About Products Protein Database Contact

chfr

Gene
CHFR
Protein
E3 ubiquitin-protein ligase CHFR
Organism
Homo sapiens
Length
664 amino acids
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.
Similarity
Belongs to the CHFR family.
Mass
73.386 kDa
Sequence
MERPEEGKQSPPPQPWGRLLRLGAEEGEPHVLLRKREWTIGRRRGCDLSFPSNKLVSGDHCRIVVDEKSGQVTLEDTSTSGTVINKLKVVKKQTCPLQTGDVIYLVYRKNEPEHNVAYLYESLSEKQGMTQESFEANKENVFHGTKDTSGAGAGRGADPRVPPSSPATQVCFEEPQPSTSTSDLFPTASASSTEPSPAGRERSSSCGSGGGGISPKGSGPSVASDEVSSFASALPDRKTASFSSLEPQDQEDLEPVKKKMRGDGDLDLNGQLLVAQPRRNAQTVHEDVRAAAGKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVQSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYVVCRQCPEYRRQAAQPPHCPAPEGEPGAPQALGDAPSTSVSLTTAVQDYVCPLQGSHALCTCCFQPMPDRRAEREQDPRVAPQQCAVCLQPFCHLYWGCTRTGCYGCLAPFCELNLGDKCLDGVLNNNSYESDILKNYLATRGLTWKNMLTESLVALQRGVFLLSDYRVTGDTVLCYCCGLRSFRELTYQYRQNIPASELPVAVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN

Gene
Chfr
Protein
E3 ubiquitin-protein ligase CHFR
Organism
Mus musculus
Length
664 amino acids
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 (By similarity).
Similarity
Belongs to the CHFR family.
Mass
73.871 kDa
Sequence
MELHGEEQPPPPQEPWGRLLRLGAEEDEPQILLWKREWTIGRRRGCDLSFPSNKLVSGDHCKLTVDEISGEVTLEDTSTNGTVINKLQVVKKQTYPLQSGDIIYLVYRKNEPEHNVAYLYESLSGKQSLTQDSLEANKENMFHVTKDCSGPGQGDDPQVPLLSPMAQTCLEEPQPSTSTSDLLPTASTSSTEPELTSAGQKHSSSSGPGNTSISPKGRSSLVANGELSSLSPVFQDKEASFSLLESKDHEELEPAKKKMKGDGELDTNLQLLVSGQRGNAQTSSEDVKDASVKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVRSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYIVCRQCPEYRRQAVQSLPCPVPESELGATLALGGEAPSTSASLPTAAPDYMCPLQGSHAICTCCFQPMPDRRAEREQDPRVAPQQCAVCLQPFCHLYWGCTRTGCFGCLAPFCELNLGDKCLDGVLNNNNYESDILKNYLATRGLTWKSVLTESLLALQRGVFMLSDYRITGNTVLCYCCGLRSFRELTYQYRQNIPASELPVTVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN

Gene
chfr
Protein
E3 ubiquitin-protein ligase CHFR
Organism
Danio rerio
Length
637 amino acids
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. 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.
Similarity
Belongs to the CHFR family.
Mass
71.73 kDa
Sequence
MTNQDSDQAWGKLVKVDASPGSEIVLINSECTVGRKKDCDLSFPANKLVSGNHCKITHDQNSGKVWLEDMSTNGTVINMSKVVKKQTHLLQNGDVIYFVYRKNEPEQNIAYVYQSITPQESASHDVEDAGREEDSDLTETESEPAPVEPVIVKPLPQSGHEDPQPSTSSSSLHFYNMPLSTCSDVSARKNPVSSSAVCKGDSTSSGSPAQTRLKWTCWTDGEPEEEMQRKRRKTDRDDPGFGSAHSDASADIPLRGASGKEKTEGATTDKMEESLTCIICQDLLYDCISVQPCMHTFCAACYSGWMERSSFCPTCRCPVERIRKNHILNNLVEAYLLQHPEKCRTEDDLRSMDARNKITQDMLQPKVERSFSDEEASSDYLFELSDNDSDISDMSQPYMMCRQCPGYRKELSSALWICESAQSESLAKTAGDGPSTSSDSTTAAPQEFRCPPQASHLICTCCLQPMPDRRFEHLPPQVSPQHCLVCQKPFCHVYWGCPRIGCHGCLARFSELNLNDKCLDGVFNGNQYESEVLQNYLSCRGMSWRHLLQDSLQALQQGLYHLSDYRITANSFLCYCCGLRTFRELAYKYRERIPPSELPDAVTNRPNCYWGRNCRTQVKAHHALKFNHICEQTRFKN

