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FLASH GENE
Symbol IGFBP5 contributors: mct - updated : 08-07-2011
HGNC name insulin-like growth factor binding protein 5
HGNC id 5474
Location 2q35      Physical location : 217.536.828 - 217.560.272
Synonym symbol(s) IGBP5, IBP5
DNA
TYPE functioning gene
STRUCTURE 23.44 kb     4 Exon(s)
10 Kb 5' upstream gene genomic sequence study
regulatory sequence Promoter (TATA box)
Binding site
text structure E-box, CACC-box and binding site for SIX5
MAPPING cloned Y linked   status provisional
Map 5'- IGFBP5 -3' - IGFBP2 - 5'
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
4 - 6333 43 272 - 1998 9883900
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Digestiveliver   lowly
 mouthtongue  highly
Endocrinethyroid   highly
Hearing/Equilibriumear   highly
Nervousbrain   lowly
 nerve   highly
Urinarykidney   predominantly
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Connective    
Muscularstriatumskeletal  
cells
SystemCellPubmedSpeciesStageRna symbol
not specificchondrocyte
cell lineage
cell lines osteosarcoma cell lines
fluid/secretion CSF (cerebro spinal fluid), present in the serum but decreasing with age after puberty
at STAGE
physiological period fetal, pregnancy
Text fetal tissues
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • invariant cysteine residues, 12 N terminal, 6 C terminal, a N terminal IGFBP motif (containing only one high-affinity binding site for IGF)
  • divided in 3 parts which are N-, L- and C- region (L-region is composed of a flexible linker structure and N- and C-regions closely contact for stabilizing their charge)
  • a central domain lacking cysteine residue, with a RGD motif
  • a 13kDa C terminal fragment (with intrinsic biological functions)
  • also a nuclear localization signal (NLS)
  • one thyroglobulin type-I domain
  • a mini-IGFBP5 (AAs 4092 of the N domain) containing a hydrophobic IGF-binding site within a novel protein fold, and mutations of key hydrophobic AAs within this region of IGFBP5 and the equivalent region of IGFBP3 dramatically reduces the affinity for IGF binding
  • secondary structure
  • 3D structure of the N domain of IGFBP-5 (aa 25101) consists of 2 alpha-helices and 5 beta-sheets; the C domain of IGFBP-5 (aa 185265) consists of an alpha-helix and 4 beta-sheets
  • HOMOLOGY
    Homologene
    FAMILY
    CATEGORY signaling cytokine growth factor
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm
    intracellular,nucleus
    text
  • in the articular cartilage extracellular matrix
  • resides mainly in the cytoplasm in cancer tissues, and subcellular localization of IGFBP5 affects its functions in host cells (
  • basic FUNCTION
  • insulin-like growth factor binding protein 5, high affinity, involved in regulation of cell growth
  • having an important role in controlling cell survival, differentiation and apoptosis
  • having IGF-independent actions during development
  • activates GNAI3 and regulates smooth muscle growth, IGF1 production, and collagen production via the alpha-subunit of GNAI3, independently of IGF1, in normal human intestinal muscle cells)
  • role in the control of growth and metabolism
  • induces formation of a FLNA-based nuclear shuttle that recruits transcription factors and regulates transcription of IGFBP5 target genes
  • has an effect on human hair shape
  • play an important role in breast cancer biology, especially in breast cancer metastasis
  • SRC and IL6 inhibit osteoblast differentiation and integrate IGFBP5 signalling
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • complexing with IGF1 and IGF2 and acid labile subunit
  • components of the IGF (insulin-like growth factor) axis
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacting with FLNA (IGFBP5 leads to dephosphorylation of FLNA with subsequent FLNA cleavage)
  • TNFRSF1A-interacting protein (interacts with TNFRSF1A through its N- and L-domains, and L-domain of IGFBP5 is a novel TNFRSF1A ligand that functions as a competitive TNF inhibitor)
  • PAPPA cleaves IGF binding protein IGFBP4 and IGFBP5
  • cell & other binding to bone cells
    REGULATION
    activated by SIX5 (contributing to specific aspects of dystrophy myotonica phenotype)
    induced by by AKT1 activation in the beta-cell
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral   LOH    
    in premalignant extravillous trophoblast
    Susceptibility to breast cancer
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS