| created | [InstanceEdit:909669] Garapati, P V, 2010-07-07 |
| dbId | 909671 |
| displayName | Phosphorylated tyrosine residue 466 on IFNAR1 acts as a dock... |
| literatureReference | |
| modified | [InstanceEdit:9833472] Stephan, Ralf, 2023-04-27 |
| schemaClass | Summation |
| text | Phosphorylated tyrosine residue 466 on IFNAR1 acts as a docking site for STAT2. Latent STAT2 is recruited to this phosphotyrosine residue via its SH2 domain (Yan et al, 1996). Infection by human respiratory syncytial virus (hRSV) leads to loss of STAT2 by ubiquitination, catalyzed by a hRSV NS1 complex with elongin C (ELOC) and cullin-5 (CUL5) acting as an E3 ubiquitin ligase, and subsequent proteasomal STAT2 degradation (Elliott et al, 2007). |
| (summation) |
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