+ |
PRKCA | down-regulates
phosphorylation
|
ITGB4 |
0.51 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124494 |
Ser1360 |
VLRSPSGsQRPSVSD |
Homo sapiens |
|
pmid |
sentence |
15121854 |
Egf stimulates a pkc-?-Dependent pathway that results in the phosphorylation of the ?4 Integrin subunit on serine residues and its redistribution to actin-rich structures together, these results highlight the importance of serine phosphorylation in regulating type ii hemidesmosome disassembly, implicate a cluster of serine residues within the connecting segment of ?4, and argue for a key role for pkc-? In regulating these structures |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124498 |
Ser1494 |
TLTRDYNsLTRSEHS |
Homo sapiens |
|
pmid |
sentence |
15121854 |
Egf stimulates a pkc-?-Dependent pathway that results in the phosphorylation of the ?4 Integrin subunit on serine residues and its redistribution to actin-rich structures together, these results highlight the importance of serine phosphorylation in regulating type ii hemidesmosome disassembly, implicate a cluster of serine residues within the connecting segment of ?4, and argue for a key role for pkc-? In regulating these structures |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKACA | down-regulates
phosphorylation
|
ITGB4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156873 |
Ser1364 |
PSGSQRPsVSDDTGC |
Homo sapiens |
|
pmid |
sentence |
17615294 |
Additionally, we show that s1360 and s1364 of beta4 are the only residues phosphorylated by pkc and pka in cells, respectivelywe have defined three regions on beta4 that together harbor all the serine and threonine phosphorylation sites and show that three serines (s1356, s1360, and s1364), previously implicated in hd regulation, prevent the interaction of beta4 with the plectin actin-binding domain when phosphorylated |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ITGB4 | up-regulates activity
binding
|
PMP22 |
0.382 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251896 |
|
|
Mus musculus |
|
pmid |
sentence |
16436605 |
PMP22 is in a complex with α6β4 integrin and laminin. PMP22 and β4 integrin are in a complex in a variety of cell types. The interaction with the integrins provides PMP22 with the ability to modulate the cell–ECM communications, as well as intracellular events. Signaling between the ECM and the intracellular compartment is essential for SC myelination, as well as cellular differentiation and motility, in general. The identification of PMP22 as a binding partner for an integrin signaling complex provides a major step toward understanding the role of this disease-linked molecule in the nervous system and in non-neural cell types. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
ITGB4 | up-regulates
binding
|
PI3K |
0.4 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252697 |
|
|
Homo sapiens |
|
pmid |
sentence |
9428518 |
Stable expression of alpha6beta4 increased carcinoma invasion in a pi3k-dependent manner, and transient expression of a constitutively active pi3k increased invasion in the absence of alpha6beta4. Ligation of alpha6beta4 stimulated significantly more pi3k activity than ligation of beta1 integrins, establishing specificity among integrins for pi3k activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Integrin Signaling |
+ |
ITGB4 | form complex
binding
|
A6/b4 integrin |
0.761 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253200 |
|
|
|
|
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 |
+ |
ITGB4 | up-regulates
binding
|
PIK3CA |
0.391 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-54530 |
|
|
Homo sapiens |
|
pmid |
sentence |
9428518 |
Stable expression of alpha6beta4 increased carcinoma invasion in a pi3k-dependent manner, and transient expression of a constitutively active pi3k increased invasion in the absence of alpha6beta4. Ligation of alpha6beta4 stimulated significantly more pi3k activity than ligation of beta1 integrins, establishing specificity among integrins for pi3k activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
F2RL1 | down-regulates quantity by repression
transcriptional regulation
|
ITGB4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254859 |
|
|
Homo sapiens |
|
pmid |
sentence |
21072196 |
PAR-2 activation up-regulated four genes more than 5 fold (DUSP6, WWOX, AREG, SERPINB2) and down-regulated another six genes more than 3 fold (TXNIP, RARG, ITGB4, CTSD, MSC and TM4SF15). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DOK1 | down-regulates activity
binding
|
ITGB4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257689 |
|
|
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 |
+ |
Kindlin | up-regulates activity
binding
|
ITGB4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259003 |
|
|
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 |
+ |
ITGB1BP1 | down-regulates activity
binding
|
ITGB4 |
0.356 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257658 |
|
|
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 |
+ |
ITGB4 | up-regulates
binding
|
PIK3CD |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-54700 |
|
|
Homo sapiens |
|
pmid |
sentence |
9428518 |
Stable expression of alpha6beta4 increased carcinoma invasion in a pi3k-dependent manner, and transient expression of a constitutively active pi3k increased invasion in the absence of alpha6beta4. Ligation of alpha6beta4 stimulated significantly more pi3k activity than ligation of beta1 integrins, establishing specificity among integrins for pi3k activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEU1 | down-regulates activity
|
ITGB4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260655 |
|
|
Homo sapiens |
HT-29 Cell |
pmid |
sentence |
19151752 |
In HT-29 cells cultured with 10% fetal bovine serum (FBS), the phosphorylation of integrin β4 was significantly decreased in NEU1-overexpressing cells and the level seemed to be inversely correlated with the sialidase activity. These results suggest that NEU1 is involved in the regulation of integrin β4 phosphorylation probably through desialylation in colon cancer cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ITGB4 | up-regulates activity
|
PTK2 |
0.57 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257720 |
|
|
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 |
+ |
ITGB4 | up-regulates
binding
|
PIK3CG |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-54703 |
|
|
Homo sapiens |
|
pmid |
sentence |
9428518 |
Stable expression of alpha6beta4 increased carcinoma invasion in a pi3k-dependent manner, and transient expression of a constitutively active pi3k increased invasion in the absence of alpha6beta4. Ligation of alpha6beta4 stimulated significantly more pi3k activity than ligation of beta1 integrins, establishing specificity among integrins for pi3k activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TLN1 | up-regulates activity
binding
|
ITGB4 |
0.484 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257627 |
|
|
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 |
+ |
ITGB4 | up-regulates
binding
|
PIK3CB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-54615 |
|
|
Homo sapiens |
|
pmid |
sentence |
9428518 |
Stable expression of alpha6beta4 increased carcinoma invasion in a pi3k-dependent manner, and transient expression of a constitutively active pi3k increased invasion in the absence of alpha6beta4. Ligation of alpha6beta4 stimulated significantly more pi3k activity than ligation of beta1 integrins, establishing specificity among integrins for pi3k activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RTKs | up-regulates activity
phosphorylation
|
ITGB4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259031 |
|
|
Homo sapiens |
|
pmid |
sentence |
30889378 |
The RTKs in turn induce phosphorylation of focal adhesion kinase (FAK) or the signaling domain of the b4 integrin. These elements recruit distinct subsets of signaling enzymes and adaptors, refining the specificity of individual partner RTKs. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Integrin Signaling |