GTF3A

Protein-coding gene in the species Homo sapiens
GTF3A
Identifiers
AliasesGTF3A, AP2, TFIIIA, general transcription factor IIIA
External IDsOMIM: 600860 MGI: 1913846 HomoloGene: 55630 GeneCards: GTF3A
Gene location (Human)
Chromosome 13 (human)
Chr.Chromosome 13 (human)[1]
Chromosome 13 (human)
Genomic location for GTF3A
Genomic location for GTF3A
Band13q12.2Start27,424,619 bp[1]
End27,435,823 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for GTF3A
Genomic location for GTF3A
Band5|5 G3Start146,885,467 bp[2]
End146,892,424 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • parotid gland

  • right ventricle

  • middle temporal gyrus

  • biceps brachii

  • thoracic diaphragm

  • palpebral conjunctiva

  • body of tongue

  • gastrocnemius muscle

  • left ventricle

  • triceps brachii muscle
Top expressed in
  • otic placode

  • saccule

  • abdominal wall

  • primitive streak

  • neural tube

  • renal corpuscle

  • external carotid artery

  • internal carotid artery

  • medial ganglionic eminence

  • vas deferens
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • nucleic acid binding
  • DNA binding
  • metal ion binding
  • RNA binding
  • 5S rRNA binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • nucleus
  • nucleoplasm
Biological process
  • rRNA transcription
  • regulation of transcription, DNA-templated
  • transcription, DNA-templated
  • transcription by RNA polymerase III
  • ribosomal large subunit biogenesis
  • ribosome biogenesis
  • regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2971

66596

Ensembl

ENSG00000122034

ENSMUSG00000016503

UniProt

Q92664

Q8VHT7

RefSeq (mRNA)

NM_002097

NM_025652

RefSeq (protein)

NP_002088

NP_079928

Location (UCSC)Chr 13: 27.42 – 27.44 MbChr 5: 146.89 – 146.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription factor IIIA is a protein that in humans is encoded by the GTF3A gene.[5][6]

It was first purified and identified as the first mammalian gene-specific activator by Roeder in 1980,[7] and later characterized by Wolffe and Brown in 1988.

The TFIIIA in Xenopus was the first zinc finger protein discovered.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000122034 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016503 – 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. ^ Arakawa H, Nagase H, Hayashi N, Ogawa M, Nagata M, Fujiwara T, et al. (Jul 1995). "Molecular cloning, characterization, and chromosomal mapping of a novel human gene (GTF3A) that is highly homologous to Xenopus transcription factor IIIA". Cytogenetics and Cell Genetics. 70 (3–4): 235–8. doi:10.1159/000134041. PMID 7789179.
  6. ^ "Entrez Gene: GTF3A general transcription factor IIIA".
  7. ^ Engelke DR, Ng SY, Shastry BS, Roeder RG (Mar 1980). "Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes". Cell. 19 (3): 717–28. doi:10.1016/S0092-8674(80)80048-1. PMID 6153931. S2CID 23955175.
  8. ^ Bruno M, Mahgoub M, Macfarlan TS (December 2019). "The Arms Race Between KRAB-Zinc Finger Proteins and Endogenous Retroelements and Its Impact on Mammals". Annual Review of Genetics. 53 (1). Annual Reviews: 393–416. doi:10.1146/annurev-genet-112618-043717. PMID 31518518. S2CID 202572327.

