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 T153I 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 T153I in RORA_HUMAN

Point mutation:	T153I
Cited point mutation:	T120I,Thr120Ile
Domain:	DNA_BIND
General numbering (NucleaRDB):	D048
Protein:	RORA_HUMAN (RORA,NR1F1, RZR)	Swiss-Prot Cross-reference table Family page
Protein isoforms	4
Other point mutations / same protein	List of mutations in RORA_HUMAN
Family alignments	1F1 ROR alpha 1F RAR-related orphan receptor (ROR,HR3) 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR
Other point mutations / same position
Reference:	Transition from monomeric to homodimeric DNA binding by nuclear receptors: identification of RevErbAalpha determinants required for RORalpha homodimer complex formation. Moraitis AN, Giguere V Mol Endocrinol 1999 Mar;13(3):431-9.	Medline
Other point mutations / same article	List
Text source	HTML and PDF full texts
Validation status	True positive

Relevant sentences:

Thr120Ile

The Thr120Ile mutation (RORm9) increases considerably the amount of dimer complexes formed (Fig. 5B(image) )
Therefore , a minimum of four amino acid changes , three in the first zinc finger module (Lys79Val , Ser80Ala , Ile88Phe) and one in the second zinc finger module (Thr120Ile) , are required to provide the ROR DBD with the ability to homodimerize on an extended DR2
The Thr120Ile mutation (RORm9) increases considerably the amount of dimer complexes formed (Fig. 5B)

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