Search Results

Overview

Uniprot ID	Q9UJA5
Protein Name	tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6
Gene Name	TRMT6
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
145	KTEFAQDKYIKKKKK
153	YIKKKKKKYEAIITV
339	GPKERGSKKDYIQEK
340	PKERGSKKDYIQEKQ
471	LKADTSLKSNASTLE
488	ETEEPAAKKRKCPES
489	TEEPAAKKRKCPESD

Function

Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA (PubMed:16043508). Together with the TRMT61A catalytic subunit, part of a mRNA N(1)-methyltransferase complex that mediates methylation of adenosine residues at the N(1) position of a small subset of mRNAs: N(1) methylation takes place in tRNA T-loop-like structures of mRNAs and is only present at low stoichiometries (PubMed:29072297, PubMed:29107537)

Protein Sequence

10 MEGSGEQPGP 20 QPQHPGDHRI 30 RDGDFVVLKR 40 EDVFKAVQVQ 50 RRKKVTFEKQ 60 WFYLDNVIGH 70 SYGTAFEVTS 80 GGSLQPKKKR 90 EEPTAETKEA 100 GTDNRNIVDD 110 GKSQKLTQDD 120 IKALKDKGIK 130 GEEIVQQLIE 140 NSTTFRDKTE 150 FAQDKYIKKK 160 KKKYEAIITV 170 VKPSTRILSI 180 MYYAREPGKI 190 NHMRYDTLAQ 200 MLTLGNIRAG 210 NKMIVMETCA 220 GLVLGAMMER 230 MGGFGSIIQL 240 YPGGGPVRAA 250 TACFGFPKSF 260 LSGLYEFPLN 270 KVDSLLHGTF 280 SAKMLSSEPK 290 DSALVEESNG 300 TLEEKQASEQ 310 ENEDSMAEAP 320 ESNHPEDQET 330 METISQDPEH 340 KGPKERGSKK 350 DYIQEKQRRQ 360 EEQRKRHLEA 370 AALLSERNAD 380 GLIVASRFHP 390 TPLLLSLLDF 400 VAPSRPFVVY 410 CQYKEPLLEC 420 YTKLRERGGV 430 INLRLSETWL 440 RNYQVLPDRS 450 HPKLLMSGGG 460 GYLLSGFTVA 470 MDNLKADTSL 480 KSNASTLESH 490 ETEEPAAKKR KCPESDS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0031515	tRNA (m1A) methyltransferase complex
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0006397	mRNA processing
Biological Process	GO:0030488	tRNA methylation

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] 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.