Sp1 transcription factor

Protein-coding gene in the species Homo sapiens

SP1

| Available structures

PDB| Ortholog search: PDBe RCSB
| List of PDB id codes

1SP1, 1SP2, 1VA1, 1VA2, 1VA3

Identifiers
Aliases| SP1, entrez:6667, Sp1 transcription factor
External IDs| OMIM: 189906 MGI: 98372 HomoloGene: 8276 GeneCards: SP1
| Gene location (Human)

Chr.| Chromosome 12 (human)[1]

Band| 12q13.13| Start| 53,380,176 bp[1]
End| 53,416,446 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 15 (mouse)[2]

Band| 15|15 F3| Start| 102,314,578 bp[2]
End| 102,344,839 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* nipple

* cancellous bone

* monocyte

* vulva

* lactiferous duct

* cardia

* thymus

* cavity of mouth

* Achilles tendon

* internal globus pallidus

| Top expressed in

* vas deferens

* conjunctival fornix

* internal carotid artery

* hair follicle

* ciliary body

* lacrimal gland

* external carotid artery

* cornea

* left colon

* right lung lobe

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* protein homodimerization activity
* HMG box domain binding
* transcription factor binding
* histone deacetylase binding
* metal ion binding
* transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding
* bHLH transcription factor binding
* protein C-terminus binding
* protein binding
* histone acetyltransferase binding
* nucleic acid binding
* sequence-specific DNA binding
* RNA polymerase II transcription regulatory region sequence-specific DNA binding
* DNA binding
* double-stranded DNA binding
* DNA-binding transcription activator activity, RNA polymerase II-specific
* DNA-binding transcription factor activity
* RNA polymerase II cis-regulatory region sequence-specific DNA binding
* core promoter sequence-specific DNA binding
* DNA-binding transcription factor activity, RNA polymerase II-specific
* cis-regulatory region sequence-specific DNA binding

Cellular component|

* cytoplasm
* nucleoplasm
* protein-DNA complex
* nucleus
* transcription repressor complex

Biological process|

* positive regulation of hydrogen sulfide biosynthetic process
* rhythmic process
* regulation of transcription by RNA polymerase II
* positive regulation of transcription, DNA-templated
* viral process
* regulation of transcription, DNA-templated
* transcription, DNA-templated
* snRNA transcription by RNA polymerase II
* cellular response to insulin stimulus
* positive regulation of transcription by RNA polymerase II
* regulation of cholesterol biosynthetic process
* positive regulation of gene expression
* positive regulation of blood vessel endothelial cell migration
* positive regulation of angiogenesis
* positive regulation of vascular endothelial cell proliferation
* response to hydroperoxide

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

6667

20683

Ensembl| |

ENSG00000185591

ENSMUSG00000001280

UniProt| |

P08047

O89090

RefSeq (mRNA)| |

NM_001251825
NM_003109
NM_138473

NM_013672

RefSeq (protein)| |

NP_001238754
NP_003100
NP_612482

NP_038700

Location (UCSC)| Chr 12: 53.38 – 53.42 Mb| Chr 15: 102.31 – 102.34 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

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

## Function[edit]

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.

## Structure[edit]

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 two glutamine-rich activation domains at its N-terminus that are believed to be necessary for promoter trans-activation.[6] SP1 most notably contains three zinc finger protein motifs at its C-terminus, by which it binds directly to DNA and allows for interaction of the protein with other transcriptional regulators. 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.[7]

## Applications[edit]

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.[8]

Recently, a putative promoter region in FTMT, and positive regulators {SP1, cAMP response element-binding protein (CREB), and Ying Yang 1 (YY1)] and negative regulators [GATA2, forkhead box protein A1 (FoxA1), and CCAAT enhancer-binding protein b (C/EBPb)] of FTMT transcription have been identified (Guaraldo et al, 2016).The effect of DFP on the DNA-binding activity of these regulators to the FTMT promoter was examined using chromatin immunoprecipitation (ChIP) assay. Among the regulators, only SP1 displayed significantly increased DNA- binding activity following DFP treatment in a dose-dependent manner. SP1 knockdown by siRNA abolished the DFP-induced increase in the mRNA levels of FTMT, indicating SP1-mediated regulation of FTMT expression in the presence of DFP. Treatment with Deferiprone increased the expression of cytoplasmic and nuclear SP1 with predominant localization in the nucleus.[9]

## Inhibitors[edit]

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.[10][11]

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.[12]

