+ |
MKNK1 | down-regulates
phosphorylation
|
SPRY2 |
0.509 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188889 |
Ser112 |
APLSRSIsTVSSGSR |
Homo sapiens |
|
pmid |
sentence |
19864419 |
The spry2/nedd4 association involves the ww domains of nedd4 and requires phosphorylation of the mnk2 kinase sites, ser(112) and ser(121), on spry2. mnk2 silencing decreased spry2-nedd4 interactions and also augmented the ability of spry2 to inhibit fibroblast growth factor signaling. endogenous and overexpressed nedd4 polyubiquitinate spry2 via lys(48) on ubiquitin and decrease its stability. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188893 |
Ser121 |
VSSGSRSsTRTSTSS |
Homo sapiens |
|
pmid |
sentence |
19864419 |
The spry2/nedd4 association involves the ww domains of nedd4 and requires phosphorylation of the mnk2 kinase sites, ser(112) and ser(121), on spry2. mnk2 silencing decreased spry2-nedd4 interactions and also augmented the ability of spry2 to inhibit fibroblast growth factor signaling. endogenous and overexpressed nedd4 polyubiquitinate spry2 via lys(48) on ubiquitin and decrease its stability. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
DYRK1A | down-regulates
phosphorylation
|
SPRY2 |
0.31 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179828 |
Thr75 |
KPAPRPStQHKHERL |
Homo sapiens |
|
pmid |
sentence |
18678649 |
We identify dyrk1a as one of the protein kinases of sprouty2. We show that dyrk1a interacts with and regulates the phosphorylation status of sprouty2. Moreover, we identify thr75 on sprouty2 as a dyrk1a phosphorylation site in vitro and in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC | up-regulates
phosphorylation
|
SPRY2 |
0.547 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-131189 |
Tyr55 |
AIRNTNEyTEGPTVV |
Homo sapiens |
|
pmid |
sentence |
15564375 |
Activation of signalling by fibroblast growth factor receptor leads to phosphorylation of the signalling attenuator human sprouty 2 (hspry2) on residue y55. we show that hspry2 is a direct substrate for src family kinases, including src itself.Phosphorylation of hspry2 is required for hspry2 to inhibit activation of the extracellular signal-regulated kinase pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SPRY2 | up-regulates
|
PTPN1 |
0.426 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95313 |
|
|
Homo sapiens |
|
pmid |
sentence |
12414790 |
Therefore, we conclude that an increase in soluble ptp1b activity contributes to the anti-migratory, but not anti-mitogenic, actions of hspry2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SPRY2 | down-regulates
|
CBLC |
0.461 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-92926 |
|
|
Homo sapiens |
|
pmid |
sentence |
12234920 |
Hspry2 prevents c-cbl-mediated ubiquitylation of egfrs. hspry2 interacts specifically with the c-cbl ring finger domain and displaces ubch7 from its binding site on the e3 ligase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEDD4 | down-regulates quantity by destabilization
polyubiquitination
|
SPRY2 |
0.399 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271425 |
|
|
Homo sapiens |
|
pmid |
sentence |
19864419 |
Endogenous and overexpressed Nedd4 polyubiquitinate Spry2 via Lys(48) on ubiquitin and decrease its stability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SPRY2 | down-regulates
binding
|
CBLB |
0.499 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83507 |
|
|
Homo sapiens |
|
pmid |
sentence |
11053437 |
One function of hspry2 in signaling processes downstream of rtks may be to modulate c-cbl physiological function such as that seen with receptor-mediated endocytosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |