Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutation-deletion analysis of a Ca(2+)-dependent phospholipid binding (CaLB) domain within p120 GAP, a GTPase-activating protein for p21 ras.

The Biochemical journal - 15 Apr 1995

Gawler D J, Zhang L J, Moran M F

Abstract excerpt

p120 GAP is a GTPase activating protein for p21 ras. It is a multidomain protein which exhibits sequence similarity with other GTPase-activating proteins, src, pleckstrin and a central portion of the protein kinase C conserved region 2 domain known as CaLB (Ca(2+)-dependent phospholipid-binding). The presence of this CaLB motif has led to the speculation that p120 GAP may be a member of a family of structurally...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Binding Sites
Share to DNA Mutational Analysis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Proteins

Share to Recombinant Fusion Proteins

Share to Sequence Deletion

Source

Open in PubMed Open full text

Identifiers

PMID: 7733887
DOI: 10.1042/bj3070487
PMCID: PMC1136674

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation-deletion analysis of a Ca(2+)-dependent phospholipid binding (CaLB) domain within p120 GAP, a GTPase-activating protein for p21 ras.PMID 7733887Read ↗

Mapping the phospholipid-binding surface and translocation determinants of the C2 domain from cytosolic phospholipase A2.Semantic proximity Read ↗

Identification of a novel phosphatidic acid binding domain in protein phosphatase-1.Semantic proximity Read ↗

A stretch of polybasic residues mediates Cdc42 GTPase-activating protein (CdGAP) binding to phosphatidylinositol 3,4,5-trisphosphate and regulates its GAP activity.Semantic proximity Read ↗

Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras.Semantic proximity Read ↗

The GTPase-activating protein Rap1GAP uses a catalytic asparagine.Semantic proximity Read ↗

Ras binding to a C-terminal region of GAP.Semantic proximity Read ↗

Molecular modelling and site-directed mutagenesis of the inositol 1,3,4,5-tetrakisphosphate-binding pleckstrin homology domain from the Ras GTPase-activating protein GAP1IP4BP.Semantic proximity Read ↗

Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity.Semantic proximity Read ↗

Biochemical characterization of the type I inositol polyphosphate 4-phosphatase C2 domain.Semantic proximity Read ↗

Interaction of p190RhoGAP with C-terminal domain of p120-catenin modulates endothelial cytoskeleton and permeability.Semantic proximity Read ↗

Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin.Semantic proximity Read ↗

Src homology region 2 domains direct protein-protein interactions in signal transduction.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.