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  • PDPK1
  • PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. (uniprot.org)
  • Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal. (uniprot.org)
  • PMID
  • Phosphatidylinositol 4-kinase (PI4-kinase) ( EC:2.7.1.67 ) [ PMID: 8194527 ] is an enzyme that acts on phosphatidylinositol (PI) in the first committed step in the production of the secondary messenger inositol-1'4'5'-trisphosphate. (ebi.ac.uk)
  • this domain seems to be distantly related to the catalytic domain of protein kinases [ PMID: 8387896 , PMID: 12151228 ]. (ebi.ac.uk)
  • HIP1R is the only known mammalian relative of huntingtin-interacting protein 1 (HIP1) [ PMID: 14732715 ]. (ebi.ac.uk)
  • They also contain an I/LWEQ (talin-like) domain, which is an actin-binding domain found in proteins that serve as linkers between the actin cytoskeleton and cellular compartments [ PMID: 20074057 ]. (ebi.ac.uk)
  • The central domain of the Sla2p/HIP1/HIP1R proteins contains a coiled-coil domain and several consensus sequences enabling protein-protein interactions [ PMID: 20074057 ]. (ebi.ac.uk)
  • Yeast Sla2p has been extensively studied: Sla2p arrives at existing endocytic patches with a ~25 seconds delay relative to clathrin and dissociates simultaneously with clathrin upon recruitment of actin-related proteins [ PMID: 15059611 , PMID: 9362070 ]. (ebi.ac.uk)
  • endocytosis
  • May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis (PubMed:14732715). (genecards.org)
  • Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. (genecards.org)
  • They are adaptor proteins that link actin to clathrin and endocytosis in the clathrin-mediated endocytosis (CME) pathway. (ebi.ac.uk)
  • End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. (ebi.ac.uk)
  • adapter
  • Acts as an adapter to drive activation of PIK3CG by beta-gamma G protein dimers. (uniprot.org)
  • Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. (uniprot.org)
  • regulation
  • Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein CROCC/Rootletin (PubMed:27623382). (genecards.org)
  • This domain is also present in a wide range of protein kinases, involved in diverse cellular functions, such as control of cell growth, regulation of cell cycle progression, a DNA damage checkpoint, recombination, and maintenance of telomere length. (ebi.ac.uk)
  • bind
  • This protein has been shown to bind CRK-associated substrate, nephrocystin, GTPase regulator associated with FAK, and the SH2 domain of GRB2. (nih.gov)
  • Using a panel of glutathione S-transferase (GST) fusion proteins of the inter-SH2 region of p85, 104 amino acids were found to bind directly the p110 protein, while deletion mutants within this region further defined the binding site to a sequence of 35 amino acids. (embl.de)
  • Plays
  • The encoded protein is an actin-binding protein that is activated by the serine/threonine kinase Akt and plays a role in cytoskeleton remodeling and cell migration. (genecards.org)
  • Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. (genecards.org)
  • residues
  • This domain, which could be narrowed down to 100 amino acid residues, associated in vitro with human Ha-Ras in a GTP-dependent manner and competed with yeast adenylyl cyclase for binding Ha-Ras. (embl-heidelberg.de)
  • The site of interaction on the p110alpha and beta isoforms of PI 3-kinase lies between amino acid residues 133 and 314. (embl.de)
  • STK s catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. (cenicafe.org)