The Full Wiki

GTF2I: Wikis

Advertisements

Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.

Encyclopedia

From Wikipedia, the free encyclopedia

edit
General transcription factor II, i

PDB rendering based on 1q60.
Available structures
1q60, 2d9b, 2dn4
Identifiers
Symbols GTF2I; WBS; BAP-135; BAP135; BTKAP1; DIWS; IB291; SPIN; TFII-I; WBSCR6
External IDs OMIM601679 MGI1202722 HomoloGene7748 GeneCards: GTF2I Gene
Orthologs
Species Human Mouse
Entrez 2969 14886
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) XM_001130609 XM_903569
RefSeq (protein) XP_001130609 XP_908662
Location (UCSC) n/a n/a
PubMed search [1] [2]

General transcription factor II-I is a protein that in humans is encoded by the GTF2I gene.[1][2][3]

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.[3]

Contents

Interactions

GTF2I has been shown to interact with USF1 (human gene),[4][5] Histone deacetylase 2,[6][7] PRKG1,[8] Myc,[9] MAPK3,[10] HDAC3,[7][11] Serum response factor[1][12] and Bruton's tyrosine kinase.[13][14][2]

References

  1. ^ a b Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL, Gilman M (Nov 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.  
  2. ^ a b Yang W, Desiderio S (Mar 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.  
  3. ^ a b "Entrez Gene: GTF2I general transcription factor II, i". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2969.  
  4. ^ Roy, A L; Du H, Gregor P D, Novina C D, Martinez E, Roeder R G (Dec. 1997). "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1". EMBO J. (ENGLAND) 16 (23): 7091–104. doi:10.1093/emboj/16.23.7091. ISSN 0261-4189. PMID 9384587.  
  5. ^ Roy, A L; Meisterernst M, Pognonec P, Roeder R G (Nov. 1991). "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature (ENGLAND) 354 (6350): 245–8. doi:10.1038/354245a0. ISSN 0028-0836. PMID 1961251.  
  6. ^ Hakimi, Mohamed-Ali; Dong Yuanshu, Lane William S, Speicher David W, Shiekhattar Ramin (Feb. 2003). "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes". J. Biol. Chem. (United States) 278 (9): 7234–9. doi:10.1074/jbc.M208992200. ISSN 0021-9258. PMID 12493763.  
  7. ^ a b Wen, Yu-Der; Cress W Douglas, Roy Ananda L, Seto Edward (Jan. 2003). "Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I". J. Biol. Chem. (United States) 278 (3): 1841–7. doi:10.1074/jbc.M206528200. ISSN 0021-9258. PMID 12393887.  
  8. ^ Casteel, Darren E; Zhuang Shunhui, Gudi Tanima, Tang Julian, Vuica Milena, Desiderio Stephen, Pilz Renate B (Aug. 2002). "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I". J. Biol. Chem. (United States) 277 (35): 32003–14. doi:10.1074/jbc.M112332200. ISSN 0021-9258. PMID 12082086.  
  9. ^ Roy, A L; Carruthers C, Gutjahr T, Roeder R G (Sep. 1993). "Direct role for Myc in transcription initiation mediated by interactions with TFII-I". Nature (ENGLAND) 365 (6444): 359–61. doi:10.1038/365359a0. ISSN 0028-0836. PMID 8377829.  
  10. ^ Kim, D W; Cochran B H (Feb. 2000). "Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter". Mol. Cell. Biol. (UNITED STATES) 20 (4): 1140–8. ISSN 0270-7306. PMID 10648599.  
  11. ^ Tussié-Luna, María Isabel; Bayarsaihan Dashzeveg, Seto Edward, Ruddle Frank H, Roy Ananda L (Oct. 2002). "Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (20): 12807–12. doi:10.1073/pnas.192464499. ISSN 0027-8424. PMID 12239342.  
  12. ^ Kim, D W; Cheriyath V, Roy A L, Cochran B H (Jun. 1998). "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Mol. Cell. Biol. (UNITED STATES) 18 (6): 3310–20. ISSN 0270-7306. PMID 9584171.  
  13. ^ Sacristán, Catarina; Tussié-Luna María Isabel, Logan Sheila M, Roy Ananda L (Feb. 2004). "Mechanism of Bruton's tyrosine kinase-mediated recruitment and regulation of TFII-I". J. Biol. Chem. (United States) 279 (8): 7147–58. doi:10.1074/jbc.M303724200. ISSN 0021-9258. PMID 14623887.  
  14. ^ Novina, C D; Kumar S, Bajpai U, Cheriyath V, Zhang K, Pillai S, Wortis H H, Roy A L (Jul. 1999). "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase". Mol. Cell. Biol. (UNITED STATES) 19 (7): 5014–24. ISSN 0270-7306. PMID 10373551.  

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.  
  • 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. doi:10.1093/hmg/7.3.325. 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. doi:10.1074/jbc.273.50.33443. 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. doi:10.1128/MCB.20.4.1140-1148.2000. 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.

Advertisements

Advertisements






Got something to say? Make a comment.
Your name
Your email address
Message