Sort   by:  
 Page size 
TranscriptomicsThe conserved ubiquitin-like protein Hub1 plays a critical role in splicing in human cells
Different from canonical ubiquitin-like proteins, Hub1 does not form covalent conjugates with substrates but binds proteins non-covalently. In Saccharomyces cerevisiae, Hub1 associates with spliceosomes and mediates alternative splicing of SRC1, without affecting pre-mRNA splicing generally. Human H...
ORGANISM(S): Homo sapiens 
2014-05-30 | E-GEOD-56878 | biostudies-arrayexpress
TranscriptomicsUBL5 is essential for pre-mRNA splicing and sister chromatid cohesion in human cells
UBL5 is an atypical ubiquitin-like protein, whose function in metazoans remains largely unexplored. We show that UBL5 is required for sister chromatid cohesion maintenance in human cells. UBL5 primarily associates with spliceosomal proteins, and UBL5 depletion decreases pre-mRNA splicing efficiency,...
ORGANISM(S): Homo sapiens 
2014-08-05 | E-GEOD-59376 | biostudies-arrayexpress
TranscriptomicsA single SR-like protein, Npl3, promotes pre-mRNA splicing in budding yeast
Mammalian SR proteins are a family of reversibly phosphorylated RNA binding proteins primarily studied for their roles in alternative splicing. While budding yeast lack alternative splicing, they do have three SR-like proteins: Npl3, Gbp2, and Hrb1. However, these have been primarily studied for the...
ORGANISM(S): Saccharomyces cerevisiae 
2008-12-30 | E-GEOD-11491 | biostudies-arrayexpress
UnknownUbiquitin-like protein UBL5 promotes the functional integrity of the Fanconi anemia pathway.
Not available
S-EPMC4491998 | biostudies-literature
UnknownUBL5 is essential for pre-mRNA splicing and sister chromatid cohesion in human cells.
Not available
S-EPMC4198039 | biostudies-literature
ProteomicsPre-mRNA splicing function of the ubiquitin-like protein Hub1/UBL-5 in Caenorhabditis elegans
The conserved ubiquitin-like protein Hub1/UBL-5 associates with proteins non-covalently. In yeast and human cells, Hub1 promotes splicing of precursor mRNAs with weak introns and alternative splicing, however, its splicing function has remained elusive in multicellular organisms. We demonstrate the ...
ORGANISM(S): Caenorhabditis elegans 
2024-05-21 | PXD033914 | Pride
Trans-splicing and c. elegans Outron-containing transcripts Spliceosome Pre-mrna splicing 
TranscriptomicsDysregulated expression and alternative splicing of genes controlling neuritogenesis and axon guidance revealed by exon-sensitive microarrays in models of neurodegeneration
This SuperSeries is composed of the following subset Series: GSE21298: Profiling wt SOD versus ALS SOD1(G93A) mutant GSE21305: Profiling neuroblastoma SH-SY5Y with Paraquat treatment Mitochondrial dysfunction has been directly or indirectly implicated in the pathogenesis of a number of neurodegener...
ORGANISM(S): Homo sapiens 
2010-12-22 | E-GEOD-21450 | biostudies-arrayexpress
GenomicsAn Rtf2 domain-containing protein influences pre-mRNA splicing and is essential for embryonic development in Arabidopsis thaliana
Alternative splicing is prevalent in plants, but little is known about its regulation in the context of developmental and signaling pathways. We describe here a new factor that influences pre-mRNA splicing and is essential for embryonic development in Arabidopsis thaliana. This factor was retrieved ...
ORGANISM(S): Arabidopsis thaliana 
2014-11-14 | E-GEOD-63238 | biostudies-arrayexpress
TranscriptomicsGenome-wide transcriptome analysis revealed extensive alternative RNA splicing in gene expression in the zoonotic parasite Schistosoma japonicum
Background: Schistosoma japonicum is a pathogen of the phylum Platyhelminths that causes zoonotic schistosomiasis endemic in China and Southeast Asian countries. Control of the disease has been hampered by the lack of efficient measures. The development of tools for diagnosis of acute and chronic i...
ORGANISM(S): Schistosoma japonicum 
2014-09-02 | E-GEOD-58564 | biostudies-arrayexpress
ProteomicsStructural basis of ubiquitination mediated by protein splicing in early Eukarya
This study is part of a project focused on the study of the ability of inteins to perform protein splicing. Our aim, in particular, is to characterize by mass spectrometry the splicing products of the ubl4- BIL2-ubl5 and of Ras, which strongly interacts with ubl4- BIL2-ubl5 precursor.
ORGANISM(S): Escherichia coli 
2021-01-18 | PXD020525 | Pride
Ubiquitin protein splicing 
Sort   by:  
 Page size