## Interactions[edit]

Sp1 transcription factor has been shown to interact with:

* AATF,[13]
* CEBPB,[14][15]
* COL1A1,[16]
* E2F1,[17][18][19]
* FOSL1,[20]
* GABPA,[21]
* HDAC1,[13][22][23][24]
* HDAC2,[23][24][25]
* HMGA1,[15]
* HCFC1,[26][27]
* HTT,[28]
* KLF6,[29]
* MEF2C,[30]
* MEF2D,[31]
* MSX1,[32]
* Myogenin,[33]
* POU2F1,[26][34]
* PPP1R13L,[35]
* PSMC5,[36][37]
* PML,[38]
* RELA,[39][40]
* SMAD3,[41][42]
* SUMO1,[36]
* SF1,[43]
* TAL1,[44]
* UBC.[36]
* WRN,[45]
* DDX3X

## References[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185591 \- Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001280 \- 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. ^ a b "Entrez Gene: Sp1 transcription factor".
6. ^ Li, Lin; He, Shihua; Sun, Jian-Min; Davie, James R (2004-08-01). "Gene regulation by Sp1 and Sp3". Biochemistry and Cell Biology. 82 (4): 460–471. doi:10.1139/o04-045. ISSN 0829-8211. PMID 15284899.
7. ^ Zhang B, Song L, Cai J, Li L, Xu H, Li M, et al. (May 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. PMC 6525466. PMID 31101117.
8. ^ Wormke M, Stoner M, Saville B, Walker K, Abdelrahim M, Burghardt R, Safe S (March 2003). "The aryl hydrocarbon receptor mediates degradation of estrogen receptor alpha through activation of proteasomes". Molecular and Cellular Biology. 23 (6): 1843–55. doi:10.1128/MCB.23.6.1843-1855.2003. PMC 149455. PMID 12612060.
9. ^ Hara Y, Yanatori I, Tanaka A, Kishi F, Lemasters JJ, Nishina S, et al. (November 2020). "Iron loss triggers mitophagy through induction of mitochondrial ferritin". EMBO Reports. 21 (11): e50202. doi:10.15252/embr.202050202. PMC 7645172. PMID 32975364.
10. ^ Choi ES, Nam JS, Jung JY, Cho NP, Cho SD (November 2014). "Modulation of specificity protein 1 by mithramycin A as a novel therapeutic strategy for cervical cancer". Scientific Reports. 4: 7162. Bibcode:2014NatSR...4E7162C. doi:10.1038/srep07162. PMC 4241519. PMID 25418289.
11. ^ 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]
12. ^ Xu X, Chen X, Xu M, Liu X, Pan B, Qin J, et al. (September 2019). "miR-375-3p suppresses tumorigenesis and partially reverses chemoresistance by targeting YAP1 and SP1 in colorectal cancer cells". Aging. 11 (18): 7357–7385. doi:10.18632/aging.102214. PMC 6781994. PMID 31543507.
13. ^ a b Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, et al. (September 2003). "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter". The Journal of Biological Chemistry. 278 (38): 36496–504. doi:10.1074/jbc.M306694200. PMID 12847090.
14. ^ Liu YW, Tseng HP, Chen LC, Chen BK, Chang WC (July 2003). "Functional cooperation of simian virus 40 promoter factor 1 and CCAAT/enhancer-binding protein beta and delta in lipopolysaccharide-induced gene activation of IL-10 in mouse macrophages". Journal of Immunology. 171 (2): 821–8. doi:10.4049/jimmunol.171.2.821. PMID 12847250.
15. ^ a b Foti D, Iuliano R, Chiefari E, Brunetti A (April 2003). "A nucleoprotein complex containing Sp1, C/EBP beta, and HMGI-Y controls human insulin receptor gene transcription". Molecular and Cellular Biology. 23 (8): 2720–32. doi:10.1128/MCB.23.8.2720-2732.2003. PMC 152545. PMID 12665574.
16. ^ Li L, Artlett CM, Jimenez SA, Hall DJ, Varga J (October 1995). "Positive regulation of human alpha 1 (I) collagen promoter activity by transcription factor Sp1". Gene. 164 (2): 229–34. doi:10.1016/0378-1119(95)00508-4. PMID 7590335.
17. ^ Lin SY, Black AR, Kostic D, Pajovic S, Hoover CN, Azizkhan JC (April 1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Molecular and Cellular Biology. 16 (4): 1668–75. doi:10.1128/mcb.16.4.1668. PMC 231153. PMID 8657142.
18. ^ Rotheneder H, Geymayer S, Haidweger E (November 1999). "Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter". Journal of Molecular Biology. 293 (5): 1005–15. doi:10.1006/jmbi.1999.3213. PMID 10547281.
19. ^ Karlseder J, Rotheneder H, Wintersberger E (April 1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Molecular and Cellular Biology. 16 (4): 1659–67. doi:10.1128/mcb.16.4.1659. PMC 231152. PMID 8657141.
20. ^ Evellin S, Galvagni F, Zippo A, Neri F, Orlandini M, Incarnato D, et al. (March 2013). "FOSL1 controls the assembly of endothelial cells into capillary tubes by direct repression of αv and β3 integrin transcription". Molecular and Cellular Biology. 33 (6): 1198–209. doi:10.1128/MCB.01054-12. PMC 3592019. PMID 23319049.
21. ^ Galvagni F, Capo S, Oliviero S (March 2001). "Sp1 and Sp3 physically interact and co-operate with GABP for the activation of the utrophin promoter". Journal of Molecular Biology. 306 (5): 985–96. doi:10.1006/jmbi.2000.4335. hdl:2318/141203. PMID 11237613. S2CID 29403871.
