| + |
TNC | up-regulates activity 
binding
|
SDC1 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281331 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19838819 |
Cells can interact with tenascin-C via cell-surface receptors including integrins α2β1,α7β1, α9β1 and αvβ3, syndecans 1 and 4, annexin II, and epidermal growth factor receptor (EGFR) amongst others (Fig. 1, Table 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SDC1 | up-regulates activity
binding
|
SDCBP |
0.75 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282622 |
|
|
Homo sapiens |
PANC-1 Cell |
| pmid |
sentence |
| 30918400 |
The Sdc1 C-terminus binds to the PDZ-domain containing protein, syntenin, and this complex is involved in assembly of multimers that organize intracellular signal transduction pathways |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARF6 | up-regulates quantity
relocalization
|
SDC1 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282623 |
|
|
Homo sapiens |
PANC-1 Cell |
| pmid |
sentence |
| 30918400 |
Moreover, expression of the constitutively active Arf6Q67L mutant in iKras* cells resulted in the generation of membrane ruffling and rescued the decrease in Sdc1 membrane localization upon Kras* extinction, whereas expression of the dominant negative Arf6T27N inhibited Sdc1 membrane localization in the presence of Kras* (Extended Data Fig.7c-e). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SDC1 | up-regulates 
|
Entosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282626 |
|
|
Homo sapiens |
PANC-1 Cell |
| pmid |
sentence |
| 40952410 |
Entosis, a form of cell-in-cell (CIC) structure formation where one cell invades and becomes internalized by another, has long been observed in various malignancies and is considered a critical cellular process in cancer progression, with potential impacts on tumor heterogeneity, survival, and metastasis. Using immunohistochemistry, flow cytometry, and entosis assays, our findings reveal that SDC1 prominently localizes at cell-cell contact points, facilitating stable intercellular adhesion and promoting entotic activity. Our study sheds light on the critical role of SDC1 in promoting CIC formation and cancer progression, highlighting its potential as a therapeutic target to disrupt entotic mechanisms in PDAC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SDC1 | up-regulates activity
binding
|
RAC1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282625 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30918400 |
To identify Sdc1 domains required for Rac1 activation and macropinocytosis, we constructed a series of Sdc1 truncation mutants24,25 that were expressed on the cell surface, except for soluble Sdc1 protein, which was detected in culture medium because it lacks the transmembrane and intra-cellular domains (Extended Data Fig.9a, b). As expected, expression of full-length Sdc1 fully rescued Rac1 activity in Sdc-depleted cells. In contrast, soluble Sdc1 failed to reactivate Rac1 (Extended Data Fig.9c), indicating the membrane localization of SDC1 is essential for macropinocytosis. Deletion of Sdc1 extra-cellular domain (ΔEct) also abolished its activity toward Rac1. However, the GAG mutant with mutated heparan sulfate modification sites exerted a partial rescue effect (Extended Data Fig.9c), suggesting heparin sulfate may not be essential for this function. Interestingly, the C30 mutant (deletion of the C-terminal 30 amino acids) also failed to rescue Rac1 activity in Sdc1-depleted cells (Extended Data Fig.9c) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SDC1 | up-regulates activity
binding
|
ERBB2 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282614 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26350464 |
We find that sites in the extracellular domains of Sdc1 and Sdc4 are responsible for capturing HER2 and EGFR, respectively, along with the α3β1 integrin. This ternary receptor complex docks with the α6β4 integrin via its cytoplasmic link with the syndecan, leading to β4 phosphorylation and downstream signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SDC1 | up-regulates activity
binding
|
A3/b1 integrin |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282616 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26350464 |
We find that sites in the extracellular domains of Sdc1 and Sdc4 are responsible for capturing HER2 and EGFR, respectively, along with the α3β1 integrin. This ternary receptor complex docks with the α6β4 integrin via its cytoplasmic link with the syndecan, leading to β4 phosphorylation and downstream signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MDK | up-regulates activity
binding
|
SDC1 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282572 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 41570933 |
Syndecans are transmembrane HSPGs that act as co-receptors for MDK, facilitating clustering with other signaling partners such as LRP1 or integrins. Syndecan-1 is critical for cell–matrix interaction and angiogenesis, and in the TME, the MDK–SDC1 complex enhances fibroblast activation, ECM deposition, and metastatic invasion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
SDC1
- 
- 