Relation Results

Summary

Name PRDX1
Full Name Peroxiredoxin-1
Synonyms Natural killer cell-enhancing factor A, NKEF-A, Proliferation-associated gene protein, PAG, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2 | PAGA, PAGB, TDPX2
Primary ID Q06830
Links - -
Type protein
Relations 10
Function Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a ro ...
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Type: Score: Layout: SPV 
0.2620.20.2270.2550.3560.20.3920.2PBKPRDX1STK4CDK4CDK2CDK1CDK6ABL1LCK

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ up-regulates img/direct-activation.png phosphorylation PRDX1 0.262
Identifier Residue Sequence Organism Cell Line
SIGNOR-166901 Ser32 QFKDISLsDYKGKYV Homo sapiens T-lymphocyte, Melanoma Cell, Skin Cancer Cell
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PRDX1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276486 Thr18 PAPNFKAtAVMPDGQ in vitro
pmid sentence
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
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
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
+ down-regulates img/direct_inhibition.png phosphorylation PRDX1 0.227
Identifier Residue Sequence Organism Cell Line
SIGNOR-87105 Thr90 CHLAWVNtPKKQGGL Homo sapiens HeLa Cell
pmid sentence
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
+ down-regulates img/direct_inhibition.png phosphorylation PRDX1 0.255
Identifier Residue Sequence Organism Cell Line
SIGNOR-87101 Thr90 CHLAWVNtPKKQGGL Homo sapiens HeLa Cell
pmid sentence
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
+ down-regulates img/direct_inhibition.png phosphorylation PRDX1 0.356
Identifier Residue Sequence Organism Cell Line
SIGNOR-87097 Thr90 CHLAWVNtPKKQGGL Homo sapiens
pmid sentence
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
+ down-regulates img/direct_inhibition.png phosphorylation PRDX1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-87113 Thr90 CHLAWVNtPKKQGGL Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PRDX1 0.392
Identifier Residue Sequence Organism Cell Line
SIGNOR-276278 Tyr194 DVQKSKEyFSKQK in vitro
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PRDX1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276277 Tyr194 DVQKSKEyFSKQK in vitro
pmid sentence
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
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