phosphatidylinositol-3,5-bisphosphate binding

phosphatidylinositol-3,5-bisphosphate binding

Item
http://www.wikidata.org/entity/Q21106094
WASH complex subunit 2CSorting nexin 3WD repeat domain, phosphoinositide interacting 2Pleckstrin homology domain containing A5Clavesin 2Clavesin 1Huntingtin interacting protein 1Sorting nexin 5Golgi brefeldin A resistant guanine nucleotide exchange factor 1Copper metabolism domain containing 1Huntingtin interacting protein 1 relatedJunctophilin 2ATPase cation transporting 13A2ArfGAP with coiled-coil, ankyrin repeat and PH domains 2WD repeat domain 45SEC14 and spectrin domain containing 1Kinesin family member 16BMAPK associated protein 1Pleckstrin homology like domain family A member 3Pleckstrin 2Sorting nexin 14Recombination activating 2SH3 and PX domains 2BWD repeat domain 45BWD repeat domain, phosphoinositide interacting 1WD repeat domain, phosphoinositide interacting 2, isoform CRA_cWASH complex subunit 2`Huntingtin interacting protein 1Huntingtin interacting protein 1 relatedCOMM domain containing 1Recombination activating gene 2ArfGAP with coiled-coil, ankyrin repeat and PH domains 2Clavesin 2Clavesin 1ATPase type 13A2Kinesin family member 16BJunctophilin 2Pleckstrin homology like domain, family A, member 3Sorting nexin 14Pleckstrin 2
P680
Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signallingPH domain-only protein PHLDA3 is a p53-regulated repressor of AktThe clavesin family, neuron-specific lipid- and clathrin-binding Sec14 proteins regulating lysosomal morphologyThe structural basis of novel endosome anchoring activity of KIF16B kinesinHuman junctophilin-2 undergoes a structural rearrangement upon binding PtdIns(3,4,5)P3 and the S101R mutation identified in hypertrophic cardiomyopathy obviates this responseCOMMD1 forms oligomeric complexes targeted to the endocytic membranes via specific interactions with phosphatidylinositol 4,5-bisphosphateWIPI3 and WIPI4 β-propellers are scaffolds for LKB1-AMPK-TSC signalling circuits in the control of autophagy.A hydrophilic cation-binding protein of Arabidopsis thaliana, AtPCaP1, is localized to plasma membrane via N-myristoylation and interacts with calmodulin and the phosphatidylinositol phosphates PtdIns(3,4,5)P(3) and PtdIns(3,5)P(2).
P921
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P680

phosphatidylinositol-3,5-bisphosphate binding

Item
http://www.wikidata.org/entity/Q21106094
description
Interacting selectively and no ...... ed at the 3' and 5' positions.
@en
moleculaire functie
@nl
name
phosphatidylinositol-3,5-bisphosphate binding
@en
type
label
phosphatidylinositol-3,5-bisphosphate binding
@en
altLabel
GO:0080025
@en
PtdIns(3,5)P2 binding
@en
prefLabel
phosphatidylinositol-3,5-bisphosphate binding
@en
P279
P2888
P31
P527
P686
P279
P2888
P31
P527
P686