| + |
COL1A1 | up-regulates activity 
binding
|
A11/b1 integrin |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253345 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12496264 |
Modeling of the alpha I domain-collagen peptide complexes could partially explain the observed preference of different I domains for certain GFOGER sequence variations. In summary, our data indicate that the GFOGER sequence in fibrillar collagens is a common recognition motif used by alpha(1)beta(1), alpha(2)beta(1), and also alpha(11)beta(1) integrins. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Kindlin | up-regulates activity
binding
|
A11/b1 integrin |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259022 |
|
|
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 |
| + |
A11/b1 integrin | up-regulates 
|
Cell_migration |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253349 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 11518510 |
In addition, alpha11beta1 mediated contraction of fibrillar collagen gels in a manner similar to alpha2beta1, and supported migration on collagen I in response to chemotactic stimuli. Our data support a role for alpha11beta1 as a receptor for interstitial collagens on mesenchymally derived cells and suggest a multifunctional role of alpha11beta1 in the recognition and organization of interstitial collagen matrices during development. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
A11/b1 integrin | up-regulates activity
|
PTK2 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257710 |
|
|
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 |
| + |
DOK1 | down-regulates activity 
binding
|
A11/b1 integrin |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257679 |
|
|
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 |
| + |
TLN1 | up-regulates activity
binding
|
A11/b1 integrin |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257617 |
|
|
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 |
| + |
ITGB1BP1 | down-regulates activity
binding
|
A11/b1 integrin |
0.734 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257648 |
|
|
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 |
| + |
ITGA11 | form complex 
binding
|
A11/b1 integrin |
0.706 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253187 |
|
|
|
|
| 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 |
| + |
COL1A2 | up-regulates activity
binding
|
A11/b1 integrin |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253346 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 12496264 |
Modeling of the alpha I domain-collagen peptide complexes could partially explain the observed preference of different I domains for certain GFOGER sequence variations. In summary, our data indicate that the GFOGER sequence in fibrillar collagens is a common recognition motif used by alpha(1)beta(1), alpha(2)beta(1), and also alpha(11)beta(1) integrins. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ITGB1 | form complex
binding
|
A11/b1 integrin |
0.706 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253188 |
|
|
|
|
| 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 |
| + |
ECM | up-regulates
|
A11/b1 integrin |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259050 |
|
|
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 |
| + |
A11/b1 integrin | up-regulates
|
Cell_adhesion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269017 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25388208 |
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
A11/b1 integrin
CPX-1818