| + |
MAPK1 | unknown
phosphorylation
|
NID1 |
0.25 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262771 |
Ser333 |
YSVPSVLsPRRAATE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 22028470 |
We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1) |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FBLN2 | up-regulates quantity by stabilization 
binding
|
NID1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282710 |
|
|
Homo sapiens |
MiaPaCa-2 Cell |
| pmid |
sentence |
| 22105367 |
MUC4 is a large transmembrane type I glycoprotein that is overexpressed in pancreatic cancer (PC) and has been shown to be associated with its progression and metastasis. Here we showed that the nidogen-like (NIDO) domain of MUC4, which is similar to the G1-domain present in the nidogen or entactin (an extracellular matrix protein), contributes to the protein-protein interaction property of MUC4.Importantly, the MUC4-NIDO domain interacts with fibulin-2, and this may be a possible mechanism through which MUC4 promotes pancreatic cancer metastasis.In the current study, we postulated that under cancer conditions, through the NIDO-domain, MUC4 present at the basal surface of the epithelial cells may competitively inhibit the normal interaction between fibulin-2 and nidogen protein of the basement membrane (BM) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NID1 | up-regulates 
|
ECM_assembly |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22105367 |
Many of the basement membrane proteins like collagenV, laminin, entactin/nidogen, and proteoglycans have specific protein-protein interaction motifs in their domain structures. These proteins interact with each other in a coordinated fashion and maintaining the supramolecular structural organization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NID1 | up-regulates quantity by stabilization
binding
|
Laminin-1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282712 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22105367 |
Nidogen (entactin) is a ubiquitous constituent of the basement membrane. It has three globular structures (G1, G2 and G3). It was shown that the G3 and G2 domains of nidogen interact with laminin and collagen IV respectively, and thus, bridges laminin and collagen IV in the basement membrane |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NID1 | up-regulates quantity by stabilization
binding
|
COL4A4 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282713 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22105367 |
Nidogen (entactin) is a ubiquitous constituent of the basement membrane. It has three globular structures (G1, G2 and G3). It was shown that the G3 and G2 domains of nidogen interact with laminin and collagen IV respectively, and thus, bridges laminin and collagen IV in the basement membrane |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
NID1
- 
- 