SNW1

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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SNW domain-containing protein 1 is a protein that in humans is encoded by the SNW1 gene.[1][2][3]

Function

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.[3]

Interactions

SNW1 has been shown to interact with:

References

  1. Folk P, Půta F, Krpejsová L, Blahůsková A, Markos A, Rabino M, Dottin RP (Nov 1996). "The homolog of chromatin binding protein Bx42 identified in Dictyostelium". Gene. 181 (1–2): 229–31. doi:10.1016/S0378-1119(96)00483-0. PMID 8973337.
  2. 2.0 2.1 Baudino TA, Kraichely DM, Jefcoat SC, Winchester SK, Partridge NC, MacDonald PN (Jun 1998). "Isolation and characterization of a novel coactivator protein, NCoA-62, involved in vitamin D-mediated transcription". The Journal of Biological Chemistry. 273 (26): 16434–41. doi:10.1074/jbc.273.26.16434. PMID 9632709.
  3. 3.0 3.1 "Entrez Gene: SNW1 SNW domain containing 1".
  4. 4.0 4.1 4.2 4.3 Zhou S, Fujimuro M, Hsieh JJ, Chen L, Hayward SD (Feb 2000). "A role for SKIP in EBNA2 activation of CBF1-repressed promoters". Journal of Virology. 74 (4): 1939–47. doi:10.1128/jvi.74.4.1939-1947.2000. PMC 111672. PMID 10644367.
  5. 5.0 5.1 Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (Nov 2001). "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". The Journal of Biological Chemistry. 276 (44): 40614–20. doi:10.1074/jbc.M106263200. PMID 11514567.
  6. 6.0 6.1 6.2 Leong GM, Subramaniam N, Figueroa J, Flanagan JL, Hayman MJ, Eisman JA, Kouzmenko AP (May 2001). "Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription". The Journal of Biological Chemistry. 276 (21): 18243–8. doi:10.1074/jbc.M010815200. PMID 11278756.
  7. 7.0 7.1 7.2 Zhou S, Fujimuro M, Hsieh JJ, Chen L, Miyamoto A, Weinmaster G, Hayward SD (Apr 2000). "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function". Molecular and Cellular Biology. 20 (7): 2400–10. doi:10.1128/mcb.20.7.2400-2410.2000. PMC 85419. PMID 10713164.
  8. Beatus P, Lundkvist J, Oberg C, Pedersen K, Lendahl U (Jun 2001). "The origin of the ankyrin repeat region in Notch intracellular domains is critical for regulation of HES promoter activity". Mechanisms of Development. 104 (1–2): 3–20. doi:10.1016/s0925-4773(01)00373-2. PMID 11404076.
  9. Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K (May 2001). "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression". Human Molecular Genetics. 10 (11): 1129–39. doi:10.1093/hmg/10.11.1129. PMID 11371506.
  10. Prathapam T, Kühne C, Banks L (Dec 2002). "Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity". Nucleic Acids Research. 30 (23): 5261–8. doi:10.1093/nar/gkf658. PMC 137971. PMID 12466551.
  11. Prathapam T, Kühne C, Hayman M, Banks L (Sep 2001). "Ski interacts with the evolutionarily conserved SNW domain of Skip". Nucleic Acids Research. 29 (17): 3469–76. doi:10.1093/nar/29.17.3469. PMC 55893. PMID 11522815.
  12. Dahl R, Wani B, Hayman MJ (Mar 1998). "The Ski oncoprotein interacts with Skip, the human homolog of Drosophila Bx42". Oncogene. 16 (12): 1579–86. doi:10.1038/sj.onc.1201687. PMID 9569025.

Further reading