RNF4
entrez
6047
canonical
uniprot
P78317
canonical
ensembl
ENSG00000063978
resolver
ensp
ENSP00000315212
resolver
ensp
ENSP00000424076
resolver
ensp
ENSP00000426615
resolver
genesymbol
RNF4
resolver
genesymbol_syn
SNURF
resolver
hgnc
HGNC:10067
resolver
uniprot
B2R6D6
resolver
uniprot
D6RF58
resolver
uniprot
Q49AR8
resolver
uniprot_entry
RNF4_HUMAN
resolver
uniprot_sec
B2R6D6
resolver
uniprot_sec
D6RF58
resolver
uniprot_sec
Q49AR8
resolver
amino_acid_sequence
MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI
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:18408734, PubMed:19307308, PubMed:35013556). Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (PubMed:18408734, PubMed:19307308, PubMed:20943951). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (PubMed:20212317). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (PubMed:19779455, PubMed:20026589). 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:12885770). Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (PubMed:35013556). {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:19307308, ECO:0000269|PubMed:19779455, ECO:0000269|PubMed:20026589, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20943951, ECO:0000269|PubMed:35013556}.
uniprot
proteins
mass_dalton
21319
uniprot
proteins
mutagenesis
MUTAGEN 136; /note="M->S: Dominant-negative E2-binding mutant, leads to increased trapping of PARP1 to chromatin; when associated with A-177."; /evidence="ECO:0000269|PubMed:35013556"; MUTAGEN 156; /note="H->A: Abolished E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:35013556"; MUTAGEN 177; /note="R->A: Dominant-negative E2-binding mutant, leads to increased trapping of PARP1 to chromatin; when associated with S-136."; /evidence="ECO:0000269|PubMed:35013556
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:35013556}.
uniprot
proteins
post_translational_modification
PTM: Sumoylated; conjugated by one or two SUMO1 moieties. {ECO:0000250|UniProtKB:O88846}.; PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:O88846}.
uniprot
proteins
pubmed
10713105
uniprot
proteins
pubmed
12885770
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15707587
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
18408734
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19307308
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19779455
uniprot
proteins
pubmed
20026589
uniprot
proteins
pubmed
20212317
uniprot
proteins
pubmed
20943951
uniprot
proteins
pubmed
23028697
uniprot
proteins
pubmed
28842558
uniprot
proteins
pubmed
35013556
uniprot
proteins
pubmed
9479498
uniprot
proteins
pubmed
9734812
uniprot
proteins
sequence_length
190
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12885770}. Nucleus {ECO:0000269|PubMed:12885770}. Nucleus, PML body {ECO:0000269|PubMed:15707587, ECO:0000269|PubMed:20943951}.
uniprot
proteins