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WormBase Tree Display for Variation: WBVar00090377

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Name Class

WBVar00090377EvidencePaper_evidenceWBPaper00001519
NamePublic_namen2195
Other_nameCE01784:p.Gly201Arg
C14F5.5.1:c.601G>A
HGVSgCHROMOSOME_X:g.7960297C>T
Sequence_detailsSMapS_parentSequenceC14F5
Flanking_sequencestggtgggaaggacagctgaacaacaggcgtgaattttcccatccaactacgtatgccctt
Mapping_targetC14F5
Type_of_mutationSubstitutiongaPaper_evidenceWBPaper00001519
SeqStatusSequenced
Variation_typeAllele
OriginSpeciesCaenorhabditis elegans
StrainWBStrain00027242
LaboratoryMT
StatusLive
AffectsGeneWBGene00004774
TranscriptC14F5.5.1 (12)
InteractorWBInteraction000519177
IsolationMutagenEMSPaper_evidenceWBPaper00001519
GeneticsInterpolated_map_positionX-0.823185
DescriptionPhenotypeWBPhenotype:0000640Person_evidenceWBPerson261
Curator_confirmedWBPerson712
Remarkweak EglPerson_evidenceWBPerson261
Curator_confirmedWBPerson712
Phenotype_not_observedWBPhenotype:0001272Paper_evidenceWBPaper00044058
Curator_confirmedWBPerson2987
Remark"We scored the vulval lineage of P7.p in four different alleles of sem-5. Two alleles, n2019 and cs15, which cause a glycine to alanine substitution in the first SH3 domain and an opal stop in the second SH3 domain, respectively, cause polarity and induction defects, whereas n2195, which causes a glycine to arginine substitution in the second SH3 domain, yields neither polarity nor induction defects. The fourth allele, n1779, which causes a glutamate to lysine substitution in the SH2 domain, results in a 13% P-Rvl phenotype, affecting polarity, but not induction (Table 1). We thus used sem-5(n1779) as the canonical allele."Paper_evidenceWBPaper00044058
Curator_confirmedWBPerson2987
EQ_annotationsAnatomy_termWBbt:0006895PATO:0000460Paper_evidenceWBPaper00044058
Curator_confirmedWBPerson2987
WBPhenotype:0002193Paper_evidenceWBPaper00044058
Curator_confirmedWBPerson2987
Remark"We scored the vulval lineage of P7.p in four different alleles of sem-5. Two alleles, n2019 and cs15, which cause a glycine to alanine substitution in the first SH3 domain and an opal stop in the second SH3 domain, respectively, cause polarity and induction defects, whereas n2195, which causes a glycine to arginine substitution in the second SH3 domain, yields neither polarity nor induction defects. The fourth allele, n1779, which causes a glutamate to lysine substitution in the SH2 domain, results in a 13% P-Rvl phenotype, affecting polarity, but not induction (Table 1). We thus used sem-5(n1779) as the canonical allele."Paper_evidenceWBPaper00044058
Curator_confirmedWBPerson2987
EQ_annotationsAnatomy_termWBbt:0006895PATO:0000460Paper_evidenceWBPaper00044058
Curator_confirmedWBPerson2987
ReferenceWBPaper00001519
WBPaper00044058
MethodSubstitution_allele