Search results for ME2

Showing 24 results out of 185

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Protein (6 results from a total of 86)

Identifier: R-HSA-8936572
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: H3C1: P68431
Identifier: R-HSA-8936573
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: H3-3A: P84243
Identifier: R-HSA-3222242
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: TP53: P04637
Identifier: R-HSA-5244518
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: H3C15: Q71DI3
Identifier: R-HSA-5244526
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: H3C1: P68431
Identifier: R-HSA-4722125
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: H3C1: P68431

Complex (6 results from a total of 47)

Identifier: R-HSA-6804382
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-6804385
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5218928
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5225638
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5625791
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5682971
Species: Homo sapiens
Compartment: nucleoplasm

Set (6 results from a total of 31)

Identifier: R-HSA-5649790
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5661118
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5218942
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5211320
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5229046
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5229041
Species: Homo sapiens
Compartment: nucleoplasm

Reaction (6 results from a total of 20)

Identifier: R-HSA-2408541
Species: Homo sapiens
Compartment: cytosol
A yet to be identified enzyme with methylselenol methyltransferase (MeSeHMT) activity is involved in the methylation of methylselenol aka methaneselenol (MeSeH) into dimethyl selenide (Me2Se) in tandem with S-adenosylmethionine (AdoMet) transforming into S-adenosylhomocysteine (AdoHcy). This reaction is inferred from the event in rat (Ohta and Suzuki 2008, Hsieh and Ganther 1977).
Identifier: R-HSA-5661123
Species: Homo sapiens
Compartment: nucleoplasm
Histone demethylases (HDMs) belong to two groups with distinct catalytic mechanisms. KDM1A and KDM1B (formerly known as Lysine Specific Demethylases 1 and 2), belong to the flavin adenine dinucleotide (FAD)-dependent amino oxidase family, releasing formaldehyde. The reaction mechanism requires a protonatable lysine epsilon-amino group, not available in trimethylated lysines (Shi et al. 2004). KDM1A and subsequently KDM1B were shown to catalyse demethylation of monomethyl and dimethyl, but not trimethyl, histone H3 at lysine 5 (H3K4) in vitro (Shi et al. 2004, Ciccone et al. 2009).
Subsequently KDM1A was found to be much more proficient at catalysing demethylation of H3K4 when part of a multiprotein complex (Lee et al. 2005) and shown to catalyse demethylation of histone H3 at lysine 10 (H3K9) in vivo when associated with the androgen receptor (Metzger et al. 2007), suggesting that its substrate specificity is modulated by interacting proteins. KDM1A is a subunit of several complexes, including CtBP, Co-REST, NRD and BRAF35 (Lan et al. 2008). It is also able to catalyse demethylation of a number of non-histone proteins (Nicholson & Chen 2009).
Identifier: R-HSA-5225602
Species: Homo sapiens
Compartment: nucleoplasm
Symmetric dimethylation of histone H3 arginine-3 (H3R2) enhances binding of WDR5, a component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC (Migliori et al. 2012).
Identifier: R-HSA-4754187
Species: Homo sapiens
Compartment: nucleoplasm
All characterized lysine demethylases other than KDM1A belong to the jumonjiC domain (JmjC) containing family.The JmjC KDMs are members of the Cupin superfamily of mononuclear Fe (II) dependent oxygenases, which are characterized by the presence of a double-stranded beta-helix core fold. The JmjC KDMs require 2 oxoglutarate (2 OG) and molecular oxygen as co substrates, producing, along with formaldehyde, succinate and carbon dioxide. This hydroxylation based mechanism does not require a protonatable lysine e amine group and consequently JmjC containing demethylases are able to demethylate tri , di and monomethylated lysines.
KDM6A (UTX), KDM6B (JMJD3), KDM6C (UTY) and KDM7A (JHDM1D) catalyse the demethylation of di or tri-methylated lysine-28 of histone H3 (H3K27Me2/3) (Agger et al. 2007, Cho et al. 2007, De Santra et al. 2007, Hong et al. 2007, Lan et al. 2007, Lee et al. 2007, Horton et al. 2010, Huang et al. 2010, Walport et al. 2014).
Identifier: R-HSA-5661114
Species: Homo sapiens
Compartment: nucleoplasm
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).
Identifier: R-HSA-4724279
Species: Homo sapiens
Compartment: nucleoplasm
All characterized lysine demethylases other than KDM1A belong to the jumonjiC domain (JmjC) containing family.The JmjC KDMs are members of the Cupin superfamily of mononuclear Fe (II) dependent oxygenases, which are characterized by the presence of a double-stranded beta-helix core fold. The JmjC KDMs require 2 oxoglutarate (2 OG) and molecular oxygen as co substrates, producing, along with formaldehyde, succinate and carbon dioxide. This hydroxylation based mechanism does not require a protonatable lysine e amine group and consequently JmjC containing demethylases are able to demethylate tri , di and monomethylated lysines.
KDM4A-D (JMJD2A-D/JHDM3A-D) catalyse the demethylation of di- or tri-methylated histone H3 at lysine-10 (H3K9Me2/3) (Cloos et al. 2006, Fodor et al. 2006, Whetstine et al. 2007), with a strong preference for Me3 (Whetstine et al. 2007). MINA, a bifunctional histone lysine demethylase and ribosomal histidine hydroxylase, demethylates trimethylated lysine-10 of histone H3 (Lu et al. 2009). KDM4A (JHDM3A) can also demethylate lysine-37 of histone H3 (H3K36Me2/3) (Klose et al. 2006).
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