GTF2F1

Protein-coding gene in the species Homo sapiens
GTF2F1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1F3U, 1I27, 1J2X, 1NHA, 1ONV, 2K7L, 5IY9, 5IYA, 5IYC, 5IYB, 5IY7, 5IY8, 5IYD, 5IY6

Identifiers
AliasesGTF2F1, general transcription factor IIF, polypeptide 1, 74kDa, BTF4, RAP74, TF2F1, TFIIF, general transcription factor IIF subunit 1
External IDsOMIM: 189968 MGI: 1923848 HomoloGene: 1585 GeneCards: GTF2F1
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for GTF2F1
Genomic location for GTF2F1
Band19p13.3Start6,379,572 bp[1]
End6,393,981 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for GTF2F1
Genomic location for GTF2F1
Band17|17 DStart57,310,405 bp[2]
End57,318,288 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cerebellum

  • cerebellar cortex

  • cerebellar hemisphere

  • prefrontal cortex

  • anterior pituitary

  • superior frontal gyrus

  • sural nerve

  • body of pancreas

  • ganglionic eminence

  • dorsolateral prefrontal cortex
Top expressed in
  • saccule

  • otic placode

  • seminiferous tubule

  • primitive streak

  • yolk sac

  • motor neuron

  • supraoptic nucleus

  • Paneth cell

  • lens

  • hair follicle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • DNA binding
  • transcription coactivator activity
  • transcription factor binding
  • protein binding
  • phosphatase activator activity
  • RNA binding
  • protein phosphatase binding
  • protein domain specific binding
  • RNA polymerase II general transcription initiation factor activity
  • promoter-specific chromatin binding
Cellular component
  • intracellular membrane-bounded organelle
  • nucleoplasm
  • transcription factor TFIIF complex
  • cell junction
  • transcription factor TFIID complex
  • nucleus
  • protein-containing complex
Biological process
  • mRNA splicing, via spliceosome
  • regulation of transcription, DNA-templated
  • transcription elongation from RNA polymerase II promoter
  • response to virus
  • 7-methylguanosine mRNA capping
  • transcription by RNA polymerase II
  • transcription, DNA-templated
  • positive regulation of viral transcription
  • transcription initiation from RNA polymerase II promoter
  • positive regulation of transcription elongation from RNA polymerase II promoter
  • positive regulation of transcription by RNA polymerase II
  • snRNA transcription by RNA polymerase II
  • fibroblast growth factor receptor signaling pathway
  • positive regulation of catalytic activity
  • RNA metabolic process
  • negative regulation of protein binding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2962

98053

Ensembl

ENSG00000125651

ENSMUSG00000002658

UniProt

P35269

Q3THK3

RefSeq (mRNA)

NM_002096

NM_133801

RefSeq (protein)

NP_002087

NP_598562

Location (UCSC)Chr 19: 6.38 – 6.39 MbChr 17: 57.31 – 57.32 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

General transcription factor IIF subunit 1 is a protein that in humans is encoded by the GTF2F1 gene.[5][6]

