TRMT112 Protein, Human (His-SUMO)

TRMT112 Protein activates various methyltransferases for rRNA, tRNA, and protein modifications. Partnering with BUD23, it methylates 18S rRNA's guanine N(7). With N6AMT1/HEMK2, it catalyzes N5-methylation of ETF1 on 'Gln-185' and monomethylates 'Lys-12' of histone H4 (H4K12me1). Collaborating with ALKBH8, TRMT112 methylates 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine in specific tRNA species. With THUMPD3, it contributes to N(2)-methylguanosine formation in various tRNA substrates. TRMT112 and METTL5 methylate adenine's 6th position in 18S rRNA. Its involvement in pre-rRNA processing aids small-subunit rRNA production, and diverse interactions with BUD23, N6AMT1/HEMK2, ALKBH8, and METTL5 highlight its regulatory functions. Interactions with THUMPD3, THUMPD2, and TRMT11 underscore its intricate role in these processes. TRMT112 Protein, Human (His-SUMO) is the recombinant human-derived TRMT112 protein, expressed by E. coli, with N-His, N-SUMO labeled tag. The total length of TRMT112 Protein, Human (His-SUMO) is 125 a.a., with molecular weight of ~30.2 kDa.

TRMT112 protein serves as an activator for a diverse range of methyltransferases involved in rRNA, tRNA, and protein modifications. Teaming up with methyltransferase BUD23, it methylates the N(7) position of a guanine in 18S rRNA, while in collaboration with N6AMT1/HEMK2, it catalyzes N5-methylation of ETF1 on 'Gln-185' and monomethylates 'Lys-12' of histone H4 (H4K12me1). Additionally, in conjunction with ALKBH8, TRMT112 participates in the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in specific tRNA species. Partnering with methyltransferase THUMPD3, it contributes to the formation of N(2)-methylguanosine in various tRNA substrates. Furthermore, TRMT112, along with METTL5, plays a crucial role in methylating the 6th position of adenine in position 1832 of 18S rRNA. Its involvement in pre-rRNA processing contributes to small-subunit rRNA production, and the formation of various heterodimers with BUD23, N6AMT1/HEMK2, ALKBH8, and METTL5 highlights its diverse regulatory functions in various methylation pathways. Interactions with THUMPD3, THUMPD2, and TRMT11 further underscore its intricate role in these processes.

Human

E. coli

N-His;N-SUMO

Q9UI30 (1M-125S)

51504  [NCBI]

MKLLTHNLLSSHVRGVGSRGFPLRLQATEVRICPVEFNPNFVARMIPKVEWSAFLEAADNLRLIQVPKGPVEGYEENEEFLRTMHHLLLEVEVIEGTLQCPESGRMFPISRGIPNMLLSEEETES

Approximately 30.2 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.