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FLASH GENE
Symbol GBP5 contributors: mct - updated : 01-10-2014
HGNC name guanylate binding protein 5
HGNC id 19895
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
12 splicing 4065 - 586 - 2010 20180847
GBP5-a
11 splicing 3957 - 586 - 2010 20180847
  • GBP5-b
  • same protein compared to GBP5-a
  • - splicing - - - - 2010 20180847
    C-terminally truncated by 97aa and has therefore lost its isoprenylation site
    EXPRESSION
    Type restricted
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestiveliver    
    Reproductivefemale systembreast   
     male systemprostate   
    Respiratorylung    
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Connectivebone   
    Muscularstriatumskeletal  
    cells
    SystemCellPubmedSpeciesStageRna symbol
    Blood/Hematopoieticmonocyte
    Lymhoid/Immunelymphocyte
    Respiratoryalveolar macrophage
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • C-terminal part, that carries the geranylgeranylation motif , C-terminal CaaX-prenylation signal, which is typical for small GTPases of the Ras family, and increases the membrane affinity of proteins
  • HOMOLOGY
    Homologene
    FAMILY interferon-gamma-inducible large GTPases family
    CATEGORY immunity/defense
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm
    text
  • GBP1, GBP3, and GBP5 were exclusively detected in the cytoplasm, whereas GBP2 and GBP4 displayed a nucleocytoplasmic distribution
  • prenylated and prenylation is required for the membrane association
  • basic FUNCTION
  • may be involved in immune response and have cancer-related functions
  • GBP1, GBP2 and GBP5 were able to redirect non-prenylated GBPs to their compartment in a prenylation-dependent manner
  • promoted selective NLRP3 inflammasome responses to pathogenic bacteria and soluble but not crystalline inflammasome priming agents
  • serves as a unique rheostat for NLRP3 inflammasome activation and extends our understanding of the inflammasome complex beyond its core machinery
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS immunity/defense
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • GBP5 promotes CASP1–mediated protection against oral Listeria infection and NLRP3-dependent inflammatory responses
  • cell & other
    REGULATION
    induced by robustly induced only by IFN-gamma and not by TNF-alpha and IL-1beta
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS