Anolis carolinensis pY/C2
※ C2 family introduction A C2 domain is a protein structural domain involved in targeting proteins to cell membranes. The typical version (PKC-C2) has a beta-sandwich composed of 8 beta-strands that co-ordinates two or three calcium ions, which bind in a cavity formed by the first and final loops of the domain, on the membrane binding face. The C2 domain of PRKCQ, the closest relative of PRKCQ in the PKC family, was found to be a novel Tyr(P)-binding domain, which could specifically bind a Tyr(P)-containing peptide derived from CDCP1, a protein known to be phosphorylated on tyrosine by activated Src kinase (1). Reference
1. Stahelin, R.V. (2012) PRKCQ C2 domain is a phosphotyrosine binding module that plays a key role in its activation . J Biol Chem, 287, 30518-28. PMID: 22787157
There are 27 genes. Reviewed (0)
or Unreviewed (27) 
※ C2 family introduction A C2 domain is a protein structural domain involved in targeting proteins to cell membranes. The typical version (PKC-C2) has a beta-sandwich composed of 8 beta-strands that co-ordinates two or three calcium ions, which bind in a cavity formed by the first and final loops of the domain, on the membrane binding face. The C2 domain of PRKCQ, the closest relative of PRKCQ in the PKC family, was found to be a novel Tyr(P)-binding domain, which could specifically bind a Tyr(P)-containing peptide derived from CDCP1, a protein known to be phosphorylated on tyrosine by activated Src kinase (1). Reference
1. Stahelin, R.V. (2012) PRKCQ C2 domain is a phosphotyrosine binding module that plays a key role in its activation . J Biol Chem, 287, 30518-28. PMID: 22787157
There are 27 genes. Reviewed (0)
or Unreviewed (27)