Fyn
The Protein Kinase FactsBook, Page: 65-67
1995
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Book Chapter Description
The Src family PTK Fyn was originally identified in fibroblasts, in endothelial cells, and subsequently, in lymphocytes. Two isoforms of the protein have been defined, with the expression of one of these, FynT, confined to the lymphoid lineage. FynT associates with components of the T-cell antigen receptor complex and has been demonstrated to be implicitly involved in T-cell receptor signaling. The second isoform of the protein, FynB, is one of an emerging group of kinases implicated in the processes of long-term potentiation and spatial learning. Substrates for both isoforms of the protein remain to be elucidated. Both isoforms of Fyn contain four conventionally defined domains. Ten amino acids located at the N-terminus of the protein mediate a low stoichiometry association with the ζ chain of the T cell receptor and with other potential signaling molecules. The N-terminus may also be myristoylated and palmityoylated, potentiating an interaction with the cytoplasmic membrane and with glycosylphosphatidylinositol-linked membrane proteins. The SH2 and SH3 domains facilitate interactions with other proteins; however, the identity of these remains enigmatic. The kinase domain contains a tyrosine autophosphorylation site (Y417) and a negative regulatory tyrosine residue located at the C-terminus (Y528).
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/B9780123247193501412; http://dx.doi.org/10.1016/b978-012324719-3/50141-2; http://linkinghub.elsevier.com/retrieve/pii/B9780123247193501412; https://linkinghub.elsevier.com/retrieve/pii/B9780123247193501412; https://dx.doi.org/10.1016/b978-012324719-3/50141-2
Elsevier BV
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