| + |
PRKCD |
phosphorylation
|
ITGB7 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249205 |
Thr783 |
PLYKSAItTTINPRF |
Mus musculus |
T-cell Lymphoma Cell |
| pmid |
sentence |
| 12682249 |
Beta7 subunit is phosphorylated even in unstimulated TK-1 cells. Activation of TK-1 cells with anti-CD3 (Fig. 5_A) and PDBu (Fig. 5_B) increased the phosphorylation 1520%. | The result shows that the fourth amino acid of the tryptic peptide was phosphorylated. This phosphorylated threonine residue is most likely the first threonine (Thr782) of threonine triplet (Thr782784). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCB |
phosphorylation
|
ITGB7 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249200 |
Thr783 |
PLYKSAItTTINPRF |
Mus musculus |
T-cell Lymphoma Cell |
| pmid |
sentence |
| 12682249 |
Beta7 subunit is phosphorylated even in unstimulated TK-1 cells. Activation of TK-1 cells with anti-CD3 (Fig. 5_A) and PDBu (Fig. 5_B) increased the phosphorylation 1520%. | The result shows that the fourth amino acid of the tryptic peptide was phosphorylated. This phosphorylated threonine residue is most likely the first threonine (Thr782) of threonine triplet (Thr782784). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ITGB7 | form complex 
binding
|
AE/b7 integrin |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253292 |
|
|
|
|
| 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 |
| + |
ITGB7 | up-regulates activity 
|
PTK2 |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257726 |
|
|
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 |
| + |
Kindlin | up-regulates activity 
binding
|
ITGB7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259009 |
|
|
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 |
| + |
ITGB1BP1 | down-regulates activity 
binding
|
ITGB7 |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257664 |
|
|
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 |
| + |
DOK1 | down-regulates activity
binding
|
ITGB7 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257695 |
|
|
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
|
ITGB7 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257633 |
|
|
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 |
| + |
ITGB7 | form complex
binding
|
A4/b7 integrin |
0.858 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253294 |
|
|
|
|
| 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
ITGB7
- 
- 