Gtf2i

General transcription factor IIi

PDB rendering based on 1q60.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2D9B, 2DN4, 2ED2, 2EJE

Identifiers

Symbols

GTF2I; BAP135; BTKAP1; DIWS; GTFII-I; IB291; SPIN; TFII-I; WBS; WBSCR6

External IDs

OMIM: 601679 MGI: 1202722 HomoloGene: 7748 GeneCards: GTF2I Gene

Gene Ontology
Molecular function	• DNA binding • sequence-specific DNA binding transcription factor activity • protein binding • mitogen-activated protein kinase binding
Cellular component	• nucleus • nucleolus • cytoplasm • cell projection • neuronal cell body
Biological process	• regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • signal transduction • embryo development • negative regulation of angiogenesis
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 7:
74.07 – 74.18 Mb

Chr 5:
134.71 – 134.79 Mb

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]

1 Interactions
2 References
3 Further reading
4 External links

Interactions [link]

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.^[2]^[13]^[14]

References [link]

^ ^a ^b Grueneberg DA, Henry RW, Brauer A, Novina CD, Cheriyath V, Roy AL, Gilman M (November 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. DOI:10.1101/gad.11.19.2482. PMC 316568. PMID 9334314. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316568.
^ ^a ^b Yang W, Desiderio S (March 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. DOI:10.1073/pnas.94.2.604. PMC 19560. PMID 9012831. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=19560.
^ ^a ^b "Entrez Gene: GTF2I general transcription factor II, i". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2969.
^ Roy, A L; Du H, Gregor P D, Novina C D, Martinez E, Roeder R G (December 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. PMC 1170311. PMID 9384587. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170311.
^ Roy, A L; Meisterernst M, Pognonec P, Roeder R G (November 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.
^ Hakimi, Mohamed-Ali; Dong Yuanshu, Lane William S, Speicher David W, Shiekhattar Ramin (February 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.
^ ^a ^b Wen, Yu-Der; Cress W Douglas, Roy Ananda L, Seto Edward (January 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.
^ Casteel, Darren E; Zhuang Shunhui, Gudi Tanima, Tang Julian, Vuica Milena, Desiderio Stephen, Pilz Renate B (August 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.
^ Roy, A L; Carruthers C, Gutjahr T, Roeder R G (September 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.
^ Kim, D W; Cochran B H (February 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. DOI:10.1128/MCB.20.4.1140-1148.2000. ISSN 0270-7306. PMC 85232. PMID 10648599. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85232.
^ Tussié-Luna, María Isabel; Bayarsaihan Dashzeveg, Seto Edward, Ruddle Frank H, Roy Ananda L (October 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. PMC 130541. PMID 12239342. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=130541.
^ Kim, D W; Cheriyath V, Roy A L, Cochran B H (June 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. PMC 108912. PMID 9584171. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=108912.
^ Sacristán, Catarina; Tussié-Luna María Isabel, Logan Sheila M, Roy Ananda L (February 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.
^ Novina, C D; Kumar S, Bajpai U, Cheriyath V, Zhang K, Pillai S, Wortis H H, Roy A L (July 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. PMC 84330. PMID 10373551. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84330.

Further reading [link]

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. PMC 1170311. PMID 9384587. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170311.
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. PMC 108912. PMID 9584171. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=108912.
Cheriyath V, Novina CD, Roy AL (1998). "TFII-I regulates Vbeta promoter activity through an initiator element.". Mol. Cell. Biol. 18 (8): 4444–54. PMC 109030. PMID 9671454. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=109030.
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. PMC 84330. PMID 10373551. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84330.
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. PMC 85232. PMID 10648599. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85232.
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. PMC 86961. PMID 11287625. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86961.
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. PMC 100260. PMID 11313464. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=100260.
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. PMC 130541. PMID 12239342. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=130541.
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.

PDB gallery

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

2dn4: Solution Structure of RSGI RUH-060, a GTF2I domain in human cDNA

External links [link]

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.

