Gene interactions and pathways from curated databases and text-mining

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CHUK — NCOA3

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Wu et al., Mol Cell Biol 2002 : Taken together, our results not only reveal the IKK mediated phosphorylation of SRC-3 to be a regulated event that plays an important role but also substantiate the role of SRC-3 in multiple signaling pathways
Zheng et al., Mol Cell Biol 2005 : Together these data demonstrate that E2-induced SRC-3 phosphorylation is dependent on a direct interaction between SRC-3 and ERalpha and can occur outside of the nucleus ... Together these data demonstrate that E2-induced SRC-3 phosphorylation is dependent on a direct interaction between SRC-3 and ERalpha and can occur outside of the nucleus
Zhou et al., Cell 2006 : In this issue of Cell, challenge this notion by revealing that the proteasomal activator REGgamma directs degradation of the steroid receptor coactivator SRC-3 by the 20S proteasome in an ATP- and ubiquitin independent manner
Lin et al., J Biochem Mol Biol 2006 : In summary, our present study showed for the first time that the 160 RAC3/SRC3 is involved in the functional transactivation of TAD of Nrf2 and that the other nuclear co-regulators such as CBP/p300, CARM1, PRMT1 and p/CAF can also transcriptionally activate this TAD of Nrf2 and that they could further enhance the transactivation activity mediated by RAC3/SRC3 ... In summary, our present study showed for the first time that the 160 RAC3/SRC3 is involved in the functional transactivation of TAD of Nrf2 and that the other nuclear co-regulators such as CBP/p300, CARM1 , PRMT1 and p/CAF can also transcriptionally activate this TAD of Nrf2 and that they could further enhance the transactivation activity mediated by RAC3/SRC3 ... In summary, our present study showed for the first time that the 160 RAC3/SRC3 is involved in the functional transactivation of TAD of Nrf2 and that the other nuclear co-regulators such as CBP/p300, CARM1, PRMT1 and p/CAF can also transcriptionally activate this TAD of Nrf2 and that they could further enhance the transactivation activity mediated by RAC3/SRC3
Mussi et al., Mol Endocrinol 2006 : Furthermore, overexpression of E2F1 significantly increases the promoter activity of the endogenous SRC-3 gene and boosts SRC-3 expression in vivo
Mc Ilroy et al., Endocr Relat Cancer 2006 (Breast Neoplasms...) : In HER2 ( human epidermal growth factor receptor 2 ) positive primary tumour cell cultures 17beta-estradiol induced a decrease in SRC-3 , whereas upregulated SRC-3 expression
Li et al., Mol Cell 2007 (Thyroid Neoplasms) : We previously demonstrated that the proteasome activator REGgamma directs degradation of the steroid receptor coactivator SRC-3 by the 20S proteasome in an ATP- and ubiquitin independent manner
Yan et al., Cancer Res 2008 (Carcinoma...) : In addition, SRC-3/AIB1 directly regulates transcription of matrix metalloproteinase (MMP)-2 and MMP-13 through its coactivation of AP-1 and PEA3 ... In addition, SRC-3/AIB1 directly regulates transcription of matrix metalloproteinase (MMP)-2 and MMP-13 through its coactivation of AP-1 and PEA3
Agoulnik et al., Steroids 2009 (Prostatic Neoplasms) : SRC-3 is required for optimal androgen dependent induction of PSA, TMPRSS2 , and PMEPA1 whereas SRA is required only for optimal induction of the TMPRSS2 gene ... SRC-3 is required for optimal androgen dependent induction of PSA, TMPRSS2, and PMEPA1 whereas SRA is required only for optimal induction of the TMPRSS2 gene ... SRC-3 is required for optimal androgen dependent induction of PSA , TMPRSS2, and PMEPA1 whereas SRA is required only for optimal induction of the TMPRSS2 gene
Wang et al., PloS one 2010 (Anoxia) : Knocking down SRC-3 , but not SRC-1 or SRC-2, using short interfering RNAs ( siRNAs ), reduced EPO transcriptional activity
Karmakar et al., Mol Endocrinol 2010 (Breast Neoplasms) : SMRT and SRC-3 bind directly in an ERalpha independent manner, and this interaction promotes E2-dependent SRC-3 binding to ERalpha measured by co-IP and SRC-3 recruitment to the cyclin D1 gene as measured by chromatin IP assays
Suen et al., J Biol Chem 1998 : SRC-3 enhanced ERalpha and progesterone receptor stimulated gene transcription in a ligand dependent manner, but stimulation of ERbeta mediated transcription was not observed