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

AC T01673 AS T00230, T00728, T00909. XX ID T01673 XX DT 15.02.1996 (created); ewi. DT 11.12.2013 (updated); asv. CO Copyright (C), QIAGEN. XX FA rfx1 XX SY EF-C; enhancer factor C; hRFX1; RF-X; RFX; XX. XX OS human, Homo sapiens OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates XX GE G003963 RFX1; HGNC: RFX1. XX HO TGT3, EP protein, MDBP, CeRFX (C. elegans), Sak1 (S. pombe), Crt1 (S. cerevisiae) T03541. XX CL C0023; fork head; XX SF member of winged-helix class of helix-turn-helix superclass of factors [15]; SF the DBD exhibits a weak sequence similarity to the bHLH domain consensus and is predicted to constitute two amphipathic helices and a linking loop [3]; SF it binds to DNA as a dimer, but dimerization is not a prerequisite for DNA-binding [3]; SF both RF-X subunits interact independently with the X-box(es) [3]; SF together with MIBP1 T02313, rfx1 constitutes the DNA-binding activity MIF-1 T01047 [12]; SF secondary structure exhibits three alpha-helical and one beta-stranded segments within the DNA-binding domain, the potential helix III region being responsible for sequence specific binding [13]; SF DNA binding domain has been identified as winged-helix, hrfx1 uses a beta-hairpin (or wing) for DNA recognition instead of recognition helix [15]; SF DBD consists of 3 alpha-helices, 3 beta-strands and 3 connecting loops [15]; SF new mode of DNA binding: beta-strands S2 and S3 and wing W1 make extensive contacts with the major groove of one half-site of the symmetric X-box, alpha-helix H3 interacts with the minor groove of the other half-site [15]; SF N-terminal transactivation domain, but activation potential can be masked by autoinhibitory domain [16]; SF can bind DNA as a homodimer or heterodimer with RFX2 or RFX3 [16]; SF possesses a split, extended dimerization domain which mediated formation of alternative homodimeric complexes [17] [19]; SF EDD is similar to the LBD of nuclear receptors by several features, it is independent on DBD, mediates dimerization and can function in alternative conformations [17] [19]; SF C-terminal acidic region may work as an autoinhibitory domain relating DNA binding by rfx1 [20]; XX CP ubiquitous, highly expressed in primary eosinophils [16]. XX FF homodimers can function as activators or repressors depending on the nature of interactions between two subunits, two distinct types of homodimers can be formed which are different in their function [17] [18] [19]; FF preferential binding to methylated sequences; FF binds to X boxes of MHC class II alpha-chain gene promoters and the HBV enhancer I [11] [5]; FF identical to EF-C, but different from NF-X [11]; FF at the HBV enhancer I, it cooperates with liver-specific factors [11]; FF it cooperatively binds to the X-Y-box pattern of MHC gene promoters with NF-Y [10]; FF inhibitory role in the regulation of proliferating cell nuclear antigen (PCNA) expression [14]; FF DNA binding activity may be regulated by phosphorylation [20]; XX IN T02313 MIBP1; rat, Rattus norvegicus. IN T01673 rfx1; human, Homo sapiens. IN T01667 rfx2; human, Homo sapiens. IN T01669 rfx2; mouse, Mus musculus. IN T01670 rfx3; human, Homo sapiens. XX MX M00626 V$EFC_Q6. MX M00280 V$RFX1_01. MX M00281 V$RFX1_02. MX M04627 V$RFX1_Q6. MX M00975 V$RFX_Q6. MX M07305 V$RFX_Q6_01. XX BS R03409. BS R02146. BS R00637. BS R00797. BS R03424. BS R32831. BS R30941. BS R71646. BS R02384. BS R03695. BS R30949. BS R59208. BS R01940. BS R59191. BS R59196. BS R11435. BS R02241. BS R04826. BS R04827. XX DR TRANSPATH: MO000025858. DR UniProtKB: P22670; XX RN [1]; RE0000111. RX PUBMED: 3133120. RA Reith W., Satola S., Herrero-Sanchez C., Amaldi I., Lisowska-Grospierre B., Griscelli C., Hadam M. R., Mach B. RT Congenital Immunodeficiency with a Regulatory Defect in MHC Class II Gene Expression Lacks a Specific HLA-DR Promoter Binding Protein, RF-X RL Cell 53:897-906 (1988). RN [2]; RE0000351. RX PUBMED: 3653073. RA Shaul Y., Ben-Levy R. RT Multiple nuclear proteins in liver cells are bound to hepatitis B virus enhancer element and its upstream sequences RL EMBO J. 6:1913-1920 (1987). RN [3]; RE0000715. RX PUBMED: 2253877. RA Reith W., Herrero-Sanchez C., Kobr M., Silacci P., Berte Ch., Barras E., Fey S., Mach B. RT MHC class II regulatory factor RFX has a novel DNA-binding domain and a functionally independent dimerization domain RL Genes Dev. 4:1528-1540 (1990). RN [4]; RE0001429. RX PUBMED: 2550788. RA Ostapchuk P., Scheirle G., Hearing P. RT Binding of Nuclear Factor EF-C to a Functional Domain of the Hepatitis B Virus Enhancer Region RL Mol. Cell. Biol. 9:2787-2797 (1989). RN [5]; RE0001485. RX PUBMED: 2304471. RA Kobr M., Reith W., Herrero-Sanchez C., Mach B. RT Two DNA-binding proteins discriminate between the promoters of different members of the major histocompatibility complex class II multigene family RL Mol. Cell. Biol. 10:965-971 (1990). RN [6]; RE0002144. RX PUBMED: 1903200. RA Hasegawa S. L., Sloan J. H., Reith W., Mach B., Boss J. M. RT Regulatory factor-X binding to mutant HLA-DRA promoter sequences RL Nucleic Acids Res. 19:1243-1248 (1991). RN [7]; RE0002392. RX PUBMED: 2498880. RA Reith W., Barras E., Satola S., Kobr M., Reinhardt D., Sanchez C. H., Mach B. RT Cloning of the major histocompatibility complex class II promoter binding protein affected in a hereditary defect in class II gene regulation RL Proc. Natl. Acad. Sci. USA 86:4200-4204 (1989). RN [8]; RE0002442. RX PUBMED: 2120707. RA Cogswell J. P., Basta P. V., Ting J. P.-Y. RT X-box-binding proteins positively and negatively regulate transcription of the HLA-DRA gene through interaction with discrete upstream W and V elements RL Proc. Natl. Acad. Sci. USA 87:7703-7707 (1990). RN [9]; RE0002729. RX PUBMED: 1850932. RA Garcia A. D., Ostapchuk P., Hearing P. RT Methylation-dependent and -independent DNA binding of nuclear factor EF-C RL Virology 182:857-860 (1991). RN [10]; RE0003796. RX PUBMED: 8290561. RA Reith W., Siegrist C. A., Durand B., Barras E., Mach B. RT Function of major histocompatibility complex class II promoters requires cooperative binding between factors RFX and NF-Y RL Proc. Natl. Acad. Sci. USA 91:554-558 (1994). RN [11]; RE0003798. RX PUBMED: 8413236. RA Siegrist C. A., Durand B., Emery P., David E., Hearing P., Mach B., Reith W. RT RFX1 is identical to enhancer factor C and functions as a transactivator of the hepatitis B virus enhancer RL Mol. Cell. Biol. 13:6375-6384 (1993). RN [12]; RE0006616. RX PUBMED: 7760800. RA Reinhold W., Emens L., Itkes A., Blake M., Ichinose I., Zajac-Kaye M. RT The myc intron-binding polypeptide associates with RFX1 in vivo and binds to the major histocompatibility complex class II promoter region, to the hepatitis B virus enhancer, and to regulatory regions of several distinct viral genes RL Mol. Cell. Biol. 15:3041-3048 (1995). RN [13]; RE0006617. RX PUBMED: 8754849. RA Emery P., Strubin M., Hofmann K., Bucher P., Mach B., Reith W. RT A consensus motif in the RFX DNA binding domain and binding domain mutants with altered specificity RL Mol. Cell. Biol. 16:4486-4494 (1996). RN [14]; RE0017028. RX PUBMED: 10336433. RA Liu M., Lee B. H., Mathews M. B. RT Involvement of RFX1 protein in the regulation of the human proliferating cell nuclear antigen promoter RL J. Biol. Chem. 274:15433-15439 (1999). RN [15]; RE0022520. RX PUBMED: 10706293. RA Gajiwala K. S., Chen H., Cornille F., Roques B. P., Reith W., Mach B., Burley S. K. RT Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding. RL Nature 403:916-921 (2000). RN [16]; RE0022525. RX PUBMED: 10330134. RA Iwama A., Pan J., Zhang P., Reith W., Mach B., Tenen D. G., Sun Z. RT Dimeric RFX proteins contribute to the activity and lineage specificity of the interleukin-5 receptor alpha promoter through activation and repression domains. RL Mol. Cell. Biol. 19:3940-3950 (1999). RN [17]; RE0022527. RX PUBMED: 10556033. RA Katan-Khaykovich Y., Spiegel I., Shaul Y. RT The dimerization/repression domain of RFX1 is related to a conserved region of its yeast homologues Crt1 and Sak1: a new function for an ancient motif. RL J. Mol. Biol. 294:121-137 (1999). RN [18]; RE0022528. RX PUBMED: 9278482. RA Katan Y., Agami R., Shaul Y. RT The transcriptional activation and repression domains of RFX1, a context-dependent regulator, can mutually neutralize their activities. RL Nucleic Acids Res. 25:3621-3628 (1997). RN [19]; RE0022530. RX PUBMED: 9733744. RA Katan-Khaykovich Y., Shaul Y. RT RFX1, a single DNA-binding protein with a split dimerization domain, generates alternative complexes. RL J. Biol. Chem. 273:24504-24512 (1998). RN [20]; RE0022531. RX PUBMED: 11358531. RA Katan-Khaykovich Y., Shaul Y. RT Nuclear import and DNA-binding activity of RFX1. Evidence for an autoinhibitory mechanism. RL Eur. J. Biochem. 268:3108-3116 (2001). XX //