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ProSeAM SILAC MS screening for CARNMT1 substrates

ABSTRACT: Click chemistry based substrates screening for CARNMT1 in Carnmt1 KO HEK293T cells.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Yoichi Shinkai

PROVIDER: PXD037965 | JPOST Repository | Thu Aug 24 00:00:00 BST 2023

REPOSITORIES: jPOST

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			Action	DRS
	191101_QE_215_Shimazu_B.raw	Raw
	191101_QE_215_Shimazu_C.raw	Raw
	200803_QE_071_Shimazu_A.raw	Raw
	200803_QE_071_Shimazu_B.raw	Raw
	CARNMT1-ProSeAM-SILAC%20result.xlsx	Xlsx

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Publications

Histidine N1-position-specific methyltransferase CARNMT1 targets C3H zinc finger proteins and modulates RNA metabolism.

Shimazu Tadahiro T Yoshimoto Rei R Kotoshiba Kaoru K Suzuki Takehiro T Matoba Shogo S Hirose Michiko M Akakabe Mai M Sohtome Yoshihiro Y Sodeoka Mikiko M Ogura Atsuo A Dohmae Naoshi N Shinkai Yoichi Y

Genes & development 20230823 15-16

Histidine (His) residues are methylated in various proteins, but their roles and regulation mechanisms remain unknown. Here, we show that carnosine N-methyltransferase 1 (CARNMT1), a known His methyltransferase of dipeptide carnosine (βAla-His), is a major His N1-position-specific methyltransferase. We found that 52 His sites in 20 proteins underwent CARNMT1-mediated methylation. The consensus methylation site for CARNMT1 was identified as Cx(F/Y)xH, a C3H zinc finger (C3H ZF) motif. CARNMT1-def ...[more]

PMID: 37612136

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