WormBase Tree Display for Variation: WBVar00090389

WBVar00090389 Evidence: Paper_evidence: WBPaper00028753
  Name: Public_name: n2231
    Other_name: JC8.6d.1:c.1255G>A
      JC8.6c.1:c.1255G>A
      CE17990:p.Ala416Thr
      CE53077:p.Ala419Thr
      CE53011:p.Ala419Thr
      JC8.6a.1:c.1264G>A
      CE17989:p.Ala422Thr
      JC8.6b.1:c.1246G>A
    HGVSg: CHROMOSOME_IV:g.13243115G>A
  Sequence_details: SMap: S_parent: Sequence: JC8
    Flanking_sequences: acaactgagctcacacaagatcttgatgcc ctccaacggatgacatcccaggaccatcta
    Mapping_target: JC8
    Type_of_mutation: Substitution: g a Paper_evidence: WBPaper00028753
    SeqStatus: Sequenced
  Variation_type: Allele
  Origin: Species: Caenorhabditis elegans
    Strain: WBStrain00027346
    Laboratory: MT
    Status: Live
  Affects: Gene: WBGene00003037
    Transcript: JC8.6d.1 (12)
      JC8.6b.1 (12)
      JC8.6c.1 (12)
      JC8.6a.1 (12)
    Interactor: WBInteraction000500868
      WBInteraction000504626
      WBInteraction000504631
  Genetics: Interpolated_map_position: IV 8.48466
  Description: Phenotype: WBPhenotype:0000059 Paper_evidence: WBPaper00038168
        Curator_confirmed: WBPerson712
        Remark: Animals show larval arrest at 26 deg C. Paper_evidence: WBPaper00038168
            Curator_confirmed: WBPerson712
        Temperature_sensitive: Heat_sensitive: 26 Paper_evidence: WBPaper00038168
              Curator_confirmed: WBPerson712
    Phenotype_not_observed: WBPhenotype:0001370 Paper_evidence: WBPaper00038427
        Curator_confirmed: WBPerson2987
        Remark: "We next tested whether LIN-54 tesmin mutations affect DRM complex formation in addition to compromising DNA binding. Using yeast two-hybrid assays, we found that both wild-type and mutant LIN-54 proteins can interact with the DRM subunit LIN-9 (Figure 2C). In addition, other DRM complex members coprecipitated in lin-54(n2231) mutant animals (Figure 2D). These observations demonstrate that the tesmin mutation does not result in an unstable protein and does not compromise the integrity of the DRM complex. We conclude that the lin-54 tesmin mutant phenotypes are most likely caused by a defect in DNA binding." Paper_evidence: WBPaper00038427
            Curator_confirmed: WBPerson2987
  Reference: WBPaper00038168
    WBPaper00038427
    WBPaper00028753
  Method: Substitution_allele