NucleaRDB: Extraction of mutation data from the literature

2005, NucleaRDB.

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 187 were found are listed after the table.

Point mutations at position K187 in NR1I3_MOUSE

Protein	NR1I3_MOUSE (O35627) Gene: Nr1i3,Ca (other point mutations)	Swiss-Prot Cross-reference table Family page
Protein isoforms	2
Position	K187
General numbering (NucleaRDB)	351
Domain	LBD HELIX 3
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 187 in 1I3 Constitutive Androstane alpha (CAR1) family Position 241 in 1I Vitamin D3-like (VDR,PXR,CAR) family Position 234 in 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR family
Reference #1	Dussault I, Lin M, Hollister K, Fan M, Termini J, Sherman MA, Forman BM Mol Cell Biol 2002 Aug;22(15):5270-80.	Medline
Text source	HTML and PDF full texts
Point mutation	K187A (True positive)
Reference #2	Andersin T, Vaisanen S, Carlberg C Mol Endocrinol 2003 Feb;17(2):234-46.	Medline
Text source	HTML full text
Point mutation	K187A (True positive)

Relevant sentences

Reference #1 (Dussault I et al.): K187A

The primers used were as follows (only the oligonucleotides representing the upper DNA strand are shown): mouse CAR K187A , 5'-ATCATCAAGTTCACCGCGGATCTGCCGCTCTTC-3' ; CAR K205E , 5'-ACCAGATCTCCCTTCTCGAGGGAGCGGCTGTGGAA-3' ; CAR loop , an insertion of three alanine residues between E345 and L346 , 5'-CTTCAGCGCTTGGAGGAAGCGGCCGCACTGTCTGCTATGACGCCG-3' ; CAR C-terminal extension , an insertion of four alanines at the end of CAR , 5'-CTCGGGGAGATTTTGCAGTGCGGCCGCGGCATGAGGCCCAGGCTTGCAT-3' ; RXR K285A , 5'-CTGGTGGAGTGGGCCGCGCGAATCCCACACTTCTCA-3' ; SRC-1 RID1m (amino acids 633 to 637 [LVQLL] , GenBank accession no
To address this question , we mutated conserved amino acid residues in H12 / AF2 (L352A and E355A) and H3 (K187A) that contribute to the hydrophobic coregulator cleft on the surface of ligand-bound nuclear receptors (8 , 11 , 37 , 43 )
In contrast , mutations in either the H12 / AF2 domain (L352A and E355A) or H3 (K187A) completely inhibited constitutive activity , and TCPOBOP failed to restore activity to wild-type levels (Fig. 1A )
Single point mutations in H12 / AF2 (L352A or E355A) or H3 (K187A) specifically resulted in the complete loss of both constitutive and ligand-induced SRC-1 recruitment (Fig. 1B , lanes 4 to 9)
Mutation of either K187A in CAR or K285A in RXR strongly reduced the association with SMRT (Fig. 3D , lanes 3 and 4) , and the combination of both mutations completely abolished the interaction (Fig. 3D , lane 5)
The primers used were as follows (only the oligonucleotides representing the upper DNA strand are shown): mouse CAR K187A , 5 -ATCATCAAGTT CACCGCGGATCTGCCGCTCTTC-3 ; CAR K205E , 5 -ACCAGATCTCCCT TCTCGAGGGAGCGGCTGTGGAA-3 ; CAR loop , an insertion of three alanine residues between E345 and L346 , 5 -CTTCAGCGCTTGGAGGAAGCG GCCGCACTGTCTGCTATGACGCCG-3 ; CAR C-terminal extension , an insertion of four alanines at the end of CAR , 5 -CTCGGGGAGATTTTGCAG TGCGGCCGCGGCATGAGGCCCAGGCTTGCAT-3 ; RXR K285A , 5 -CTG GTGGAGTGGGCCGCGCGAATCCCACACTTCTCA-3 ; SRC-1 RID1m (amino acids 633 to 637 [LVQLL] , GenBank accession no
In contrast , mutations in either the H12 / AF2 domain (L352A and E355A) or H3 (K187A) completely inhibited constitutive ac
FIG

Reference #2 (Andersin T et al.): K187A

Using standard nonsaturating TIF2 amounts (0.1 痢) , both K187A and E355A displayed a clear interaction with TIF2 in the absence of ligand
B , Heterodimers of in vitro translated CARK187A and CARE355A protein with RXR protein were formed in the presence of solvent , TCPOBOP , androstanol , or a combination of both

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