| + |
A1/b1 integrin | up-regulates activity 
|
PTK2 |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257701 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ECM | up-regulates 
|
A1/b1 integrin |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259035 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30889378 |
Upon binding to the extracellular matrix (ECM), the integrins organize the cytoskeleton and activate intracellular signaling, regulating complex cellular behaviors, including survival, proliferation, migration, and various cell fate transitions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
COL4A1 | up-regulates activity
binding
|
A1/b1 integrin |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272353 |
|
|
|
|
| pmid |
sentence |
| 35267698 |
Integrins constitute a major group of receptors for extracellular matrix components, including collagens.|Among the four types, the signaling mechanism of α1β1 and α2β1 integrins has especially been reported. These integrins bind to both collagen types I and IV; however, their affinities differ: α1β1 has a higher affinity for collagen type IV, while α2β1 preferentially binds to collagen type I [13,23]. |
|
| Publications: |
1 |
| + |
Laminin-1 | up-regulates activity
binding
|
A1/b1 integrin |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253254 |
|
|
|
|
| pmid |
sentence |
| 9361014 |
Using integrin-specific antibodies, recognition sites for the alpha1beta1 and alpha2beta1 integrins were identified in the short arms of both laminin alpha1- and alpha2-chain isoforms. Comparisons with a beta-alpha chimeric short arm protein possessing beta1-chain domain VI further localized these activities to alpha-chain domain VI. |
|
| Publications: |
1 |
| + |
Kindlin | up-regulates activity
binding
|
A1/b1 integrin |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259000 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29544897 |
Kindlins bind with β-integrin cytoplasmic tails and execute broad biological functions including directed cell migration, proliferation, differentiation and survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ITGA1 | form complex 
binding
|
A1/b1 integrin |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253169 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
| + |
ITGB1BP1 | down-regulates activity 
binding
|
A1/b1 integrin |
0.753 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257639 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19118207 |
Integrins also bind to many PTBdomain-containing proteins (Calderwood et al., 2003) – including Dok1 and integrincytoplasmic-domain-associated protein 1 (ICAP1) – and these can compete with talin for binding to integrin and so can impair activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
COL1A1 | up-regulates activity
binding
|
A1/b1 integrin |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253247 |
|
|
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 12123670 |
We have developed a cell-free assay for binding of solubilized beta1 integrins to their physiologically relevant ligands using an electrochemiluminescent detection method|Binding was clearly optimal for the presumed physiological ligands, i.e., collagen IV for a1b1, collagen I for a2b1, VCAM-Ig for a4b1, fibronectin (the 120-kDa cell attachment fragment was used) for a5b1, and laminin for a6b1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COL4A4 | up-regulates activity
binding
|
A1/b1 integrin |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272350 |
|
|
|
|
| pmid |
sentence |
| 35267698 |
Integrins constitute a major group of receptors for extracellular matrix components, including collagens.|Among the four types, the signaling mechanism of α1β1 and α2β1 integrins has especially been reported. These integrins bind to both collagen types I and IV; however, their affinities differ: α1β1 has a higher affinity for collagen type IV, while α2β1 preferentially binds to collagen type I [13,23]. |
|
| Publications: |
1 |
| + |
ITGB1 | form complex
binding
|
A1/b1 integrin |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253170 |
|
|
|
|
| pmid |
sentence |
| 16988024 |
Integrins are one of the major families of cell adhesion receptors (Humphries, 2000; Hynes, 2002). All integrins are non-covalently-linked, heterodimeric molecules containing an α and a β subunit. Both subunits are type I transmembrane proteins, containing large extracellular domains and mostly short cytoplasmic domains (Springer and Wang, 2004; Arnaout et al., 2005). Mammalian genomes contain 18 α subunit and 8 β subunit genes, and to date 24 different α,β combinations have been identified at the protein level. Although some subunits only appear in a single heterodimer, twelve integrins contain the β1 subunit, and five contain αV. |
|
| Publications: |
1 |
| Pathways: | Integrin Signaling |
| + |
DOK1 | down-regulates activity
binding
|
A1/b1 integrin |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257670 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19118207 |
