Poecilia formosa pY/Other
※ Other family introduction RKIP contains a novel phospho-amino acid binding domain. Substitutions in the ligand binding site of RKIP compromise the stability of the phosphorylated Raf-RKIP complex. Notably, PKM2 binds directly and selectively to tyrosine (Tyr, Y)-phosphorylated peptides, and expression of the phosphotyrosine-binding form of PKM2 is required for the rapid growth of cancer cells (1).
1. Kaneko T, Joshi R, Li SS. (2012) Phosphotyrosine recognition domains: the typical, the atypical and the versatile. Cell Commun Signal, 10(1), 32. PMID: 23134684
There are 8 genes. Reviewed (0)
or Unreviewed (8) 
※ Other family introduction RKIP contains a novel phospho-amino acid binding domain. Substitutions in the ligand binding site of RKIP compromise the stability of the phosphorylated Raf-RKIP complex. Notably, PKM2 binds directly and selectively to tyrosine (Tyr, Y)-phosphorylated peptides, and expression of the phosphotyrosine-binding form of PKM2 is required for the rapid growth of cancer cells (1).
1. Kaneko T, Joshi R, Li SS. (2012) Phosphotyrosine recognition domains: the typical, the atypical and the versatile. Cell Commun Signal, 10(1), 32. PMID: 23134684
There are 8 genes. Reviewed (0)
or Unreviewed (8)