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SPEN encodes a hormone inducible transcriptional repressor.
Showing 10 out of 22 products:
Human Polyclonal SPEN Primary Antibody for ELISA - ABIN547637
Hiriart, Gruffat, Buisson, Mikaelian, Keppler, Meresse, Mercher, Bernard, Sergeant, Manet: Interaction of the Epstein-Barr virus mRNA export factor EB2 with human Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links Spen proteins with splicing regulation and mRNA export. in The Journal of biological chemistry 2005
Human Polyclonal SPEN Primary Antibody for ICC, IF - ABIN4355627
McHugh, Chen, Chow, Surka, Tran, McDonel, Pandya-Jones, Blanco, Burghard, Moradian, Sweredoski, Shishkin, Su, Lander, Hess, Plath, Guttman: The Xist lncRNA interacts directly with SHARP to silence transcription through HDAC3. in Nature 2015
Human Polyclonal SPEN Primary Antibody for IP - ABIN188790
Korfanty, Stokowy, Chadalski, Toma-Jonik, Vydra, Widłak, Wojtaś, Gielniewski, Widlak: SPEN protein expression and interactions with chromatin in mouse testicular cells. in Reproduction (Cambridge, England) 2018
our data demonstrate a role for SPEN in the regulation of primary cilia formation and cell migration in breast cancer cells, which may collectively explain why its expression is associated with time to metastasis in cohorts of patients with ERalpha-negative breast cancers.
SPEN is a novel tumor-suppressor gene that may be clinically useful as a predictive biomarker of tamoxifen response in ERalpha-positive breast cancers.
SPEN mutations were associated with diffuse large B-cell lymphoma with hepatitis C virus infection.
Phosphorylation of the CK2 site on SMRT significantly increased affinity for SHARP.
A structural study of the RNA binding properties of the RNA recognition motifs of SHARP.
These results demonstrate a role for the inactivation of SHARP transcription in DM1 biology.
MINT3 and MINT17 were informative for patient grouping to predict local recurrence in rectal cancer patients
SHARP is a novel component of the HDAC corepressor complex, recruited by RBP-Jkappa to repress transcription of target genes in the absence of activated Notch.
the conserved function of the SPOC domain of SHARP is to mediate interaction with SMRT/NCoR corepressors, and that Spen proteins play an essential role in the repression complex
both the androgen receptor interacting domains of the coactivator SRC1 and of the corepressor SMRT compete for interaction with the androgen receptor N-terminus
Pak1-SHARP interaction plays an essential role in enhancing the corepressor functions of SHARP, thereby modulating Notch signaling in human cancer cells.
Msx2-interacting protein(MINT), human interacts with the UbcH8.
SHARP gene and protein expression is elevated in human colon and ovarian endometrioid adenocarcinomas carrying gene defects leading to beta-catenin dysregulation.
In functional assays, corepressor ETO, but not AML1/ETO, augments SHARP-mediated repression in an histone deacetylase-dependent manner.
Spenito, a small Spen family member, counteracted Spen function in fat regulation. Finally, mouse Spen and Spenito transcript levels scaled directly with body fat in vivo, suggesting a conserved role in fat liberation and catabolism. This study demonstrates that Spen is a key regulator of energy balance and provides a molecular context to understand the metabolic defects that arise from Spen dysfunction.
Spen is required for gene repression by Xist. Spen is not required for Xist RNA localization and the recruitment of chromatin modifications.
Spen is required for Xist-mediated silencing.
results suggest that Xist silences transcription by directly interacting with SHARP, recruiting SMRT, activating HDAC3, and deacetylating histones to exclude Pol II across the X chromosome
MINT forms a high affinity complex with CSL; the domains of MINT and CSL that are necessary and sufficient for complex formation are delineated
MINT plays an important role in tooth development, in particular, epithelial morphogenesis
Notch1 in concert with Notch2 contributes to the morphogenesis of renal vesicles into S-shaped bodies in a RBP-J-dependent manner.
Msx2-interacting nuclear target protein (MINT) competed with the intracellular region of Notch for binding to a DNA binding protein RBP-J and suppressed the transactivation activity of Notch signaling.
Stra13, Dec and Sharp (Mint) bHLH repressors are dynamically regulated during mammary gland development and may function to regulate apoptosis
MINT enhances Runx2 activation of multiprotein complexes assembled by the OCFRE
MINT is involved in CRYBP1-mediated Col2a1 gene repression and may play a role in regulation of cartilage development
Mint deficiency impairs differentiation of early T progenitors into double-negative cells, suggesting that Notch/RBP-J signaling negatively regulates DN1-DN2 transition
This gene encodes a hormone inducible transcriptional repressor. Repression of transcription by this gene product can occur through interactions with other repressors, by the recruitment of proteins involved in histone deacetylation, or through sequestration of transcriptional activators. The product of this gene contains a carboxy-terminal domain that permits binding to other corepressor proteins. This domain also permits interaction with members of the NuRD complex, a nucleosome remodeling protein complex that contains deacetylase activity. In addition, this repressor contains several RNA recognition motifs that confer binding to a steroid receptor RNA coactivator\; this binding can modulate the activity of both liganded and nonliganded steroid receptors.
Msx2 interacting nuclear target (MINT) homolog
, SMART/HDAC1 associated repressor protein
, SMART/HDAC1-associated repressor protein
, msx2-interacting protein
, nuclear receptor transcription cofactor
, spen homolog, transcriptional regulator (Drosophila)
, Msx2 interacting nuclear target protein