+ |
Class II MHC:Antigen | up-regulates activity
binding
|
CD4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267990 |
|
|
Homo sapiens |
|
pmid |
sentence |
31001252 |
Extracellular domain of CD4, which is responsible for the recognition of its ligands, is composed of four globular Ig-like domains (D1-D4). The N-terminal D1 domain binds to a segment of the non-polymorphic β2 domain of MHC class II. CD4 is required for the recognition of most antigens in vivo. The presence of the CD4 coreceptor enhances T cell sensitivity to antigens |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | T cell activation |
+ |
UFD1 | down-regulates quantity by destabilization
binding
|
CD4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252421 |
|
|
Homo sapiens |
|
pmid |
sentence |
20442859 |
These findings ascribe specific functions to each of the components of the VCP-UFD1L-NPL4 complex in Vpu-mediated CD4 degradation: VCP energizes the process through ATP binding and hydrolysis, UFD1L binds ubiquitinated CD4 through recognition of K48 Ub chains, and NPL4 stabilizes UFD1L. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SCF-betaTRCP | down-regulates quantity by destabilization
polyubiquitination
|
CD4 |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272615 |
|
|
Homo sapiens |
|
pmid |
sentence |
11893391 |
Degradation of the HIV receptor CD4 by the proteasome, mediated by the HIV-1 protein Vpu, is crucial for the release of fully infectious virions. To promote CD4 degradation Vpu has to be phosphorylated on a motif DSGXXS, which is conserved in several signalling proteins known to be degraded by the proteasome upon phosphorylation. Such phosphorylation is required for the interaction of Vpu with the ubiquitin ligase SCF-beta-TrCP that triggers CD4 degradation by the proteasome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |