RFFL
entrez
117584
canonical
uniprot
Q8WZ73
canonical
ensembl
ENSG00000092871
resolver
ensp
ENSP00000378096
resolver
genesymbol
RFFL
resolver
genesymbol_syn
RNF189
resolver
genesymbol_syn
RNF34L
resolver
hgnc
HGNC:24821
resolver
uniprot
E1P633
resolver
uniprot
Q8NHW0
resolver
uniprot
Q8TBY7
resolver
uniprot
Q96BE6
resolver
uniprot_entry
RFFL_HUMAN
resolver
uniprot_sec
E1P633
resolver
uniprot_sec
Q8NHW0
resolver
uniprot_sec
Q8TBY7
resolver
uniprot_sec
Q96BE6
resolver
amino_acid_sequence
MWATCCNWFCLDGQPEEVPPPQGARMQAYSNPGYSSFPSPTGLEPSCKSCGAHFANTARKQTCLDCKKNFCMTCSSQVGNGPRLCLLCQRFRATAFQREELMKMKVKDLRDYLSLHDISTEMCREKEELVLLVLGQQPVISQEDRTRASTLSPDFPEQQAFLTQPHSSMVPPTSPNLPSSSAQATSVPPAQVQENQQANGHVSQDQEEPVYLESVARVPAEDETQSIDSEDSFVPGRRASLSDLTDLEDIEGLTVRQLKEILARNFVNYKGCCEKWELMERVTRLYKDQKGLQHLVSGAEDQNGGAVPSGLEENLCKICMDSPIDCVLLECGHMVTCTKCGKRMNECPICRQYVIRAVHVFRS
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling. {ECO:0000269|PubMed:15069192, ECO:0000269|PubMed:17121812, ECO:0000269|PubMed:18382127, ECO:0000269|PubMed:18450452, ECO:0000269|PubMed:22609986}.
uniprot
proteins
mass_dalton
40514
uniprot
proteins
mutagenesis
MUTAGEN 333; /note="H->A: Loss of E3 ubiquitin protein ligase activity."; /evidence="ECO:0000269|PubMed:15069192
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15069192}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Undergoes caspase-mediated cleavage upon death-receptor activation, by TNFSF10 for instance. May be mediated by the caspases CASP8 and CASP10 in a negative feedback loop.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15069192
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15576038
uniprot
proteins
pubmed
17121812
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18382127
uniprot
proteins
pubmed
18450452
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
22609986
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
363
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The FYVE-type zinc finger may mediate phosphatidylinositol phosphate-binding and control subcellular localization.
uniprot
proteins