| + |
SGK1 | down-regulates quantity
phosphorylation
|
NCSTN |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280122 |
Ser437 |
FLRARNIsGVVLADH |
Homo sapiens |
|
| pmid |
sentence |
| 22590650 |
Furthermore, SGK1 directly bound to and phosphorylated Nicastrin on Ser437, thereby promoting protein degradation.|We showed that SGK1 downregulates Nicastrin protein levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SGK1 | down-regulates quantity by destabilization
phosphorylation
|
NCSTN |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276415 |
Ser437 |
FLRARNIsGVVLADH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22590650 |
SGK1 directly bound to and phosphorylated NCT on Ser437, thereby promoting protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NCSTN | up-regulates
binding
|
APH1A |
0.967 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12297508 |
We 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. Similar to the loss of presenilin or nicastrin, the inactivation of endogenous maph-1 using small interfering rnas results in the decrease of presenilin levels, accumulation of gamma-secretase substrates (app carboxyl-terminal fragments), and reduction of gamma-secretase products (amyloid-beta peptides and the intracellular domains of app and notch). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96250 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12471034 |
We 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. Similar to the loss of presenilin or nicastrin, the inactivation of endogenous maph-1 using small interfering rnas results in the decrease of presenilin levels, accumulation of gamma-secretase substrates (app carboxyl-terminal fragments), and reduction of gamma-secretase products (amyloid-beta peptides and the intracellular domains of app and notch). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103611 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12857757 |
We 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. Similar to the loss of presenilin or nicastrin, the inactivation of endogenous maph-1 using small interfering rnas results in the decrease of presenilin levels, accumulation of gamma-secretase substrates (app carboxyl-terminal fragments), and reduction of gamma-secretase products (amyloid-beta peptides and the intracellular domains of app and notch). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
APH1B | up-regulates
binding
|
NCSTN |
0.94 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93307 |
|
|
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.These data indicate that maph-1 is probably a functional component of the gamma-secretase complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NCSTN | up-regulates
binding
|
PSEN1 |
0.965 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118852 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14572442 |
Nicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96253 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12471034 |
Nicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98724 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12603837 |
Nicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| Pathways: | Alzheimer |
| + |
NCSTN | form complex
binding
|
gamma-secretase |
0.964 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25610395 |
-Secretase is a four subunit, 19-pass transmembrane enzymeBiochemical studies indicated that -secretase activity is catalyzed by the presenilin (PS)-containing macromolecular complex (Li et al., 2000a). The search for other components of the complex revealed three additional proteins: nicastrin (Nct), anterior pharynx-defective-1 (Aph-1), and presenilin enhancer-2 (Pen-2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
APH1A | up-regulates
binding
|
NCSTN |
0.967 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93259 |
|
|
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 |
0.941 |
| 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 |