| UniProt ID | RNF5_HUMAN | |
|---|---|---|
| UniProt AC | Q99942 | |
| Protein Name | E3 ubiquitin-protein ligase RNF5 | |
| Gene Name | RNF5 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 180 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein. Mitochondrion membrane. Endoplasmic reticulum membrane. Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles. |
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| Protein Description | Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin and Salmonella type III secreted protein sopA. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses.. | |
| Protein Sequence | MAAAEEEDGGPEGPNRERGGAGATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPERQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDTGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGTGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAAAEEEDG ------CCCCCCCCC | 18.51 | 19413330 | |
| 68 | Ubiquitination | RQECPVCKAGISREK HHCCCCCCCCCCHHH | 50.29 | 21890473 | |
| 75 | Ubiquitination | KAGISREKVVPLYGR CCCCCHHHEECCCCC | 47.63 | 21890473 | |
| 84 | Phosphorylation | VPLYGRGSQKPQDPR ECCCCCCCCCCCCCC | 33.40 | 23917254 | |
| 86 | Ubiquitination | LYGRGSQKPQDPRLK CCCCCCCCCCCCCCC | 46.47 | 21890473 | |
| 93 | Ubiquitination | KPQDPRLKTPPRPQG CCCCCCCCCCCCCCC | 61.33 | 21890473 | |
| 94 | Phosphorylation | PQDPRLKTPPRPQGQ CCCCCCCCCCCCCCC | 43.02 | 26055452 | |
| 107 | Phosphorylation | GQRPAPESRGGFQPF CCCCCCCCCCCCCCC | 34.86 | 23403867 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of RNF5_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RNF5_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 RNF5_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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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
