RFX1

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Regulatory factor X, 1 (influences HLA class II expression)
File:PBB Protein RFX1 image.jpg
PDB rendering based on 1dp7.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols RFX1 ; EF-C
External IDs Template:OMIM5 Template:MGI HomoloGene2189
RNA expression pattern
File:PBB GE RFX1 206321 at tn.png
File:PBB GE RFX1 222012 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Regulatory factor X, 1 (influences HLA class II expression), also known as RFX1, is a human gene.[1]

This gene is a member of the regulatory factor X gene family, which encodes transcription factors that contain a highly-conserved winged helix DNA binding domain. The protein encoded by this gene is structurally related to regulatory factors X2, X3, X4, and X5. It is a transcriptional activator that can bind DNA as a monomer or as a heterodimer with RFX family members X2, X3, and X5, but not with X4. This protein binds to the X-boxes of MHC class II genes and is essential for their expression. Also, it can bind to an inverted repeat that is required for expression of hepatitis B virus genes.[1]

References

  1. 1.0 1.1 "Entrez Gene: RFX1 regulatory factor X, 1 (influences HLA class II expression)".

Further reading

  • Pugliatti L, Derré J, Berger R; et al. (1992). "The genes for MHC class II regulatory factors RFX1 and RFX2 are located on the short arm of chromosome 19". Genomics. 13 (4): 1307–10. PMID 1505960.
  • Herrero Sanchez C, Reith W, Silacci P, Mach B (1992). "The DNA-binding defect observed in major histocompatibility complex class II regulatory mutants concerns only one member of a family of complexes binding to the X boxes of class II promoters". Mol. Cell. Biol. 12 (9): 4076–83. PMID 1508204.
  • Reith W, Herrero-Sanchez C, Kobr M; et al. (1991). "MHC class II regulatory factor RFX has a novel DNA-binding domain and a functionally independent dimerization domain". Genes Dev. 4 (9): 1528–40. PMID 2253877.
  • Sáfrány G, Perry RP (1993). "Transcription factor RFX1 helps control the promoter of the mouse ribosomal protein-encoding gene rpL30 by binding to its alpha element". Gene. 132 (2): 279–83. PMID 8224874.
  • Reith W, Ucla C, Barras E; et al. (1994). "RFX1, a transactivator of hepatitis B virus enhancer I, belongs to a novel family of homodimeric and heterodimeric DNA-binding proteins". Mol. Cell. Biol. 14 (2): 1230–44. PMID 8289803.
  • Siegrist CA, Durand B, Emery P; et al. (1993). "RFX1 is identical to enhancer factor C and functions as a transactivator of the hepatitis B virus enhancer". Mol. Cell. Biol. 13 (10): 6375–84. PMID 8413236.
  • Emery P, Durand B, Mach B, Reith W (1996). "RFX proteins, a novel family of DNA binding proteins conserved in the eukaryotic kingdom". Nucleic Acids Res. 24 (5): 803–7. PMID 8600444.
  • Doyle J, Hoffman S, Ucla C; et al. (1996). "Locations of human and mouse genes encoding the RFX1 and RFX2 transcription factor proteins". Genomics. 35 (1): 227–30. doi:10.1006/geno.1996.0343. PMID 8661125.
  • Agami R, Shaul Y (1998). "The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genes". Oncogene. 16 (14): 1779–88. doi:10.1038/sj.onc.1201708. PMID 9583676.
  • Katan-Khaykovich Y, Shaul Y (1998). "RFX1, a single DNA-binding protein with a split dimerization domain, generates alternative complexes". J. Biol. Chem. 273 (38): 24504–12. PMID 9733744.
  • Iwama A, Pan J, Zhang P; et al. (1999). "Dimeric RFX proteins contribute to the activity and lineage specificity of the interleukin-5 receptor alpha promoter through activation and repression domains". Mol. Cell. Biol. 19 (6): 3940–50. PMID 10330134.
  • Zajac-Kaye M, Ben-Baruch N, Kastanos E; et al. (2000). "Induction of Myc-intron-binding polypeptides MIBP1 and RFX1 during retinoic acid-mediated differentiation of haemopoietic cells". Biochem. J. 345 Pt 3: 535–41. PMID 10642512.
  • Katan-Khaykovich Y, Shaul Y (2001). "Nuclear import and DNA-binding activity of RFX1. Evidence for an autoinhibitory mechanism". Eur. J. Biochem. 268 (10): 3108–16. PMID 11358531.
  • Morotomi-Yano K, Yano K, Saito H; et al. (2002). "Human regulatory factor X 4 (RFX4) is a testis-specific dimeric DNA-binding protein that cooperates with other human RFX members". J. Biol. Chem. 277 (1): 836–42. doi:10.1074/jbc.M108638200. PMID 11682486.
  • Sengupta PK, Fargo J, Smith BD (2002). "The RFX family interacts at the collagen (COL1A2) start site and represses transcription". J. Biol. Chem. 277 (28): 24926–37. doi:10.1074/jbc.M111712200. PMID 11986307.
  • Nakayama A, Murakami H, Maeyama N; et al. (2003). "Role for RFX transcription factors in non-neuronal cell-specific inactivation of the microtubule-associated protein MAP1A promoter". J. Biol. Chem. 278 (1): 233–40. doi:10.1074/jbc.M209574200. PMID 12411430.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Norquay LD, Yang X, Sheppard P; et al. (2003). "RFX1 and NF-1 associate with P sequences of the human growth hormone locus in pituitary chromatin". Mol. Endocrinol. 17 (6): 1027–38. doi:10.1210/me.2003-0025. PMID 12624117.
  • Maijgren S, Sur I, Nilsson M, Toftgård R (2004). "Involvement of RFX proteins in transcriptional activation from a Ras-responsive enhancer element". Arch. Dermatol. Res. 295 (11): 482–9. doi:10.1007/s00403-004-0456-5. PMID 15024578.
  • Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.

External links


This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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