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Overview

Uniprot IDF1S431
Protein NameAlanine--tRNA ligase
Gene NameAARS1
OrganismSus scrofa

Kla Sites from experimental identification

Position Flanking peptide
19 QRFIDFFKRNEHTYV
231 RETDGVLKPLPKKSI
235 GVLKPLPKKSIDTGM
338 AVRYSHEKLNASRGF
396 GRRILDRKIQSLGDS
451 ERKLAQLKSQGKGAG
558 VDDSSEDKTEFTVKN
564 DKTEFTVKNAQVRGG
74 SRAANTQKCIRAGGK
761 VTGAEAQKALRKADS
765 EAQKALRKADSLMKS
788 KAQTAPNKDVQREIA
81 KCIRAGGKHNDLDDV
933 MDGKGGGKDVSAQAT

Function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain. In presence of high levels of lactate, also acts as a protein lactyltransferase that mediates lactylation of lysine residues in target proteins, such as TEAD1, TP53/p53 and YAP1. Protein lactylation takes place in a two-step reaction: lactate is first activated by ATP to form lactate-AMP and then transferred to lysine residues of target proteins. Acts as an inhibitor of TP53/p53 activity by catalyzing lactylation of TP53/p53. Acts as a positive regulator of the Hippo pathway by mediating lactylation of TEAD1 and YAP1

Protein Sequence

10 MHSTLTASEI 20 RQRFIDFFKR 30 NEHTYVHSSA 40 TIPLDDPTLL 50 FANAGMNQFK 60 PIFLNTIDPS 70 HPMAKLSRAA 80 NTQKCIRAGG 90 KHNDLDDVGK 100 DVYHHTFFEM 110 LGSWSFGDYF 120 KELACKMALE 130 LLTQEFGIPV 140 ERLYVTYFGG 150 DEAAGLEPDL 160 ECKQIWQNLG 170 LDDSKILPGN 180 MKDNFWEMGD 190 TGPCGPCSEI 200 HYDRIGGRDA 210 AHLVNQDDPN 220 VLEIWNLVFI 230 QYNRETDGVL 240 KPLPKKSIDT 250 GMGLERLVSV 260 LQNKMSNYDT 270 DLFVPYFEAI 280 QKGTGARPYT 290 GKVGADDADG 300 IDMAYRVLAD 310 HARTITVALA 320 DGGRPDNTGR 330 GYVLRRILRR 340 AVRYSHEKLN 350 ASRGFFATLV 360 DVVVQSLGDA 370 FPELKKDPDM 380 VKDIINEEEV 390 QFLKTLSRGR 400 RILDRKIQSL 410 GDSKTIPGDT 420 AWLLYDTYGF 430 PVDLTGLIAE 440 EKGLVVDMDG 450 FEEERKLAQL 460 KSQGKGAGGE 470 DLIMLDIYAI 480 EELRERGLEA 490 TDDSPKYNYH 500 SDSSGSYVFE 510 SAVATVMALR 520 RDRMFVEEVC 530 TGQECGVVLD 540 KTCFYAEQGG 550 QIYDEGYLVK 560 VDDSSEDKTE 570 FTVKNAQVRG 580 GYVLHIGTIY 590 GSLKVGDQVR 600 LFIDEPRRRP 610 VMSNHTATHI 620 LNFALRSVLG 630 EADQRGSLVA 640 PDLRFDFTAK 650 GAMSTQQIKK 660 AEELANEMIE 670 AAKPVYAQNC 680 PLAAAKAIQG 690 LRAVFDETYP 700 DPVRVVSIGV 710 PVSELLDDPS 720 GPAGSLTSVE 730 FCGGTHLQNS 740 SHAGAFVIVS 750 EEAIAKGIRR 760 IVAVTGAEAQ 770 KALRKADSLM 780 KSLCAMEAKV 790 KAQTAPNKDV 800 QREIADLGEA 810 LATAVIPQWQ 820 KDEFRENLRS 830 LKKVMDDLDR 840 ASKADVQKRV 850 LERTKQLIDS 860 NPNQPLVILE 870 MESGASAKAL 880 NEALKLFKTH 890 SPQTSAMLFT 900 VDNEAGKIIC 910 LCQVPQNIAN 920 RGLKASEWVQ 930 QVSGLMDGKG 940 GGKDVSAQAT 950 GKNVGCLQEA 960 LQLATSFAQL RLEDVKN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005634 nucleus
Molecular Function GO:0004813 alanine-tRNA ligase activity
Molecular Function GO:0002161 aminoacyl-tRNA deacylase activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0141207 peptide lactyltransferase (ATP-dependent) activity
Molecular Function GO:0002196 Ser-tRNA(Ala) deacylase activity
Molecular Function GO:0000049 tRNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006419 alanyl-tRNA aminoacylation
Biological Process GO:1901797 negative regulation of signal transduction by p53 class mediator
Biological Process GO:0035332 positive regulation of hippo signaling
Biological Process GO:0140018 regulation of cytoplasmic translational fidelity
Biological Process GO:0006400 tRNA modification

Reference

[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.