Integrins also bind to many PTBdomain-containing proteins (Calderwood et al., 2003) – including Dok1 and integrincytoplasmic-domain-associated protein 1 (ICAP1) – and these can compete with talin for binding to integrin and so can impair activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
TLN1 | up-regulates activity
binding
|
A1/b1 integrin |
0.684 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257608 |
|
|
Mus musculus |
Blood Platelet |
| pmid |
sentence |
| 19118207 |
Over the past 10 years, the binding of talin to the cytoplasmic tail of integrin-β subunits has been established to have a key role in integrin activation. Binding of the phosphotyrosinebinding (PTB)-domain-like subdomain of the protein 4.1, ezrin, radixin, moesin (FERM) domain of talin to the conserved WxxxNP(I/L)Y motif of the β-integrin tail permits additional weaker interactions between talin and the membrane-proximal region of the tail that trigger integrin activation, probably through the disruption of inhibitory interactions between α- and β-subunit cytoplasmic tails. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Integrin Signaling |
| + |
TGFBI | up-regulates activity
binding
|
A1/b1 integrin |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253269 |
|
|
|
|
| pmid |
sentence |
| 26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
| Publications: |
1 |
| + |
COL1A2 | up-regulates activity
binding
|
A1/b1 integrin |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253248 |
|
|
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 12123670 |
We have developed a cell-free assay for binding of solubilized beta1 integrins to their physiologically relevant ligands using an electrochemiluminescent detection method|Binding was clearly optimal for the presumed physiological ligands, i.e., collagen IV for a1b1, collagen I for a2b1, VCAM-Ig for a4b1, fibronectin (the 120-kDa cell attachment fragment was used) for a5b1, and laminin for a6b1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COL4A3 | up-regulates activity
binding
|
A1/b1 integrin |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272351 |
|
|
|
|
| pmid |
sentence |
| 35267698 |
Integrins constitute a major group of receptors for extracellular matrix components, including collagens.|Among the four types, the signaling mechanism of α1β1 and α2β1 integrins has especially been reported. These integrins bind to both collagen types I and IV; however, their affinities differ: α1β1 has a higher affinity for collagen type IV, while α2β1 preferentially binds to collagen type I [13,23]. |
|
| Publications: |
1 |
| + |
COL4A5 | up-regulates activity
binding
|
A1/b1 integrin |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272349 |
|
|
|
|
| pmid |
sentence |
| 35267698 |
Integrins constitute a major group of receptors for extracellular matrix components, including collagens.|Among the four types, the signaling mechanism of α1β1 and α2β1 integrins has especially been reported. These integrins bind to both collagen types I and IV; however, their affinities differ: α1β1 has a higher affinity for collagen type IV, while α2β1 preferentially binds to collagen type I [13,23]. |
|
| Publications: |
1 |
| + |
COL4A6 | up-regulates activity
binding
|
A1/b1 integrin |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272352 |
|
|
|
|
| pmid |
sentence |
| 35267698 |
Integrins constitute a major group of receptors for extracellular matrix components, including collagens.|Among the four types, the signaling mechanism of α1β1 and α2β1 integrins has especially been reported. These integrins bind to both collagen types I and IV; however, their affinities differ: α1β1 has a higher affinity for collagen type IV, while α2β1 preferentially binds to collagen type I [13,23]. |
|
| Publications: |
1 |
| + |
COL4A2 | up-regulates activity
binding
|
A1/b1 integrin |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272348 |
|
|
|
|
| pmid |
sentence |
| 35267698 |
Integrins constitute a major group of receptors for extracellular matrix components, including collagens.|Among the four types, the signaling mechanism of α1β1 and α2β1 integrins has especially been reported. These integrins bind to both collagen types I and IV; however, their affinities differ: α1β1 has a higher affinity for collagen type IV, while α2β1 preferentially binds to collagen type I [13,23]. |
|
| Publications: |
1 |
| + |
A1/b1 integrin | up-regulates
|
Cell_adhesion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269008 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25388208 |
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SEMA7A | up-regulates activity
binding
|
A1/b1 integrin |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253249 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17377534 |
Semaphorin 7A initiates T-cell-mediated inflammatory responses through alpha1beta1 integrin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
A1/b1 integrin
CPX-1798