Search Results

Overview

Uniprot IDP14868
Protein NameAspartate--tRNA ligase, cytoplasmic
Gene NameDARS1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
453 GIDLEKIKAYIDSFR
9 PSASASRKSQEKPRE

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

Protein Sequence

10 MPSASASRKS 20 QEKPREIMDA 30 AEDYAKERYG 40 ISSMIQSQEK 50 PDRVLVRVRD 60 LTIQKADEVV 70 WVRARVHTSR 80 AKGKQCFLVL 90 RQQQFNVQAL 100 VAVGDHASKQ 110 MVKFAANINK 120 ESIVDVEGVV 130 RKVNQKIGSC 140 TQQDVELHVQ 150 KIYVISLAEP 160 RLPLQLDDAV 170 RPEAEGEEEG 180 RATVNQDTRL 190 DNRVIDLRTS 200 TSQAVFRLQS 210 GICHLFRETL 220 INKGFVEIQT 230 PKIISAASEG 240 GANVFTVSYF 250 KNNAYLAQSP 260 QLYKQMCICA 270 DFEKVFSIGP 280 VFRAEDSNTH 290 RHLTEFVGLD 300 IEMAFNYHYH 310 EVMEEIADTM 320 VQIFKGLQER 330 FQTEIQTVNK 340 QFPCEPFKFL 350 EPTLRLEYCE 360 ALAMLREAGV 370 EMGDEDDLST 380 PNEKLLGHLV 390 KEKYDTDFYI 400 LDKYPLAVRP 410 FYTMPDPRNP 420 KQSNSYDMFM 430 RGEEILSGAQ 440 RIHDPQLLTE 450 RALHHGIDLE 460 KIKAYIDSFR 470 FGAPPHAGGG 480 IGLERVTMLF 490 LGLHNVRQTS 500 MFPRDPKRLT P

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:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0045202 synapse
Molecular Function GO:0004046 aminoacylase activity
Molecular Function GO:0004815 aspartate-tRNA ligase activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006422 aspartyl-tRNA aminoacylation
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0006412 translation
Biological Process GO:0006418 tRNA aminoacylation for protein translation

Reference

[1] 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.

[2] 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.