SMART: Pfam domain hSH3

The domain within your query sequence starts at position 731 and ends at position 819; the E-value for the hSH3 domain shown below is 2.9e-46.

LRKKFKYDGEIRVLYSTKVASSLTSKKWGARDLQIKPGESLEVIQSTDDTKVLCRNEEGK
YGYVLRSYLVDNDGEIYDDIADGCIYDND

hSH3

PFAM accession number:	PF14603
Interpro abstract (IPR029294):	This domain corresponds to the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein, also known as FYN-binding protein. This domain shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides [ (PUBMED:15062083) ]. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered [ (PUBMED:20661443) ]. Instead, the hSH3 domain functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides [ (PUBMED:15062083) (PUBMED:16831444) (PUBMED:15843031) ].

PFAM accession number:

PF14603

Interpro abstract (IPR029294):

This domain corresponds to the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein, also known as FYN-binding protein. This domain shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides [ (PUBMED:15062083) ]. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered [ (PUBMED:20661443) ]. Instead, the hSH3 domain functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides [ (PUBMED:15062083) (PUBMED:16831444) (PUBMED:15843031) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry hSH3