WHSC1 (KMT3G), NSD1 (KMT3B), SMYD2 (KMT3C) methylate lysine-37 of histone H3 (H3K36)

Stable Identifier
R-HSA-4827383
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
WHSC1, NSD1, SMYD2 methylate lysine-37 of histone H3
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Methylation of histone H3 lysine-37 (H3K36) is tightly associated with actively transcribed genes and appears to correspond primarily with coding regions (Wagner & Carpenter 2011).

WHSC1 (KMT3G, NSD2, MMSET), a member of the SET2 family, dimethylates H3K36 when provided with nucleosome substrates (Li et al 2009; Qiao et al. 2011). Dimethylation of histone H3 at lysine-37 (H3K36me2) is thought to be the principal chromatin-regulatory activity of WHSC1 (Kuo et al. 2011), SMYD2 (KMT3C) (Brown et al 2006) and NSD1 (KMT3B) (Li et al. 2009, Qiao et al. 2011).

Literature References
PubMed ID Title Journal Year
22099308 NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming

Kuo, AJ, Cheung, P, Chen, K, Zee, BM, Kioi, M, Lauring, J, Xi, Y, Park, BH, Shi, X, Garcia, BA, Li, W, Gozani, O

Mol. Cell 2011
16805913 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

Brown, MA, Sims, RJ, Gottlieb, PD, Tucker, PW

Mol. Cancer 2006
19808676 The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate

Li, Y, Trojer, P, Xu, CF, Cheung, P, Kuo, A, Drury, WJ, Qiao, Q, Neubert, TA, Xu, RM, Gozani, O, Reinberg, D

J. Biol. Chem. 2009
21196496 The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation

Qiao, Q, Li, Y, Chen, Z, Wang, M, Reinberg, D, Xu, RM

J. Biol. Chem. 2011
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
histone-lysine N-methyltransferase activity of WHSC1, NSD1, SMYD2, ASH1L [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
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