| + |
ITGB3 | form complex 
binding
|
AIIB/b3 integrin |
0.947 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253198 |
|
|
|
|
| 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 |
| + |
AIIB/b3 integrin | up-regulates activity 
binding
|
FGA |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253359 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 16418530 |
In response to agonist stimulation, the αIIbβ3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AIIB/b3 integrin | up-regulates 
|
Cell_adhesion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269022 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25388208 |
Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CIB1 | down-regulates activity 
binding
|
AIIB/b3 integrin |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253357 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 16418530 |
In response to agonist stimulation, the alphaIIbbeta3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. This process contributes to both normal hemostasis and thrombosis. Activation of alphaIIbbeta3 is believed to occur in part via engagement of the beta3 cytoplasmic tail with talin; however, the role of the alphaIIb tail and its potential binding partners in regulating alphaIIbbeta3 activation is less clear. We report that calcium and integrin binding protein 1 (CIB1), which interacts directly with the alphaIIb tail, is an endogenous inhibitor of alphaIIbbeta3 activation; overexpression of CIB1 in megakaryocytes blocks agonist-induced alphaIIbbeta3 activation, whereas reduction of endogenous CIB1 via RNA interference enhances activation. CIB1 appears to inhibit integrin activation by competing with talin for binding to alphaIIbbeta3, thus providing a model for tightly controlled regulation of alphaIIbbeta3 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AIIB/b3 integrin | up-regulates activity
binding
|
PTPN1 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261800 |
|
|
|
|
| pmid |
sentence |
| 16115959 |
N this study, we demonstrate an essential role for protein-tyrosine phosphatase (PTP)-1B in this process. In resting platelets, c-Src forms a complex with alphaIIbbeta3 and Csk, which phosphorylates c-Src tyrosine 529 to maintain c-Src autoinhibition. Fibrinogen binding to alphaIIbbeta3 triggers PTP-1B recruitment to the alphaIIbbeta3-c-Src-Csk complex in a manner that is dependent on c-Src and specific tyrosine (tyrosine 152 and 153) and proline (proline 309 and 310) residues in PTP-1B. Studies of PTP-1B-deficient mouse platelets indicate that PTP-1B is required for fibrinogen-dependent Csk dissociation from alphaIIbbeta3, dephosphorylation of c-Src tyrosine 529, and c-Src activation. |
|
| Publications: |
1 |
| + |
DOK1 | down-regulates activity
binding
|
AIIB/b3 integrin |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257686 |
|
|
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 |
| + |
ITGB1BP1 | down-regulates activity
binding
|
AIIB/b3 integrin |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257655 |
|
|
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
|
AIIB/b3 integrin |
0.688 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253358 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 16418530 |
In response to agonist stimulation, the alphaIIbbeta3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. This process contributes to both normal hemostasis and thrombosis. Activation of alphaIIbbeta3 is believed to occur in part via engagement of the beta3 cytoplasmic tail with talin; however, the role of the alphaIIb tail and its potential binding partners in regulating alphaIIbbeta3 activation is less clear. We report that calcium and integrin binding protein 1 (CIB1), which interacts directly with the alphaIIb tail, is an endogenous inhibitor of alphaIIbbeta3 activation; overexpression of CIB1 in megakaryocytes blocks agonist-induced alphaIIbbeta3 activation, whereas reduction of endogenous CIB1 via RNA interference enhances activation. CIB1 appears to inhibit integrin activation by competing with talin for binding to alphaIIbbeta3, thus providing a model for tightly controlled regulation of alphaIIbbeta3 activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257624 |
|
|
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: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
AIIB/b3 integrin | up-regulates
|
Platelet_Adhesion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261867 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 25297919 |
VWF binding to GPIb-IX-V induces platelet activation, converting the major integrin αIIbβ3 from a low affinity to a high affinity receptor capable of engaging the C4 domain of VWF. This last step is essential for stable adhesion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AIIB/b3 integrin | up-regulates activity
|
PTK2 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257717 |
|
|
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 |
| + |
AIIB/b3 integrin | up-regulates
|
Platelet_aggregation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266067 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18278053 |
Activated alphaIIbbeta3 integrins bind fibrinogen, vWF and fibronectin, thus allowing firm platelet adhesion and platelet aggregation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
VWF | up-regulates activity
binding
|
AIIB/b3 integrin |
0.674 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261854 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 25297919 |
Many studies have contributed to shed light on the importance of von Willebrand factor (VWF) interaction with its platelet receptors, glycoprotein (GP) Ib-IX-V and αIIbβ3 integrin, in promoting primary platelet adhesion and aggregation following vessel injury |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CIB2 | up-regulates activity
binding
|
AIIB/b3 integrin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269669 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35408910 |
So far, two integrins have been found to interact with CIB2: αIIbβ3 is expressed by platelets and megakaryocytes and, apparently, a common target for all CIB family members, at odds with α7Bβ1D, which seems to be CIB2-specific and is expressed in skeletal muscles. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F-actin_assembly | down-regulates activity
relocalization
|
AIIB/b3 integrin |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261864 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27871158 |
Integrin αIIbβ3 is retained by the actin cytoskeleton in resting platelets but is released to the cell surface during platelet activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AIIB/b3 integrin | up-regulates activity
binding
|
FGB |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253361 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 16418530 |
In response to agonist stimulation, the αIIbβ3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AIIB/b3 integrin | up-regulates activity
binding
|
FGG |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253360 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 16418530 |
In response to agonist stimulation, the αIIbβ3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITGA2B | form complex
binding
|
AIIB/b3 integrin |
0.947 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253197 |
|
|
|
|
| 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 |
3.0
AIIB/b3 integrin
CPX-1799