SMART: Pfam domain INPP5B

The domain within your query sequence starts at position 1 and ends at position 150; the E-value for the INPP5B_PH domain shown below is 4.3e-61.

MDQSVAIQETLVEGEYCVIAVQGVLCKGDSRQSRLLGLVRYRLENDAQEHALFLYTHRRM
AITGDDVSLDQIVPLSKDFMLEEVSPDGELYILGSDVTVQLNTAELKLVFQLPFGSHTRT
FLQEVARACPGFDPETRDPEFEWLSRHTCA

INPP5B_PH

PFAM accession number:	PF16776
Interpro abstract (IPR031896):	This entry represents the PH domain found in the N terminus of type II inositol 1,4,5-trisphosphate 5-phosphatase (INPP5B). The structure of this domain has been revealed [ (PUBMED:19536138) ]. INPP5B hydrolyses phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signalling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signalling events [ (PUBMED:7721860) ]. INPP5B contains a PH domain, a 5-phosphatase domain, an ASH domain and a Rho-GAP domain. It shares ~45% sequence identity with OCRL1 (not included in this entry) and has the same domain organization. However, a loop in the Rho GAP domain contains a second clathrin box which is absent in INPP5B. INPP5B shares most interacting partners with OCRL, except for clathrin and the endocytic clathrin adaptor AP-2 [ (PUBMED:22381590) ].

PFAM accession number:

PF16776

Interpro abstract (IPR031896):

This entry represents the PH domain found in the N terminus of type II inositol 1,4,5-trisphosphate 5-phosphatase (INPP5B). The structure of this domain has been revealed [ (PUBMED:19536138) ]. INPP5B hydrolyses phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signalling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signalling events [ (PUBMED:7721860) ].

INPP5B contains a PH domain, a 5-phosphatase domain, an ASH domain and a Rho-GAP domain. It shares ~45% sequence identity with OCRL1 (not included in this entry) and has the same domain organization. However, a loop in the Rho GAP domain contains a second clathrin box which is absent in INPP5B. INPP5B shares most interacting partners with OCRL, except for clathrin and the endocytic clathrin adaptor AP-2 [ (PUBMED:22381590) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry INPP5B_PH