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Search results 1 to 17 out of 17 for Fyb

0.009s

Type

Details

Score

Publication

9207119 | J:41750

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

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Publication

11553777 | -

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

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Protein

O35601

Organism:	Mus musculus/domesticus
Length:	819
Fragment?:	false

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Protein Coding Gene

MGI:1346327 | Fyb1

Type:	protein_coding_gene
Organism:	mouse, laboratory

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Protein

O35601-2

Organism:	Mus musculus/domesticus
Length:	773
Fragment?:	false

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Publication

15848169 | J:98236

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

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Protein Domain

IPR035540 | FYB_hSH3

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 [, , ].

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Publication

10497204 | J:57919

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

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Publication

15062083 | -

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

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Publication

16831444 | -

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

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Publication

15843031 | -

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

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Publication

10640723 | -

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

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Publication

10747096 | J:156075

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

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Publication

11739662 | -

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

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Protein

Q3TA12

Organism:	Mus musculus/domesticus
Length:	263
Fragment?:	true

•

Protein

F6V072

Organism:	Mus musculus/domesticus
Length:	183
Fragment?:	true

•

Protein

B2RUR0

Organism:	Mus musculus/domesticus
Length:	819
Fragment?:	false

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