|Other Names||Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of H2AFY and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL.|
|Cellular Location||Nucleus. Nucleus speckle.|
|Tissue Location||Widely expressed.|
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This gene encodes a protein that may modulate thetranscriptional repression activities of death-associated protein 6(DAXX), which interacts with histone deacetylase, core histones,and other histone-associated proteins. In mouse, the encodedprotein binds to the putative leucine zipper domain of macroH2A1.2,a variant H2A histone that is enriched on inactivated Xchromosomes. The BTB/POZ domain of this protein has been shown inother proteins to mediate transcriptional repression and tointeract with components of histone deacetylase co-repressorcomplexes. Alternative splicing of this gene results in multipletranscript variants encoding the same protein. [provided byRefSeq].
Rose, J. Phd, et al. Mol. Med. (2010) In press :Zhuang, M., et al. Mol. Cell 36(1):39-50(2009)Liu, J., et al. Science 323(5918):1218-1222(2009)Bunce, M.W., et al. J. Biol. Chem. 283(13):8678-8686(2008)Byun, B., et al. Biofactors 31 (3-4), 165-169 (2007) :
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