Search Results

Overview

Uniprot IDQ15046
Protein NameLysine--tRNA ligase
Gene NameKARS1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
141 AKRASGGKLIFYDLR
17 KVDGSEPKLSKNELK
20 GSEPKLSKNELKRRL
41 AEKEAKQKELSEKQL
519 FEEQAKAKAAGDDEA

Function

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (PubMed:18029264, PubMed:18272479, PubMed:9278442). When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages (PubMed:15851690). Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity (PubMed:14975237, PubMed:19524539, PubMed:23159739, PubMed:5338216)

Protein Sequence

10 MAAVQAAEVK 20 VDGSEPKLSK 30 NELKRRLKAE 40 KKVAEKEAKQ 50 KELSEKQLSQ 60 ATAAATNHTT 70 DNGVGPEEES 80 VDPNQYYKIR 90 SQAIHQLKVN 100 GEDPYPHKFH 110 VDISLTDFIQ 120 KYSHLQPGDH 130 LTDITLKVAG 140 RIHAKRASGG 150 KLIFYDLRGE 160 GVKLQVMANS 170 RNYKSEEEFI 180 HINNKLRRGD 190 IIGVQGNPGK 200 TKKGELSIIP 210 YEITLLSPCL 220 HMLPHLHFGL 230 KDKETRYRQR 240 YLDLILNDFV 250 RQKFIIRSKI 260 ITYIRSFLDE 270 LGFLEIETPM 280 MNIIPGGAVA 290 KPFITYHNEL 300 DMNLYMRIAP 310 ELYHKMLVVG 320 GIDRVYEIGR 330 QFRNEGIDLT 340 HNPEFTTCEF 350 YMAYADYHDL 360 MEITEKMVSG 370 MVKHITGSYK 380 VTYHPDGPEG 390 QAYDVDFTPP 400 FRRINMVEEL 410 EKALGMKLPE 420 TNLFETEETR 430 KILDDICVAK 440 AVECPPPRTT 450 ARLLDKLVGE 460 FLEVTCINPT 470 FICDHPQIMS 480 PLAKWHRSKE 490 GLTERFELFV 500 MKKEICNAYT 510 ELNDPMRQRQ 520 LFEEQAKAKA 530 AGDDEAMFID 540 ENFCTALEYG 550 LPPTAGWGMG 560 IDRVAMFLTD 570 SNNIKEVLLF 580 PAMKPEDKKE 590 NVATTDTLES TTVGTSV

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:0005615 extracellular space
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0016597 amino acid binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0003877 ATP:ADP adenylyltransferase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0004824 lysine-tRNA ligase activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0000049 tRNA binding
Biological Process GO:0002276 basophil activation involved in immune response
Biological Process GO:0015966 diadenosine tetraphosphate biosynthetic process
Biological Process GO:0070371 ERK1 and ERK2 cascade
Biological Process GO:0006430 lysyl-tRNA aminoacylation
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0002863 positive regulation of inflammatory response to antigenic stimulus
Biological Process GO:0043032 positive regulation of macrophage activation
Biological Process GO:0010165 response to X-ray
Biological Process GO:0006418 tRNA aminoacylation for protein translation
Biological Process GO:0008033 tRNA processing

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] 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] 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.

[4] 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.