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GTF2F1

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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; OMA:GTF2F1 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)
Chromosome 19 (human)Genomic location for GTF2F1Genomic location for GTF2F1
Band19p13.3Start6,379,572 bp
End6,393,981 bp
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)
Chromosome 17 (mouse)Genomic location for GTF2F1Genomic location for GTF2F1
Band17|17 DStart57,310,405 bp
End57,318,288 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Cerebellum

  • cerebellar cortex

  • cerebellar hemisphere

  • left testis

  • right hemisphere of cerebellum

  • right testis

  • left ovary

  • prefrontal cortex

  • anterior pituitary

  • superior frontal gyrus
Top expressed in
  • saccule

  • otic placode

  • otic vesicle

  • seminiferous tubule

  • neural layer of retina

  • tail of embryo

  • primitive streak

  • primary oocyte

  • yolk sac

  • genital tubercle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
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
Wikidata
View/Edit HumanView/Edit Mouse

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

Interactions

GTF2F1 has been shown to interact with:

See also

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000125651Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000002658Ensembl, 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. ^ 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. ^ 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. ^ 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

External links

PDB gallery
  • 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
Transcription factors and intracellular receptors
(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.

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