The domain within your query sequence starts at position 5 and ends at position 98; the E-value for the PH domain shown below is 1.6e-10.
TILEEILIKRSQQKKKTSPLNYKERLFVLTKSVLSYYEGRAEKKYRKGVIDISKIKCVEI VKNDDGVIPCQNKFPFQSTKQGPMGEEVKRRNKE
PH |
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PFAM accession number: | PF00169 |
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Interpro abstract (IPR001849): | Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of proteins. The domains can bind phosphatidylinositol within biological membranes and proteins such as the beta/gamma subunits of heterotrimeric G proteins [ (PUBMED:8074669) ] and protein kinase C [ (PUBMED:7522330) ]. Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. The 3D structure of several PH domains has been determined [ (PUBMED:7634082) ]. All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets, followed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length, making the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain. Proteins reported to contain one more PH domains belong to the following families:
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This is a PFAM domain. For full annotation and more information, please see the PFAM entry PH