UniProt ID | RNF41_HUMAN | |
---|---|---|
UniProt AC | Q9H4P4 | |
Protein Name | E3 ubiquitin-protein ligase NRDP1 | |
Gene Name | RNF41 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 317 | |
Subcellular Localization | ||
Protein Description | Acts as E3 ubiquitin-protein ligase and regulates the degradation of target proteins. Polyubiquitinates MYD88. Negatively regulates MYD88-dependent production of proinflammatory cytokines. Can promote TRIF-dependent production of type I interferon and inhibits infection with vesicular stomatitis virus (By similarity). Promotes also activation of TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through maintaining basal levels of cytokine receptors, RNF41 is involved in the control of hematopoietic progenitor cell differentiation into myeloerythroid lineages (By similarity). Contributes to the maintenance of steady-state ERBB3 levels by mediating its growth factor-independent degradation. Involved in the degradation of the inhibitor of apoptosis BIRC6 and thus is an important regulator of cell death by promoting apoptosis. Acts also as a PRKN modifier that accelerates its degradation, resulting in a reduction of PRKN activity, influencing the balance of intracellular redox state. The RNF41-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control. [PubMed: 24949970] | |
Protein Sequence | MGYDVTRFQGDVDEDLICPICSGVLEEPVQAPHCEHAFCNACITQWFSQQQTCPVDRSVVTVAHLRPVPRIMRNMLSKLQIACDNAVFGCSAVVRLDNLMSHLSDCEHNPKRPVTCEQGCGLEMPKDELPNHNCIKHLRSVVQQQQTRIAELEKTSAEHKHQLAEQKRDIQLLKAYMRAIRSVNPNLQNLEETIEYNEILEWVNSLQPARVTRWGGMISTPDAVLQAVIKRSLVESGCPASIVNELIENAHERSWPQGLATLETRQMNRRYYENYVAKRIPGKQAVVVMACENQHMGDDMVQEPGLVMIFAHGVEEI | |
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 |
---|---|---|---|---|---|
103 | Ubiquitination | LDNLMSHLSDCEHNP HHHHHHHHHCCCCCC | 3.47 | 21890473 | |
106 | S-nitrosylation | LMSHLSDCEHNPKRP HHHHHHCCCCCCCCC | 5.28 | 24105792 | |
134 | S-nitrosylation | DELPNHNCIKHLRSV CCCCCCHHHHHHHHH | 3.22 | 24105792 | |
136 | Ubiquitination | LPNHNCIKHLRSVVQ CCCCHHHHHHHHHHH | 38.49 | - | |
154 | Ubiquitination | TRIAELEKTSAEHKH HHHHHHHHHHHHHHH | 61.48 | - | |
167 | Acetylation | KHQLAEQKRDIQLLK HHHHHHHHHHHHHHH | 43.47 | 30591977 | |
167 | Ubiquitination | KHQLAEQKRDIQLLK HHHHHHHHHHHHHHH | 43.47 | - | |
174 | Ubiquitination | KRDIQLLKAYMRAIR HHHHHHHHHHHHHHH | 46.17 | 21890473 | |
238 | S-nitrosylation | RSLVESGCPASIVNE HHHHHCCCCHHHHHH | 3.37 | 24105792 | |
254 | Phosphorylation | IENAHERSWPQGLAT HHHHHHCCCCCHHHH | 39.87 | - | |
264 | Phosphorylation | QGLATLETRQMNRRY CHHHHHHHHHHHHHH | 29.34 | 24850871 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RNF41_HUMAN !! |
* 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 RNF41_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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