CHFR

This gene encodes an E3 ubiquitin-protein ligase required for the maintenance of the antephase checkpoint that regulates cell cycle entry into mitosis and, therefore, may play a key role in cell cycle progression and tumorigenesis. The encoded protein has an N-terminal forkhead-associated domain, a central RING-finger domain, and a cysteine-rich C-terminal region. Alternatively spliced transcript variants that encode different protein isoforms have been described. [provided by RefSeq, Mar 2014]

Checkpoint With Forkhead And Ring Finger Domains

E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response 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 involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote 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.

Cell division Source: UniProtKB-KW
Meiotic spindle checkpoint Source: UniProtKB
Mitotic cell cycle checkpoint Source: UniProtKB
Modification-dependent protein catabolic process Source: UniProtKB
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
Positive regulation of protein ubiquitination Source: Ensembl
Protein destabilization Source: Ensembl
Protein polyubiquitination Source: UniProtKB
Protein ubiquitination Source: GO_Central
Ubiquitin-dependent protein catabolic process Source: GO_Central

PML body

Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc finger, the protein is also covalently poly-ADP-ribosylated by PARP1.
Autoubiquitinated; may regulate its cellular level.
Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity.