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SET and MYND domain containing 2

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Target not currently curated in GtoImmuPdb

Target id: 2714

Nomenclature: SET and MYND domain containing 2

Family: 2.1.1.43 Histone methyltransferases (HMTs)

Gene and Protein Information Click here for help
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 433 1q32.3 SMYD2 SET and MYND domain containing 2
Mouse - 433 1 H6 Smyd2 SET and MYND domain containing 2
Rat - 433 13q27 Smyd2 SET and MYND domain containing 2
Previous and Unofficial Names Click here for help
KMT3C
Database Links Click here for help
BRENDA
CATH/Gene3D
ChEMBL Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
KEGG Gene
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RefSeq Protein
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Selected 3D Structures Click here for help
Image of receptor 3D structure from RCSB PDB
Description:  Structural basis of substrate methylation and Inhibition of SMYD2.
PDB Id:  3S7B
Ligand:  AZ505
Resolution:  2.42Å
Species:  Human
References:  2
Enzyme Reaction Click here for help
EC Number: 2.1.1.43

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Inhibitors
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
LLY-507 Small molecule or natural product Primary target of this compound Ligand has a PDB structure Hs Inhibition >7.8 pIC50 3
pIC50 >7.8 (IC50 <1.5x10-8 M) [3]
BAY-598 Small molecule or natural product Primary target of this compound Ligand has a PDB structure Hs Inhibition 7.6 pIC50 4
pIC50 7.6 (IC50 2.7x10-8 M) [4]
Description: Measuring inhibition of methylation of p53K370 in vitro
AZ505 Small molecule or natural product Ligand has a PDB structure Hs Inhibition 6.9 pIC50 2
pIC50 6.9 (IC50 1.2x10-7 M) [2]
General Comments
SMYD2 methylates histone and non-histone proteins. The enzyme methylates histone H3 ' at lusine 4 (H3K4me) and dimethylates histone H3 at lysine 36 (H3K36me2) [1]. SMYD2 modulation of chromatin structure is reported to modulate cell proliferation [1].

References

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1. Brown MA, Sims 3rd RJ, Gottlieb PD, Tucker PW. (2006) Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol. Cancer, 5: 26. [PMID:16805913]

2. Ferguson AD, Larsen NA, Howard T, Pollard H, Green I, Grande C, Cheung T, Garcia-Arenas R, Cowen S, Wu J et al.. (2011) Structural basis of substrate methylation and inhibition of SMYD2. Structure, 19 (9): 1262-73. [PMID:21782458]

3. SGC. LLY-507: A chemical probe for SMYD2 protein lysine methyltransferase. Accessed on 03/03/2015. Modified on 03/03/2015. thesgc.org, http://www.thesgc.org/chemical-probes/LLY-507

4. Structural Genomics Consortium. BAY-598 A selective chemical probe for SMYD2. Accessed on 11/12/2015. Modified on 11/12/2015. The Structural Genomics Consortium, http://www.thesgc.org/chemical-probes/BAY-598

How to cite this page

2.1.1.43 Histone methyltransferases (HMTs): SET and MYND domain containing 2. Last modified on 11/12/2015. Accessed on 21/10/2020. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2714.