| + |
PRKDC | up-regulates 
phosphorylation
|
CASP2 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183895 |
Ser139 |
LSCDYDLsLPFPVCE |
Homo sapiens |
|
| pmid |
sentence |
| 19203584 |
Here we show that dna damage induced by gamma-radiation triggers the phosphorylation of nuclear caspase-2 at the s122 site within its prodomain, leading to its cleavage and activation. This phosphorylation is carried out by the nuclear serine/threonine protein kinase dna-pkcs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates 
phosphorylation
|
CASP2 |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140836 |
Ser157 |
LYKKLRLsTDTVEHS |
Homo sapiens |
|
| pmid |
sentence |
| 16193064 |
Here we show that protein kinase (pk) ck2 phosphorylates procaspase-2 directly at serine-157. When intracellular pkck2 activity is low or downregulated by specific inhibitors, procaspase-2 is dephosphorylated, dimerized, and activated in a piddosome-independent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CA | up-regulates activity
dephosphorylation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248564 |
Ser164 |
STDTVEHsLDNKDGP |
in vitro |
|
| pmid |
sentence |
| 19531356 |
nutrient-replete oocytes inhibit C2 via S135 phosphorylation catalyzed by calcium/calmodulin-dependent protein kinase II. We now show that C2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. Moreover, we determined that S135 dephosphorylation is catalyzed by protein phosphatase-1 (PP1), which directly binds C2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP1CB | up-regulates activity
dephosphorylation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248576 |
Ser164 |
STDTVEHsLDNKDGP |
in vitro |
|
| pmid |
sentence |
| 19531356 |
Nutrient-replete oocytes inhibit C2 via S135 phosphorylation catalyzed by calcium/calmodulin-dependent protein kinase II. We now show that C2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. Moreover, we determined that S135 dephosphorylation is catalyzed by protein phosphatase-1 (PP1), which directly binds C2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PP1 | up-regulates activity
dephosphorylation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264661 |
Ser164 |
STDTVEHsLDNKDGP |
in vitro |
|
| pmid |
sentence |
| 19531356 |
Nutrient-replete oocytes inhibit C2 via S135 phosphorylation catalyzed by calcium/calmodulin-dependent protein kinase II. We now show that C2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. Moreover, we determined that S135 dephosphorylation is catalyzed by protein phosphatase-1 (PP1), which directly binds C2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP1CC | up-regulates activity
dephosphorylation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248503 |
Ser164 |
STDTVEHsLDNKDGP |
in vitro |
|
| pmid |
sentence |
| 19531356 |
nutrient-replete oocytes inhibit C2 via S135 phosphorylation catalyzed by calcium/calmodulin-dependent protein kinase II. We now show that C2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. Moreover, we determined that S135 dephosphorylation is catalyzed by protein phosphatase-1 (PP1), which directly binds C2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CASP2 | form complex 
binding
|
Caspase 2 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256389 |
|
|
|
|
| pmid |
sentence |
| 21828056 |
Like other caspases, caspase-2 is synthesized as an inactive zymogen. The zymogen sequence includes a long prodomain containing a CARD followed by a large domain, a linker, and a small domain. Caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit (p19) and the small subunit (p12). This p19/p12 dimer self-associates to form the active caspase-2 |
|
| Publications: |
1 |
| + |
CASP2 | form complex
binding
|
Caspase-2 PIDDosome |
0.858 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262641 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20158568 |
The PIDDosome consists of the proteins PIDD, RAIDD and caspase-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BIRC2 | down-regulates
binding
|
CASP2 |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146738 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16701639 |
However, among hiap1, hiap2 and xiap, only hiap2 binds and inhibits caspase-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUNX3 | up-regulates quantity by expression 
transcriptional regulation
|
CASP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255094 |
|
|
Homo sapiens |
MKN-1 Cell |
| pmid |
sentence |
| 17956589 |
Comprehensive analysis using a cDNA microarray showed that RUNX3 upregulated 17 apoptosis-related genes (including FADD, TRAF6, caspase-2, ING1, ING4, Calpain 10, and DNase1) and downregulated 135 apoptosis-related genes (including FLIP, PEA15, TXN2, HSPD1, IKK, and TIAL1) in MKN-1 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CASP2
- 
- 