Rnf4
entrez
29274
canonical
uniprot
O88846
canonical
ensembl
ENSRNOG00000013930
resolver
ensembl
ENSRNOG00055016978
resolver
ensembl
ENSRNOG00060016549
resolver
ensembl
ENSRNOG00065028885
resolver
ensp
ENSRNOP00000096496
resolver
ensp
ENSRNOP00055023237
resolver
ensp
ENSRNOP00060022905
resolver
ensp
ENSRNOP00065040980
resolver
enst
ENSRNOT00000095762
resolver
enst
ENSRNOT00055028879
resolver
enst
ENSRNOT00060028458
resolver
enst
ENSRNOT00065049898
resolver
genesymbol
Rnf4
resolver
genesymbol_syn
Snurf
resolver
uniprot_entry
RNF4_RAT
resolver
amino_acid_sequence
MSTRNPQRKRRGGAVNSRQTQKRTRETTSTPEISLEAEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSKDKDVYVTTHTPRSTKDEGTTGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation (PubMed:14987998, PubMed:15707587, PubMed:18408734). Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (PubMed:15707587, PubMed:20943951). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (By similarity). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (By similarity). Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation (PubMed:11319220, PubMed:9710597). Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (By similarity). {ECO:0000250|UniProtKB:P78317, ECO:0000269|PubMed:11319220, ECO:0000269|PubMed:14987998, ECO:0000269|PubMed:15707587, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:20943951, ECO:0000269|PubMed:9710597}.
uniprot
proteins
mass_dalton
21897
uniprot
proteins
mutagenesis
MUTAGEN 8..11; /note="RKRR->AAAA: Altered DNA-binding activity."; /evidence="ECO:0000269|PubMed:11319220"; MUTAGEN 40..43; /note="IELV->AEAA: No effect. Loss of binding and ubiquitination of poly-SUMO chains; when associated with 50-A--A-53; 61-A--A-63 and 71-A--A-74."; /evidence="ECO:0000269|PubMed:18408734"; MUTAGEN 50..53; /note="IVDL->AADA: Alters binding to poly-SUMO chains. Loss of binding and ubiquitination of poly-SUMO chains; when associated with 40-A--A-43; 61-A--A-63 and 71-A--A-74."; /evidence="ECO:0000269|PubMed:18408734"; MUTAGEN 61..63; /note="VVV->AAA: No effect. Loss of binding and ubiquitination of poly-SUMO chains; when associated with 40-A--A-43; 50-A--A-53 and 71-A--A-74."; /evidence="ECO:0000269|PubMed:18408734"; MUTAGEN 71..74; /note="VVIV->AAAA: No effect. Loss of binding and ubiquitination of poly-SUMO chains; when associated with 40-A--A-43; 50-A--A-53 and 61-A--A-63."; /evidence="ECO:0000269|PubMed:18408734"; MUTAGEN 136; /note="C->S: Loss of ubiquitination activity; when associated with S-139."; /evidence="ECO:0000269|PubMed:14987998"; MUTAGEN 139; /note="C->S: Loss of ubiquitination activity; when associated with S-136."; /evidence="ECO:0000269|PubMed:14987998"; MUTAGEN 177; /note="C->S: Loss of ubiquitination activity; when associated with S-180."; /evidence="ECO:0000269|PubMed:14987998"; MUTAGEN 180; /note="C->S: Loss of ubiquitination activity; when associated with S-177."; /evidence="ECO:0000269|PubMed:14987998
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18408734}.
uniprot
proteins
post_translational_modification
PTM: Sumoylated; conjugated by one or two SUMO1 moieties. {ECO:0000269|PubMed:15707587}.; PTM: Autoubiquitinated. {ECO:0000269|PubMed:14987998}.
uniprot
proteins
pubmed
11319220
uniprot
proteins
pubmed
14987998
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15707587
uniprot
proteins
pubmed
18408734
uniprot
proteins
pubmed
20681948
uniprot
proteins
pubmed
20943951
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
9710597
uniprot
proteins
sequence_length
194
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78317}. Nucleus {ECO:0000269|PubMed:11319220, ECO:0000269|PubMed:9710597}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20943951}. Nucleus, PML body {ECO:0000269|PubMed:20943951}.
uniprot
proteins