This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
Facts about Histone-lysine N-methyltransferase SETD1B.
The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro.
Human | |
---|---|
Gene Name: | SETD1B |
Uniprot: | Q9UPS6 |
Entrez: | 23067 |
Belongs to: |
---|
class V-like SAM-binding methyltransferase superfamily |
EC 2.1.1; FLJ20803; histone-lysine N-methyltransferase SETD1B; hSET1B; KIAA1076EC 2.1.1.43; KMT2GSET1B; Lysine N-methyltransferase 2G; SET domain containing 1B; SET domain-containing protein 1B; Set1B
Mass (kDA):
212.803 kDA
Human | |
---|---|
Location: | 12q24.31 |
Sequence: | 12; NC_000012.12 (121803665..121832656) |
Nucleus speckle. Chromosome. Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1A, suggesting that SETD1A and SET1B each bind to a unique set of target genes.
PMID: 22927943 by Lee J.H., et al. Rbm15-Mkl1 interacts with the Setd1b histone H3-Lys4 methyltransferase via a SPOC domain that is required for cytokine- independent proliferation.
PMID: 17355966 by Lee J.-H., et al. Identification and characterization of the human Set1B histone H3- Lys4 methyltransferase complex.