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UnknownDLC1 activation requires lipid interaction through a polybasic region preceding the RhoGAP domain.
Not available
S-EPMC2762136 | biostudies-literature
UnknownA Non-Canonical Calmodulin Target Motif Comprising a Polybasic Region and Lipidated Terminal Residue Regulates Localization.
Not available
S-EPMC7216078 | biostudies-literature
UnknownPhosphatidylinositol (4,5)-bisphosphate modulates Nox5 localization via an N-terminal polybasic region.
Not available
S-EPMC2555958 | biostudies-literature
UnknownElucidating the Membrane Binding Process of a Disordered Protein: Dynamic Interplay of Anionic Lipids and the Polybasic Region.
Not available
S-EPMC10979486 | biostudies-literature
UnknownTargeting of murine leukemia virus gag to the plasma membrane is mediated by PI(4,5)P2/PS and a polybasic region in the matrix.
Not available
S-EPMC2798412 | biostudies-literature
UnknownThe subcellular localization of type I p21-activated kinases is controlled by the disordered variable region and polybasic sequences.
Not available
S-EPMC6768646 | biostudies-literature
UnknownThe Polybasic Region of the Polysialyltransferase ST8Sia-IV Binds Directly to the Neural Cell Adhesion Molecule, NCAM.
Not available
S-EPMC5577389 | biostudies-literature
UnknownSAF-A/hnRNP U binds polyphosphoinositides via a lysine rich polybasic motif located in the SAP domain.
Not available
S-EPMC10082394 | biostudies-literature
ProteomicsRegulation of the DLC3 tumor suppressor by a novel phosphoswitch
Deleted in Liver Cancer 3 (DLC3) is a Rho GTPase-activating protein (RhoGAP) that plays a crucial role in maintaining adherens junction integrity and coordinating polarized vesicle transport by modulating Rho activity at the plasma membrane and endomembranes. By employing bioinformatical sequence an...
ORGANISM(S): Homo sapiens (Human) 
2024-06-04 | PXD045808 | Pride
Cytokinesis Gtpase activating protein Rho signaling Polybasic region Membrane binding 
UnknownPolybasic RKKR motif in the linker region of lipid droplet (LD)-associated protein CIDEC inhibits LD fusion activity by interacting with acidic phospholipids.
Not available
S-EPMC6302180 | biostudies-literature
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