Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Identification and characterization of CAC1 as a novel CDK2-associated cullin.
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CACUL1/CAC1 is a 369-aa cullin-domain protein that physically associates with CDK2, promotes CDK2 kinase activity, and is required for G1/S progression and proliferation; highly expressed in cancers.
"CAC1 interacts with CDK2 and promotes the kinase activity of CDK2 protein, we propose that CAC1 is a novel cell cycle associated protein capable of promoting cell proliferation."
Negative regulation of ERα by a novel protein CAC1 through association with histone demethylase LSD1.
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CAC1 binds ERalpha via its CoRNR box and, in association with LSD1, functions as an ERalpha corepressor, increasing H3K9me3 at ERalpha target promoters.
"CAC1, associated with LSD1, functions as an ERα corepressor, implicating a potential antitumor target in ERα-positive breast cancer."
Armc5 deletion causes developmental defects and compromises T-cell immune responses.
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CACUL1 was recovered as one of 16 ARMC5-binding partners in a yeast two-hybrid screen; the study characterizes ARMC5, not CACUL1.
"Yeast 2-hybrid assays identify 16 ARMC5-binding partners."
CACUL1/CAC1 Regulates the Antioxidant Response by Stabilizing Nrf2.
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CACUL1 binds the Cul3-Keap1-Rbx1 ubiquitin-ligase complex and attenuates Nrf2 ubiquitination, stabilizing Nrf2 (half-life ~10 -> ~30 min) and sensitizing cells for the antioxidant (ARE) response; CACUL1 is itself oxidative-stress-induced.
"we further assessed CACUL1 binding with Keap1, Cul3 and Rbx1, the components of the Ubiquitin ligase responsible for Nrf2 ubiquitination."
CACUL1 reciprocally regulates SIRT1 and LSD1 to repress PPARγ and inhibit adipogenesis.
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CACUL1 is a SIRT1-interacting protein that physically binds PPARgamma and represses its transcriptional activity by coordinating SIRT1 and LSD1 at target promoters (altering H3K9 acetylation/methylation), suppressing adipocyte differentiation.
"CACUL1, identified as a novel SIRT1 interacting protein, physically interacts with PPARγ and represses its transcriptional activity, suppressing adipocyte differentiation"