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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.


L3MBTL2, h-l(3)mbt-like, L(3)mbt-like 2
Top mentioned proteins: Histone, Polycomb, PRC1, RU1, TDG
Papers on L3MBTL2
Acquired genetic alterations in tumor cells dictate the development of high-risk neuroblastoma and clinical outcomes.
Aravindan et al., Oklahoma City, United States. In Bmc Cancer, 2014
Array CGH analysis of individual clones of MSDACs revealed genetic alterations in chromosomes 1, 7, 8, and 22, corresponding to a gain in the copy numbers of LOC100288142, CD1C, CFHR3, FOXP2, MDFIC, RALYL, CSMD3, SAMD12-AS1, and MAL2, and a loss in ADAM5, LOC400927, APOBEC3B, RPL3, MGAT3, SLC25A17, EP300, L3MBTL2, SERHL, POLDIP3, A4GALT, and TTLL1.
SUMOylation of the polycomb group protein L3MBTL2 facilitates repression of its target genes.
Suske et al., Braunschweig, Germany. In Nucleic Acids Res, 2014
Lethal(3) malignant brain tumour like 2 (L3MBTL2) is an integral component of the polycomb repressive complex 1.6 (PRC1.6)
A screen for hydroxymethylcytosine and formylcytosine binding proteins suggests functions in transcription and chromatin regulation.
Reik et al., In Genome Biol, 2012
Only a few proteins were identified with a preference for 5hmC (such as RPL26, PRP8 and the DNA mismatch repair protein MHS6), but proteins with a strong preference for 5fC were more numerous, including transcriptional regulators (FOXK1, FOXK2, FOXP1, FOXP4 and FOXI3), DNA repair factors (TDG and MPG) and chromatin regulators (EHMT1, L3MBTL2 and all components of the NuRD complex).
L3MBTL2 protein acts in concert with PcG protein-mediated monoubiquitination of H2A to establish a repressive chromatin structure.
Reinberg et al., New York City, United States. In Mol Cell, 2011
Our findings highlight a PcG/L3MBTL2 collaboration that attains repressive chromatin without entailing histone lysine methylation marks.
Histone deacetylase 3 is selectively involved in L3MBTL2-mediated transcriptional repression.
Yoon et al., South Korea. In Febs Lett, 2010
This is the first report that L(3)mbt-like 2 (L3MBTL2) specifically interacts with the histone deacetylase domain of histone deacetylase 3 (HDAC3) via its MBT domain.
SUMO engages multiple corepressors to regulate chromatin structure and transcription.
Gill et al., Boston, United States. In Epigenetics, 2009
A surprising diversity of proteins has been identified to be recruited to promoters in a SUMO-dependent manner, including the histone deacetylase HDAC2, the histone demethylase LSD1, the histone methyltransferase SETDB1, the nucleosome remodeling ATPase Mi-2, and chromatin-associated proteins HP1 and L3MBTL1 and L3MBTL2.
Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2.
Min et al., Toronto, Canada. In Nucleic Acids Res, 2009
High-resolution crystallographic analysis of the four MBT repeats of L3MBTL2 reveals its unique asymmetric rhomboid architecture, as well as binding mechanism, which preclude the interaction of the first three MBT repeats with methylated peptides.
Solution structure of the FCS zinc finger domain of the human polycomb group protein L(3)mbt-like 2.
Bycroft et al., Cambridge, United Kingdom. In Protein Sci, 2009
determination of the solution structure of the FCS zinc finger of L3MBTL2; structure consists of a beta-hairpin followed by an alpha-helix; structure is consistent with the proposal that FCS zinc fingers bind to regulatory RNAs
Structural studies of a four-MBT repeat protein MBTD1.
Min et al., Toronto, Canada. In Plos One, 2008
The crystal structure of MBTD1 reveals its similarity to another four-MBT-repeat protein L3MBTL2, which binds lower methylated lysine histones.
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