Search Results

Overview

Uniprot IDP26639
Protein NameThreonine--tRNA ligase 1, cytoplasmic
Gene NameTARS1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
12 KASSPSGKMGGEEKP
223 FERLEVKKETLLAMF
243 KCRILNEKVNTPTTT
279 IKALKIHKNSSTYWE
288 SSTYWEGKADMETLQ
319 EKFQEEAKNRDHRKI
36 EGGKKKNKEGSGDGG
681 LVVGEKEKISGTVNI
712 IERLQQLKEFRSKQA

Function

Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:25824639, PubMed:31374204). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage (By similarity)

Protein Sequence

10 MFEEKASSPS 20 GKMGGEEKPI 30 GAGEEKQKEG 40 GKKKNKEGSG 50 DGGRAELNPW 60 PEYIYTRLEM 70 YNILKAEHDS 80 ILAEKAEKDS 90 KPIKVTLPDG 100 KQVDAESWKT 110 TPYQIACGIS 120 QGLADNTVIA 130 KVNNVVWDLD 140 RPLEEDCTLE 150 LLKFEDEEAQ 160 AVYWHSSAHI 170 MGEAMERVYG 180 GCLCYGPPIE 190 NGFYYDMYLE 200 EGGVSSNDFS 210 SLEALCKKII 220 KEKQAFERLE 230 VKKETLLAMF 240 KYNKFKCRIL 250 NEKVNTPTTT 260 VYRCGPLIDL 270 CRGPHVRHTG 280 KIKALKIHKN 290 SSTYWEGKAD 300 METLQRIYGI 310 SFPDPKMLKE 320 WEKFQEEAKN 330 RDHRKIGRDQ 340 ELYFFHELSP 350 GSCFFLPKGA 360 YIYNALIEFI 370 RSEYRKRGFQ 380 EVVTPNIFNS 390 RLWMTSGHWQ 400 HYSENMFSFE 410 VEKELFALKP 420 MNCPGHCLMF 430 DHRPRSWREL 440 PLRLADFGVL 450 HRNELSGALT 460 GLTRVRRFQQ 470 DDAHIFCAME 480 QIEDEIKGCL 490 DFLRTVYSVF 500 GFSFKLNLST 510 RPEKFLGDIE 520 VWDQAEKQLE 530 NSLNEFGEKW 540 ELNSGDGAFY 550 GPKIDIQIKD 560 AIGRYHQCAT 570 IQLDFQLPIR 580 FNLTYVSHDG 590 DDKKRPVIVH 600 RAILGSVERM 610 IAILTENYGG 620 KWPFWLSPRQ 630 VMVVPVGPTC 640 DEYAQKVRQQ 650 FHDAKFMADI 660 DLDPGCTLNK 670 KIRNAQLAQY 680 NFILVVGEKE 690 KISGTVNIRT 700 RDNKVHGERT 710 ISETIERLQQ 720 LKEFRSKQAE EEF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0004829 threonine-tRNA ligase activity
Molecular Function GO:0000049 tRNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006435 threonyl-tRNA aminoacylation

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] 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.

[3] 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.

[4] 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.

[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.