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 205 were found are listed after the table.

Point mutations at position K205 in NR1I3_MOUSE

Protein	NR1I3_MOUSE (O35627) Gene: Nr1i3,Ca (other point mutations)	Swiss-Prot Cross-reference table Family page
Protein isoforms	2
Position	K205
General numbering (NucleaRDB)	456
Domain	LBD HELIX 4
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 205 in 1I3 Constitutive Androstane alpha (CAR1) family Position 259 in 1I Vitamin D3-like (VDR,PXR,CAR) family Position 252 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	K205E (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	K205A (True positive)

Relevant sentences

Reference #2 (Andersin T et al.): K205A

We agree with Dussault et al. (32 ) concerning the impact of K205 , since the mutant K205A has a similar functional profile as C357A (data not shown)

Reference #1 (Dussault I et al.): K205E

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
First , we created a K205E mutation that replaces a positively charged lysine with a negatively charged glutamate residue , which is incapable of neutralizing the C terminus of H12
Indeed , the K205E mutant was not constitutively active in transfection experiments (Fig. 5A )
This loss of activity did not result from a global defect in CAR activity because the K205E mutant retained the ability to bind DNA as an RXR heterodimer (data not shown)
In addition to losing constitutive activity , the K205E mutant exhibited only a weak response to TCPOBOP , and TCPOBOP failed to activate androstanol-repressed receptor , unlike in wild-type CAR (Fig. 5A )
Moreover , the K205E mutant failed to recruit coactivator in response to TCPOBOP (Fig. 5B )
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

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