Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Name Email address

Details on Person Methylation of histone H3 lysine-37 (H3K36) is tightly assoc...

Class:IdSummation:5638331
_displayNameMethylation of histone H3 lysine-37 (H3K36) is tightly assoc...
_timestamp2016-07-04 13:07:15
created[InstanceEdit:5638320] Jupe, Steve, 2014-11-13
literatureReference[LiteratureReference:5638145] Understanding the language of Lys36 methylation at histone H3
[LiteratureReference:3301907] The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate
[LiteratureReference:5173306] NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming
[LiteratureReference:5638155] 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
[LiteratureReference:5638166] The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation
[LiteratureReference:8876769] Trithorax-group protein ASH1 methylates histone H3 lysine 36
[LiteratureReference:8876764] Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism
[LiteratureReference:8876779] Ash1l methylates Lys36 of histone H3 independently of transcriptional elongation to counteract polycomb silencing
[LiteratureReference:8876739] Histone methyltransferase Ash1L mediates activity-dependent repression of neurexin-1α
modified[InstanceEdit:5651814] Jupe, Steve, 2014-11-25
[InstanceEdit:5669201] Jupe, Steve, 2015-01-30
[InstanceEdit:5674398] Jupe, Steve, 2015-02-12
[InstanceEdit:8878382] Jupe, Steve, 2016-07-04
textMethylation 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). ASH1L can perform histone H3 lysine-37 di-methylation (Tanaka et al. 2007, An et al. 2011, Miyazaki et al. 2013, Zhu et al. 2016).
(summation)[Reaction:5638157] WHSC1 (KMT3G), NSD1 (KMT3B), SMYD2 (KMT3C), ASH1L methylate methyl-lysine-37 of histone H3 (H3K36) [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by Methylation of histone H3 lysine-37 (H3K36) is tightly assoc... (5638331)
Follow Reactome