Search Results

Overview

Uniprot IDP41250
Protein NameGlycine--tRNA ligase
Gene NameGARS1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
108 RKRVLEAKELALQPK
115 KELALQPKDDIVDRA
197 KTSGHVDKFADFMVK
219 FRADHLLKAHLQKLM
230 QKLMSDKKCSVEKKS
426 KVGISPDKLRFRQHM
477 SCHARATKVPLVAEK
484 KVPLVAEKPLKEPKT
487 LVAEKPLKEPKTVNV
501 VVQFEPSKGAIGKAY
506 PSKGAIGKAYKKDAK
733 FEGQETGKKETIEE*
734 EGQETGKKETIEE**
85 VRKLKEDKAPQVDVD
93 APQVDVDKAVAELKA
99 DKAVAELKARKRVLE

Function

Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP) (PubMed:17544401, PubMed:24898252, PubMed:28675565). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis (PubMed:19710017)

Protein Sequence

10 MPSPRPVLLR 20 GARAALLLLL 30 PPRLLARPSL 40 LLRRSLSAAS 50 CPPISLPAAA 60 SRSSMDGAGA 70 EEVLAPLRLA 80 VRQQGDLVRK 90 LKEDKAPQVD 100 VDKAVAELKA 110 RKRVLEAKEL 120 ALQPKDDIVD 130 RAKMEDTLKR 140 RFFYDQAFAI 150 YGGVSGLYDF 160 GPVGCALKNN 170 IIQTWRQHFI 180 QEEQILEIDC 190 TMLTPEPVLK 200 TSGHVDKFAD 210 FMVKDVKNGE 220 CFRADHLLKA 230 HLQKLMSDKK 240 CSVEKKSEME 250 SVLAQLDNYG 260 QQELADLFVN 270 YNVKSPITGN 280 DLSPPVSFNL 290 MFKTFIGPGG 300 NMPGYLRPET 310 AQGIFLNFKR 320 LLEFNQGKLP 330 FAAAQIGNSF 340 RNEISPRSGL 350 IRVREFTMAE 360 IEHFVDPSEK 370 DHPKFQNVAD 380 LHLYLYSAKA 390 QVSGQSARKM 400 RLGDAVEQGV 410 INNTVLGYFI 420 GRIYLYLTKV 430 GISPDKLRFR 440 QHMENEMAHY 450 ACDCWDAESK 460 TSYGWIEIVG 470 CADRSCYDLS 480 CHARATKVPL 490 VAEKPLKEPK 500 TVNVVQFEPS 510 KGAIGKAYKK 520 DAKLVMEYLA 530 ICDECYITEM 540 EMLLNEKGEF 550 TIETEGKTFQ 560 LTKDMINVKR 570 FQKTLYVEEV 580 VPNVIEPSFG 590 LGRIMYTVFE 600 HTFHVREGDE 610 QRTFFSFPAV 620 VAPFKCSVLP 630 LSQNQEFMPF 640 VKELSEALTR 650 HGVSHKVDDS 660 SGSIGRRYAR 670 TDEIGVAFGV 680 TIDFDTVNKT 690 PHTATLRDRD 700 SMRQIRAEIS 710 ELPSIVQDLA 720 NGNITWADVE 730 ARYPLFEGQE TGKKETIEE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030424 axon
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0030141 secretory granule
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0141192 ATP:ATP adenylyltransferase activity
Molecular Function GO:0004081 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
Molecular Function GO:0004820 glycine-tRNA ligase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0046983 protein dimerization activity
Biological Process GO:0015966 diadenosine tetraphosphate biosynthetic process
Biological Process GO:0070150 mitochondrial glycyl-tRNA aminoacylation
Biological Process GO:0006418 tRNA aminoacylation for protein translation

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] 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.

[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] 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.

[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.