GTF2I

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General transcription factor II, i
PDB rendering based on 1q60.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols GTF2I ; WBS; BAP-135; BAP135; BTKAP1; DIWS; IB291; SPIN; TFII-I; WBSCR6
External IDs Template:OMIM5 Template:MGI HomoloGene: 7748
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

General transcription factor II, i, also known as GTF2I, is a human gene.[1]

This gene encodes a multifunctional phosphoprotein with roles in transcription and signal transduction. It is deleted in Williams-Beuren syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at chromosome 7q11.23. The exon(s) encoding 5' UTR has not been fully defined, but this gene is known to contain at least 34 exons, and its alternative splicing generates 4 transcript variants.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: GTF2I general transcription factor II, i".

Further reading

  • Roy AL, Meisterernst M, Pognonec P, Roeder RG (1992). "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature. 354 (6350): 245–8. doi:10.1038/354245a0. PMID 1961251.
  • Roy AL, Carruthers C, Gutjahr T, Roeder RG (1993). "Direct role for Myc in transcription initiation mediated by interactions with TFII-I". Nature. 365 (6444): 359–61. doi:10.1038/365359a0. PMID 8377829.
  • Yang W, Desiderio S (1997). "BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement". Proc. Natl. Acad. Sci. U.S.A. 94 (2): 604–9. PMID 9012831.
  • Grueneberg DA, Henry RW, Brauer A; et al. (1997). "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I". Genes Dev. 11 (19): 2482–93. PMID 9334314.
  • Roy AL, Du H, Gregor PD; et al. (1998). "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1". EMBO J. 16 (23): 7091–104. doi:10.1093/emboj/16.23.7091. PMID 9384587.
  • Pérez Jurado LA, Wang YK, Peoples R; et al. (1998). "A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, a phosphorylation target of BTK". Hum. Mol. Genet. 7 (3): 325–34. PMID 9466987.
  • Kim DW, Cheriyath V, Roy AL, Cochran BH (1998). "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Mol. Cell. Biol. 18 (6): 3310–20. PMID 9584171.
  • Cheriyath V, Novina CD, Roy AL (1998). "TFII-I regulates Vbeta promoter activity through an initiator element". Mol. Cell. Biol. 18 (8): 4444–54. PMID 9671454.
  • Novina CD, Cheriyath V, Roy AL (1999). "Regulation of TFII-I activity by phosphorylation". J. Biol. Chem. 273 (50): 33443–8. PMID 9837922.
  • Novina CD, Kumar S, Bajpai U; et al. (1999). "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase". Mol. Cell. Biol. 19 (7): 5014–24. PMID 10373551.
  • Kim DW, Cochran BH (2000). "Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter". Mol. Cell. Biol. 20 (4): 1140–8. PMID 10648599.
  • Cheriyath V, Roy AL (2000). "Alternatively spliced isoforms of TFII-I. Complex formation, nuclear translocation, and differential gene regulation". J. Biol. Chem. 275 (34): 26300–8. doi:10.1074/jbc.M002980200. PMID 10854432.
  • Parker R, Phan T, Baumeister P; et al. (2001). "Identification of TFII-I as the endoplasmic reticulum stress response element binding factor ERSF: its autoregulation by stress and interaction with ATF6". Mol. Cell. Biol. 21 (9): 3220–33. doi:10.1128/MCB.21.9.3220-3233.2001. PMID 11287625.
  • Kim DW, Cochran BH (2001). "JAK2 activates TFII-I and regulates its interaction with extracellular signal-regulated kinase". Mol. Cell. Biol. 21 (10): 3387–97. doi:10.1128/MCB.21.10.3387-3397.2000. PMID 11313464.
  • Egloff AM, Desiderio S (2001). "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I". J. Biol. Chem. 276 (30): 27806–15. doi:10.1074/jbc.M103692200. PMID 11373296.
  • Cheriyath V, Desgranges ZP, Roy AL (2002). "c-Src-dependent transcriptional activation of TFII-I". J. Biol. Chem. 277 (25): 22798–805. doi:10.1074/jbc.M202956200. PMID 11934902.
  • Casteel DE, Zhuang S, Gudi T; et al. (2002). "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I". J. Biol. Chem. 277 (35): 32003–14. doi:10.1074/jbc.M112332200. PMID 12082086.
  • Tussie-Luna MI, Michel B, Hakre S, Roy AL (2003). "The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta /Siz2 is a transcriptional cofactor for TFII-I". J. Biol. Chem. 277 (45): 43185–93. doi:10.1074/jbc.M207635200. PMID 12193603.
  • Tussié-Luna MI, Bayarsaihan D, Seto E; et al. (2002). "Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta". Proc. Natl. Acad. Sci. U.S.A. 99 (20): 12807–12. doi:10.1073/pnas.192464499. PMID 12239342.
  • Wen YD, Cress WD, Roy AL, Seto E (2003). "Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I". J. Biol. Chem. 278 (3): 1841–7. doi:10.1074/jbc.M206528200. PMID 12393887.

External links


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

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