Recombinant Human KMT3C / SMYD2 protein
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Recombinant Human KMT3C / SMYD2 protein is a Human Full Length protein, in the 1 to 433 aa range, expressed in Baculovirus infected Sf9 cells, with >80%, suitable for SDS-PAGE.
View Alternative Names
KMT3C, SMYD2, N-lysine methyltransferase SMYD2, HSKM-B, Histone methyltransferase SMYD2, Lysine N-methyltransferase 3C, SET and MYND domain-containing protein 2
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human KMT3C / SMYD2 protein (AB196427)
10% SDS-PAGE analysis of 4 μg ab196427 with Coomassie staining.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
KMT3C/SMYD2 plays important roles in gene regulation and cellular processes. It functions as a part of a protein complex affecting transcriptional activation and repression via chromatin remodeling. The methylation activity of SMYD2 extends to p53 an important tumor suppressor linking it to the regulation of cell cycle and apoptosis. This enzymatic activity impacts cellular growth and differentiation interfacing with the larger network of cellular gene expression control and protein function modulation.
Pathways
Research shows KMT3C/SMYD2 being active in the p53 and AKT signaling pathways fundamental to cell survival proliferation and apoptosis. In the context of the p53 pathway SMYD2 methylates p53 which may impact its tumor suppressor functions. SMYD2 also interacts with proteins like RB1 and HDAC1 integrating into broader cell regulatory networks. These interactions facilitate SMYD2's influence on pathways that govern important cellular processes such as growth and DNA damage response.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Sequence similarities
Belongs to the class V-like SAM-binding methyltransferase superfamily.
Subcellular localisation
Nucleus
Target data
Product promise
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