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


AC T08433 XX ID T08433 XX DT 19.01.2006 (created); din. DT 10.04.2014 (updated); spk. CO Copyright (C), QIAGEN. XX FA RXR-alpha XX SY NR2B1; retinoid X receptor alpha; RXR; RXR-alpha; RXRA. XX OS human, Homo sapiens OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates XX GE G004834 RXRA; HGNC: RXRA. XX CL C0002; CC (rec). XX SZ 462 AA; 50.8 kDa (cDNA) (calc.), 54 kDa (SDS) XX SQ MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPING SQ MGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVP SQ AHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLID SQ KRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAEL SQ AVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVIL SQ LRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDM SQ QMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLL SQ RLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT XX SC translated from EMBL #X52773 XX FT 66 459 PF00478; IMP dehydrogenase / GMP reductase domai. FT 129 212 DNA-binding domain [34]. FT 132 203 SM00399; c4gold. FT 132 207 PS51030; NUCLEAR_REC_DBD_2. FT 133 208 PF00105; Zinc finger, C4 type (two domains). FT 135 155 zinc finger 1 (C-X2-C-X13-C-X2-C) [33]. FT 153 157 P-Box [33]. FT 171 190 zinc finger 2 (C-X5-C-X9-C-X2-C) [33]. FT 172 176 D-Box [33]. FT 201 209 T-box, involved in heterodimer formation with RAR-alpha [34]. FT 270 429 SM00430; holi. FT 273 454 PF00104; Ligand-binding domain of nuclear hormon. FT 410 432 helix 10 [35]. FT 437 456 helix 11 [35]. XX IN T08796 ASC-2; human, Homo sapiens. IN T08910 Bcl-3; human, Homo sapiens. IN T10260 CLOCK; human, Homo sapiens. IN T34265 COPS2; human, Homo sapiens. IN T33929 DRIP205-isoform1; human, Homo sapiens. IN T33762 DRIP205; human, Homo sapiens. IN T08300 ER-alpha-L; human, Homo sapiens. IN T17427 ER-beta; mouse, Mus musculus. IN T09602 ER; Mammalia. IN T09632 FXR; human, Homo sapiens. IN T09633 FXR; rat, Rattus norvegicus. IN T09300 FXRbeta; mouse, Mus musculus. IN T28749 HMGN3; human, Homo sapiens. IN T00414 IkappaB-beta; human, Homo sapiens. IN T08888 LXRalpha-isoform1; human, Homo sapiens. IN T04909 MOP4; human, Homo sapiens. IN T11196 MOP4; human, Homo sapiens. IN T04688 NCOR1; mouse, Mus musculus. IN T10361 Oct-2; Mammalia. IN T23091 p300; Mammalia. IN T10456 p50; human, Homo sapiens. IN T00641 POU2F1-isoform1; human, Homo sapiens. IN T00643 POU2F1; rat, Rattus norvegicus. IN T08628 POU2F1; Mammalia. IN T08431 PPARalpha; mouse, Mus musculus. IN T05332 PPARgamma2; mouse, Mus musculus. IN T00594 RelA-p65-isoform1; human, Homo sapiens. IN T10397 RelA-p65; Mammalia. IN T08947 SHP; mouse, Mus musculus. IN T08256 SRC-1A; human, Homo sapiens. IN T22422 SRC3-xbb2; human, Homo sapiens. IN T01152 T3R-alpha1; human, Homo sapiens. IN T08264 T3R-beta; human, Homo sapiens. IN T08520 TBP-isoform1; human, Homo sapiens. IN T14175 TBP; Mammalia. IN T19335 TIF1a-short; human, Homo sapiens. IN T08482 VDR-isoform1; human, Homo sapiens. IN T00885 VDR; human, Homo sapiens. IN T09401 VDR; mouse, Mus musculus. XX MX M00966 V$DR3_Q4. MX M00965 V$DR4_Q2. MX M07280 V$NR1NR2_Q3. MX M00518 V$PPARA_02. MX M02272 V$RXRRAR_01. MX M00963 V$T3R_Q6. XX BS R03988. BS R09991. BS R09969. BS R09956. BS R11591. BS R11592. BS R11593. BS R11594. BS R11595. BS R11596. BS R11597. BS R11598. BS R11604. BS R11605. BS R11606. BS R11607. BS R11608. BS R11609. BS R11610. BS R11611. BS R11612. BS R11613. BS R11614. BS R11615. BS R11616. BS R11617. BS R11618. BS R11619. BS R11621. BS R11622. BS R11480. BS R11481. BS R11482. BS R11483. BS R11484. BS R11485. BS R11486. BS R11487. BS R11488. BS