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SPOP encodes a protein that may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. Additionally we are shipping Speckle-Type POZ Protein Antibodies (57) and Speckle-Type POZ Protein Kits (20) and many more products for this protein.
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Dzip1 (show DZIP1 Proteins)-dependent stabilization of Spop/HIB is evolutionarily conserved and essential for proper regulation of Gli (show GLI1 Proteins)/Ci proteins in the Hh pathway.
methylation status of SPOP promoter can be used as a novel epigenetic biomarker and a therapeutic target in colorectal cancer.
these data highlight SPOP as an important regulator of luminal epithelial cell proliferation and c-MYC (show MYC Proteins) expression in prostate physiology, identify c-MYC (show MYC Proteins) as a novel bona fide SPOP substrate, and help explain the frequent inactivation of SPOP in human prostate adenocarcinoma.
Results elucidate the tumor-suppressor role of SPOP in prostate cancer in which it acts as a negative regulator of BET protein stability and also provide a molecular mechanism for resistance to BET inhibitors in individuals with prostate cancer bearing SPOP mutations.
SPOP mutation in endometrial cancer increased degradation of BRD2 (show BRD2 Proteins), BRD3 (show BRD3 Proteins) and BRD4 (show BRD4 Proteins) proteins. SPOP mutation in prostate cancer increased expression of BRD2 (show BRD2 Proteins), BRD3 (show BRD3 Proteins) and BRD4 (show BRD4 Proteins) proteins.
Prostate cancer-derived SPOP mutants failed to interact with Cdc20 (show CDC20 Proteins) to promote its degradation. As a result, SPOP-deficient prostate cancer cells with elevated Cdc20 (show CDC20 Proteins) expression became resistant to a pharmacological Cdc20 (show CDC20 Proteins) inhibitor.
While wild-type SPOP localizes to liquid nuclear speckles, self-association-deficient SPOP mutants have a diffuse distribution in the nucleus. SPOP oligomerizes through its BTB and BACK domains.
SPOP mutation activates both PI3K (show PIK3CA Proteins)/mTOR (show FRAP1 Proteins) and androgen receptor (show AR Proteins) signaling, effectively uncoupling the normal negative feedback between these two pathways.
SPOP-containing complex regulates SETD2 stability and H3K36me3-coupled alternative splicing.
The levels of SPOP significantly decreased, while the levels of SIRT2 (show SIRT2 Proteins) significantly increased in non-small cell lung cancer (NSCLC) cell lines, compared to normal bronchial epithelial cell line and NSCLC specimens, compared to the paired non-tumor lung tissue.
hese findings reveal novel molecular events underlying the regulation of INF2 (show INF2 Proteins) function and localization, and provided insights in understanding the relationship between SPOP mutations and dysregulation of mitochondrial dynamics in prostate cancer.
Speckle-type pox virus and zinc finger (POZ) protein (SPOP) regulates endometrial stromal cell decidualization in mice and that hormones regulate the expression of SPOP. This study suggests that ubiquitination may be involved in embryonic implantation.
These results implicate SPOP as a novel participant in DNA double strand break repair and suggest that SPOP mutation drives prostate tumorigenesis in part through genomic instability.
miR (show MLXIP Proteins)-145 has a role in post-transcriptional regulation of SPOP expression in selected tissues.
similar S/T-rich motifs are present in Gli (show GLI1 Proteins) proteins as well as in numerous HIB-interacting proteins and mediate Gli (show GLI1 Proteins) degradation by SPOP
MacroH2A1.2 (show H2AFY Proteins) binds the nuclear protein Spop.
Interaction of endogenous PDX-1 (show PDX1 Proteins) and PCIF1 in MIN6 insulinoma (show RPS15 Proteins) cells, is demonstarted.
This gene encodes a protein that may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. In mouse, the encoded protein binds to the putative leucine zipper domain of macroH2A1.2, a variant H2A histone that is enriched on inactivated X chromosomes. The BTB/POZ domain of this protein has been shown in other proteins to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes. Alternative splicing of this gene results in multiple transcript variants encoding the same protein.
speckle-type POZ protein
, Speckle-type POZ protein
, speckle-type POZ protein-like
, HIB homolog 1
, speckle-type POZ protein B
, roadkill homolog 1
, PDX-1 C-terminal-interacting factor 1