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Sequence of this protein is as follows: MERPEEGKQS PPPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF PSNKLVSGDH CRIVVDEKSG QVTLEDTSTS GTVINKLKVV KKQTCPLQTG DVIYLVYRKN EPEHNVAYLY ESLSEKQGMT QESFDTSGAG AGRGADPRVP PSSPATQVCF EEPQPSTSTS DLFPTASASS TEPSPAGRER SSSCGSGGGG ISPKGSGPSV ASDEVSSFAS ALPDRKTASF SSLEPQDQED LEPVKKKMRG DGDLDLNGQL LVAQPRRNAQ TVHEDVRAAA GKPDKMEETL TCIICQDLLH DCVSLQPCMH TFCAACYSGW MERSSLCPTC RCPVERICKN HILNNLVEAY LIQHPDKSRS EEDVQSMDAR NKITQDMLQP KVRRSFSDEE GSSEDLLELS DVDSESSDIS QPYVVCRQCP EYRRQAAQPP HCPAPEGEPG APQALGDAPS TSVSLTTAVQ DYVCPLQGSH ALCTCCFQPM PDRRVEREQD PRVAPQQCAV CLQPFCHLYW GCTRTGCYGC LAPFCELNLG DKCLDGVLNN NSYESDILKN YLATRGLTWK NMLTESLVAL QRGVFLLSDY RVTGDTVLCY CCGLRSFREL TYQYRQNIPA SELPVAVTSR PDCYWGRNCR TQVKAHHAMK FNHICEQTRF KN
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.
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Protein Aliases: Checkpoint with forkhead and RING finger domains protein; E3 ubiquitin-protein ligase CHFR; FLJ10796; FLJ33629; RING finger protein 196; RING-type E3 ubiquitin transferase CHFR
Gene Aliases: CHFR; RNF116; RNF196
UniProt ID: (Human) Q96EP1
Entrez Gene ID: (Human) 55743
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