R11489. BS R11585. BS R11490. BS R11491. BS R11492. BS R11493. BS R11494. BS R11495. BS R11496. BS R11497. BS R11498. BS R11499. BS R11500. BS R11501. BS R11502. BS R11503. BS R11504. BS R11505. BS R11506. BS R11507. BS R11508. BS R11509. BS R11510. BS R11511. BS R11512. BS R11513. BS R11514. BS R11515. BS R11516. BS R11517. BS R11518. BS R11519. BS R11520. BS R11521. BS R11522. BS R11523. BS R11524. BS R11525. BS R11526. BS R11527. BS R11528. BS R11529. BS R11530. BS R11531. BS R11532. BS R11533. BS R11534. BS R11535. BS R11536. BS R11537. BS R11538. BS R11539. BS R11540. BS R11541. BS R11542. BS R11543. BS R11544. BS R11545. BS R11546. BS R11547. BS R11548. BS R11549. BS R11550. BS R11551. BS R11555. BS R11556. BS R11557. BS R11558. BS R11559. BS R11560. BS R11561. BS R11562. BS R11563. BS R11564. BS R11565. BS R11566. BS R11567. BS R11568. BS R11572. BS R11573. BS R11574. BS R11575. BS R11576. BS R11577. BS R11578. BS R11579. BS R11580. BS R11581. BS R11582. BS R11583. BS R11584. BS R03933. BS R03964. BS R03965. BS R03966. BS R03967. BS R03968. BS R03969. BS R03970. BS R03971. BS R03972. BS R03973. BS R03974. BS R03975. BS R03976. BS R03977. BS R03978. BS R03979. BS R03981. BS R28150. BS R03937. BS R03938. BS R03985. BS R04403. BS R04405. BS R10082. BS R10083. BS R10084. BS R10085. BS R03939. BS R03940. BS R03953. BS R03980. BS R03984. BS R04508. BS R04765. BS R04766. BS R04767. BS R04777. BS R10034. BS R10023. BS R01673. BS R01193. BS R10018. BS R09990. BS R03934. BS R04519. BS R38690. BS R23147. BS R10031. BS R03960. BS R09992. BS R28148. BS R12767. BS R03929. BS R13314. BS R13317. BS R10067. BS R22383. BS R22384. BS R56149. BS R59022. BS R28149. BS R27612. BS R27477. BS R12750. BS R10053. BS R04761. BS R08504. BS R33255. BS R33258. BS R12027. BS R04634. BS R04635. BS R03987. BS R03986. BS R04760. BS R01188. BS R10068. BS R03932. BS R09968. BS R20554. BS R11773. BS R11775. BS R38694. BS R10022. BS R03931. BS R04185. XX DR TRANSPATH: MO000057731. DR EMBL: X52773; HSRARLP. DR UniProtKB: P19793; RXRA_HUMAN. DR PDB: 1lbd. XX RN [1]; RE0010799. RX PUBMED: 7667283. RA Schulman I. G., Chakravarti D., Juguilon H., Romo A., Evans R. M. RT Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation RL Proc. Natl. Acad. Sci. USA 92:8288-8292 (1995). RN [2]; RE0016043. RX PUBMED: 8621574. RA Miyata K. S., McCaw S. E., Patel H. V., Rachubinski R. A., Capone J. P. RT The orphan nuclear hormone receptor LXR alpha interacts with the peroxisome proliferator-activated receptor and inhibits peroxisome proliferator signaling RL J. Biol. Chem. 271:9189-9192 (1996). RN [3]; RE0016189. RX PUBMED: 7774010. RA Forman B. M., Goode E., Chen J., Oro A. E., Bradley D. J., Perlmann T., Noonan D. J., Burka L. T., McMorris T., Lamph W. W., et a. l. RT Identification of a nuclear receptor that is activated by farnesol metabolites RL Cell 81:687-693 (1995). RN [4]; RE0017308. RX PUBMED: 9115274. RA Thenot S., Henriquet C., Rochefort H., Cavailles V. RT Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1 RL J. Biol. Chem. 272:12062-12068 (1997). RN [5]; RE0023352. RX PUBMED: 12529392. RA Otte K., Kranz H., Kober I., Thompson P., Hoefer M., Haubold B., Remmel B., Voss H., Kaiser C., Albers M., Cheruvallath Z., Jackson D., Casari G., Koegl M., Paabo S., Mous J., Kremoser C., Deuschle U. RT Identification of farnesoid X receptor beta as a novel mammalian nuclear receptor sensing lanosterol. RL Mol. Cell. Biol. 23:864-872 (2003). RN [6]; RE0025974. RX PUBMED: 9653119. RA Yuan C. X., Ito M., Fondell J. D., Fu Z. Y., Roeder R. G. RT The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion RL Proc. Natl. Acad. Sci. USA 95:7939-44 (1998). RN [7]; RE0027683. RX PUBMED: 10517671. RA Monden T., Kishi M., Hosoya T., Satoh T., Wondisford F. E., Hollenberg A. N., Yamada M., Mori M. RT p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) on peroxisome proliferator-activated receptor-gamma/RXR heterodimers. RL Mol. Endocrinol. 