Tensin/EPS8 phosphotyrosine-binding domain
IPR013625
Definition
The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) of tensin tends to be found at the C terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 ([interpro:IPR000980]) domain and a region similar to the tumour suppressor PTEN PMID:11023826. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif PMID:14592531. The PTB domain is also found in the epidermal growth factor receptor kinase substrate 8 (EPS8). PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules PMID:10610414. 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 lack tyrosine residues altogether PMID:11911882. 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 PMID:11994738. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains PMID:15567406.
8 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...