Relation Results

Summary

Name A2/b1 integrin
Primary ID SIGNOR-C160
Links CPX-1801
Type complex
Formed by ITGA2, ITGB1
Relations 19

Viewer

Type: Score: Layout: SPV 
0.3630.4370.6260.4860.5310.4350.3190.7510.70.7530.7510.6050.4730.590.70.4270.3610.456KindlinA2/b1 integrinCOL4A4COL1A1COL4A1Laminin-1COL4A3DOK1ITGA2Cell_adhesionITGB1BP1ITGB1TLN1COL4A2PTK2ECMCOL4A6COL21A1COL2A1

Relations

Regulator
Mechanism
target
score
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.363
Identifier Residue Sequence Organism Cell Line
SIGNOR-259014 Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.437
Identifier Residue Sequence Organism Cell Line
SIGNOR-253245 Homo sapiens K-562 Cell
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.626
Identifier Residue Sequence Organism Cell Line
SIGNOR-272346
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.486
Identifier Residue Sequence Organism Cell Line
SIGNOR-253242 Homo sapiens K-562 Cell
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.531
Identifier Residue Sequence Organism Cell Line
SIGNOR-253255
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.435
Identifier Residue Sequence Organism Cell Line
SIGNOR-253244 Homo sapiens K-562 Cell
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png binding A2/b1 integrin 0.319
Identifier Residue Sequence Organism Cell Line
SIGNOR-257671 Homo sapiens
pmid sentence
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
+ form complex img/form-complex.png binding A2/b1 integrin 0.751
Identifier Residue Sequence Organism Cell Line
SIGNOR-253171
pmid sentence
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
+ up-regulates img/indirect-activation.png Cell_adhesion 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-269009 Homo sapiens
pmid sentence
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png binding A2/b1 integrin 0.753
Identifier Residue Sequence Organism Cell Line
SIGNOR-257640 Homo sapiens
pmid sentence
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
+ form complex img/form-complex.png binding A2/b1 integrin 0.751
Identifier Residue Sequence Organism Cell Line
SIGNOR-253172
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.605
Identifier Residue Sequence Organism Cell Line
SIGNOR-257609 Mus musculus Blood Platelet
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.473
Identifier Residue Sequence Organism Cell Line
SIGNOR-253243 Homo sapiens K-562 Cell
pmid sentence
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
+ up-regulates activity img/indirect-activation.png PTK2 0.59
Identifier Residue Sequence Organism Cell Line
SIGNOR-257702 Homo sapiens
pmid sentence
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
+ up-regulates img/direct-activation.png binding A2/b1 integrin 0.626
Identifier Residue Sequence Organism Cell Line
SIGNOR-31787 Homo sapiens
pmid sentence
Both a2b1- and a1b1- inegrins are implicated in chondrocyte adhesion to native collagene i and ii
Publications: 1 Organism: Homo Sapiens
+ up-regulates img/direct-activation.png A2/b1 integrin 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-259043 Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.427
Identifier Residue Sequence Organism Cell Line
SIGNOR-253246 Homo sapiens K-562 Cell
pmid sentence
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
+ up-regulates activity img/direct-activation.png binding A2/b1 integrin 0.361
Identifier Residue Sequence Organism Cell Line
SIGNOR-272347
pmid sentence
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
+ up-regulates img/direct-activation.png binding A2/b1 integrin 0.456
Identifier Residue Sequence Organism Cell Line
SIGNOR-31881 Homo sapiens
pmid sentence
Both a2b1- and a1b1- integrins are implicated in chondrocyte adhesion to native collagene i and ii
Publications: 1 Organism: Homo Sapiens
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