Gene
chfr
Protein
E3 ubiquitin-protein ligase CHFR
Organism
Xenopus tropicalis
Length
626 amino acids
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. 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.
Similarity
Belongs to the CHFR family.
Mass
69.961 kDa
Sequence
MDGLGEKKPWGKLSRLLGAETESSSELFLYKKEWTIGRKKACDLSFPGNKLVSGEHCKITVNEESGSVSLEDTSTNGTVINKLKVVKKQTYPLKNGDVIYVVYRKNEPEQNVAYLYKSLNQAEDSMQNPADTSGSEEADTQTLSSQDDQLSYEEPQPSTSTSSLFSTPTTSASEPACTLLYKSQASVPGVQLESGEKSGESLEGHSSTSDATAHEKGSLGPPKKRMRTEDLWTGNKNLVSASCSKGASDESKTPSMKPDKMEETLTCIICQELLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPEKCRSEEDRCSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYTVCRQCPGYVRHNIQPPPYPPPSDTEASRTQGDAPSTSTNFPTATQEYVCPSHGSHVICTCCFQPMPDRRAEREHNSHVAPQQCTICLEPFCHMYWGCNRMGCFGCLAPFCELNLGDKCLDGVLNNNNYESDILKNYLASRGLTWKDMLNESLSAAQRGVFMLPDYRINGTTVLCYFCGLRNFRILTYQYRQNIPASELPVTVTSRPNCYWGRNCRTQVKAHHAMKFNHICEQTRFKN

Gene
chfr
Protein
E3 ubiquitin-protein ligase CHFR
Organism
Xenopus laevis
Length
625 amino acids
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. 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.
Similarity
Belongs to the CHFR family.
Mass
70.019 kDa
Sequence
MEGLDEKKPWGKLSRLLGAETDSSSELFLYKKEWTIGRKKACDLSFPGNKLVSGEHCKITVNEESGEVSLEDTSTNGTVINKLKVIRKQTYPLKNGDVIYVVYRKNEPEQNVAYLYKSLNQGQDSLHDPADTSGSEEAETQTLSSQDDQLSYEEPQPSTSTSSLFSTPTTSAIPGVQLESAEKSGESLGGHSSTSDASPAIRASIPKSNLSTQEQGSLGPPKKRIRTEDHWTTNKNFVPASCPIGASDESKTPSMKPDKMEETLTCIICQELLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPEKCRSEEDRCSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYTVCRQCPGFVRHSMQPPPYPPPSDTETSRTQGDAPSTSTNFPTATQEYVCPSHGSHVICTCCFQPMPDRRAEREHNSHVAPQQCTICLEPFCHMYWGCNRMGCFGCLAPFCELNLGDKCLDGVLNNNNYESDILKNYLASRGLTWKDMLNESLAAVQRGVFMLPDYRINGTTVLCYFCGLRNFRILTYQYRQNIPASELPVTVTSRPNCYWGRNCRTQVKAHHAMKFNHICEQTRFKN

Gene
CHFR
Protein
E3 ubiquitin-protein ligase CHFR
Organism
Pongo abelii
Length
571 amino acids
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.
Similarity
Belongs to the CHFR family.
Mass
63.873 kDa
Sequence
MERPEEGKQSPPPQPWGRLLRLGAEEGEPYVLLRKREWTIGRRRGCDLSFPSNKLVSGDHCRIAVDEKSGQVTLEDTSTSGTVINKLKVVKKQTCPLQTGDVIYLVYRKNEPEHRSGGGGISPKGSGPSVASDEVSSFATALPDRKTASFSSLEPQDQEDLEPMKKKMRGDGDLDLNGQLLVAQPRRNAQTVHEDVRAAAGKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVQSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYVVCRQCPEYRRQAAQPPPCPAPEGEPGVPQALVDAPSTSVSLTTVQDYVCPLQGSHALCTCCFQPMPDRRAEREQNPRVAPQQCAVCLQPFCHLYWGCTRTGCFGCLAPFCELNLGDKCLDGVLNNNSYESDILKNYLATRGLTWKNMLTESLVALQRGVFLLSDYRVTGDTILCYCCGLRSFRELTYQYRQNIPASELPVAVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN