GTF2I

Protein-coding gene in the species Homo sapiens
GTF2I
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2D9B, 2DN4, 2ED2, 2EJE

Identifiers
AliasesGTF2I, BAP135, BTKAP1, DIWS, GTFII-I, IB291, SPIN, TFII-I, WBS, WBSCR6, general transcription factor IIi
External IDsOMIM: 601679; MGI: 1202722; HomoloGene: 7748; GeneCards: GTF2I; OMA:GTF2I - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for GTF2I
Genomic location for GTF2I
Band7q11.23Start74,650,231 bp[1]
End74,760,692 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for GTF2I
Genomic location for GTF2I
Band5 G2|5 74.48 cMStart134,237,834 bp[2]
End134,314,760 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ganglionic eminence

  • epithelium of colon

  • sural nerve

  • ventricular zone

  • right uterine tube

  • right adrenal cortex

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • right ovary

  • body of pancreas
Top expressed in
  • utricle

  • spermatocyte

  • molar

  • primitive streak

  • vestibular sensory epithelium

  • superior surface of tongue

  • medullary collecting duct

  • renal corpuscle

  • retinal pigment epithelium

  • ciliary body
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • mitogen-activated protein kinase binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • DNA binding
  • DNA-binding transcription factor activity
Cellular component
  • neuronal cell body
  • cell projection
  • membrane
  • nucleus
  • cytoplasm
  • nucleoplasm
Biological process
  • negative regulation of angiogenesis
  • transcription, DNA-templated
  • transcription initiation from RNA polymerase II promoter
  • regulation of transcription, DNA-templated
  • signal transduction
  • negative regulation of cytosolic calcium ion concentration
  • transition between slow and fast fiber
  • regulation of transcription by RNA polymerase II
  • transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2969

14886

Ensembl

ENSG00000263001

ENSMUSG00000060261

UniProt

P78347

Q9ESZ8

RefSeq (mRNA)
NM_001163636
NM_001280800
NM_001518
NM_032999
NM_033000

NM_033001

NM_001080746
NM_001080747
NM_001080748
NM_001080749
NM_010365

NM_001359062
NM_001359063
NM_001359064
NM_001359065
NM_001359066
NM_001359067

RefSeq (protein)
NP_001157108
NP_001267729
NP_001509
NP_127492
NP_127493

NP_127494

NP_001074215
NP_001074216
NP_001074217
NP_001074218
NP_034495

NP_001345991
NP_001345992
NP_001345993
NP_001345994
NP_001345995
NP_001345996

Location (UCSC)Chr 7: 74.65 – 74.76 MbChr 5: 134.24 – 134.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

General transcription factor II-I is a protein that in humans is encoded by the GTF2I gene.[5][6][7]

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.[8] 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.[7] 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:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000263001 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000060261 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL, Gilman M (Oct 1997). "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. doi:10.1101/gad.11.19.2482. PMC 316568. PMID 9334314.
  6. ^ a b Yang W, Desiderio S (Jan 1997). "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. Bibcode:1997PNAS...94..604Y. doi:10.1073/pnas.94.2.604. PMC 19560. PMID 9012831.
  7. ^ a b "Entrez Gene: GTF2I general transcription factor II, i".
  8. ^ Roy AL (June 2017). "Pathophysiology of TFII-I: Old Guard Wearing New Hats". Trends in Molecular Medicine. 23 (6): 501–511. doi:10.1016/j.molmed.2017.04.002. PMC 5504908. PMID 28461154.
  9. ^ Sacristán C, Tussié-Luna MI, Logan SM, Roy AL (Feb 2004). "Mechanism of Bruton's tyrosine kinase-mediated recruitment and regulation of TFII-I". The Journal of Biological Chemistry. 279 (8): 7147–58. doi:10.1074/jbc.M303724200. PMID 14623887.
  10. ^ Novina CD, Kumar S, Bajpai U, Cheriyath V, Zhang K, Pillai S, Wortis HH, Roy AL (Jul 1999). "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase". Molecular and Cellular Biology. 19 (7): 5014–24. doi:10.1128/mcb.19.7.5014. PMC 84330. PMID 10373551.
  11. ^ a b Wen YD, Cress WD, Roy AL, Seto E (Jan 2003). "Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I". The Journal of Biological Chemistry. 278 (3): 1841–7. doi:10.1074/jbc.M206528200. PMID 12393887.
  12. ^ Tussié-Luna MI, Bayarsaihan D, Seto E, Ruddle FH, Roy AL (Oct 2002). "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. Bibcode:2002PNAS...9912807T. doi:10.1073/pnas.192464499. PMC 130541. PMID 12239342.
  13. ^ Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R (Feb 2003). "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. doi:10.1074/jbc.M208992200. PMID 12493763.
  14. ^ Kim DW, Cochran BH (Feb 2000). "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. doi:10.1128/mcb.20.4.1140-1148.2000. PMC 85232. PMID 10648599.
  15. ^ Roy AL, Carruthers C, Gutjahr T, Roeder RG (Sep 1993). "Direct role for Myc in transcription initiation mediated by interactions with TFII-I". Nature. 365 (6444): 359–61. Bibcode:1993Natur.365..359R. doi:10.1038/365359a0. PMID 8377829. S2CID 4354157.
  16. ^ Casteel DE, Zhuang S, Gudi T, Tang J, Vuica M, Desiderio S, Pilz RB (Aug 2002). "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. doi:10.1074/jbc.M112332200. PMID 12082086.
  17. ^ Kim DW, Cheriyath V, Roy AL, Cochran BH (Jun 1998). "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Molecular and Cellular Biology. 18 (6): 3310–20. doi:10.1128/mcb.18.6.3310. PMC 108912. PMID 9584171.
  18. ^ Roy AL, Du H, Gregor PD, Novina CD, Martinez E, Roeder RG (Dec 1997). "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. doi:10.1093/emboj/16.23.7091. PMC 1170311. PMID 9384587.
  19. ^ Roy AL, Meisterernst M, Pognonec P, Roeder RG (Nov 1991). "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature. 354 (6350): 245–8. Bibcode:1991Natur.354..245R. doi:10.1038/354245a0. PMID 1961251. S2CID 4260885.