Further reading

  • Engelke DR, Ng SY, Shastry BS, Roeder RG (Mar 1980). "Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes". Cell. 19 (3): 717–28. doi:10.1016/S0092-8674(80)80048-1. PMID 6153931. S2CID 23955175.
  • Murphy JE, Keen JH (May 1992). "Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia". The Journal of Biological Chemistry. 267 (15): 10850–5. doi:10.1016/S0021-9258(19)50096-5. PMID 1587861.
  • Seifart KH, Wang L, Waldschmidt R, Jahn D, Wingender E (January 1989). "Purification of human transcription factor IIIA and its interaction with a chemically synthesized gene encoding human 5 S rRNA". The Journal of Biological Chemistry. 264 (3): 1702–9. doi:10.1016/S0021-9258(18)94243-2. PMID 2912980.
  • Drew PD, Nagle JW, Canning RD, Ozato K, Biddison WE, Becker KG (July 1995). "Cloning and expression analysis of a human cDNA homologous to Xenopus TFIIIA". Gene. 159 (2): 215–8. doi:10.1016/0378-1119(95)00145-V. PMID 7622052.
  • Moorefield B, Roeder RG (August 1994). "Purification and characterization of human transcription factor IIIA". The Journal of Biological Chemistry. 269 (33): 20857–65. doi:10.1016/S0021-9258(17)31901-4. PMID 8063702.
  • Fridell RA, Fischer U, Lührmann R, Meyer BE, Meinkoth JL, Malim MH, Cullen BR (April 1996). "Amphibian transcription factor IIIA proteins contain a sequence element functionally equivalent to the nuclear export signal of human immunodeficiency virus type 1 Rev". Proceedings of the National Academy of Sciences of the United States of America. 93 (7): 2936–40. Bibcode:1996PNAS...93.2936F. doi:10.1073/pnas.93.7.2936. PMC 39738. PMID 8610146.
  • Oettel S, Härtel F, Kober I, Iben S, Seifart KH (June 1997). "Human transcription factors IIIC2 , IIIC1 and a novel component IIIC0 fulfil different aspects of DNA binding to various pol III genes". Nucleic Acids Research. 25 (12): 2440–7. doi:10.1093/nar/25.12.2440. PMC 146769. PMID 9171097.
  • Moreland RJ, Dresser ME, Rodgers JS, Roe BA, Conaway JW, Conaway RC, Hanas JS (May 2000). "Identification of a transcription factor IIIA-interacting protein". Nucleic Acids Research. 28 (9): 1986–93. doi:10.1093/nar/28.9.1986. PMC 103300. PMID 10756201.
  • Rao DS, Chang JC, Kumar PD, Mizukami I, Smithson GM, Bradley SV, et al. (November 2001). "Huntingtin interacting protein 1 Is a clathrin coat binding protein required for differentiation of late spermatogenic progenitors". Molecular and Cellular Biology. 21 (22): 7796–806. doi:10.1128/MCB.21.22.7796-7806.2001. PMC 99949. PMID 11604514.
  • Hanas JS, Hocker JR, Cheng YG, Lerner MR, Brackett DJ, Lightfoot SA, et al. (January 2002). "cDNA cloning, DNA binding, and evolution of mammalian transcription factor IIIA". Gene. 282 (1–2): 43–52. doi:10.1016/S0378-1119(01)00796-X. PMID 11814676.
  • Weser S, Riemann J, Seifart KH, Meissner W (May 2003). "Assembly and isolation of intermediate steps of transcription complexes formed on the human 5S rRNA gene". Nucleic Acids Research. 31 (9): 2408–16. doi:10.1093/nar/gkg345. PMC 154231. PMID 12711686.
  • Pellikainen JM, Ropponen KM, Kataja VV, Kellokoski JK, Eskelinen MJ, Kosma VM (November 2004). "Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis". Clinical Cancer Research. 10 (22): 7621–8. doi:10.1158/1078-0432.CCR-04-1061. PMID 15569994.
  • Paing MM, Johnston CA, Siderovski DP, Trejo J (April 2006). "Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization". Molecular and Cellular Biology. 26 (8): 3231–42. doi:10.1128/MCB.26.8.3231-3242.2006. PMC 1446942. PMID 16581796.
  • Yamashita A, Takada T, Nemoto K, Yamamoto G, Torii R (July 2006). "Transient suppression of PPARgamma directed ES cells into an osteoblastic lineage". FEBS Letters. 580 (17): 4121–5. doi:10.1016/j.febslet.2006.06.057. PMID 16828750. S2CID 84554520.
  • Schwartz B, Melnikova VO, Tellez C, Mourad-Zeidan A, Blehm K, Zhao YJ, et al. (June 2007). "Loss of AP-2alpha results in deregulation of E-cadherin and MMP-9 and an increase in tumorigenicity of colon cancer cells in vivo". Oncogene. 26 (28): 4049–58. doi:10.1038/sj.onc.1210193. PMID 17224907.

External links

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

  • v
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(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
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