biological Process	GO:0034198	cellular response to amino acid starvation
Biological Process	GO:0071230	cellular response to amino acid stimulus
Biological Process	GO:0071233	cellular response to L-leucine
Biological Process	GO:1990253	cellular response to leucine starvation
Biological Process	GO:0006425	glutaminyl-tRNA aminoacylation
Biological Process	GO:0006429	leucyl-tRNA aminoacylation
Biological Process	GO:1904263	positive regulation of TORC1 signaling
Biological Process	GO:0006418	tRNA aminoacylation for protein translation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] 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.

[6] 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.

[7] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[8] 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.