13:1695-703 (1999). RN [8]; RE0028212. RX PUBMED: 9372944. RA Seol W., Chung M., Moore D. D. RT Novel receptor interaction and repression domains in the orphan receptor SHP. RL Mol. Cell. Biol. 17:7126-31 (1997). RN [9]; RE0031544. RX PUBMED: 11250942. RA Issa L. L., Leong G. M., Barry J. B., Sutherland R. L., Eisman J. A. RT Glucocorticoid receptor-interacting protein-1 and receptor-associated coactivator-3 differentially interact with the vitamin D receptor (VDR) and regulate VDR-retinoid X receptor transcriptional cross-talk. RL Endocrinology 142:1606-15 (2001). RN [10]; RE0038010. RX PUBMED: 10347167. RA Heinlein C. A., Ting H. J., Yeh S., Chang C. RT Identification of ARA70 as a ligand-enhanced coactivator for the peroxisome proliferator-activated receptor gamma RL J. Biol. Chem. 274:16147-52 (1999). RN [11]; RE0039064. RX PUBMED: 10022764. RA Miyata K. S., McCaw S. E., Meertens L. M., Patel H. V., Rachubinski R. A., Capone J. P. RT Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor alpha and liver-X-receptor alpha RL Mol. Cell. Endocrinol. 146:69-76 (1998). RN [12]; RE0039941. RX PUBMED: 11682061. RA Bastie J. N., Despouy G., Balitrand N., Rochette-Egly C., Chomienne C., Delva L. RT The novel co-activator CRABPII binds to RARalpha and RXRalpha via two nuclear receptor interacting domains and does not require the AF-2 'core' RL FEBS Lett. 507:67-73 (2001). RN [13]; RE0042804. RX PUBMED: 10454579. RA Kim H. J., Yi J. Y., Sung H. S., Moore D. D., Jhun B. H., Lee Y. C., Lee J. W. RT Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation RL Mol. Cell. Biol. 19:6323-32 (1999). RN [14]; RE0047290. RX PUBMED: 7876247. RA MacDonald P. N., Sherman D. R., Dowd D. R., Jefcoat S. C. Jr, DeLisle R. K. RT The vitamin D receptor interacts with general transcription factor IIB RL J. Biol. Chem. 270:4748-52 (1995). RN [15]; RE0047527. RX PUBMED: 10866662. RA Mahajan M. A., Samuels H. H. RT A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. RL Mol. Cell. Biol. 20:5048-5063 (2000). RN [16]; RE0047548. RX PUBMED: 10733574. RA Rachez C., Gamble M., Chang C. P., Atkins G. B., Lazar M. A., Freedman L. P. RT The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes. RL Mol. Cell. Biol. 20:2718-2726 (2000). RN [17]; RE0047599. RX PUBMED: 11739747. RA Ko L., Cardona G. R., Henrion-Caude A., Chin W. W. RT Identification and characterization of a tissue-specific coactivator, GT198, that interacts with the DNA-binding domains of nuclear receptors. RL Mol. Cell. Biol. 22:357-369 (2002). RN [18]; RE0047600. RX PUBMED: 9717844. RA Lee S. K., Choi H. S., Song M. R., Lee M. O., Lee J. W. RT Estrogen receptor, a common interaction partner for a subset of nuclear receptors. RL Mol. Endocrinol. 12:1184-1192 (1998). RN [19]; RE0047636. RX PUBMED: 9148917. RA Collingwood T. N., Butler A., Tone Y., Clifton-Bligh R. J., Parker M. G., Chatterjee V. K. RT Thyroid hormone-mediated enhancement of heterodimer formation between thyroid hormone receptor beta and retinoid X receptor. RL J. Biol. Chem. 272:13060-13065 (1997). RN [20]; RE0047680. RX PUBMED: 9812988. RA Na S. Y., Choi H. S., Kim J. W., Na D. S., Lee J. W. RT Bcl3, an IkappaB protein, as a novel transcription coactivator of the retinoid X receptor. RL J. Biol. Chem. 273:30933-30938 (1998). RN [21]; RE0047685. RX PUBMED: 10490654. RA Li D., Desai-Yajnik V., Lo E., Schapira M., Abagyan R., Samuels H. H. RT NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors. RL Mol. Cell. Biol. 19:7191-7202 (1999). RN [22]; RE0047728. RX PUBMED: 8887632. RA L'Horset F., Dauvois S., Heery D. M., Cavailles V., Parker M. G. RT RIP-140 interacts with multiple nuclear receptors by means of two distinct sites. RL Mol. Cell. Biol. 16:6029-6036 (1996). RN [23]; RE0047744. RX PUBMED: 7776974. RA Lee J. W., Choi H. S., Gyuris J., Brent R., Moore D. D. RT Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. RL Mol. Endocrinol. 9:243-254 (1995). RN [24]; RE0047948. RX PUBMED: 10383413. RA Kakizawa T., Miyamoto T., Ichikawa K., Kaneko A., Suzuki S., Hara M., Nagasawa T., Takeda T., Mori J., Kumagai M., Hashizume K. RT Functional interaction between Oct-1 and retinoid X receptor. RL J. Biol. Chem. 274:19103-19108 (1999). RN [25]; RE0048879. RX PUBMED: 11818500. RA Marimuthu A., Feng W., Tagami T., Nguyen H., Jameson J. L., Fletterick R. J., Baxter J. D., West B. L. RT TR surfaces and conformations required to bind nuclear receptor corepressor. RL Mol. Endocrinol. 16:271-286 (2002). RN [26]; RE0051855. RX PUBMED: 10809746. RA Chen S., Cui J., Nakamura K., Ribeiro R. C., West B. L., Gardner D. G. RT Coactivator-vitamin D receptor interactions mediate inhibition of the atrial natriuretic peptide promoter. RL J. Biol. Chem. 275:15039-15048 (2000). RN [27]; RE0051975. RX PUBMED: 11075811. RA Liu Y. Y., Nguyen C., Peleg S. RT Regulation of ligand-induced heterodimerization and coactivator interaction by the activation function-2 domain of the vitamin D receptor. RL Mol. Endocrinol. 14:1776-1787 (2000). RN [28]; RE0051983. RX PUBMED: 12529369. RA Barry J. B., Leong G. M., Church W. B., Issa L. L., Eisman J. A., Gardiner E. M. RT Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues. RL J. Biol. Chem. 278:8224-8228 (2003). RN [29]; RE0051998. RX PUBMED: 17595320. RA Schedlich L. J., Muthukaruppan A., O'Han M. K., Baxter R. C. RT Insulin-like growth factor binding protein-5 interacts with the vitamin D receptor and modulates the vitamin D response in osteoblasts. RL Mol. Endocrinol. 21:2378-2390 (2007). RN [30]; RE0053416. RX PUBMED: 11514567. RA Zhang C., Baudino T. A., Dowd D. R., Tokumaru H., Wang W., MacDonald P. N. RT Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription. RL J. Biol. Chem. 276:40614-40620 (2001). RN [31]; RE0056137. RX PUBMED: 10377179. RA Solomon C., White J. H., Kremer R. RT Mitogen-activated protein kinase inhibits 1,25-dihydroxyvitamin D3-dependent signal transduction by phosphorylating human retinoid X receptor alpha. RL J. Clin. Invest. 103:1729-1735 (1999). RN [32]; RE0060774. RX PUBMED: 16608838. RA Gu X., Ke S., Liu D., Sheng T., Thomas P. E., Rabson A. B., Gallo M. A., Xie W., Tian Y. RT Role of NF-kappaB in regulation of PXR-mediated gene expression: a mechanism for the suppression of cytochrome P-450 3A4 by proinflammatory agents. RL J. Biol. Chem. 281:17882-17889 (2006). RN [33]; RE0000793. RX PUBMED: 8392478. RA Perlmann T., Rangarajan P. N., Umesono K., Evans R. M. RT Determinants for selective RAR and TR recognition of direct repeat HREs RL Genes Dev. 7:1411-1422 (1993). RN [34]; RE0022229. RX PUBMED: 10698945. RA Rastinejad F., Wagner T., Zhao Q., Khorasanizadeh S. RT Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1. RL EMBO J. 19:1045-1054 (2000). RN [35]; RE0049022. RX PUBMED: 9660764. RA Chinpaisal C., Lee C. H., Wei L. N. RT Mechanisms of the mouse orphan nuclear receptor TR2-11-mediated gene suppression. RL J. Biol. Chem. 273:18077-18085 (1998). XX //