RFX1

From Wikipedia, the free encyclopedia


Regulatory factor X, 1 (influences HLA class II expression)
PDB rendering based on 1dp7.
Available structures: 1dp7
Identifiers
Symbol(s) RFX1; EF-C
External IDs OMIM: 600006 MGI: 105982 HomoloGene: 2189
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5989 19724
Ensembl ENSG00000132005 ENSMUSG00000031706
Uniprot P22670 Q3V383
Refseq NM_002918 (mRNA)
NP_002909 (protein)		 NM_009055 (mRNA)
NP_033081 (protein)
Location Chr 19: 13.93 - 13.98 Mb Chr 8: 86.96 - 86.99 Mb
Pubmed search [1] [2]

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]

[edit] References

  1. ^ a b Entrez Gene: RFX1 regulatory factor X, 1 (influences HLA class II expression).

[edit] 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. 

[edit] External links


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v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH)
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1
(1.3) bHLH-ZIP
MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4
GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)
(2.3) Cys2His2
ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6
(2.5) Alternating composition
AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B
(3) Helix-turn-helix
domains
ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1
(3.2) Paired box
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)
HSF (1, 2, 4)
(3.5) Tryptophan clusters
ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2
(3.6) TEA domain
transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)
(4.2) STAT
STAT (1, 2, 3, 4, 5, 6)
(4.3) p53
(4.4) MADS box
Mef2 (A, B, C, D) • SRF
HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1
(4.10) Cold-shock domain
(4.11) Runt
(0) Other
transcription factors
(0.2) HMGI(Y)
HMGA (1, 2) • HBP1
Rb • RBL1 • RBL2
(0.5) AP-2/EREBP-related factors
Apetala 2 • EREBP • B3
(0.6) Miscellaneous
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD