Sp1 transcription factor

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Protein SP1 PDB 1sp1.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesSP1, entrez:6667, Sp1 transcription factor
External IDsOMIM: 189906 MGI: 98372 HomoloGene: 8276 GeneCards: SP1
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for SP1
Genomic location for SP1
Band12q13.13Start53,380,176 bp[1]
End53,416,446 bp[1]
RNA expression pattern
PBB GE SP1 214732 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 12: 53.38 – 53.42 MbChr 15: 102.41 – 102.44 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Transcription factor Sp1, also known as specificity protein 1* is a protein that in humans is encoded by the SP1 gene.[5]


The protein encoded by this gene is a zinc finger transcription factor that binds to GC-rich motifs of many promoters. The encoded protein is involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Post-translational modifications such as phosphorylation, acetylation, O-GlcNAcylation, and proteolytic processing significantly affect the activity of this protein, which can be an activator or a repressor.[5]

In the SV40 virus, Sp1 binds to the GC boxes in the regulatory region (RR) of the genome.


SP1 belongs to the Sp/KLF family of transcription factors. The protein is 785 amino acids long, with a molecular weight of 81 kDa. The SP1 transcription factor contains a zinc finger protein motif, by which it binds directly to DNA and enhances gene transcription. Its zinc fingers are of the Cys2/His2 type and bind the consensus sequence 5'-(G/T)GGGCGG(G/A)(G/A)(C/T)-3' (GC box element). Some 12,000 SP-1 binding sites are found in the human genome.[6]


Sp1 has been used as a control protein to compare with when studying the increase or decrease of the aryl hydrocarbon receptor and/or the estrogen receptor, since it binds to both and generally remains at a relatively constant level.[7]


Plicamycin, an antineoplastic antibiotic produced by Streptomyces plicatus, and Withaferin A, a steroidal lactone from Withania somnifera plant are known to inhibit Sp1 transcription factor.[8][9]

miR-375-5p microRNA significantly decreased expression of SP1 and YAP1 in colorectal cancer cells. SP1 and YAP1 mRNAs are direct targets of miR-375-5p.[10]


Sp1 transcription factor has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185591 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001280 - Ensembl, May 2017
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  6. ^ Zhang, Bosen; Song, Liwei; Cai, Jiali; Li, Lei; Xu, Hong; Li, Mengying; Wang, Jiamin; Shi, Minmin; Chen, Hao; Jia, Hao; Hou, Zhaoyuan (2019). "The LIM protein Ajuba/SP1 complex forms a feed forward loop to induce SP1 target genes and promote pancreatic cancer cell proliferation". Journal of Experimental & Clinical Cancer Research. 38 (1): 205. doi:10.1186/s13046-019-1203-2. ISSN 1756-9966. PMC 6525466. PMID 31101117.
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  9. ^ Prasanna KS, Shilpa P, Salimath BP (2009). "Withaferin A suppresses the expression of vascular endothelial growth factor in Ehrlich ascites tumor cells via Sp1 transcription" (PDF). Current Trends in Biotechnology and Pharmacy. 3 (2): 138–148.[permanent dead link]
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  21. ^ a b Zhang Y, Dufau ML (September 2002). "Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex". The Journal of Biological Chemistry. 277 (36): 33431–8. doi:10.1074/jbc.M204417200. PMID 12091390.
  22. ^ a b Sun JM, Chen HY, Moniwa M, Litchfield DW, Seto E, Davie JR (September 2002). "The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2". The Journal of Biological Chemistry. 277 (39): 35783–6. doi:10.1074/jbc.C200378200. PMID 12176973.
  23. ^ Won J, Yim J, Kim TK (October 2002). "Sp1 and Sp3 recruit histone deacetylase to repress transcription of human telomerase reverse transcriptase (hTERT) promoter in normal human somatic cells". The Journal of Biological Chemistry. 277 (41): 38230–8. doi:10.1074/jbc.M206064200. PMID 12151407.
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  25. ^ Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W (April 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes & Development. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
  26. ^ Li SH, Cheng AL, Zhou H, Lam S, Rao M, Li H, Li XJ (March 2002). "Interaction of Huntington disease protein with transcriptional activator Sp1". Molecular and Cellular Biology. 22 (5): 1277–87. doi:10.1128/MCB.22.5.1277-1287.2002. PMC 134707. PMID 11839795.
  27. ^ Botella LM, Sánchez-Elsner T, Sanz-Rodriguez F, Kojima S, Shimada J, Guerrero-Esteo M, et al. (December 2002). "Transcriptional activation of endoglin and transforming growth factor-beta signaling components by cooperative interaction between Sp1 and KLF6: their potential role in the response to vascular injury". Blood. 100 (12): 4001–10. doi:10.1182/blood.V100.12.4001. PMID 12433697.
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  29. ^ Park SY, Shin HM, Han TH (September 2002). "Synergistic interaction of MEF2D and Sp1 in activation of the CD14 promoter". Molecular Immunology. 39 (1–2): 25–30. doi:10.1016/S0161-5890(02)00055-X. PMID 12213324.
  30. ^ Shetty S, Takahashi T, Matsui H, Ayengar R, Raghow R (May 1999). "Transcriptional autorepression of Msx1 gene is mediated by interactions of Msx1 protein with a multi-protein transcriptional complex containing TATA-binding protein, Sp1 and cAMP-response-element-binding protein-binding protein (CBP/p300)". The Biochemical Journal. 339 ( Pt 3) (3): 751–8. doi:10.1042/0264-6021:3390751. PMC 1220213. PMID 10215616.
  31. ^ Biesiada E, Hamamori Y, Kedes L, Sartorelli V (April 1999). "Myogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoter". Molecular and Cellular Biology. 19 (4): 2577–84. doi:10.1128/mcb.19.4.2577. PMC 84050. PMID 10082523.
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Further reading[edit]

External links[edit]

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