AC T01673
AS T00230, T00728, T00909.
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ID T01673
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DT 15.02.1996 (created); ewi.
DT 11.12.2013 (updated); asv.
CO Copyright (C), QIAGEN.
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FA rfx1
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SY EF-C; enhancer factor C; hRFX1; RF-X; RFX; XX.
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OS human, Homo sapiens
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates
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GE G003963 RFX1; HGNC: RFX1.
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HO TGT3, EP protein, MDBP, CeRFX (C. elegans), Sak1 (S. pombe), Crt1 (S. cerevisiae) T03541.
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CL C0023; fork head; 3.3.3.0.1.
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].
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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];
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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.
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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.
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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.
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DR TRANSPATH: MO000025858.
DR UniProtKB: P22670;
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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).
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