http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID271105

Outgoing Links

Predicate Object
abstract Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases. PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They 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). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
title PTKc_Src_Fyn_like
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20731320
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30843268
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30173186
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/15293076
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9745660
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24646317
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1665299
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28818232
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/29490705
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25398221
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23409690
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17991259
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23310880
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24038836
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20618191
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5811997
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24111452
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8437194
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19373338
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/32152494
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23954667
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ02977

Total number of triples: 25.