Interactions

GTF2F1 has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125651 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002658 – 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. ^ Finkelstein A, Kostrub CF, Li J, Chavez DP, Wang BQ, Fang SM, Greenblatt J, Burton ZF (March 1992). "A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II". Nature. 355 (6359): 464–7. Bibcode:1992Natur.355..464F. doi:10.1038/355464a0. PMID 1734284. S2CID 1241044.
  6. ^ "Entrez Gene: GTF2F1 general transcription factor IIF, polypeptide 1, 74kDa".
  7. ^ Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J (October 1998). "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. 273 (42): 27593–601. doi:10.1074/jbc.273.42.27593. PMID 9765293.
  8. ^ a b c d e f Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. Bibcode:1997PNAS...94.5605S. doi:10.1073/pnas.94.11.5605. PMC 20825. PMID 9159119.
  9. ^ Kim MK, Nikodem VM (October 1999). "hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation". Mol. Cell. Biol. 19 (10): 6833–44. doi:10.1128/MCB.19.10.6833. PMC 84680. PMID 10490622.
  10. ^ Suñé C, Hayashi T, Liu Y, Lane WS, Young RA, Garcia-Blanco MA (October 1997). "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription". Mol. Cell. Biol. 17 (10): 6029–39. doi:10.1128/MCB.17.10.6029. PMC 232452. PMID 9315662.
  11. ^ Cho H, Orphanides G, Sun X, Yang XJ, Ogryzko V, Lees E, Nakatani Y, Reinberg D (September 1998). "A human RNA polymerase II complex containing factors that modify chromatin structure". Mol. Cell. Biol. 18 (9): 5355–63. doi:10.1128/MCB.18.9.5355. PMC 109120. PMID 9710619.
  12. ^ Joliot V, Demma M, Prywes R (February 1995). "Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor". Nature. 373 (6515): 632–5. Bibcode:1995Natur.373..632J. doi:10.1038/373632a0. PMID 7854423. S2CID 47196160.
  13. ^ Zhu H, Joliot V, Prywes R (February 1994). "Role of transcription factor TFIIF in serum response factor-activated transcription". J. Biol. Chem. 269 (5): 3489–97. doi:10.1016/S0021-9258(17)41889-8. PMID 8106390.
  14. ^ Dikstein R, Ruppert S, Tjian R (March 1996). "TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74". Cell. 84 (5): 781–90. doi:10.1016/s0092-8674(00)81055-7. PMID 8625415. S2CID 18490534.
  15. ^ a b Ruppert S, Tjian R (November 1995). "Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation". Genes Dev. 9 (22): 2747–55. doi:10.1101/gad.9.22.2747. PMID 7590250.
  16. ^ Siegert JL, Robbins PD (January 1999). "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250". Mol. Cell. Biol. 19 (1): 846–54. doi:10.1128/MCB.19.1.846. PMC 83941. PMID 9858607.
  17. ^ a b Malik S, Guermah M, Roeder RG (March 1998). "A dynamic model for PC4 coactivator function in RNA polymerase II transcription". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2192–7. Bibcode:1998PNAS...95.2192M. doi:10.1073/pnas.95.5.2192. PMC 19292. PMID 9482861.
  18. ^ Fang SM, Burton ZF (May 1996). "RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding". J. Biol. Chem. 271 (20): 11703–9. doi:10.1074/jbc.271.20.11703. PMID 8662660.

