UniProt ID | RNF4_RAT | |
---|---|---|
UniProt AC | O88846 | |
Protein Name | E3 ubiquitin-protein ligase RNF4 | |
Gene Name | Rnf4 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 194 | |
Subcellular Localization | Cytoplasm. Nucleus. Nucleus, PML body. Nucleus, nucleoplasm. | |
Protein Description | 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. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. 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.. | |
Protein Sequence | MSTRNPQRKRRGGAVNSRQTQKRTRETTSTPEISLEAEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSKDKDVYVTTHTPRSTKDEGTTGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | Ubiquitination | STRNPQRKRRGGAVN CCCCHHHHCCCCCCC | 41.00 | - | |
94 | Phosphorylation | LRQDHADSCVVSSDD CCHHCCCCEEECCCH | 15.03 | 25575281 | |
98 | Phosphorylation | HADSCVVSSDDEELS CCCCEEECCCHHHHH | 13.98 | 27097102 | |
99 | Phosphorylation | ADSCVVSSDDEELSK CCCEEECCCHHHHHC | 37.15 | 27097102 | |
105 | Phosphorylation | SSDDEELSKDKDVYV CCCHHHHHCCCCEEE | 41.93 | 25575281 | |
111 | Phosphorylation | LSKDKDVYVTTHTPR HHCCCCEEEEECCCC | 11.38 | 25575281 | |
113 | Phosphorylation | KDKDVYVTTHTPRST CCCCEEEEECCCCCC | 8.65 | 25575281 | |
114 | Phosphorylation | DKDVYVTTHTPRSTK CCCEEEEECCCCCCC | 17.44 | 25575281 | |
116 | Phosphorylation | DVYVTTHTPRSTKDE CEEEEECCCCCCCCC | 20.50 | 25575281 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RNF4_RAT !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RNF4_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
UB2D1_HUMAN | UBE2D1 | physical | 22842904 | |
UBC_HUMAN | UBC | physical | 22842904 | |
RNF4_RAT | Rnf4 | physical | 22842904 | |
H2A3_RAT | Hist3h2a | physical | 11319220 | |
H2B1_RAT | Hist1h2bl | physical | 11319220 | |
RNF4_RAT | Rnf4 | physical | 24882209 | |
UB2D1_HUMAN | UBE2D1 | physical | 24882209 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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