Search results for MBD1

Showing 10 results out of 10

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Species

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Compartments

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Protein (4 results from a total of 4)

Identifier: R-HSA-417134
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: MBD1: Q9UIS9
Identifier: R-HSA-4090331
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: Q9UIS9
Identifier: R-HSA-4090332
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: P63165
Identifier: R-HSA-4090416
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: P63165

Reaction (2 results from a total of 2)

Identifier: R-HSA-4090288
Species: Homo sapiens
Compartment: nucleoplasm
PIAS1,3 SUMOylates MBD1 at lysine-499 and lysine-538 of the reference sequence (lysine-450 and lysine-489 of isoform 5) with SUMO1 (Lyst et al. 2006, Uchimura et al. 2006). SUMOylated MBD1 does not form a complex with SETDB1 and does not repress transcription.
Identifier: R-HSA-6810139
Species: Homo sapiens
Compartment: nucleoplasm
In human cell lines and tissues activation of HOXA2 chromatin by retinoic acid occurs through loss of methylation at lysine-27 of histone H3 (H3K27), dissociation of polycomb repressive complexes, and gain of methylation at H3K4 (Lee et al. 2007 Supplementary, Sakamoto et al. 2007, Sessa et al. 2007). The change in chromatin may be produced by euchromatin spreading from distant 3' retinoic acid response elements. DNA methylation and MBD1 also appear to play a role in maintaining repression at HOXA2 in HeLa cells (Sakamoto et al. 2007). The histone demethylase KDM6A binds HOXA2 (Lee et al. 2007 Supplementary) and may participate in removing H3K27 methylation. KDM6A associates with histone methyltransferases KMT2C,D (MLL2,3) which may participate in methylating H3K4 in embryonal carcinoma cells (Lee et al. 2007, also observed at other HOXA genes in Lan et al. 2007). The conformation of the entire HOXA cluster in the nucleus changes during differentiation of a myeloid leukemia cell line and the conformation changes correlate with gene activity, H3K27me2,3 occurence, and proximity to CTCF binding sites (Rousseau et al. 2014, see also Lonfat and Duboule 2015).

Complex (3 results from a total of 3)

Identifier: R-HSA-4090342
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-6810133
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5617490
Species: Homo sapiens
Compartment: nucleoplasm

Pathway (1 results from a total of 1)

Identifier: R-HSA-3899300
Species: Homo sapiens
Compartment: nucleoplasm
SUMO1,2, and 3 are predominantly located in the nucleus and targets of SUMOylation are predominantly nuclear. Transcription cofactors are nuclear proteins that generally do not bind DNA themselves but interact with DNA-bound factors and influence transcription. SUMOylation of transcription cofactors usually inhibits the activity of the cofactor (reviewed in Girdwood et al. 2004, Gill 2005, Lyst and Stancheva 2007, Garcia-Dominguez and Reyes 2009). In the cases of coactivators such as PPARGC1A (PGC-1alpha) this results in decreased transcription; in the cases of corepressors such as MBD1 this results in increased transcription.
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