CHFR
entrez
55743
canonical
uniprot
Q96EP1
canonical
ensembl
ENSG00000072609
resolver
ensp
ENSP00000266880
resolver
ensp
ENSP00000392395
resolver
ensp
ENSP00000398735
resolver
ensp
ENSP00000416431
resolver
ensp
ENSP00000572590
resolver
genesymbol
CHFR
resolver
genesymbol_syn
RNF196
resolver
hgnc
HGNC:20455
resolver
uniprot
A6NEN5
resolver
uniprot
B4DZ77
resolver
uniprot
B4E2L6
resolver
uniprot
Q96SL3
resolver
uniprot
Q9NRT4
resolver
uniprot
Q9NT32
resolver
uniprot
Q9NVD5
resolver
uniprot_entry
CHFR_HUMAN
resolver
uniprot_sec
A6NEN5
resolver
uniprot_sec
B4DZ77
resolver
uniprot_sec
B4E2L6
resolver
uniprot_sec
Q96SL3
resolver
uniprot_sec
Q9NRT4
resolver
uniprot_sec
Q9NT32
resolver
uniprot_sec
Q9NVD5
resolver
amino_acid_sequence
MERPEEGKQSPPPQPWGRLLRLGAEEGEPHVLLRKREWTIGRRRGCDLSFPSNKLVSGDHCRIVVDEKSGQVTLEDTSTSGTVINKLKVVKKQTCPLQTGDVIYLVYRKNEPEHNVAYLYESLSEKQGMTQESFEANKENVFHGTKDTSGAGAGRGADPRVPPSSPATQVCFEEPQPSTSTSDLFPTASASSTEPSPAGRERSSSCGSGGGGISPKGSGPSVASDEVSSFASALPDRKTASFSSLEPQDQEDLEPVKKKMRGDGDLDLNGQLLVAQPRRNAQTVHEDVRAAAGKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVQSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYVVCRQCPEYRRQAAQPPHCPAPEGEPGAPQALGDAPSTSVSLTTAVQDYVCPLQGSHALCTCCFQPMPDRRAEREQDPRVAPQQCAVCLQPFCHLYWGCTRTGCYGCLAPFCELNLGDKCLDGVLNNNSYESDILKNYLATRGLTWKNMLTESLVALQRGVFLLSDYRVTGDTVLCYCCGLRSFRELTYQYRQNIPASELPVAVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
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. {ECO:0000269|PubMed:10935642, ECO:0000269|PubMed:11807090, ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:14694445, ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:19182791}.
uniprot
proteins
mass_dalton
73386
uniprot
proteins
mutagenesis
MUTAGEN 39; /note="T->A: Abolishes phosphorylation but not autoubiquitination; when associated with A-205."; /evidence="ECO:0000269|PubMed:14638868"; MUTAGEN 205; /note="S->A: Abolishes phosphorylation but not autoubiquitination; when associated with A-39."; /evidence="ECO:0000269|PubMed:14638868"; MUTAGEN 306; /note="I->A: Abolishes autoubiquitination. Does not affect phosphorylation."; /evidence="ECO:0000269|PubMed:11807090, ECO:0000269|PubMed:19182791"; MUTAGEN 332; /note="W->A: Abolishes autoubiquitination in vitro."; /evidence="ECO:0000269|PubMed:11807090"; MUTAGEN 632; /note="R->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1."; /evidence="ECO:0000269|PubMed:18172500"; MUTAGEN 635; /note="C->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-641."; /evidence="ECO:0000269|PubMed:18172500"; MUTAGEN 641; /note="C->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-635."; /evidence="ECO:0000269|PubMed:18172500"; MUTAGEN 642; /note="R->A: Impairs poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1."; /evidence="ECO:0000269|PubMed:18172500"; MUTAGEN 644; /note="Q->A: Impairs poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1."; /evidence="ECO:0000269|PubMed:18172500
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: 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.; PTM: Autoubiquitinated; may regulate its cellular level. {ECO:0000269|PubMed:11807090, ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:19182791}.; PTM: Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity. {ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:14638868}.
uniprot
proteins
protein_family
CHFR family
uniprot
proteins
pubmed
10935642
uniprot
proteins
pubmed
11807090
uniprot
proteins
pubmed
11912157
uniprot
proteins
pubmed
11948416
uniprot
proteins
pubmed
12121644
uniprot
proteins
pubmed
12538348
uniprot
proteins
pubmed
12810945
uniprot
proteins
pubmed
14562038
uniprot
proteins
pubmed
14612512
uniprot
proteins
pubmed
14638868
uniprot
proteins
pubmed
14694445
uniprot
proteins
pubmed
14695171
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15467728
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18172500
uniprot
proteins
pubmed
18335050
uniprot
proteins
pubmed
19182791
uniprot
proteins
pubmed
23186163
uniprot
proteins
sequence_length
664
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:11912157, ECO:0000269|PubMed:15467728, ECO:0000269|PubMed:18172500}.
uniprot
proteins