+ |
LRIG1 | down-regulates
|
LRIG3 |
0.442 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202177 |
|
|
Homo sapiens |
|
pmid |
sentence |
23723069 |
Lrig1 destabilizes lrig3, limiting lrig3's positive effects on receptors and identifying lrig3 as a new target of lrig1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRIG1 | down-regulates
binding
|
EGFR |
0.726 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127304 |
|
|
Homo sapiens |
|
pmid |
sentence |
15282549 |
Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
CBL | down-regulates
ubiquitination
|
LRIG1 |
0.572 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127289 |
|
|
Homo sapiens |
|
pmid |
sentence |
15282549 |
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
LRIG1 | down-regulates
ubiquitination
|
ERBB4 |
0.591 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139954 |
|
|
Homo sapiens |
|
pmid |
sentence |
16123311 |
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRIG1 | up-regulates
binding
|
CBLC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127301 |
|
|
Homo sapiens |
|
pmid |
sentence |
15282549 |
Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
LRIG1 | down-regulates
ubiquitination
|
ERBB2 |
0.412 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139948 |
|
|
Homo sapiens |
|
pmid |
sentence |
16123311 |
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRIG1 | down-regulates
|
ERBB4 |
0.591 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202146 |
|
|
Homo sapiens |
|
pmid |
sentence |
23723069 |
Lrig1 is a negative regulator of oncogenic receptor tyrosine kinases, including erbb and met receptors, and promotes receptor degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRIG1 | up-regulates
binding
|
CBL |
0.572 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127298 |
|
|
Homo sapiens |
|
pmid |
sentence |
15282549 |
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
LRIG1 | down-regulates
|
ERBB2 |
0.412 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202143 |
|
|
Homo sapiens |
|
pmid |
sentence |
23723069 |
Lrig1 is a negative regulator of oncogenic receptor tyrosine kinases, including erbb and met receptors, and promotes receptor degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CBLC | down-regulates
ubiquitination
|
LRIG1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127292 |
|
|
Homo sapiens |
|
pmid |
sentence |
15282549 |
Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skin |
+ |
LRIG1 | down-regulates
ubiquitination
|
ERBB3 |
0.446 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-139951 |
|
|
Homo sapiens |
|
pmid |
sentence |
16123311 |
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRIG1 | down-regulates
ubiquitination
|
ErbB receptor family |
0.727 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269872 |
|
|
Homo sapiens |
|
pmid |
sentence |
16123311 |
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |