Recombinant Human METTL11A protein (His tag) is a Human Full Length protein, in the 1 to 223 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by NTMT2-mediated monomethylation (PubMed:24090352). Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.
C9orf32, METTL11A, NRMT, NRMT1, AD-003, NTMT1, N-terminal Xaa-Pro-Lys N-methyltransferase 1, Alpha N-terminal protein methyltransferase 1A, Methyltransferase-like protein 11A, N-terminal RCC1 methyltransferase, X-Pro-Lys N-terminal protein methyltransferase 1A, NTM1A
Recombinant Human METTL11A protein (His tag) is a Human Full Length protein, in the 1 to 223 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.32% Tris HCl
ab211312 was purified using conventional chromatography techniques.
Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by NTMT2-mediated monomethylation (PubMed:24090352). Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.
Belongs to the methyltransferase superfamily. NTM1 family.
METTL11A also known as PCMT1 or methyltransferase-like protein 11A functions mechanically as a protein methyltransferase specifically responsible for the methylation of the N-terminal alpha-amino group on proteins. This methylation process affects the function and stability of target proteins. METTL11A exhibits a molecular mass of approximately 32 kDa. It is widely expressed in human tissues particularly in the liver and brain indicating its important role in different physiological contexts.
The enzyme influences protein interactions by modifying proteins at the molecular level impacting their stability and function. METTL11A contributes to various processes including protein repair and turnover mechanisms. It may operate independently or within larger protein complexes though further research is necessary to identify specific complex partners. This enzymatic activity is fundamental for maintaining protein homeostasis and ensuring proper cellular function.
METTL11A engages in the protein methylation pathway which is vital for regulating protein function and interactions. This pathway often involves other key proteins such as PCMT1 that work together to methylate proteins and modify their activities. Additionally METTL11A plays a significant role in the protein repair pathway where it repairs damaged proteins assisting in the prevention of cellular stress and damage.
METTL11A could have implications in neurological disorders like Alzheimer's disease. Alzheimer's has been linked to disrupted protein metabolism where the absence or malfunction of METTL11A activity affects protein stability and accumulation. Furthermore METTL11A's interactions with proteins such as PCMT1 might complicate the protein methylation processes potentially contributing to liver disease by disrupting normal cellular protein functions in the liver emphasizing the importance of METTL11A in disease contexts.
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15% SDS-PAGE analysis of ab211312 (3 μg).
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