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FLASH GENE
Symbol CCDC88A contributors: mct/npt/pgu - updated : 03-03-2012
HGNC name coiled-coil domain containing 88A
HGNC id 25523
Location 2p16.1      Physical location : 55.514.977 - 55.647.057
Synonym name
  • hook-related protein 1
  • girders of actin filament
  • girdin
  • Akt phosphorylation enhancer
  • G alpha-interacting vesicle-associated protein
  • Synonym symbol(s) APE, GIV, GRDN, HkRP1, GIRDIN, KIAA1212, FLJ10392, DKFZp686D0630
    DNA
    TYPE functioning gene
    STRUCTURE 132.08 kb     32 Exon(s)
    MAPPING cloned Y linked N status confirmed
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    32 splicing 9746 212.5 1843 - 2005 15749703
  • lacking an alternate segment in the 3' coding region compared to variant 1
  • 33 splicing 9827 215.8 1870 - 2005 15749703
    - - 9605 - 1796 - 2005 15749703
    EXPRESSION
    Type
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestivemouth   moderately
     pancreas exocrine   lowly
     pharynx   moderately
     salivary gland   moderately
    Lymphoid/Immunelymph node   predominantly
    Nervousbrain   highly
     nerve   highly
    Reproductivemale systemtestis  highly
    Urinarykidney   lowly
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Blood / hematopoieticbone marrow  highly
    Muscular   moderately
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • N-terminus containing a putative microtubule-binding domain that can bind microtubules in the Hook protein
  • the central region of each protein is comprised of an extensive coiled-coil domain
  • several conserved domains, including a unique C-terminal HkRP domain, that causes an accumulation of internal membranes with an electron-dense coat
  • NUCB1 and NUCB2, two highly homologous calcium-binding proteins, share a common motif with CCDC88A for Galpha(i) binding and activation
  • conjugated PhosphoP
    mono polymer homomer , dimer
    HOMOLOGY
    interspecies homolog to rattus Ccdc88a (93.2 pc)
    homolog to murine Ccdc88a (94.9 pc)
    Homologene
    FAMILY
  • Hook-related protein (HkRP) family
  • CCDC88 family
  • CATEGORY regulatory
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    intracellular,cytoplasm,organelle,endosome
    intracellular,cytoplasm,cytosolic,vesicle
    text
  • lamellipodium
  • localized to the cell membrane through interaction with phosphoinositides
  • basic FUNCTION
  • enhancing phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB
  • being essential for the integrity of the actin cytoskeleton and for cell migration
  • required for formation of actin stress fibers and lamellipodia
  • may be involved in membrane sorting in the early endosome
  • involved in the process of tubulation of sorting nexin-1 positive membranes from early endosome subdomains
  • important role in tumor progression in which the Akt signaling pathway is aberrantly activated
  • may play a role in Galpha-mediated effects on vesicle trafficking within the Golgi and/or between the ER and the Golgi
  • CCDC88A/GNAI3 coupling is essential for cell migration during wound healing, macrophage chemotaxis, and tumor cell migration
  • serves as a nonreceptor guanine nucleotide exchange factors for G alpha i through an evolutionarily conserved motif
  • metastasis-related protein and an independent adverse prognosticator that may serve as a useful adjunct to traditional staging strategies in colorectal carcinoma
  • CCDC88A and its AKT-mediated phosphorylation have major roles in the migration and proliferation of vascular smooth muscle cells (VSMCs) and vascular remodeling
  • important intrinsic factor that specifically governs neuroblast chain migration along the rostral migratory stream
  • enhances AKT activation downstream of multiple growth factor- and G protein (heterotrimeric guanosine 5prime -triphosphate-binding protein)-coupled receptors to trigger cell migration and cancer invasion
  • CELLULAR PROCESS cell life, proliferation/growth
    nucleotide, replication
    cell organization/biogenesis
    cell migration & motility
    PHYSIOLOGICAL PROCESS
    text
  • lamellipodium biogenesis
  • regulation of actin cytoskeleton organization and biogenesis
  • regulation of cell proliferation
  • PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • non-phosphorylated form interacting with phosphatidylinositol 4-phosphate and weakly with phosphatidylinositol 3-phosphate
  • interacting with microtubules
  • interacting with actin through its C-terminal domain
  • interacting with the C-terminus of AKT1/PKB
  • binds members of the Galpha(i) and Galpha subfamilies of heterotrimeric G proteins
  • is a GNAI3 binding partner
  • interacting with G alpha(i3) (activation of G alpha(i3) by CCDC88A is essential for biological functions associated with G alpha(i3) activation)
  • tyrosine phosphoprotein that directly binds to and activates phosphoinositide 3-kinase (PI3K)
  • cell & other
    REGULATION
    Other phosphorylation induced by epidermal growth factor (EGF) in a phosphoinositide 3-kinase (PI3K)-dependent manner
    phosphorylation by AKT1/PKB is necessary for the delocalization from the cell membrane and for cell migration
    phosphorylated by the stimulation of insulin-like growth factor (IGF-I)
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    miscelleaneousvascular 
    AKT/CCDC88A signaling pathway is a potential target for the development of new therapeutics for vascular diseases
    ANIMAL & CELL MODELS