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TRANSFAC FACTOR TABLE, Release 2017.2 - public - 2017-06-30, (C) QIAGEN


AC T16715 XX ID T16715 XX DT 25.09.2009 (created); smt. DT 11.12.2015 (updated); sup. CO Copyright (C), QIAGEN. XX FA RXR-gamma XX SY NR2B3; retinoid X receptor gamma; RXR-gamma; RXRG. XX OS mouse, Mus musculus OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae XX GE G006696 Rxrg. XX CL C0002; CC (rec). XX SZ 463 AA; 50.9 kDa (cDNA) (calc.). XX SQ MYGNYSHFMKFPTGFGGSPGHTGSTSMSPSVALPTGKPMDSHPSYTDTPVSAPRTLSAVG SQ TPLNALGSPYRVITSAMGPPSGALAAPPGINLVAPPSSQLNVVNSVSSSEDIKPLPGLPG SQ IGNMNYPSTSPGSLVKHICAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLIYTCRDNKD SQ CLIDKRQRNRCQYCRYQKCLVMGMKREAVQEERQRSRERAESEAECASSSHEDMPVERIL SQ EAELAVEPKTESYGDMNVENSTNDPVTNICHAADKQLFTLVEWAKRIPHFSDLTLEDQVI SQ LLRAGWNELLIASFSHRSVSVQDGILLATGLHVHRSSAHSAGVGSIFDRVLTELVSKMKD SQ MQMDKSELGCLRAIVLFNPDAKGLSNPSEVETLREKVYATLEAYTKQKYPEQPGRFAKLL SQ LRLPALRSIGLKCLEHLFFFKLIGDTPIDSFLMEMLETPLQIT XX SC Swiss-Prot#P28705 XX FT 1 138 region A/B (modulating transactivation functions) [3]. FT 37 411 PF00478; IMP dehydrogenase / GMP reductase domai. FT 136 207 SM00399; c4gold. FT 136 211 PS51030; NUCLEAR_REC_DBD_2. FT 137 212 PF00105; Zinc finger, C4 type (two domains). FT 139 204 region C (DNA-binding, dimerization) [3]. FT 205 213 T-box, functional: important for dimerization with T01354 [7]. FT 205 228 region D (hinge region) [3]. FT 229 463 region E/F (ligand-binding, dimerization, activating function 2) [3]. FT 271 430 SM00430; holi. FT 274 455 PF00104; Ligand-binding domain of nuclear hormon. XX IN T08888 LXRalpha-isoform1; human, Homo sapiens. XX MX M00963 V$T3R_Q6. XX BS R03935. BS R03936. BS R08504. BS R11727. XX DR TRANSPATH: MO000161932. DR EMBL: M84819; DR EMBL: X66225; DR UniProtKB: P28705; XX RN [1]; RE0000265. RX PUBMED: 1310259. RA Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewski T., Chen J.-Y., Staub A., Garnier J.-M., Mader S., Chambon P. RT Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently RL Cell 68:377-395 (1992). RN [2]; RE0000270. RX PUBMED: 1326406. RA Nagpal S., Saunders M., Kastner P., Durand B., Nakshatri H., Chambon P. RT Promoter context-and response element-dependent specificity of the transcriptional activation and modulating functions of retinoic acid receptors RL Cell 70:1007-1019 (1992). RN [3]; RE0000789. RX PUBMED: 1312497. RA Mangelsdorf D. J., Borgmeyer U., Heyman R. A., Zhou J. Y., Ong E. S., Oro A. E., Kakizuka A., Evans R. M. RT Characterization of three RXR genes that mediate the action of 9-cis retinoic acid RL Genes Dev. 6:329-344 (1992). RN [4]; RE0002413. RX PUBMED: 2554307. RA Hamada K., Gleason S., Levi B.-Z., Hirschfeld S., Apella E., Ozato K. RT H-2RIIBP, a member of the nuclear hormone receptor superfamily that binds to both the regulatory element of major histocompatibility class I genes and the estrogen response element RL Proc. Natl. Acad. Sci. USA 86:8289-8293 (1989). RN [5]; RE0003240. RX PUBMED: 8127707. RA Muscat G. E. O., Mynett-Johnson L., Dowhan D., Downes M., Griggs R. RT Activation of MyoD gene transcription by 3, 4, 3'-triiodo-L-thyronine: a direct role for the thyroid hormone and retinoid X receptors RL Nucleic Acids Res. 22:583-591 (1994). RN [6]; RE0013625. RX PUBMED: 10219237. RA Nuclear Receptors Nomenclature Committee. RT A unified nomenclature system for the nuclear receptor superfamily RL Cell 97:161-163 (1999). RN [7]; RE0017065. RX PUBMED: 9242684. RA IJpenberg A., Jeannin E., Wahli W., Desvergne B. RT Polarity and specific sequence requirements of peroxisome proliferator-activated receptor (PPAR)/retinoid X receptor heterodimer binding to DNA. A functional analysis of the malic enzyme gene PPAR response element RL J. Biol. Chem. 272:20108-20117 (1997). XX //