Identification of the MLL2 complex as a coactivator for estrogen receptor alpha (Q24316007)

ASH2 like, histone lysine methyltransferase complex subunit

GOA release 2020-03-11

1 reference

Lysine methyltransferase 2D

GOA release 2020-03-11

1 reference

Journal of Biological Chemistry

GOA release 2020-03-11

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Rigen Mo

1

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Sambasiva M Rao

series ordinal

2

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Yi-Jun Zhu

series ordinal

3

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language of work or name

English

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publication date

9 June 2006

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published in

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volume

281

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issue

23

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page(s)

15714-20

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cites work

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The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro

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p300 is a component of an estrogen receptor coactivator complex

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Ligand-selective potentiation of rat mineralocorticoid receptor activation function 1 by a CBP-containing histone acetyltransferase complex

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Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities

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Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae

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Translating the Histone Code

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The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion

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Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins

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Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus

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The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4

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ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation

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Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF

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Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression

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Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha

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Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function

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Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

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Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription

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Menin and MLL cooperatively regulate expression of cyclin-dependent kinase inhibitors

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MLL targets SET domain methyltransferase activity to Hox gene promoters

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AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer

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EWS and ATF-1 gene fusion induced by t(12;22) translocation in malignant melanoma of soft parts

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The hormone-binding domains of the estrogen and glucocorticoid receptors contain an inducible transcription activation function

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inferred from DOI database lookup

7 January 2021

based on heuristic

Catalogue of chromosome aberrations in cancer

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