+ |
ABL1 | down-regulates activity
phosphorylation
|
PRDX2 |
0.289 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276280 |
Tyr193 |
NVDDSKEyFSKHN |
in vitro |
|
pmid |
sentence |
20178744 |
Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. To determine whether Prxs are phosphorylated, we subjected recombinant human PrxI and II to an in vitro kinase assay with two nonreceptor PTKs, Lck and Abl, in the presence of [γ-32P]ATP. Both PTKs phosphorylated PrxI and PrxII. Phosphorylation of the wild-type protein was detected, whereas that of the Y194F mutant was not (Figure 1B), indicating that Tyr194 is the only site of tyrosine phosphorylation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
LCK | down-regulates activity
phosphorylation
|
PRDX2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276279 |
Tyr193 |
NVDDSKEyFSKHN |
in vitro |
|
pmid |
sentence |
20178744 |
Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. To determine whether Prxs are phosphorylated, we subjected recombinant human PrxI and II to an in vitro kinase assay with two nonreceptor PTKs, Lck and Abl, in the presence of [γ-32P]ATP. Both PTKs phosphorylated PrxI and PrxII. Phosphorylation of the wild-type protein was detected, whereas that of the Y194F mutant was not (Figure 1B), indicating that Tyr194 is the only site of tyrosine phosphorylation. |
|
Publications: |
1 |
Organism: |
In Vitro |