Search Results

Overview

Uniprot IDP54577
Protein NameTyrosine--tRNA ligase, cytoplasmic
Gene NameYARS1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
119 LEKLKFIKGTDYQLS
146 VVTQHDSKKAGAEVV
147 VTQHDSKKAGAEVVK
190 FGGIDQRKIFTFAEK
282 FVILRDEKWGGNKTY
327 LLDPIREKFNTPALK
335 FNTPALKKLASAAYP
348 YPDPSKQKPMAKGPA
356 PMAKGPAKNSEPEEV
474 VFVKGYEKGQPDEEL
513 KQTNFMTKLGSISCK

Function

Tyrosine--tRNA ligase that catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (Probable) (PubMed:25533949). Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity (PubMed:25533949). Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 (PubMed:25533949)

Protein Sequence

10 MGDAPSPEEK 20 LHLITRNLQE 30 VLGEEKLKEI 40 LKERELKIYW 50 GTATTGKPHV 60 AYFVPMSKIA 70 DFLKAGCEVT 80 ILFADLHAYL 90 DNMKAPWELL 100 ELRVSYYENV 110 IKAMLESIGV 120 PLEKLKFIKG 130 TDYQLSKEYT 140 LDVYRLSSVV 150 TQHDSKKAGA 160 EVVKQVEHPL 170 LSGLLYPGLQ 180 ALDEEYLKVD 190 AQFGGIDQRK 200 IFTFAEKYLP 210 ALGYSKRVHL 220 MNPMVPGLTG 230 SKMSSSEEES 240 KIDLLDRKED 250 VKKKLKKAFC 260 EPGNVENNGV 270 LSFIKHVLFP 280 LKSEFVILRD 290 EKWGGNKTYT 300 AYVDLEKDFA 310 AEVVHPGDLK 320 NSVEVALNKL 330 LDPIREKFNT 340 PALKKLASAA 350 YPDPSKQKPM 360 AKGPAKNSEP 370 EEVIPSRLDI 380 RVGKIITVEK 390 HPDADSLYVE 400 KIDVGEAEPR 410 TVVSGLVQFV 420 PKEELQDRLV 430 VVLCNLKPQK 440 MRGVESQGML 450 LCASIEGINR 460 QVEPLDPPAG 470 SAPGEHVFVK 480 GYEKGQPDEE 490 LKPKKKVFEK 500 LQADFKISEE 510 CIAQWKQTNF 520 MTKLGSISCK SLKGGNIS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0005153 interleukin-8 receptor binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0036094 small molecule binding
Molecular Function GO:0000049 tRNA binding
Molecular Function GO:0004831 tyrosine-tRNA ligase activity
Biological Process GO:0006915 apoptotic process
Biological Process GO:0042594 response to starvation
Biological Process GO:0006437 tyrosyl-tRNA aminoacylation

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] 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.

[7] 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.

[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.