Protein Name:
E3 ubiquitin-protein ligase MARCHF8
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UniprotKB/SwissProt ID: Q9DBD2 (Q9DBD2)
Gene Name:
Marchf8
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that plays several important roles in innate immunity and adaptive immunity (PubMed:16785530, PubMed:35503863). Mediates ubiquitination of CD86 and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. Possesses a very broad antiviral activity by specifically inactivating different viral fusion proteins. Targets and ubiquitinates cytoplasmic lysine residues of viral envelope glycoproteins with single transmembrane domains leading to their lysosomal degradation. Mediates the regulation of constitutive ubiquitination and trafficking of the viral restriction factor BST2 within the endocytic pathway. Plays a role in maintenance of immune tolerance to self by promoting the turnover and proteasomal degradation of PD-L1/CD274 via ubiquitination. Catalyzes the 'Lys-63'-linked polyubiquitylation of cGAS thereby inhibiting its DNA binding ability and impairing its antiviral innate immunity (PubMed:35503863). Negatively regulates IL7-mediated T-cell homeostasis by mediating 'Lys-27'-linked polyubiquitination of IL7R, leading to its lysosomal degradation (By similarity)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Golgi apparatus membrane. Endoplasmic reticulum membrane. Cytoplasmic vesicle membrane. Lysosome membrane. Early endosome membrane
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of Q9DBD2
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
237 |
AYNRVIYVQN C PETSKKNIFE |
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