| 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 | ||
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* 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 | ||||||
|---|---|---|---|---|---|---|
| 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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