| Post Translational Modifications | 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. |
| Function | 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. |
| Protein Name | E3 Ubiquitin-Protein Ligase ChfrCheckpoint With Forkhead And Ring Finger Domains ProteinRing Finger Protein 196Ring-Type E3 Ubiquitin Transferase Chfr |
| Cellular Localisation | NucleusPml Body |
| Alternative Protein Names | E3 Ubiquitin-Protein Ligase Chfr proteinCheckpoint With Forkhead And Ring Finger Domains Protein proteinRing Finger Protein 196 proteinRing-Type E3 Ubiquitin Transferase Chfr proteinCHFR proteinRNF196 protein |
Information sourced from Uniprot.org
