| + |
PBK | up-regulates 
phosphorylation
|
PRDX1 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166901 |
Ser32 |
QFKDISLsDYKGKYV |
Homo sapiens |
T-lymphocyte, Melanoma Cell, Skin Cancer Cell |
| pmid |
sentence |
| 20647304 |
We report that prx1 is newly discovered direct target of topk. Our results demonstrate that topk phosphorylation of prx1 at ser-32 inhibits uvb-induced apoptosis in rpmi7951 melanoma cells by increasing prx1 peroxidase activity and decreasing the intracellular accumulation of h2o2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK4 | down-regulates activity 
phosphorylation
|
PRDX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276486 |
Thr18 |
PAPNFKAtAVMPDGQ |
in vitro |
|
| pmid |
sentence |
| 23386615 |
Mst1 inactivates Prdx1 by phosphorylating it at Thr-90 and Thr-183, leading to accumulation of hydrogen peroxide in cells.Prdx1 is phosphorylated by Mst1 predominantly at Thr-18, Thr-90, and Thr-183. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276485 |
Thr183 |
GWKPGSDtIKPDVQK |
in vitro |
|
| pmid |
sentence |
| 23386615 |
Mst1 inactivates Prdx1 by phosphorylating it at Thr-90 and Thr-183, leading to accumulation of hydrogen peroxide in cells.Prdx1 is phosphorylated by Mst1 predominantly at Thr-18, Thr-90, and Thr-183. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276487 |
Thr90 |
CHLAWVNtPKKQGGL |
in vitro |
|
| pmid |
sentence |
| 23386615 |
Mst1 inactivates Prdx1 by phosphorylating it at Thr-90 and Thr-183, leading to accumulation of hydrogen peroxide in cells.Prdx1 is phosphorylated by Mst1 predominantly at Thr-18, Thr-90, and Thr-183. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CDK4 | down-regulates
phosphorylation
|
PRDX1 |
0.227 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87105 |
Thr90 |
CHLAWVNtPKKQGGL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11986303 |
Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%.Prx i was also phosphorylated, with an efficiency similar to that observed with cdc2, when incubated in vitro with cdk2, cdk4, or cdk6 that had been immunoprecipitated from hela cell lysates with specific antibodies (data not shown). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
PRDX1 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87097 |
Thr90 |
CHLAWVNtPKKQGGL |
Homo sapiens |
|
| pmid |
sentence |
| 11986303 |
Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK6 | down-regulates
phosphorylation
|
PRDX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87113 |
Thr90 |
CHLAWVNtPKKQGGL |
Homo sapiens |
|
| pmid |
sentence |
| 11986303 |
Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%.Prx i was also phosphorylated, with an efficiency similar to that observed with cdc2, when incubated in vitro with cdk2, cdk4, or cdk6 that had been immunoprecipitated from hela cell lysates with specific antibodies (data not shown). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 | down-regulates
phosphorylation
|
PRDX1 |
0.256 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87101 |
Thr90 |
CHLAWVNtPKKQGGL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11986303 |
Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%.Prx i was also phosphorylated, with an efficiency similar to that observed with cdc2, when incubated in vitro with cdk2, cdk4, or cdk6 that had been immunoprecipitated from hela cell lysates with specific antibodies (data not shown). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK | down-regulates activity
phosphorylation
|
PRDX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276277 |
Tyr194 |
DVQKSKEyFSKQK |
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 |
| + |
ABL1 | down-regulates activity
phosphorylation
|
PRDX1 |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276278 |
Tyr194 |
DVQKSKEyFSKQK |
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 |
3.0
PRDX1
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