22. ^ Singh J, Murata K, Itahana Y, Desprez PY (March 2002). "Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex". Oncogene. 21 (12): 1812–22. doi:10.1038/sj.onc.1205252. PMID 11896613.
23. ^ 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.
24. ^ 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.
25. ^ 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.
26. ^ a b Gunther M, Laithier M, Brison O (July 2000). "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening". Molecular and Cellular Biochemistry. 210 (1–2): 131–42. doi:10.1023/A:1007177623283. PMID 10976766. S2CID 1339642.
27. ^ 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.
28. ^ 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.
29. ^ 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.
30. ^ Krainc D, Bai G, Okamoto S, Carles M, Kusiak JW, Brent RN, Lipton SA (October 1998). "Synergistic activation of the N-methyl-D-aspartate receptor subunit 1 promoter by myocyte enhancer factor 2C and Sp1". The Journal of Biological Chemistry. 273 (40): 26218–24. doi:10.1074/jbc.273.40.26218. PMID 9748305.
31. ^ 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.
32. ^ 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 (3): 751–8. doi:10.1042/0264-6021:3390751. PMC 1220213. PMID 10215616.
33. ^ 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.
34. ^ Ström AC, Forsberg M, Lillhager P, Westin G (June 1996). "The transcription factors Sp1 and Oct-1 interact physically to regulate human U2 snRNA gene expression". Nucleic Acids Research. 24 (11): 1981–6. doi:10.1093/nar/24.11.1981. PMC 145891. PMID 8668525.
35. ^ Takada N, Sanda T, Okamoto H, Yang JP, Asamitsu K, Sarol L, et al. (August 2002). "RelA-associated inhibitor blocks transcription of human immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1 actions". Journal of Virology. 76 (16): 8019–30. doi:10.1128/JVI.76.16.8019-8030.2002. PMC 155123. PMID 12134007.
36. ^ a b c Wang YT, Chuang JY, Shen MR, Yang WB, Chang WC, Hung JJ (July 2008). "Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process". Journal of Molecular Biology. 380 (5): 869–85. doi:10.1016/j.jmb.2008.05.043. PMID 18572193.
37. ^ Su K, Yang X, Roos MD, Paterson AJ, Kudlow JE (June 2000). "Human Sug1/p45 is involved in the proteasome-dependent degradation of Sp1". The Biochemical Journal. 348 (2): 281–9. doi:10.1042/0264-6021:3480281. PMC 1221064. PMID 10816420.
38. ^ Vallian S, Chin KV, Chang KS (December 1998). "The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter". Molecular and Cellular Biology. 18 (12): 7147–56. doi:10.1128/mcb.18.12.7147. PMC 109296. PMID 9819401.
39. ^ Kuang PP, Berk JL, Rishikof DC, Foster JA, Humphries DE, Ricupero DA, Goldstein RH (July 2002). "NF-kappaB induced by IL-1beta inhibits elastin transcription and myofibroblast phenotype". American Journal of Physiology. Cell Physiology. 283 (1): C58-65. doi:10.1152/ajpcell.00314.2001. PMID 12055073. S2CID 15753719.
40. ^ Sif S, Gilmore TD (November 1994). "Interaction of the v-Rel oncoprotein with cellular transcription factor Sp1". Journal of Virology. 68 (11): 7131–8. doi:10.1128/JVI.68.11.7131-7138.1994. PMC 237152. PMID 7933095.
41. ^ Botella LM, Sánchez-Elsner T, Rius C, Corbí A, Bernabéu C (September 2001). "Identification of a critical Sp1 site within the endoglin promoter and its involvement in the transforming growth factor-beta stimulation". The Journal of Biological Chemistry. 276 (37): 34486–94. doi:10.1074/jbc.M011611200. PMID 11432852.
42. ^ Poncelet AC, Schnaper HW (March 2001). "Sp1 and Smad proteins cooperate to mediate transforming growth factor-beta 1-induced alpha 2(I) collagen expression in human glomerular mesangial cells". The Journal of Biological Chemistry. 276 (10): 6983–92. doi:10.1074/jbc.M006442200. PMID 11114293.
43. ^ Sugawara T, Saito M, Fujimoto S (August 2000). "Sp1 and SF-1 interact and cooperate in the regulation of human steroidogenic acute regulatory protein gene expression". Endocrinology. 141 (8): 2895–903. doi:10.1210/endo.141.8.7602. PMID 10919277.
44. ^ Lécuyer E, Herblot S, Saint-Denis M, Martin R, Begley CG, Porcher C, et al. (October 2002). "The SCL complex regulates c-kit expression in hematopoietic cells through functional interaction with Sp1". Blood. 100 (7): 2430–40. doi:10.1182/blood-2002-02-0568. PMID 12239153.
45. ^ Yamabe Y, Shimamoto A, Goto M, Yokota J, Sugawara M, Furuichi Y (November 1998). "Sp1-mediated transcription of the Werner helicase gene is modulated by Rb and p53". Molecular and Cellular Biology. 18 (11): 6191–200. doi:10.1128/mcb.18.11.6191. PMC 109206. PMID 9774636.