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, JDP2, 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, L3) · NFIL3 · NRL · NRF (1, 2, 3) · XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLH (2, 9) · BMAL (ARNTL, ARNTL2) · CLOCK · EPAS1 · FIGLA · HAND (1, 2) · HES (5, 6) · HEY (1, 2, L) · HES1 · HIF (1A, 3A) · ID (1, 2, 3, 4) · LYL1 · MESP2 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) · Neurogenins (1, 2, 3) · NeuroD (1, 2) · NPAS (1, 2, 3) · OLIG (1, 2) · Pho4 · Scleraxis · SIM (1, 2) · TAL (1, 2) · Twist · USF1

(1.3) bHLH-ZIP	AP-4 · MAX · MITF · MNT · MLX · MXI1 · Myc · SREBP (1, 2)

(1.4) NF-1	NFI (A, B, C, X) · SMAD (R-SMAD (1, 2, 3, 5, 9) - I-SMAD (6, 7) - 4)

(1.5) RF-X	RFX (1, 2, 3, 4, 5, 6, ANK)

(1.6) Basic helix-span-helix (bHSH)	AP-2 (α, β, γ, δ, ε)

(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 (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ)) 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) · TRPS1

(2.3) Cys₂His₂	General transcription factors (TFIIA, TFIIB, TFIID, TFIIE (1, 2), TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2)) ATBF1 · BCL (6, 11A, 11B) · CTCF · E4F1 · EGR (1, 2, 3, 4) · ERV3 · GFI1 · GLI-Krüppel family (1, 2, 3, REST, S2, YY1) · HIC (1, 2) · HIVEP (1, 2, 3) · IKZF (1, 2, 3) · ILF (2, 3) · KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17) · MTF1 · MYT1 · OSR1 · PRDM9 · SALL (1, 2, 3, 4) · SP (1, 2, 4, 7, 8) · TSHZ3 · WT1 · Zbtb7 (7A, 7B) · ZBTB (11, 16, 17, 20, 32, 33, 40) · 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, 300, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 644, 649, 655)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE · DIDO1 · GRLF1 · ING (1, 2, 4) · JARID (1A, 1B, 1C, 1D, 2) · JMJD1B

(3) Helix-turn-helix domains

(3.1) Homeodomain	ARX · CDX (1, 2) · CRX · CUTL1 · DBX (1, 2) · DLX (3, 4, 5) · EMX (1, 2) · EN (1, 2) · FHL (1, 2, 3) · HESX1 · HHEX · HLX · Homeobox (A1, A2, 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, C12, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) · HOPX · IRX (1, 2, 3, 4, 5, 6, MKX) · LMX (1A, 1B) · MEIS (1, 2) · MEOX2 · MNX1 · MSX (1, 2) · NANOG · NKX (2-1, 2-2, 2-3, 2-5, 3-1, 3-2, 6-1, 6-2) · NOBOX · PBX (1, 2, 3) · PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) · PHOX (2A, 2B) · PITX (1, 2, 3) · POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX (1, 2) · PDX1 · SATB2 · SHOX2 · SIX (1, 2, 3, 4, 5) · VAX1 · ZEB (1, 2)

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) · FOX proteins (A1, A2, A3, C1, C2, D3, D4, E1, E3, F1, G1, H1, I1, J1, J2, K1, K2, L2, M1, N1, N3, O1, O3, O4, P1, P2, P3, P4)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (2, 4, 5) · EGF · ELK (1, 3, 4) · ERF · ETS (1, 2, ERG, SPIB) · 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, 3, 4)

(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	p53 · TBX (1, 2, 3, 5, 19, 21, 22, Brachyury, TBR1, TBR2) · TP63

(4.4) MADS box	Mef2 (A, B, C, D) · SRF

(4.6) TATA binding proteins	TBP · TBPL1

(4.7) High-mobility group	BBX · HMGB (1, 2, 3, 4) · HMGN (1, 2, 3, 4) · HNF (1A, 1B) · LEF1 · SOX (1, 2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21) · SRY · SSRP1 · TCF (3, 4) · TOX (1, 2, 3, 4)

(4.9) Grainyhead	TFCP2

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) · HBP1

(0.3) Pocket domain	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 · NFY (A, B, C) · Rho/Sigma

see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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