METTL11A Protein, Human

The METTL11A protein methylates the N-terminus of target proteins, specifically catalyzing monomethylation, dimethylation, or trimethylation of exposed α-amino groups in the [Ala/Gly/Ser]-Pro-Lys motif. METTL11A Protein, Human is the recombinant human-derived METTL11A protein, expressed by E. coli.

METTL11A protein functions as a distributive alpha-N-methyltransferase, exhibiting the capability to methylate the N-termini of target proteins that contain the specific N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys upon cleavage of the initiator methionine. This enzymatic activity results in mono-, di-, or tri-methylation of the exposed alpha-amino group of Ala, Gly, or Ser residues in the [Ala/Gly/Ser]-Pro-Lys motif, as well as mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some substrates may undergo priming by NTMT2-mediated monomethylation. METTL11A is responsible for the trimethylation of the N-terminal Gly in CENPA after the removal of Met-1 and plays a crucial role in the N-terminal methylation of various proteins, including KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A, and SET. During mitosis, METTL11A is required for normal bipolar spindle formation and chromosome segregation, exerting its effects through its action on RCC1. These diverse methylation activities highlight METTL11A's role in regulating crucial cellular processes and protein functions.

Human

E. coli

Tag Free

Q9BV86-1 (T2-R223)

28989  [NCBI]

Partial

TSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR

Approximately 25.5 kDa,based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.