Sort   by:  
 Page size 
ProteomicsPhosphorylation of CPSF6 RS-like domain
Cleavage factor I mammalian (CFIm) complex, composed of cleavage and polyadenylation specificity factor CPSF6, regulates alternative polyadenylation (APA). CPSF6 has a RS-like domain which plays role in protein -protein interactions. This interaction might have role in alternative polyadenylation s...
ORGANISM(S): Homo sapiens (Human) 
2019-04-01 | PXD012713 | Pride
Cfim68 Cpsf6 Rs domain Rs-like domain Apa 
UnknownJumonji domain containing protein 6 (Jmjd6) modulates splicing and specifically interacts with arginine-serine-rich (RS) domains of SR- and SR-like proteins.
Not available
S-EPMC4081092 | biostudies-literature
TranscriptomicsDeletion of the RS domain in RBM20 leads to dilated cardiomyopathy
Human patients carrying genetic mutations in RBM20 develop a clinically aggressive dilated cardiomyopathy (DCM) characterized by early onset heart failure, high mortality, and sudden death, which is recapitulated in animal models. RBM20 has two primary domains, an RNA recognition motif (RRM) that bi...
ORGANISM(S): Mus musculus 
2023-01-02 | GSE212799 | GEO
GenomicsDeletion of the RS domain in RBM20 leads to dilated cardiomyopathy
Deletion of the RS domain in RBM20 leads to dilated cardiomyopathy
PRJNA877291 | ENA
ProteomicsSRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23
Here we characterized SRSF1’s interactome using proximity labeling and mass spectrometry. This approach yielded 190 proteins enriched in the SRSF1 samples, independently of the N- or C-terminal location of the biotin-labeling domain. The detected proteins reflect established functions of SRSF1 in pr...
ORGANISM(S): Homo sapiens (Human) 
2024-04-30 | PXD048180 | Pride
Bioid srsf1 interactome ddx23 affinity proteomics 
TranscriptomicsThe Nuclear Immune Receptor RPS4 Is Required for RRS1SLH1-Dependent Constitutive Defense Activation in Arabidopsis thaliana.
Plant nucleotide-binding leucine-rich repeat (NB-LRR) disease resistance (R) proteins recognize specific “avirulent” pathogen effectors and activate immune responses. NB-LRR proteins structurally and functionally resemble mammalian Nod-like receptors (NLRs). How NB-LRR and NLR proteins activate defe...
ORGANISM(S): Arabidopsis thaliana 
2014-11-21 | E-GEOD-48247 | biostudies-arrayexpress
TranscriptomicsThe Nuclear Immune Receptor RPS4 Is Required for RRS1SLH1-Dependent Constitutive Defense Activation in Arabidopsis thaliana.
Plant nucleotide-binding leucine-rich repeat (NB-LRR) disease resistance (R) proteins recognize specific M-bM-^@M-^\avirulentM-bM-^@M-^] pathogen effectors and activate immune responses. NB-LRR proteins structurally and functionally resemble mammalian Nod-like receptors (NLRs). How NB-LRR and NLR pr...
ORGANISM(S): Arabidopsis thaliana 
2014-11-21 | E-GEOD-51116 | biostudies-arrayexpress
TranscriptomicsThe structure and target identification of the tandem RRM of yeast Npl3 bound to RNA reveal a cooperative sequence-specific recognition and an RNA chaperone role in splicing
The conserved SR-like protein Npl3 promotes the splicing of diverse pre-mRNAs. However, the RNA sequence(s) recognized by the RNA Recognition Motifs (RRM1 & RRM2) of Npl3 during the splicing reaction remain elusive. Here, we developed a split-iCRAC approach in vivo to determine the consensus sequenc...
ORGANISM(S): Saccharomyces cerevisiae 
2022-12-01 | E-MTAB-11736 | biostudies-arrayexpress
TranscriptomicsA role for Fkbp6 and the chaperone machinery in piRNA amplification and transposon silencing
Epigenetic silencing of transposons by Piwi-interacting RNAs (piRNAs) constitutes an RNA-based genome defense mechanism. Piwi endonuclease action amplifies the piRNA pool by generating new piRNAs from target transcripts by a poorly understood mechanism. Here, we identified mouse Fkbp6 as a factor in...
ORGANISM(S): Bombyx mori 
2012-09-04 | E-GEOD-39203 | biostudies-arrayexpress
TranscriptomicsChIP-chip from Ehrlichia chaffeensis-infected THP-1 cells with ankyrin repeat-containing protein, p200
Host genes interacting with ankyrin repeat-containing protein, p200, in Ehrlichia chaffeensis-infected monocytes. Chromatin immunoprecipitation (ChIP) together with microarray (chip) analysis demonstrated enrichment of relatively small subset (n=456) of host cell genes associated with molecular and ...
ORGANISM(S): Homo sapiens 
2010-05-16 | E-GEOD-13464 | biostudies-arrayexpress
Sort   by:  
 Page size