Biology:GTF2I
Generic protein structure example |
General transcription factor II-I is a protein that in humans is encoded by the GTF2I gene.[1][2][3]
Function
This gene encodes a multifunctional phosphoprotein, TFII-I, with roles in transcription and signal transduction. Haploinsuffiency (deletion of one copy) of the GTF2I gene is noted in Williams-Beuren syndrome, a multisystem developmental disorder caused by the deletion of contiguous genes at chromosome 7q11.23. It is duplicated in the 7q11.23 duplication syndrome.[4] 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 in humans.[3] A single gain-of-function point mutation in GTF2I is also found in certain Thymomas. Single nucleotide polymorphism (SNP) in GTF2I is correlated to autoimmune disorders.
Interactions
GTF2I has been shown to interact with:
- Bruton's tyrosine kinase,[2][5][6]
- HDAC3,[7][8]
- Histone deacetylase 2,[7][9]
- MAPK3,[10]
- Myc,[11]
- PRKG1,[12]
- Serum response factor[1][13] and
- USF1 (human gene).[14][15]
References
- ↑ 1.0 1.1 "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I". Genes & Development 11 (19): 2482–93. Oct 1997. doi:10.1101/gad.11.19.2482. PMID 9334314.
- ↑ 2.0 2.1 "BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement". Proceedings of the National Academy of Sciences of the United States of America 94 (2): 604–9. Jan 1997. doi:10.1073/pnas.94.2.604. PMID 9012831. Bibcode: 1997PNAS...94..604Y.
- ↑ 3.0 3.1 "Entrez Gene: GTF2I general transcription factor II, i". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2969.
- ↑ "Pathophysiology of TFII-I: Old Guard Wearing New Hats". Trends in Molecular Medicine 23 (6): 501–511. June 2017. doi:10.1016/j.molmed.2017.04.002. PMID 28461154.
- ↑ "Mechanism of Bruton's tyrosine kinase-mediated recruitment and regulation of TFII-I". The Journal of Biological Chemistry 279 (8): 7147–58. Feb 2004. doi:10.1074/jbc.M303724200. PMID 14623887.
- ↑ "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase". Molecular and Cellular Biology 19 (7): 5014–24. Jul 1999. doi:10.1128/mcb.19.7.5014. PMID 10373551.
- ↑ 7.0 7.1 "Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I". The Journal of Biological Chemistry 278 (3): 1841–7. Jan 2003. doi:10.1074/jbc.M206528200. PMID 12393887.
- ↑ "Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta". Proceedings of the National Academy of Sciences of the United States of America 99 (20): 12807–12. Oct 2002. doi:10.1073/pnas.192464499. PMID 12239342. Bibcode: 2002PNAS...9912807T.
- ↑ "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes". The Journal of Biological Chemistry 278 (9): 7234–9. Feb 2003. doi:10.1074/jbc.M208992200. PMID 12493763.
- ↑ "Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter". Molecular and Cellular Biology 20 (4): 1140–8. Feb 2000. doi:10.1128/mcb.20.4.1140-1148.2000. PMID 10648599.
- ↑ "Direct role for Myc in transcription initiation mediated by interactions with TFII-I". Nature 365 (6444): 359–61. Sep 1993. doi:10.1038/365359a0. PMID 8377829. Bibcode: 1993Natur.365..359R.
- ↑ "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I". The Journal of Biological Chemistry 277 (35): 32003–14. Aug 2002. doi:10.1074/jbc.M112332200. PMID 12082086.
- ↑ "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Molecular and Cellular Biology 18 (6): 3310–20. Jun 1998. doi:10.1128/mcb.18.6.3310. PMID 9584171.
- ↑ "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1". The EMBO Journal 16 (23): 7091–104. Dec 1997. doi:10.1093/emboj/16.23.7091. PMID 9384587.
- ↑ "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature 354 (6350): 245–8. Nov 1991. doi:10.1038/354245a0. PMID 1961251. Bibcode: 1991Natur.354..245R.
Further reading
- "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature 354 (6350): 245–8. Nov 1991. doi:10.1038/354245a0. PMID 1961251. Bibcode: 1991Natur.354..245R.
- "Direct role for Myc in transcription initiation mediated by interactions with TFII-I". Nature 365 (6444): 359–61. Sep 1993. doi:10.1038/365359a0. PMID 8377829. Bibcode: 1993Natur.365..359R.
- "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1". The EMBO Journal 16 (23): 7091–104. Dec 1997. doi:10.1093/emboj/16.23.7091. PMID 9384587.
- "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". Human Molecular Genetics 7 (3): 325–34. Mar 1998. doi:10.1093/hmg/7.3.325. PMID 9466987.
- "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Molecular and Cellular Biology 18 (6): 3310–20. Jun 1998. doi:10.1128/mcb.18.6.3310. PMID 9584171.
- "TFII-I regulates Vbeta promoter activity through an initiator element". Molecular and Cellular Biology 18 (8): 4444–54. Aug 1998. doi:10.1128/mcb.18.8.4444. PMID 9671454.
- "Regulation of TFII-I activity by phosphorylation". The Journal of Biological Chemistry 273 (50): 33443–8. Dec 1998. doi:10.1074/jbc.273.50.33443. PMID 9837922.
- "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase". Molecular and Cellular Biology 19 (7): 5014–24. Jul 1999. doi:10.1128/mcb.19.7.5014. PMID 10373551.
- "Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter". Molecular and Cellular Biology 20 (4): 1140–8. Feb 2000. doi:10.1128/MCB.20.4.1140-1148.2000. PMID 10648599.
- "Alternatively spliced isoforms of TFII-I. Complex formation, nuclear translocation, and differential gene regulation". The Journal of Biological Chemistry 275 (34): 26300–8. Aug 2000. doi:10.1074/jbc.M002980200. PMID 10854432.
- "Identification of TFII-I as the endoplasmic reticulum stress response element binding factor ERSF: its autoregulation by stress and interaction with ATF6". Molecular and Cellular Biology 21 (9): 3220–33. May 2001. doi:10.1128/MCB.21.9.3220-3233.2001. PMID 11287625.
- "JAK2 activates TFII-I and regulates its interaction with extracellular signal-regulated kinase". Molecular and Cellular Biology 21 (10): 3387–97. May 2001. doi:10.1128/MCB.21.10.3387-3397.2000. PMID 11313464.
- "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I". The Journal of Biological Chemistry 276 (30): 27806–15. Jul 2001. doi:10.1074/jbc.M103692200. PMID 11373296.
- "c-Src-dependent transcriptional activation of TFII-I". The Journal of Biological Chemistry 277 (25): 22798–805. Jun 2002. doi:10.1074/jbc.M202956200. PMID 11934902.
- "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I". The Journal of Biological Chemistry 277 (35): 32003–14. Aug 2002. doi:10.1074/jbc.M112332200. PMID 12082086.
- "The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta /Siz2 is a transcriptional cofactor for TFII-I". The Journal of Biological Chemistry 277 (45): 43185–93. Nov 2002. doi:10.1074/jbc.M207635200. PMID 12193603.
- "Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta". Proceedings of the National Academy of Sciences of the United States of America 99 (20): 12807–12. Oct 2002. doi:10.1073/pnas.192464499. PMID 12239342. Bibcode: 2002PNAS...9912807T.
- "Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I". The Journal of Biological Chemistry 278 (3): 1841–7. Jan 2003. doi:10.1074/jbc.M206528200. PMID 12393887.
External links
- GTF2I+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Original source: https://en.wikipedia.org/wiki/GTF2I.
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