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Lysine-rich coiled-coil protein 1 (KRCC1) is a nuclear protein, enriched at chromatin and characterized by a lysine-rich coiled-coil C-terminal region[1][2]. It consists of 259 amino acids and contains computationally predicted nuclear localization signals (NLS), contributing to its predominant nuclear localization[1]. KRCC1 is frequently overexpressed in high-grade serous ovarian cancer and its elevated expression correlates with poor overall survival and chemoresistance[1][2]. The protein interacts with histone deacetylases (HDAC1, HDAC2) and the serine/threonine phosphatase PP1CC, modulating chromatin structure and DNA repair processes[1][2]. Functionally, KRCC1 is involved in the DNA damage response, especially via regulation of CHK1-mediated checkpoint activation, homologous recombination, and cell cycle progression. Knockdown or inhibition of KRCC1 induces apoptosis, impairs cancer cell invasion, increases histone acetylation, and leads to enhanced DNA damage signaling[1][2]. These findings support KRCC1 as a promising therapeutic target in ovarian cancer and possibly other malignancies due to its role in cell survival and genomic stability[1][2].
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