Type |
Details |
Score |
Publication |
First Author: |
da Silva AJ |
Year: |
1997 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production. |
Volume: |
94 |
Issue: |
14 |
Pages: |
7493-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Geng L |
Year: |
2001 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Adaptor FYB (Fyn-binding protein) regulates integrin-mediated adhesion and mediator release: differential involvement of the FYB SH3 domain. |
Volume: |
98 |
Issue: |
20 |
Pages: |
11527-32 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
819
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
773
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Yuan M |
Year: |
2005 |
Journal: |
FEBS Lett |
Title: |
Fyn binding protein, Fyb, interacts with mammalian actin binding protein, mAbp1. |
Volume: |
579 |
Issue: |
11 |
Pages: |
2339-47 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
FYN-binding protein 1 (FYB1), also known as ADAP or SLAP, is an adapter protein in beta 1 integrin signalling and T lymphocyte migration []. It has been found to co-localise with F-actin in membrane ruffles, adhesion plaques/podosomes and phagocytic cups [, ]. In activated T cells, Fyb/SLAP associates with Ena/VASP family proteins and may link T cell signalling to the actin cytoskeleton remodelling []. FYB1 also interacts with mammalian actin binding protein 1 (mAbp1) that affects F-actin dynamics [].The SH3 domain of FYB adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterised by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides; instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides [, , ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Veale M |
Year: |
1999 |
Journal: |
J Biol Chem |
Title: |
Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130) interacts with SLP-76 and up-regulates interleukin 2 production. |
Volume: |
274 |
Issue: |
40 |
Pages: |
28427-35 |
|
•
•
•
•
•
|
Publication |
First Author: |
Heuer K |
Year: |
2004 |
Journal: |
Structure |
Title: |
Structure of a helically extended SH3 domain of the T cell adapter protein ADAP. |
Volume: |
12 |
Issue: |
4 |
Pages: |
603-10 |
|
•
•
•
•
•
|
Publication |
First Author: |
Heuer K |
Year: |
2006 |
Journal: |
J Mol Biol |
Title: |
Lipid-binding hSH3 domains in immune cell adapter proteins. |
Volume: |
361 |
Issue: |
1 |
Pages: |
94-104 |
|
•
•
•
•
•
|
Publication |
First Author: |
Heuer K |
Year: |
2005 |
Journal: |
J Mol Biol |
Title: |
The helically extended SH3 domain of the T cell adaptor protein ADAP is a novel lipid interaction domain. |
Volume: |
348 |
Issue: |
4 |
Pages: |
1025-35 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hunter AJ |
Year: |
2000 |
Journal: |
J Immunol |
Title: |
Cutting edge: a novel function for the SLAP-130/FYB adapter protein in beta 1 integrin signaling and T lymphocyte migration. |
Volume: |
164 |
Issue: |
3 |
Pages: |
1143-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Krause M |
Year: |
2000 |
Journal: |
J Cell Biol |
Title: |
Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. |
Volume: |
149 |
Issue: |
1 |
Pages: |
181-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
Coppolino MG |
Year: |
2001 |
Journal: |
J Cell Sci |
Title: |
Evidence for a molecular complex consisting of Fyb/SLAP, SLP-76, Nck, VASP and WASP that links the actin cytoskeleton to Fcgamma receptor signalling during phagocytosis. |
Volume: |
114 |
Issue: |
Pt 23 |
Pages: |
4307-18 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
263
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
183
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
819
|
Fragment?: |
false |
|
•
•
•
•
•
|