Further reading

  • Kato H, Sumimoto H, Pognonec P, Chen CH, Rosen CA, Roeder RG (1992). "HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors". Genes Dev. 6 (4): 655–66. doi:10.1101/gad.6.4.655. PMID 1559613.
  • Aso T, Vasavada HA, Kawaguchi T, Germino FJ, Ganguly S, Kitajima S, Weissman SM, Yasukochi Y (1992). "Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF". Nature. 355 (6359): 461–4. Bibcode:1992Natur.355..461A. doi:10.1038/355461a0. PMID 1734283. S2CID 4312708.
  • Adams MD, Kerlavage AR, Fleischmann RD, Fuldner RA, Bult CJ, Lee NH, Kirkness EF, Weinstock KG, Gocayne JD, White O (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence". Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
  • Ruppert S, Tjian R (1995). "Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation". Genes Dev. 9 (22): 2747–55. doi:10.1101/gad.9.22.2747. PMID 7590250.
  • Hisatake K, Ohta T, Takada R, Guermah M, Horikoshi M, Nakatani Y, Roeder RG (1995). "Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8195–9. Bibcode:1995PNAS...92.8195H. doi:10.1073/pnas.92.18.8195. PMC 41123. PMID 7667268.
  • Joliot V, Demma M, Prywes R (1995). "Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor". Nature. 373 (6515): 632–5. Bibcode:1995Natur.373..632J. doi:10.1038/373632a0. PMID 7854423. S2CID 47196160.
  • Zhu H, Joliot V, Prywes R (1994). "Role of transcription factor TFIIF in serum response factor-activated transcription". J. Biol. Chem. 269 (5): 3489–97. doi:10.1016/S0021-9258(17)41889-8. PMID 8106390.
  • Yonaha M, Aso T, Kobayashi Y, Vasavada H, Yasukochi Y, Weissman SM, Kitajima S (1993). "Domain structure of a human general transcription initiation factor, TFIIF". Nucleic Acids Res. 21 (2): 273–9. doi:10.1093/nar/21.2.273. PMC 309103. PMID 8441635.
  • Aso T, Tsai P, Kawaguchi T, Menninger JC, Kitajima S, Yasukochi Y, Ward DC, Weissman SM (1993). "Assignment of the human GTF2F1 gene to chromosome 19p13.3". Genomics. 16 (1): 252–3. doi:10.1006/geno.1993.1168. PMID 8486367.
  • Dikstein R, Ruppert S, Tjian R (1996). "TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74". Cell. 84 (5): 781–90. doi:10.1016/S0092-8674(00)81055-7. PMID 8625415. S2CID 18490534.
  • Fang SM, Burton ZF (1996). "RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding". J. Biol. Chem. 271 (20): 11703–9. doi:10.1074/jbc.271.20.11703. PMID 8662660.
  • McEwan IJ, Dahlman-Wright K, Ford J, Wright AP (1996). "Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding". Biochemistry. 35 (29): 9584–93. doi:10.1021/bi960793v. PMID 8755740.
  • Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science. 274 (5287): 605–10. Bibcode:1996Sci...274..605Z. doi:10.1126/science.274.5287.605. PMID 8849451. S2CID 13266489.
  • Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain". Nature. 384 (6607): 375–8. Bibcode:1996Natur.384..375P. doi:10.1038/384375a0. PMID 8934526. S2CID 4278432.
  • Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Mol. Cell. Biol. 17 (4): 1817–23. doi:10.1128/mcb.17.4.1817. PMC 232028. PMID 9121429.
  • Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. Bibcode:1997PNAS...94.5605S. doi:10.1073/pnas.94.11.5605. PMC 20825. PMID 9159119.
  • McEwan IJ, Gustafsson J (1997). "Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF". Proc. Natl. Acad. Sci. U.S.A. 94 (16): 8485–90. Bibcode:1997PNAS...94.8485M. doi:10.1073/pnas.94.16.8485. PMC 22967. PMID 9238003.
  • Newberry EP, Latifi T, Battaile JT, Towler DA (1997). "Structure-function analysis of Msx2-mediated transcriptional suppression". Biochemistry. 36 (34): 10451–62. doi:10.1021/bi971008x. PMID 9265625.
  • O'Brien T, Tjian R (1998). "Functional analysis of the human TAFII250 N-terminal kinase domain". Mol. Cell. 1 (6): 905–11. doi:10.1016/S1097-2765(00)80089-1. PMID 9660973.

External links

  • v
  • t
  • e
  • 1f3u: CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF
    1f3u: CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF
  • 1i27: CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF THE RAP74 SUBUNIT OF HUMAN TRANSCRIPTION FACTOR IIF (TFIIF)
    1i27: CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF THE RAP74 SUBUNIT OF HUMAN TRANSCRIPTION FACTOR IIF (TFIIF)
  • 1j2x: Crystal structure of RAP74 C-terminal domain complexed with FCP1 C-terminal peptide
    1j2x: Crystal structure of RAP74 C-terminal domain complexed with FCP1 C-terminal peptide
  • 1nha: Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF
    1nha: Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF
  • 1onv: NMR Structure of a Complex Containing the TFIIF Subunit RAP74 and the RNAP II CTD Phosphatase FCP1
    1onv: NMR Structure of a Complex Containing the TFIIF Subunit RAP74 and the RNAP II CTD Phosphatase FCP1
  • 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

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