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c-Abl (show ABL1 Proteins) promotes TGF-beta (show TGFB1 Proteins)-induced SKIP/Smad3 (show SMAD3 Proteins) interaction.
Upon step 1 catalysis, Cwc25 (show CWC25 Proteins) contacts with the branch-site region, and enhanced crosslinks of Prp8 and Prp45 with nucleotides surrounding the branch-site were observed.
Rab1A (show RAB1A Proteins) regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP
Results show that SNW1 directly associates with EFTUD2 (show EFTUD2 Proteins) 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 (show CDCA5 Proteins) and the APC (show APC Proteins)/C subunit APC2.
High SKIP expression was detected in clinical HCC (show FAM126A Proteins) 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 (show EFNA5 Proteins) transactivation.
Arl8 (show ARL5B Proteins) 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 (show TGFB1 Proteins) 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.
interaction with vitamin D receptor (show VDR Proteins) helix H10 (show H1F0 Proteins) 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