Further reading

  • Roy AL, Meisterernst M, Pognonec P, Roeder RG (Nov 1991). "Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF". Nature. 354 (6350): 245–8. Bibcode:1991Natur.354..245R. doi:10.1038/354245a0. PMID 1961251. S2CID 4260885.
  • Roy AL, Carruthers C, Gutjahr T, Roeder RG (Sep 1993). "Direct role for Myc in transcription initiation mediated by interactions with TFII-I". Nature. 365 (6444): 359–61. Bibcode:1993Natur.365..359R. doi:10.1038/365359a0. PMID 8377829. S2CID 4354157.
  • Roy AL, Du H, Gregor PD, Novina CD, Martinez E, Roeder RG (Dec 1997). "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. doi:10.1093/emboj/16.23.7091. PMC 1170311. PMID 9384587.
  • Pérez Jurado LA, Wang YK, Peoples R, Coloma A, Cruces J, Francke U (Mar 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". Human Molecular Genetics. 7 (3): 325–34. doi:10.1093/hmg/7.3.325. PMID 9466987.
  • Kim DW, Cheriyath V, Roy AL, Cochran BH (Jun 1998). "TFII-I enhances activation of the c-fos promoter through interactions with upstream elements". Molecular and Cellular Biology. 18 (6): 3310–20. doi:10.1128/mcb.18.6.3310. PMC 108912. PMID 9584171.
  • Cheriyath V, Novina CD, Roy AL (Aug 1998). "TFII-I regulates Vbeta promoter activity through an initiator element". Molecular and Cellular Biology. 18 (8): 4444–54. doi:10.1128/mcb.18.8.4444. PMC 109030. PMID 9671454.
  • Novina CD, Cheriyath V, Roy AL (Dec 1998). "Regulation of TFII-I activity by phosphorylation". The Journal of Biological Chemistry. 273 (50): 33443–8. doi:10.1074/jbc.273.50.33443. PMID 9837922.
  • Novina CD, Kumar S, Bajpai U, Cheriyath V, Zhang K, Pillai S, Wortis HH, Roy AL (Jul 1999). "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase". Molecular and Cellular Biology. 19 (7): 5014–24. doi:10.1128/mcb.19.7.5014. PMC 84330. PMID 10373551.
  • Kim DW, Cochran BH (Feb 2000). "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. doi:10.1128/MCB.20.4.1140-1148.2000. PMC 85232. PMID 10648599.
  • Cheriyath V, Roy AL (Aug 2000). "Alternatively spliced isoforms of TFII-I. Complex formation, nuclear translocation, and differential gene regulation". The Journal of Biological Chemistry. 275 (34): 26300–8. doi:10.1074/jbc.M002980200. PMID 10854432.
  • Parker R, Phan T, Baumeister P, Roy B, Cheriyath V, Roy AL, Lee AS (May 2001). "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. doi:10.1128/MCB.21.9.3220-3233.2001. PMC 86961. PMID 11287625.
  • Kim DW, Cochran BH (May 2001). "JAK2 activates TFII-I and regulates its interaction with extracellular signal-regulated kinase". Molecular and Cellular Biology. 21 (10): 3387–97. doi:10.1128/MCB.21.10.3387-3397.2000. PMC 100260. PMID 11313464.
  • Egloff AM, Desiderio S (Jul 2001). "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. doi:10.1074/jbc.M103692200. PMID 11373296.
  • Cheriyath V, Desgranges ZP, Roy AL (Jun 2002). "c-Src-dependent transcriptional activation of TFII-I". The Journal of Biological Chemistry. 277 (25): 22798–805. doi:10.1074/jbc.M202956200. PMID 11934902.
  • Casteel DE, Zhuang S, Gudi T, Tang J, Vuica M, Desiderio S, Pilz RB (Aug 2002). "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. doi:10.1074/jbc.M112332200. PMID 12082086.
  • Tussie-Luna MI, Michel B, Hakre S, Roy AL (Nov 2002). "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. doi:10.1074/jbc.M207635200. PMID 12193603.
  • Tussié-Luna MI, Bayarsaihan D, Seto E, Ruddle FH, Roy AL (Oct 2002). "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. Bibcode:2002PNAS...9912807T. doi:10.1073/pnas.192464499. PMC 130541. PMID 12239342.
  • Wen YD, Cress WD, Roy AL, Seto E (Jan 2003). "Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I". The Journal of Biological Chemistry. 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.

  • v
  • t
  • e
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    1q60: Solution Structure of RSGI RUH-004, a GTF2I domain in Mouse cDNA
  • 2d9b: Solution Structure of RSGI RUH-052, a GTF2I domain in human cDNA
    2d9b: Solution Structure of RSGI RUH-052, a GTF2I domain in human cDNA
  • 2dn4: Solution Structure of RSGI RUH-060, a GTF2I domain in human cDNA
    2dn4: Solution Structure of RSGI RUH-060, a GTF2I domain in human cDNA
  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies