Literature summary for 2.1.1.348 extracted from

Du, Y.; Hou, G.; Zhang, H.; Dou, J.; He, J.; Guo, Y.; Li, L.; Chen, R.; Wang, Y.; Deng, R.; Huang, J.; Jiang, B.; Xu, M.; Cheng, J.; Chen, G.Q.; Zhao, X.; Yu, J.
SUMOylation of the m6A-RNA methyltransferase METTL3 modulates its function (2018), Nucleic Acids Res., 46, 5195-5208 .

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Protein Variants

Protein Variants	Comment	Organism
K177R/K211R/K212R/K215R	mutation in subunit METTL3. SUMOylation of the mutant is reduced compared to that of METTL3 wild-type in H1299 stable cell lines	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q86U44 and Q9HCE5	Q86U44 i.e. catalytic subunit METTL3, Q9HCE5 i.e non-catalytic subunit METTL14	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
sumoylation	METTL3 is modified by SUMO1 mainly at lysine residues K177, K211, K212 and K215, which can be reduced by an SUMO1-specific protease SENP1. SUMOylation of METTL3 does not alter its stability, localization and interaction with METTL14 and WTAP, but significantly represses its m6A methytransferase activity resulting in the decrease of m6A levels in mRNAs	Homo sapiens

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Release 2023.1 (January 2023)