## Further reading[edit]

* Dreier B, Beerli RR, Segal DJ, Flippin JD, Barbas CF (August 2001). "Development of zinc finger domains for recognition of the 5'-ANN-3' family of DNA sequences and their use in the construction of artificial transcription factors". The Journal of Biological Chemistry. 276 (31): 29466–78. doi:10.1074/jbc.M102604200. PMID 11340073.
* Tseng L, Gao J, Mazella J, Zhu HH, Lane B (September 1997). "Differentiation-dependent and cell-specific regulation of the hIGFBP-1 gene in human endometrium". Annals of the New York Academy of Sciences. 828 (1): 27–37. Bibcode:1997NYASA.828...27T. doi:10.1111/j.1749-6632.1997.tb48521.x. PMID 9329821. S2CID 1601677.
* Dyson N (August 1998). "The regulation of E2F by pRB-family proteins". Genes & Development. 12 (15): 2245–62. doi:10.1101/gad.12.15.2245. PMID 9694791.
* Zhang Y, Dufau ML (June 2003). "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes". The Journal of Steroid Biochemistry and Molecular Biology. 85 (2–5): 401–14. doi:10.1016/S0960-0760(03)00230-9. PMID 12943729. S2CID 28512341.
* Kino T, Pavlakis GN (April 2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1". DNA and Cell Biology. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377.
* Seelamgari A, Maddukuri A, Berro R, de la Fuente C, Kehn K, Deng L, et al. (September 2004). "Role of viral regulatory and accessory proteins in HIV-1 replication". Frontiers in Bioscience. 9 (1–3): 2388–413. doi:10.2741/1403. PMID 15353294.
* Le Rouzic E, Benichou S (February 2005). "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology. 2: 11. doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353.
* Kamine J, Chinnadurai G (June 1992). "Synergistic activation of the human immunodeficiency virus type 1 promoter by the viral Tat protein and cellular transcription factor Sp1". Journal of Virology. 66 (6): 3932–6. doi:10.1128/JVI.66.6.3932-3936.1992. PMC 241184. PMID 1583736.
* Szpirer J, Szpirer C, Riviere M, Levan G, Marynen P, Cassiman JJ, et al. (September 1991). "The Sp1 transcription factor gene (SP1) and the 1,25-dihydroxyvitamin D3 receptor gene (VDR) are colocalized on human chromosome arm 12q and rat chromosome 7". Genomics. 11 (1): 168–73. doi:10.1016/0888-7543(91)90114-T. PMID 1662663.
* Gumucio DL, Rood KL, Blanchard-McQuate KL, Gray TA, Saulino A, Collins FS (October 1991). "Interaction of Sp1 with the human gamma globin promoter: binding and transactivation of normal and mutant promoters". Blood. 78 (7): 1853–63. doi:10.1182/blood.V78.7.1853.1853. PMID 1912570.
* Kamine J, Subramanian T, Chinnadurai G (October 1991). "Sp1-dependent activation of a synthetic promoter by human immunodeficiency virus type 1 Tat protein". Proceedings of the National Academy of Sciences of the United States of America. 88 (19): 8510–4. Bibcode:1991PNAS...88.8510K. doi:10.1073/pnas.88.19.8510. PMC 52538. PMID 1924310.
* Courey AJ, Holtzman DA, Jackson SP, Tjian R (December 1989). "Synergistic activation by the glutamine-rich domains of human transcription factor Sp1". Cell. 59 (5): 827–36. doi:10.1016/0092-8674(89)90606-5. PMID 2512012. S2CID 2910480.
