To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS. To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017. From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate
4,5-bisphonate (PI(4,5) P2 or PIP2) at the 3-position of the inositol ring,
and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3), which, in
turns, initiates a vast array of signaling events. PI3Ks can be grouped into
three classes based on their domain organization. Class I PI3Ks are
heterodimers consisting of a p110 catalytic subunit and a regulatory subunit
of either the p85 type (associated with the class IA p110 isoforms p110α,
p110β or p110delta) or the p101 type (associated with the class IB p110
isoform p110γ). Common to all catalytic subunits are the N-terminal
adaptor-binding domain (ABD) (see <PDOC51544>) that binds to p85, the Ras-binding domain (RBD), the putative membrane-binding domain (C2), the helical
domain of unknown function, and the kinase catalytic domain (see <PDOC00710>).
Class II PI3Ks lack the ABD domain and are distinguished by a carboxy terminal
C2 domain (see <PDOC00380>). Class III enzymes lack the ABD and RBD domains
The PI3K C2 domain is an eight-stranded antiparallel β-sandwich consisting
of two four-stranded β-sheets (see <PDB:1E8X>) [1,2,3,4].
The profile we developed covers the entire PI3K C2 domain.
August 2011 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Miled N., Yan Y., Hon W.-C., Perisic O., Zvelebil M., Inbar Y., Schneidman-Duhovny D., Wolfson H.J., Backer J.M., Williams R.L.
Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit.
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.