http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID198191

Outgoing Links

Predicate Object
abstract N-terminal Src homology 2 (SH2) domain found in Zeta-chain-associated protein kinase 70 (ZAP-70) and Spleen tyrosine kinase (Syk) proteins. ZAP-70 and Syk comprise a family of hematopoietic cell specific protein tyrosine kinases (PTKs) that are required for antigen and antibody receptor function. ZAP-70 is expressed in T and natural killer (NK) cells and Syk is expressed in B cells, mast cells, polymorphonuclear leukocytes, platelets, macrophages, and immature T cells. They are required for the proper development of T and B cells, immune receptors, and activating NK cells. They consist of two N-terminal Src homology 2 (SH2) domains and a C-terminal kinase domain separated from the SH2 domains by a linker or hinge region. Phosphorylation of both tyrosine residues within the Immunoreceptor Tyrosine-based Activation Motifs (ITAM; consensus sequence Yxx[LI]x(7,8)Yxx[LI]) by the Src-family PTKs is required for efficient interaction of ZAP-70 and Syk with the receptor subunits and for receptor function. ZAP-70 forms two phosphotyrosine binding pockets, one of which is shared by both SH2 domains. In Syk the two SH2 domains do not form such a phosphotyrosine-binding site. The SH2 domains here are believed to function independently. In addition, the two SH2 domains of Syk display flexibility in their relative orientation, allowing Syk to accommodate a greater variety of spacing sequences between the ITAM phosphotyrosines and singly phosphorylated non-classical ITAM ligands. This model contains the N-terminus SH2 domains of both Syk and Zap70. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.
title SH2_N-SH2_Zap70_Syk_like
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25340860
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9111237
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25986119
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19225940
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14024896
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3115251
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4057825
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24033208
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACC4FL3_A
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACC4FL2_A
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCNP_001167638
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCF1N9Y5
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCNP_001070
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP48025
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ64725
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCNP_003168
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP43403
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP43405
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCP43404

Total number of triples: 22.