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Search results 301 to 319 out of 319 for Frs2

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Type Details Score
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
Publication
First Author: Dhalluin C
Year: 2000
Journal: Mol Cell
Title: Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors.
Volume: 6
Issue: 4
Pages: 921-9
Publication
First Author: Koshiba S
Year: 2010
Journal: J Struct Funct Genomics
Title: Structural basis for the recognition of nucleophosmin-anaplastic lymphoma kinase oncoprotein by the phosphotyrosine binding domain of Suc1-associated neurotrophic factor-induced tyrosine-phosphorylated target-2.
Volume: 11
Issue: 2
Pages: 125-41
Publication  
First Author: Sain N
Year: 2016
Journal: Sci Rep
Title: Understanding the molecular basis of substrate binding specificity of PTB domains.
Volume: 6
Pages: 31418
Protein Domain
Type: Domain
Description: FRS2 (also called Suc1-associated neurotrophic factor (SNT)-induced tyrosine-phosphorylated target) proteins are membrane-anchored adaptor proteins. They are composed of an N-terminal myristoylation site followed by a phosphotyrosine binding (PTB) domain, which has a PH-like fold, and a C-terminal effector domain containing multiple tyrosine and serine/threonine phosphorylation site. The FRS2/SNT proteins show increased tyrosine phosphorylation by activated receptors, such as fibroblast growth factor receptor (FGFR) and TrkA, recruit SH2 domain containing proteins such as Grb2, and mediate signals from activated receptors to a variety of downstream pathways. The PTB domains of the SNT proteins directly interact with the canonical NPXpY motif of TrkA in a phosphorylation dependent manner, they directly bind to the juxtamembrane region of FGFR in a phosphorylation-independent manner [, ]. This domain can also be found in FRS3 []. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lacking tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This domain is part of the IRS-like subgroup [, ].
Publication
First Author: Brewer JR
Year: 2015
Journal: Genes Dev
Title: Fgfr1 regulates development through the combinatorial use of signaling proteins.
Volume: 29
Issue: 17
Pages: 1863-74
Publication
First Author: Manchado E
Year: 2016
Journal: Nature
Title: A combinatorial strategy for treating KRAS-mutant lung cancer.
Volume: 534
Issue: 7609
Pages: 647-51
Publication
First Author: Dabrowski A
Year: 2015
Journal: Development
Title: Distinct sets of FGF receptors sculpt excitatory and inhibitory synaptogenesis.
Volume: 142
Issue: 10
Pages: 1818-30
Publication
First Author: Hryciw T
Year: 2010
Journal: J Neurochem
Title: The fibroblast growth factor receptor substrate 3 adapter is a developmentally regulated microtubule-associated protein expressed in migrating and differentiated neurons.
Volume: 112
Issue: 4
Pages: 924-39
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 1319  
Fragment?: false
Protein  
Organism: Mus musculus/domesticus
Length:  
Protein
Organism: Mus musculus/domesticus
Length: 492  
Fragment?: false
Publication
First Author: Uhlik MT
Year: 2005
Journal: J Mol Biol
Title: Structural and evolutionary division of phosphotyrosine binding (PTB) domains.
Volume: 345
Issue: 1
Pages: 1-20