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.
Details on Person All characterised lysine demethylases other than KDM1A belon...
| Class:Id | Summation:4722129 |
|---|---|
| _displayName | All characterised lysine demethylases other than KDM1A belon... |
| _timestamp | 2018-12-19 16:39:46 |
| created | [InstanceEdit:4722136] Jupe, S, 2013-10-22 |
| literatureReference | [LiteratureReference:3214867] Histone demethylation by a family of JmjC domain-containing proteins [LiteratureReference:4687034] The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36 |
| modified | [InstanceEdit:4722138] Jupe, S, 2013-10-22 [InstanceEdit:4724281] Jupe, S, 2013-10-23 [InstanceEdit:4960918] Garapati, P V, 2013-11-04 [InstanceEdit:5423073] Jupe, Steve, 2014-05-08 [InstanceEdit:8862791] Jupe, Steve, 2016-03-01 [InstanceEdit:9632255] D'Eustachio, Peter, 2018-12-17 [InstanceEdit:9632432] D'Eustachio, Peter, 2018-12-18 [InstanceEdit:9632433] D'Eustachio, Peter, 2018-12-18 [InstanceEdit:9632519] D'Eustachio, Peter, 2018-12-19 |
| text | All characterised lysine demethylases other than KDM1A belong to the jumonji C-domain (JmjC) containing family, members of the Cupin superfamily of mononuclear Fe (II)-dependent oxygenases. They require 2-oxoglutarate (2-OG) and molecular oxygen as co-substrates, producing succinate and carbon dioxide. This hydroxylation-based mechanism does not require a protonatable lysine epsilon-amine group and consequently JmjC-containing demethylases are able to demethylate tri-, di- and monomethylated lysines. The first reported JmjC-containing demethylases were KDM2A and KDM2B (JHDM1A/B, FBXL11/10). These demethylate lysine-37 of histone H3 when mono- or di-methylated (H3K36Me1/2) (Tsukada et al. 2006). KDM4A (JHDM3A) can demethylate mono-, di and trimethylated lysine-37 of histone H3 (Klose et al. 2006). KDM8 was initially thought to demethylate dimethylated lysine-37 of histone H3 (Hsia et al. 2010) but later work indicates that, consistent with its closer structural similarity to JmjC hydroxylases, the enzyme lacks histone demethylase activity and rather hydroxylates arginine residues of proteins RPS6 and RCCD1 (Wilkins et al. 2018). |
| (summation) | [Reaction:5661114] KDM2A, KDM2B, KDM4A demethylate Me2K37-histone H3 [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by All characterised lysine demethylases other than KDM1A belon... (4722129)
