+ |
PRKCA | up-regulates quantity by stabilization
phosphorylation
|
VTN |
0.323 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248962 |
Ser381 |
RNRKGYRsQRGHSRG |
in vitro |
|
pmid |
sentence |
9030777 |
Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PRKCG | up-regulates quantity by stabilization
phosphorylation
|
VTN |
0.288 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248964 |
Ser381 |
RNRKGYRsQRGHSRG |
in vitro |
|
pmid |
sentence |
9030777 |
Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PRKCB | up-regulates quantity by stabilization
phosphorylation
|
VTN |
0.307 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248963 |
Ser381 |
RNRKGYRsQRGHSRG |
in vitro |
|
pmid |
sentence |
9030777 |
Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PRKACA |
phosphorylation
|
VTN |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250072 |
Ser397 |
NQNSRRPsRATWLSL |
in vitro |
|
pmid |
sentence |
1706595 |
Phosphorylation of vitronectin by protein kinase A is stoichiometric (approx. 1 mol/mol), that it is targeted to one site (Ser-378) at the C-terminal edge of the heparin-binding domain. gh the role of phosphorylation by PKA remains to be established, the identification of Ser-378 as the sole site for PKA action, and the proximity of the phosphorylation site to the point of cleavage that converts V75 into V65 10' focuses attention on a putative role for PKA in the modulation of this cleavage. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CSNK2A1 | up-regulates activity
phosphorylation
|
VTN |
0.333 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250970 |
Thr69 |
VTRGDVFtMPEDEYT |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
9733784 |
Therefore, we expressed Vn in a baculovirus system and show (i) that the CKII phosphorylation of wt-Vn enhances the adhesion of bovine aorta endothelial cells; (ii) that the double mutant T50E/T57E (in which the neutral Thr residues are replaced by the negatively charged Glu residues considered analogs of Thr-P) has a significantly enhanced capacity to promote cell adhesion and to accelerate cell spreading when compared with either wild-type Vn or to the neutral T50A/T57A mutant |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250971 |
Thr76 |
TMPEDEYtVYDDGEE |
Mus musculus |
|
pmid |
sentence |
9733784 |
Therefore, we expressed Vn in a baculovirus system and show (i) that the CKII phosphorylation of wt-Vn enhances the adhesion of bovine aorta endothelial cells; (ii) that the double mutant T50E/T57E (in which the neutral Thr residues are replaced by the negatively charged Glu residues considered analogs of Thr-P) has a significantly enhanced capacity to promote cell adhesion and to accelerate cell spreading when compared with either wild-type Vn or to the neutral T50A/T57A mutant |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
FGG | down-regulates activity
binding
|
VTN |
0.431 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251969 |
|
|
Homo sapiens |
|
pmid |
sentence |
2243140 |
Fibrinogen y-chain carboxyterminal (GQQHHLGGAKQAGDV) peptides inhibit fibrinogen, fibronectin (Fn), vitronectin, and von Willebrand factor (vWF) binding to the platelet glycoprotein Ilb-Illa complex (GP lIbII1a). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VTN | up-regulates activity
binding
|
A8/b1 integrin |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253307 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
7559467 |
The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |