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

Ankyrin repeat, family A

Top mentioned proteins: BLS, Histone, RFX5, histone deacetylase, RFX
Papers on ANKRA2
Ankyrin repeats of ANKRA2 recognize a PxLPxL motif on the 3M syndrome protein CCDC8.
Yang et al., Montréal, Canada. In Structure, May 2015
We have recently demonstrated that ankyrin repeats of ANKRA2 and the paralogous bare lymphocyte syndrome transcription factor RFXANK recognize PxLPxL/I motifs shared by megalin, three histone deacetylases, and RFX5.
Whole transcriptome sequencing identifies tumor-specific mutations in human oral squamous cell carcinoma.
Sheng et al., Cambridge, United States. In Bmc Med Genomics, 2012
We further identified 515 significantly mutated genes (SMGs) and 156 tumor-specific disruptive genes (TDGs), with six genes in both sets, including ANKRA2, GTF2H5, STOML1, NUP37, PPP1R26, and TAF1L.
Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat tumbler lock.
Min et al., Toronto, Canada. In Sci Signal, 2012
Ankyrin repeat family A protein 2 (ANKRA2) interacts with the plasma membrane receptor megalin and the class IIa histone deacetylases HDAC4 and HDAC5.
Association of single nucleotide polymorphisms in the ANKRA2 and CD180 genes with bovine respiratory disease and presence of Mycobacterium avium subsp. paratuberculosis(1).
Smith et al., United States. In Anim Genet, 2011
The objective was to determine whether single nucleotide polymorphisms (SNPs) in the ANKRA2 and CD180 genes are associated with incidence of bovine respiratory disease (BRD) and presence of Mycobacterium avium subsp.
FOXD1 Duplication Causes Branchial Defects and Interacts with the TFAP2A Gene Implicated in the Branchio-Oculo-Facial Syndrome in Causing Eye Effects in Zebrafish.
Vermeesch et al., Leuven, Belgium. In Mol Syndromol, 2009
Molecular cytogenetic delineation of the duplication demonstrated that only 7 genes are affected: LOC100289045, RGNEF, UTP15, ANKRA2, FUNDC2P1, BTF3 and FOXD1.
SUMO modification regulates the transcriptional repressor function of aryl hydrocarbon receptor repressor.
Fujii-Kuriyama et al., Tsukuba, Japan. In J Biol Chem, 2009
SUMOylation of the three lysine residues is important for the interaction between AhRR and ANKRA2, HDAC4, and HDAC5, which are important corepressors for AhRR.
Molecular mechanism of transcriptional repression of AhR repressor involving ANKRA2, HDAC4, and HDAC5.
Fujii-Kuriyama et al., Tsukuba, Japan. In Biochem Biophys Res Commun, 2008
The inhibitory activity of AhRR is sensitive to a histone deacetylase (HDAC) inhibitor, trichostatin A. By using the yeast two-hybrid screening method with the C-terminal sequence of AhRR as bait, we identified a binding partner, Ankyrin-repeat protein2 (ANKRA2), a protein known to interact with HDAC4 and HDAC5.
Class II histone deacetylases confer signal responsiveness to the ankyrin-repeat proteins ANKRA2 and RFXANK.
Olson et al., Westminster, United States. In Mol Biol Cell, 2006
Class II histone deacetylases (HDACs)4 and HDAC5 interact with the ankyrin repeats of ANKRA2 and regulatory factor X-associated ankyrin-containing protein and, through association with RFXANK, repress MHC II promoter activation
New functions of the major histocompatibility complex class II-specific transcription factor RFXANK revealed by a high-resolution mutagenesis study.
Reith et al., Genève, Switzerland. In Mol Cell Biol, 2005
We discovered that ANKRA2, the closest paralogue of RFXANK, can substitute for RFXANK in the activation of MHC-II genes and that this ability is mediated by its ankyrin repeat domain (ARD).
Identification of the ankyrin repeat proteins ANKRA and RFXANK as novel partners of class IIa histone deacetylases.
Yang et al., Montréal, Canada. In J Biol Chem, 2005
ANKRA, RFXANK, and CIITA are novel targets of class IIa HDACs which may deacetylases play a role in regulating MHCII expression
Evolutionary conservation and characterization of the bare lymphocyte syndrome transcription factor RFX-B and its paralogue ANKRA2.
Boss et al., Atlanta, United States. In Immunogenetics, 2005
Sequence comparison and analysis of the RFX-B proteins showed that RFX-B and a closely related protein, ANKRA2, are present in humans to bony fish and that specific domains are highly conserved.
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