About SH2D1 / SH2 Domain Protein:
A protein usually found within the Src oncoprotein, Src Homology 2 is a conserved protein domain. While it’s primarily seen in the Src oncoprotein, it also turns up in some specific intracellular signal-transducing proteins. Finding it outside of these is rare, and they shouldn’t be found outside the adaptor proteins.
SH2 domains are only know to bind phosphorylated tyrosine residue, although this is typically if a target protein with a longer peptide motif. Out of the currently known pTyr-recognition domains, that makes SH2 the largest one to behave in such a way.
SH2 Domain Protein Diversity
The prominence of SH2 domains isn’t too diverse. While they don’t turn up in yeast and things of a similar makeup, they can be found in the boundary between animalia and protozoa. It can also be found in Dictyostelium discoideum.
Within the human body, studies have shown that there are 120 domains across 115 proteins in the human genome. That highlights a rapid rate of expansion across the domains.
SH2 domains focus on recognizing tyrosine residues’ phosphorylated state. In doing so, it allows for the localization of these sites. There are multiple reactions involved in this process, such as sending a signal through membranes, which are then “sensed” by receptors. These will then result in other actions that focus on activating and localizing the site.
Once the process is completed, gene expressions and other responses should have altered patterns. In essence, the SH2 domain can be seen as a regulatory module that focuses on intracellular signalling cascades.
It typically interacts well with target peptides that contain high volumes of phosphotyrosine.