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Human SRSF1 Protein expressed in Wheat germ - ABIN1319738
Aissat, de Becdelièvre, Golmard, Vasseur, Costa, Chaoui, Martin, Costes, Goossens, Girodon, Fanen, Hinzpeter: Combined computational-experimental analyses of CFTR exon strength uncover predictability of exon-skipping level. in Human mutation 2013
DLP (show DMD Proteins) and ASF1 are part of a predeposition complex, which is recruited by XNP (show ATRX Proteins) and is necessary to prevent DNA exposure in the nucleus.
ASF1 cellular levels are tightly controlled by distinct pathways and provide a molecular mechanism for post-translational regulation of dASF1 and hASF1a (show ASF1A Proteins) by TLK (show TLK2 Proteins) kinases.
dASF1 has a direct role in modifying chromatin structure during DNA replication and this function of dASF1 is important for the processivity of the replication machinery.
Asf1 is directed via interactions with sequence-specific complexes to mediate silencing of specific target genes.
Histone chaperones ASF1 and NAP1 (show NAP1L1 Proteins) differentially modulate removal of active histone marks by LID-RPD3 (show HDAC1 Proteins) complexes during NOTCH (show NOTCH1 Proteins) silencing.
high level of SF2, as a novel oncoprotein in RCC (show XRCC1 Proteins), was significantly associated with poor survival in a large cohort of RCC (show XRCC1 Proteins) specimens. Taken together, our study presents a road map for the prediction and validation of miR (show MLXIP Proteins)-766-3p/SF2 axis and thus imparts a therapeutic way for further RCC (show XRCC1 Proteins) progression.
The authors found that RNA recognition motif 1 (RRM1 (show RRM1 Proteins)) in SRSF1 binds PP1 (show PPA1 Proteins) and represses its catalytic function through an allosteric mechanism.
We present a joint atomistic molecular dynamics (MD) and experimental study of two RRM-containing proteins bound with their single-stranded target RNAs, namely the Fox-1 (show A2BP1 Proteins) and SRSF1 complexes.The simulations predict unanticipated specific participation of Arg142 at the protein-RNA interface of the SRFS1 complex, which is subsequently confirmed by NMR and ITC measurements
Using NMR spectroscopy with two separately expressed domains of SRSF1, we showed that several residues in the RNA-binding motif 2 interact with the N-terminal region of the RS domain (RS1 (show RS1 Proteins)).
Especially, in SRSF1 morphants, bone cartilage formation was reduced in the brain and Nkx-2.5 (show NKX2-5 Proteins) expression was dramatically reduced in the heart of SRSF1 morphants. In addition, a dramatic reduction in functional chordin (show CHRD Proteins) RNA in SRSF1 morphants was observed suggesting that chordin (show CHRD Proteins) is one of the targets of SRSF1. Thus, we concluded that SRSF1 is an essential factor for pattern formation including heart, cartilage and germ lay
results strongly support SRSF1 as a prognostic biomarker in SCLC and provide a rationale for personalized therapy in SCLC
NSrp70 (show NSRP1 Proteins) acts as a new molecular counterpart for alternative splicing of target RNA, counteracting SRSF1 and SRSF2 (show SRSF2 Proteins) splicing activity.
we have identified for the first time a potential mechanism that involves the essential splicing factor (show SLU7 Proteins) ASF/SF2 through which morphine regulates splicing specificity of the MOR (show OPRM1 Proteins) encoding gene, OPRM1 (show OPRM1 Proteins).
Global splicing analysis with RNA-seq revealed that exons carrying the hnRNP H (show HNRNPH1 Proteins)-binding GGGGG motif are predisposed to be skipped compared to those carrying the SRSF1-binding GGAGG motif in both human and mouse brains.
We present experimental evidence that splicing factor (show SLU7 Proteins) SRSF1, SRSF2 (show SRSF2 Proteins), U2AF35 (show U2AF1 Proteins), U2AF65 (show U2AF59 Proteins) and KHSRP (show KHSRP Proteins) expression levels in gastrointestinal tract (colon, gastric and pancreatic) tumors differ compare to healthy tissues and in cell lines
The expression levels of three splicing factors, ESRP1 (show ESRP1 Proteins), PTB (show PTBP1 Proteins) and SF2/ASF, are significantly altered during cardiac hypertrophy in mice.
RRP1B suppresses metastatic progression by altering the transcriptome through its interaction with splicing regulators such as SRSF1
Deletion of RRM1 (show RRM1 Proteins) eliminated the splicing activity of SRSF1 and thus cellular transformation.
Specific effects on regulated splicing by SR proteins SRSF1 and SRSF2 (show SRSF2 Proteins) depends on a complex set of relationships with multiple other SR proteins in mammalian genomes.
Treatment with IL-17 (show IL17A Proteins) prolongs the half-life of chemokine (show CCL1 Proteins) CXCL1 (show CXCL1 Proteins) mRNA via the adaptor TRAF5 (show TRAF5 Proteins) and the splicing-regulatory factor SF2 (ASF).
analysis of the miRNA-mediated interaction between leukemia/lymphoma-related factor (LRF (show ZBTB7A Proteins)) and alternative splicing factor/splicing factor (show SLU7 Proteins) 2 (ASF/SF2) affects cell senescence and apoptosis
Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 (show SMN1 Proteins) causes spinal muscular atrophy in the absence of SMN1 (show SMN1 Proteins)
Both hnRNP A1 (show HNRNPA1 Proteins) and alternative splicing factor/splicing factor (show SLU7 Proteins) 2 contents rose in adenomas and during injury-induced hyperplasia compared to control lungs
These results highlight the requirement of Sfrs1-mediated alternative splicing for the survival of retinal neurons, with sensitivity defined by the window of time in which the neuron was generated.
This gene encodes a member of the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. The protein binds to pre-mRNA transcripts and components of the spliceosome, and can either activate or repress splicing depending on the location of the pre-mRNA binding site. The protein's ability to activate splicing is regulated by phosphorylation and interactions with other splicing factor associated proteins. Multiple transcript variants encoding different isoforms have been found for this gene. In addition, a pseudogene of this gene has been found on chromosome 13.
, anti- silencing function 1
, anti-silencing factor
, splicing factor, arginine/serine-rich 1 (splicing factor 2, alternate splicing factor)
, SR splicing factor 1
, alternative-splicing factor 1
, pre-mRNA-splicing factor SF2, P33 subunit
, splicing factor 2
, splicing factor, arginine/serine-rich 1
, splicing factor arginine/serine-rich 1
, splicing factor, arginine/serine-rich 1B
, pre-mRNA-splicing factor SRp30a
, splicing factor, arginine/serine-rich 1 (ASF/SF2)
, serine/arginine-rich splicing factor 1B
, splicing factor, arginine/serine-rich 1b