NucleaRDB: Extraction of mutation data from the literature

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This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes different point mutations at a given position and provides links to other documents. The sentence(s) where the point mutations in NR1I3_MOUSE at position 354 were found are listed after the table.

Point mutations at position G354 in NR1I3_MOUSE

ProteinNR1I3_MOUSE (O35627)    Gene: Nr1i3,Ca    (other point mutations)Swiss-Prot
Cross-reference table
Family page
Protein isoforms2
PositionG354
General numbering (NucleaRDB) 1249
DomainLBD HELIX 12
Family alignments 1I3 Constitutive Androstane alpha (CAR1)
1I Vitamin D3-like (VDR,PXR,CAR)
1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR
Other point mutations at the same position Position 354 in 1I3 Constitutive Androstane alpha (CAR1) family
Position 414 in 1I Vitamin D3-like (VDR,PXR,CAR) family
Position 402 in 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR family
Reference #1Ueda A, Kakizaki S, Negishi M, Sueyoshi T
Mol Pharmacol 2002 Jun;61(6):1284-8.		Medline
Text sourceHTML and PDF full texts
Point mutationG354Q (True positive)
Reference #2Andersin T, Vaisanen S, Carlberg C
Mol Endocrinol 2003 Feb;17(2):234-46.		Medline
Text sourceHTML full text
Point mutationG354A (True positive)

Relevant sentences

Reference #2 (Andersin T et al.): G354A
  • In the case of the mutants L353A , G354A , I356A , and C357A this combined ligand treatment resulted in additive agonistic effect

  • The point mutants L352A , L353A , E355A , I356A , and C357A and the AF-2 deletion reduced the basal activity by 90% or more , S358A by 75% , and G354A by only 10%

  • The ligand-dependent interaction profile of the mutant G354A with TIF2 was found to be very similar to that of wild-type CAR

Reference #1 (Ueda A et al.): G354Q
  • Accordingly , Thr350 and Gly354 were mutated to methionine (mCAR T350M) and glutamine (mCAR G354Q) , respectively

  • The mutant mCAR T350M lost its ability to show repressed activity by progesterone , whereas mCAR G354Q retained a degree of repression by progesterone (Fig. 2 A)

  • The double mutation (mCAR T350M / G354Q) showed activity similar to that of the Thr350 mutant (mCAR T350M)

  • These residues , Thr350 and Gly354 , in mCAR were singularly and doubly mutated to the corresponding residues in hCAR: T350M , G354Q , and dm , respectively

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F.Horn (nucleardbcmbi.kun.nl), 21-Apr-2005