RNF4_RAT - dbPTM
RNF4_RAT - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9UbiquitinationSTRNPQRKRRGGAVN
CCCCHHHHCCCCCCC
41.00-
94PhosphorylationLRQDHADSCVVSSDD
CCHHCCCCEEECCCH
15.0325575281
98PhosphorylationHADSCVVSSDDEELS
CCCCEEECCCHHHHH
13.9827097102
99PhosphorylationADSCVVSSDDEELSK
CCCEEECCCHHHHHC
37.1527097102
105PhosphorylationSSDDEELSKDKDVYV
CCCHHHHHCCCCEEE
41.9325575281
111PhosphorylationLSKDKDVYVTTHTPR
HHCCCCEEEEECCCC
11.3825575281
113PhosphorylationKDKDVYVTTHTPRST
CCCCEEEEECCCCCC
8.6525575281
114PhosphorylationDKDVYVTTHTPRSTK
CCCEEEEECCCCCCC
17.4425575281
116PhosphorylationDVYVTTHTPRSTKDE
CEEEEECCCCCCCCC
20.5025575281

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseRnf4O88846
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF4_RAT !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2D1_HUMANUBE2D1physical
22842904
UBC_HUMANUBCphysical
22842904
RNF4_RATRnf4physical
22842904
H2A3_RATHist3h2aphysical
11319220
H2B1_RATHist1h2blphysical
11319220
RNF4_RATRnf4physical
24882209
UB2D1_HUMANUBE2D1physical
24882209

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNF4_RAT

loading...

Related Literatures of Post-Translational Modification

TOP