| UniProt ID | RN128_MOUSE | |
|---|---|---|
| UniProt AC | Q9D304 | |
| Protein Name | E3 ubiquitin-protein ligase RNF128 | |
| Gene Name | Rnf128 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 428 | |
| Subcellular Localization |
Endomembrane system Single-pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partiall |
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| Protein Description | E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals (By similarity).. | |
| Protein Sequence | MGPPPGIGVYCRGGCGAARLLAWCFLLALSPHAPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPVSGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLASERGASGAVIFNFPGTRNEVIPMSHPGAGDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQSRKQRQLKADAKKAIGKLQLRTLKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHIFHKTCVDPWLLEHRTCPMCKCDILKALGIEVDVEDGSVSLQVPVSNEASNTASPHEEDSRSETASSGYASVQGADEPPLEEHAQSANENLQLVNHEANSVAVDVVPHVDNPTFEEDETPDQEAAVREIKS | |
| 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 |
|---|---|---|---|---|---|
| 48 | N-linked_Glycosylation | AVWTAYLNVSWRVPH EEEEEEEEEEEECCC | 17.07 | - | |
| 59 | N-linked_Glycosylation | RVPHTGVNRTVWELS ECCCCCCCCEEEEEC | 34.94 | - | |
| 101 | N-linked_Glycosylation | NACNPHTNFTVPTVW HCCCCCCCCCCCCCC | 27.79 | - | |
| 151 | Phosphorylation | VIFNFPGTRNEVIPM EEECCCCCCCCEECC | 30.47 | - | |
| 159 | Phosphorylation | RNEVIPMSHPGAGDI CCCEECCCCCCCCCE | 22.60 | - | |
| 257 | Ubiquitination | DAKKAIGKLQLRTLK HHHHHHHHHHHHHHH | 27.26 | - | |
| 323 | Ubiquitination | MCKCDILKALGIEVD CCCCHHHHHHCCEEE | 41.73 | - |
| 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 RN128_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RN128_MOUSE !! | ||||||
* 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 RN128_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| P53_MOUSE | Trp53 | physical | 23370271 | |
| TBK1_MOUSE | Tbk1 | physical | 27776110 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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