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 the selected point mutation and provides links to other documents. The sentence(s) where the point mutation K187A was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation K187A in NR1I3_MOUSE

Point mutation:	K187A
Domain:	LBD HELIX 3
General numbering (NucleaRDB):	351
Protein:	NR1I3_MOUSE (Nr1i3,Ca)	Swiss-Prot Cross-reference table Family page
Protein isoforms	2
Other point mutations / same protein / same position	Point mutations at position 187 in NR1I3_MOUSE
Other point mutations / same protein	List of mutations in NR1I3_MOUSE
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 / 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:	The critical role of carboxy-terminal amino acids in ligand-dependent and -independent transactivation of the constitutive androstane receptor. Andersin T, Vaisanen S, Carlberg C Mol Endocrinol 2003 Feb;17(2):234-46.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	True positive

Relevant sentences:

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