| + |
CASP3 | up-regulates activity 
cleavage
|
PSEN2 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261743 |
Asp326 |
YDPEMEEdSYDSFGE |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261749 |
Asp329 |
EMEEDSYdSFGEPSY |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Alzheimer |
| + |
CASP7 | up-regulates activity
cleavage
|
PSEN2 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261746 |
Asp326 |
YDPEMEEdSYDSFGE |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261751 |
Asp329 |
EMEEDSYdSFGEPSY |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CASP1 | up-regulates activity
cleavage
|
PSEN2 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261747 |
Asp326 |
YDPEMEEdSYDSFGE |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261748 |
Asp329 |
EMEEDSYdSFGEPSY |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CASP8 | up-regulates activity
cleavage
|
PSEN2 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261744 |
Asp326 |
YDPEMEEdSYDSFGE |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261752 |
Asp329 |
EMEEDSYdSFGEPSY |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Alzheimer |
| + |
CASP6 | up-regulates activity
cleavage
|
PSEN2 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261745 |
Asp326 |
YDPEMEEdSYDSFGE |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261750 |
Asp329 |
EMEEDSYdSFGEPSY |
in vitro |
|
| pmid |
sentence |
| 10069390 |
In decreasing order of activity, caspase-8, -3, -1, -6 and -7 proteolysed PS2 at the recognition site D326SYD329. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK1D |
phosphorylation
|
PSEN2 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250799 |
Ser19 |
EVCDERTsLMSAESP |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250803 |
Ser7 |
sDSEEEVC |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250804 |
Ser9 |
LTFMASDsEEEVCDE |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK1A1 |
phosphorylation
|
PSEN2 |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250790 |
Ser19 |
EVCDERTsLMSAESP |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250791 |
Ser7 |
sDSEEEVC |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250792 |
Ser9 |
LTFMASDsEEEVCDE |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK2A1 |
phosphorylation
|
PSEN2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250932 |
Ser19 |
EVCDERTsLMSAESP |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250936 |
Ser7 |
sDSEEEVC |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250937 |
Ser9 |
LTFMASDsEEEVCDE |
in vitro |
|
| pmid |
sentence |
| 8972483 |
In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK1D | up-regulates activity
phosphorylation
|
PSEN2 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250800 |
Ser327 |
DPEMEEDsYDSFGEP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250801 |
Ser330 |
MEEDSYDsFGEPSYP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250802 |
Ser335 |
YDSFGEPsYPEVFEP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK2A1 | up-regulates activity
phosphorylation
|
PSEN2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250933 |
Ser327 |
DPEMEEDsYDSFGEP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250934 |
Ser330 |
MEEDSYDsFGEPSYP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250935 |
Ser335 |
YDSFGEPsYPEVFEP |
in vitro |
|
| pmid |
sentence |
| 9558331 |
In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ESR1 | up-regulates quantity by expression 
transcriptional regulation
|
PSEN2 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271691 |
|
|
|
|
| pmid |
sentence |
| 14764652 |
Estrogen-induced transcriptional activities of both ERalpha and ERbeta and mRNA expression of estrogen-responsive genes, including pS2, c-myc, and cyclin D1, were suppressed by PP5 but enhanced by PP5 antisense oligonucleotide. |
|
| Publications: |
1 |
| + |
APH1A | up-regulates
binding
|
PSEN2 |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93265 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12297508 |
Gamma secretase subunit. Leads to ps1/ps2 eterodimer complex stabilisation. By using co-immunoprecipitation and nickel affinity pull-down approaches, we now show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
APH1B | up-regulates
binding
|
PSEN2 |
0.903 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93310 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12297508 |
By using co-immunoprecipitation and nickel affinity pull-down approaches, we now show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NCSTN | up-regulates
binding
|
PSEN2 |
0.938 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81936 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10993067 |
Nicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
3.0
PSEN2
- 
- 