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c-Abl promotes TGF-beta-induced SKIP/Smad3 interaction.
Higher SKIP expression is associated with poor prognosis in malignant pleural mesothelioma
Upon step 1 catalysis, Cwc25 contacts with the branch-site region, and enhanced crosslinks of Prp8 and Prp45 with nucleotides surrounding the branch-site were observed.
Rab1A regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP
Results show that SNW1 directly associates with EFTUD2 and SNRNP200 and that disruption of SNW1 association with these proteins promotes the apoptosis of breast cancer cells.
A transcriptome-wide analysis revealed that SNW1 or PRPF8 depletion affects the splicing of specific introns in a subset of pre-mRNAs, including pre-mRNAs encoding the cohesion protein sororin and the APC/C subunit APC2.
SKIP overexpression is involved in the pathogenesis of breast cancer.
High SKIP expression was detected in clinical HCC samples.
SKIP increased 5alpha-dihydrotestosterone (DHT) induced N-terminal/C-terminal AR interaction from 12-fold to almost 300-fold in a two-hybrid assay, and enhanced AR ligand-independent AF-1 transactivation.
Arl8 and SKIP are required for lysosomes to distribute away from the microtubule-organizing center. We identify two kinesin light chain binding motifs in SKIP that are required for lysosomes to accumulate kinesin-1 and redistribute to the cell periphery.
SKIP is required for epithelial mesenchymal transition and invasiveness induced by TGF-beta1 in transformed cells.
This suggests that transcription of stress response genes, unlike, e.g., the SNW1-sensitive mitosis-specific genes, can proceed uncoupled from regulators that normally function under physiological conditions.
molecular model for the binding mode of SKIP to PPIL1 which emphasizes the versatility of cyclophilin-type PPIases to engage in additional interactions with other proteins apart from active site contacts despite their limited surface area.
SKIP is essential for p53 stress-induced expression of the p21
The large disordered region in SKIP provides an interaction platform. Its disorder-order transition, induced by PPIL1 binding, may adapt the requirement for a large structural rearrangement occurred in the activation of spliceosome
SIRT1 associates with SKI-interacting protein (SKIP) and modulates its activity as a coactivator of retinoic acid receptor.
may couple vitamin D receptor-mediated transcription and RNA splicing
These results show that the human SKIP gene can functionally substitute for the mRNA splicing gene PRP45 of S. cerevisiae.
SKIIP plays independent roles in transcription elongation and pre-mRNA splicing.
SKIP binds with CHES1 in a region within the final 66 hydrophobic residues, and thus defining a new protein-protein interaction domain of SKIP.
interaction with vitamin D receptor helix H10 residues
This gene, a member of the SNW gene family, encodes a coactivator that enhances transcription from some Pol II promoters. This coactivator can bind to the ligand-binding domain of the vitamin D receptor and to retinoid receptors to enhance vitamin D-, retinoic acid-, estrogen-, and glucocorticoid-mediated gene expression. It can also function as a splicing factor by interacting with poly(A)-binding protein 2 to directly control the expression of muscle-specific genes at the transcriptional level. Finally, the protein may be involved in oncogenesis since it interacts with a region of SKI oncoproteins that is required for transforming activity.
SKI interacting protein
, nuclear protein SkiP
, nuclear protein skip
, SKI-interacting protein
, SNW domain-containing protein 1
, homolog of Drosophila BX42
, nuclear receptor coactivator NCoA-62
, nuclear receptor coactivator, 62-kD
, ski-interacting protein