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SNIP1  -  Smad nuclear interacting protein 1

Homo sapiens

Synonyms: FHA domain-containing protein SNIP1, Smad nuclear-interacting protein 1
 
 
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High impact information on SNIP1

  • SNIP1 gene was first identified through a yeast two-hybrid system, using Smad1 as the bait [1].
  • The carboxyl terminus of SNIP1 interacts with Smad1 and Smad2 in yeast two-hybrid as well as in mammalian overexpression systems [2].
  • Overexpression of full-length SNIP1 or its amino terminus is sufficient to inhibit multiple gene responses to TGF-beta and CBP/p300, as well as the formation of a Smad4/p300 complex [2].
  • Thus, SNIP1 is a nuclear inhibitor of CBP/p300 and its level of expression in specific cell types has important physiological consequences by setting a threshold for TGF-beta-induced transcriptional activation involving CBP/p300 [2].
  • Studies in Xenopus laevis further suggest that SNIP1 plays a role in regulating dorsomedial mesoderm formation by the TGF-beta family member nodal [2].
  • A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction [2].
 

Biological context of SNIP1

 

Anatomical context of SNIP1

  • Here, we have used short interfering RNAs (siRNAs) to knockdown SNIP1 expression in human cell lines [3].
 

Associations of SNIP1 with chemical compounds

 

Regulatory relationships of SNIP1

  • SNIP1 itself is induced upon serum stimulation immediately prior to cyclin D1 expression [3].
 

Other interactions of SNIP1

  • SNIP1 is a recently discovered novel repressor of CBP/p300 [6].
  • The patent number associated with the production of SNIP1 antibody is US6906179.

 

 

 

 

 

References

  1. A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs). Lin, Y., Martin, J., Gruendler, C., Farley, J., Meng, X., Li, B.Y., Lechleider, R., Huff, C., Kim, R.H., Grasser, W.A., Paralkar, V., Wang, T. BMC. Cell. Biol. (2002) [Pubmed]
  2. A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction. Kim, R.H., Wang, D., Tsang, M., Martin, J., Huff, C., de Caestecker, M.P., Parks, W.T., Meng, X., Lechleider, R.J., Wang, T., Roberts, A.B. Genes Dev. (2000) [Pubmed]
  3. The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression. Roche, K.C., Wiechens, N., Owen-Hughes, T., Perkins, N.D. Oncogene (2004) [Pubmed]
  4. SNIP1 Is a Candidate Modifier of the Transcriptional Activity of c-Myc on E Box-Dependent Target Genes. Fujii, M., Lyakh, L.A., Bracken, C.P., Fukuoka, J., Hayakawa, M., Tsukiyama, T., Soll, S.J., Harris, M., Rocha, S., Roche, K.C., Tominaga, S., Jen, J., Perkins, N.D., Lechleider, R.J., Roberts, A.B. Mol. Cell (2006) [Pubmed]
  5. p300 regulates the synergy of steroidogenic factor-1 and early growth response-1 in activating luteinizing hormone-beta subunit gene. Mouillet, J.F., Sonnenberg-Hirche, C., Yan, X., Sadovsky, Y. J. Biol. Chem. (2004) [Pubmed]
  6. A novel link between the proteasome pathway and the signal transduction pathway of the bone morphogenetic proteins (BMPs). Lin, Y., Martin, J., Gruendler, C., Farley, J., Meng, X., Li, B.Y., Lechleider, R., Huff, C., Kim, R.H., Grasser, W.A., Paralkar, V., Wang, T. BMC Cell Biol. (2002) [Pubmed]
 
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