caution:PubMed:11807090 and PubMed:11912157 report that it can ubiquitinate and promote the degradation of substrates. PubMed:11807090 reports that, in Xenopus extracts, it ubiquitinates PLK, a protein kinase involved in mitotic progression. However, as experiments have been done either in vitro or with extracts from Xenopus, there is actually little evidence for a role for CHFR in protein degradation in vivo.,developmental stage:Weakly expressed in G1 phase, and highly expressed during S phase.,disease:Defects in CHFR may be involved in colon, lung and esophageal cancers and non small cell lung carcinomas (NSCLC). In addition, CHFR gene is silenced in many primary cancers because of CpG methylation and deacetylated histones on its promoter region. This however raises the question of whether CHFR silencing is a consequence or a cause of primary cancers.,domain:The FHA domain may be required to interact with phosphorylated proteins.,function:E3 ubiquitin-protein ligase required to transiently arrest cells in early prophase when they are exposed to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably promotes the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress. This suggests that it may be involved in signaling the presence of mitotic stress caused by microtubule poisons.,pathway:Protein modification; protein ubiquitination.,PTM:Autoubiquitinated in vitro.,PTM:Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity). Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity.,similarity:Contains 1 FHA domain.,similarity:Contains 1 RING-type zinc finger.,tissue specificity:Ubiquitous.,
Nucleus, PML body .
Ubiquitous.