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FLASH GENE
Symbol TFIP11 contributors: mct/npt - updated : 20-01-2021
HGNC name tuftelin interacting protein 11
HGNC id 17165
Location 22q12.1      Physical location : 26.887.893 - 26.908.437
Synonym name
  • septin and tuftelin-interacting protein 1
  • tuftelin-interacting protein, 39-KDa
  • Synonym symbol(s) TIP39, FLJ22086, DKFZP434B194, Spp382, NTR, bK445C9.6, STIP, STIP-1
    DNA
    TYPE functioning gene
    STRUCTURE 22.35 kb     16 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked N status provisional
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    16 - 2941 - 837 - 2005 15868102
    15 - 2864 - 837 - 2005 15868102
    15 - 3535 - 838 - 2005 15868102
    13 - 3235 - 806 - 2005 15868102
    15 - 3504 - 837 - 2005 15868102
    15 - 3788 - 837 - 2005 15868102
    15 - 3574 - 837 - 2005 15868102
    EXPRESSION
    Type ubiquitous
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestivemouth   highly
    Reproductivefemale systemovary  highly
     male systemtestis  highly
    Skin/Tegumentskin     Homo sapiens
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Blood / hematopoieticbone marrow  highly
    cell lineage
    cell lines
    fluid/secretion umbilical cord blood
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • N-terminal region with a G-patch, which is a highly conserved domain of many RNA-processing proteins (Wen 2008)
  • a poly-Asp domain
  • a protein domain believed to be involved in RNA binding
  • a signature motif of RNA-processing proteins that is responsible for TFIP11DHX15 interactions (Tannukit 2009)
  • a atypical nuclear localization signal domain (AAs 701706) (VKDKFN)
  • a domain contained within amino acids 711735 distinct speckled nuclear localization
  • a TFIP11 nuclear speckle-targeting sequence (TFIP11-STS)
  • HOMOLOGY
    interspecies homolog to murine Tfip11
    homolog to rattus LOC288718
    Homologene
    FAMILY
  • TFP11/STIP family
  • parathyroid hormone ligand family
  • CATEGORY unknown/unspecified
    SUBCELLULAR LOCALIZATION extracellular
        intracellular
    intracellular,cytoplasm
    intracellular,nucleus,nucleoplasm,nuclear bodies,nuclear speckles
    intracellular,nucleus,nucleolus
    text with CCNL1 and EWSR1 frequently co-localize to speckled nuclear domains (Tannukit 2008)
    basic FUNCTION
  • may have a role in the differenciation of ameloblasts and odontoblasts or in the forming enamel extracellular matrix
  • may be splicing factor
  • displaying a unique and characteristic subnuclear localization pattern, in close proximity to SC35 nuclear speckles (Wen 2008)
  • may play a role in spliceosome disassembly allowing for the release of the bound lariat-intron (Tannukit 2008)
  • with CCNL1 and EWSR1, participate in a common cellular activity related to RNA splicing events (Tannukit 2008)
  • in cooperation with DHX15 mediates the transition from the intron large complex to the intron small complex, leading to efficient debranching and turnover of excised introns (Yoshimoto 2009)
  • can induce decorin expression and enhance wound repair
  • TFIP11-PTH2R system appears to be a previously unrecognized mechanism for regulation of extracellular matrix formation and wound repair
  • TFIP11, AMBN, and AMELX play an important role in dental caries
  • CELLULAR PROCESS cell life, differentiation
    PHYSIOLOGICAL PROCESS ossification
    PATHWAY
    metabolism
    signaling
    a component
  • protein component of the spliceosome complex that promotes the release of the lariat-intron during late-stage splicing through a direct recruitment and interaction with DHX15 (Tannukit 2009)
  • INTERACTION
    DNA binding
    RNA
    small molecule
    protein
  • interacts with TUFT1
  • cyclin L1 (CCNL1) and Ewing sarcoma breakpoint region 1 protein (EWSR1) are interacting partners of tuftelin-interacting protein 11 (Tannukit 2008)
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility to dental erosion
    Variant & Polymorphism other
  • significant associations between enamel loss and AMELX, tuftelin 1 (TUFT1), and tuftelin-interacting protein 11 (TFIP11)
  • Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • mice lacking Tip39 signaling showed memory impairment selectively under conditions of novelty-induced arousa
  • Tip39-deficient mice had delayed repair that was associated with formation of abnormal collagen bundles