http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID212937
Outgoing Links
Predicate | Object |
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abstract | Src homology 3 domain of Lyn Protein Tyrosine Kinase. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. |
title | SH3_Lyn |
isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7870172 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8437194 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30161326 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9911965 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5811997 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28818232 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28202433 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23409691 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32196844 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20078414 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14626783 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3705388 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22116658 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24119054 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/260048 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24043821 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30843268 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13881394 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5807742 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12647906 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1665299 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4749202 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4323303 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19373338 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20618191 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/27488499 |
type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 34.