+ |
SOCS5 | down-regulates quantity
binding
|
EGFR |
0.458 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271516 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15590694 |
SOCS5 Can Physically Associate with the EGFR. The complex recruited by SOCS proteins is composed of ElonginBC, Cullin, and Roc1 (15, 16). Together, this complex has E3 ubiquitin ligase activity. We suspect that the role of the SB domain is to mediate coupling of EGFR with the Elongin-Cullin-Roc E3 ubiquitin ligase complex, resulting in enhanced EGFR degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SOCS5 | up-regulates activity
binding
|
VCB-Cul2 |
0.478 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271522 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
15590694 |
SOCS5 Can Physically Associate with the EGFR. The complex recruited by SOCS proteins is composed of ElonginBC, Cullin, and Roc1 (15, 16). Together, this complex has E3 ubiquitin ligase activity. We suspect that the role of the SB domain is to mediate coupling of EGFR with the Elongin-Cullin-Roc E3 ubiquitin ligase complex, resulting in enhanced EGFR degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |