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

Bromodomain and PHD finger containing, 1

BR140, Brpf1, bromodomain containing protein,, Br140 protein
The protein encoded by this gene is expressed ubiquitously and at the highest level in testes and spermatogonia. The protein is localized within nuclei, and it is very similar in structure to two zinc finger proteins, AF10 and AF17. It is suggested that these proteins form a family of regulatory proteins. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Histone, histone acetyltransferase, N-acetyl-beta-D-glucosaminidase, CAN, ACID
Papers on BR140
Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation.
New
Kutateladze et al., Aurora, United States. In Nucleic Acids Res, Feb 2016
BRPF1 (bromodomain PHD finger 1) is a core subunit of the MOZ histone acetyltransferase (HAT) complex, critical for normal developmental programs and implicated in acute leukemias.
Phenoscape: Identifying Candidate Genes for Evolutionary Phenotypes.
New
Westerfield et al., Saskatoon, Canada. In Mol Biol Evol, Jan 2016
The experimental results were consistent with the hypotheses that these features evolved through disruption in developmental pathways at, or upstream of, brpf1 and eda/edar for the ancestral losses of basihyal element and scales, respectively.
The chromatin regulator BRPF3 preferentially activates the HBO1 acetyltransferase but is dispensable for mouse development and survival.
New
Yang et al., Canada. In J Biol Chem, Jan 2016
This is in stark contrast to Brpf1 and Brpf2, whose loss causes lethality at E9.5 and E15.5, respectively.
MOZ and MORF acetyltransferases: Molecular interaction, animal development and human disease.
Review
New
Yang, Montréal, Canada. In Biochim Biophys Acta, Aug 2015
They form tetrameric complexes with BRPF1 (bromodomain- and PHD finger-containing protein 1) and two small non-catalytic subunits.
Structure-Guided Design of IACS-9571, a Selective High-Affinity Dual TRIM24-BRPF1 Bromodomain Inhibitor.
New
Andersen et al., Houston, United States. In J Med Chem, Aug 2015
UNASSIGNED: The bromodomain containing proteins TRIM24 (tripartite motif containing protein 24) and BRPF1 (bromodomain and PHD finger containing protein 1) are involved in the epigenetic regulation of gene expression and have been implicated in human cancer.
The chromatin regulator Brpf1 regulates embryo development and cell proliferation.
New
Yang et al., Montréal, Canada. In J Biol Chem, Jun 2015
BRPF1 (bromodomain- and PHD finger-containing protein 1) is a unique chromatin regulator possessing two PHD fingers, one bromodomain and a PWWP domain for recognizing multiple histone modifications.
Deficiency of the chromatin regulator BRPF1 causes abnormal brain development.
New
Yang et al., Montréal, Canada. In J Biol Chem, Apr 2015
The multivalent chromatin regulator BRPF1 (bromodomain- and plant homeodomain-linked (PHD) zinc finger-containing protein 1) recognizes different epigenetic marks and activates three histone acetyltransferases, so it is both a reader and a co-writer of the epigenetic language.
The lysine acetyltransferase activator Brpf1 governs dentate gyrus development through neural stem cells and progenitors.
New
Yang et al., Montréal, Canada. In Plos Genet, Mar 2015
Bromodomain- and PHD finger-containing protein 1 (BRPF1) is a multidomain histone binder and a master activator of three lysine acetyltransferases, MOZ, MORF and HBO1, which are also known as KAT6A, KAT6B and KAT7, respectively.
1,3-Dimethyl Benzimidazolones Are Potent, Selective Inhibitors of the BRPF1 Bromodomain.
Watson et al., Heidelberg, Germany. In Acs Med Chem Lett, 2014
Here, we report the discovery, binding mode, and structure-activity relationship (SAR) of the first potent, selective series of inhibitors of the BRPF1 bromodomain.
Structural insights into recognition of acetylated histone ligands by the BRPF1 bromodomain.
Glass et al., Colchester, United States. In Febs Lett, 2014
Bromodomain-PHD finger protein 1 (BRPF1) is part of the MOZ HAT complex and contains a unique combination of domains typically found in chromatin-associated factors, which include plant homeodomain (PHD) fingers, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain.
The MOZ histone acetyltransferase in epigenetic signaling and disease.
Review
Glass et al., Colchester, United States. In J Cell Physiol, 2014
It functions as a quaternary complex with the bromodomain PHD finger protein 1 (BRPF1), the human Esa1-associated factor 6 homolog (hEAF6), and the inhibitor of growth 5 (ING5).
Crystallization and preliminary X-ray diffraction analysis of the BRPF1 bromodomain in complex with its H2AK5ac and H4K12ac histone-peptide ligands.
Glass et al., Colchester, United States. In Acta Crystallogr Sect F Struct Biol Commun, 2014
The bromodomain-PHD finger protein 1 (BRPF1) is an essential subunit of the monocytic leukemia zinc (MOZ) histone acetyltransferase (HAT) complex and is required for complex formation and enzymatic activation.
Expression atlas of the multivalent epigenetic regulator Brpf1 and its requirement for survival of mouse embryos.
Yang et al., Montréal, Canada. In Epigenetics, 2014
Bromodomain- and PHD finger-containing protein 1 (BRPF1) is a unique epigenetic regulator that contains multiple structural domains for recognizing different chromatin modifications.
Molecular insights into the recognition of N-terminal histone modifications by the BRPF1 bromodomain.
Glass et al., Colchester, United States. In J Mol Biol, 2014
The MOZ HAT functions as a quaternary complex with the bromodomain-PHD finger protein 1 (BRPF1), inhibitor of growth 5 (ING5), and hEaf6 subunits.
Bromodomain-PHD finger protein 1 is critical for leukemogenesis associated with MOZ-TIF2 fusion.
Kitabayashi et al., Tokyo, Japan. In Int J Hematol, 2014
To assess the functional role of HOX upregulation in leukemogenesis by MOZ-TIF2, we focused on bromodomain-PHD finger protein 1 (BRPF1), a component of the MOZ complex that carries out histone acetylation for generating and maintaining proper epigenetic programs in hematopoietic cells.
Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1.
GeneRIF
Bycroft et al., Cambridge, United Kingdom. In Nat Struct Mol Biol, 2010
Identified is the PWWP domain of bromo and plant homeodomain (PHD) finger-containing protein 1 (BRPF1) as a histone H3 (H3K36me3) binding module; determined is the structure of this domain in complex with an H3K36me3-derived peptide.
The multidomain protein Brpf1 binds histones and is required for Hox gene expression and segmental identity.
GeneRIF
Hammerschmidt et al., Freiburg, Germany. In Development, 2008
Data conclude that Brpf1, coordinated by its particular set of domains, acts by multiple mechanisms to mediate Moz-dependent histone acetylation and to mark Hox genes for maintained expression throughout vertebrate development.
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