* Harrich D, Garcia J, Wu F, Mitsuyasu R, Gonazalez J, Gaynor R (June 1989). "Role of SP1-binding domains in in vivo transcriptional regulation of the human immunodeficiency virus type 1 long terminal repeat". Journal of Virology. 63 (6): 2585–91. doi:10.1128/JVI.63.6.2585-2591.1989. PMC 250732. PMID 2657100.
* Jackson SP, Tjian R (October 1988). "O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation". Cell. 55 (1): 125–33. doi:10.1016/0092-8674(88)90015-3. PMID 3139301. S2CID 42523965.
* Kadonaga JT, Carner KR, Masiarz FR, Tjian R (December 1987). "Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain". Cell. 51 (6): 1079–90. doi:10.1016/0092-8674(87)90594-0. PMID 3319186. S2CID 19383553.
* Zhang R, Min W, Sessa WC (June 1995). "Functional analysis of the human endothelial nitric oxide synthase promoter. Sp1 and GATA factors are necessary for basal transcription in endothelial cells". The Journal of Biological Chemistry. 270 (25): 15320–6. doi:10.1074/jbc.270.25.15320. PMID 7541039.
* Hagen G, Dennig J, Preiss A, Beato M, Suske G (October 1995). "Functional analyses of the transcription factor Sp4 reveal properties distinct from Sp1 and Sp3". The Journal of Biological Chemistry. 270 (42): 24989–94. doi:10.1074/jbc.270.42.24989. PMID 7559627.
* Datta PK, Raychaudhuri P, Bagchi S (October 1995). "Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription". Molecular and Cellular Biology. 15 (10): 5444–52. doi:10.1128/mcb.15.10.5444. PMC 230794. PMID 7565695.
* Wang L, Mukherjee S, Jia F, Narayan O, Zhao LJ (October 1995). "Interaction of virion protein Vpr of human immunodeficiency virus type 1 with cellular transcription factor Sp1 and trans-activation of viral long terminal repeat". The Journal of Biological Chemistry. 270 (43): 25564–9. doi:10.1074/jbc.270.43.25564. PMID 7592727.
* Howcroft TK, Palmer LA, Brown J, Rellahan B, Kashanchi F, Brady JN, Singer DS (July 1995). "HIV Tat represses transcription through Sp1-like elements in the basal promoter". Immunity. 3 (1): 127–38. doi:10.1016/1074-7613(95)90165-5. PMID 7621073.
* Ferrari N, Desmarais D, Royal A (July 1995). "Transcriptional activation of the neuronal peripherin-encoding gene depends on a G + C-rich element that binds Sp1 in vitro and in vivo". Gene. 159 (2): 159–65. doi:10.1016/0378-1119(95)00140-2. PMID 7622044.
* Tan NY, Midgley VC, Kavurma MM, Santiago FS, Luo X, Peden R, et al. (February 2008). "Angiotensin II-inducible platelet-derived growth factor-D transcription requires specific Ser/Thr residues in the second zinc finger region of Sp1". Circulation Research. 102 (4): e38-51. doi:10.1161/CIRCRESAHA.107.167395. PMID 18258854.

## External links[edit]

* Sp1+Transcription+Factor at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
* FactorBook SP1

* v
* t
* e

PDB gallery

* 1sp1: NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F3, MINIMIZED AVERAGE STRUCTURE

* 1sp2: NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F2, MINIMIZED AVERAGE STRUCTURE

* 1va1: Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 1)

* 1va2: Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 2)

* 1va3: Solution Structure of Transcription Factor Sp1 DNA Binding Domain (Zinc Finger 3)

* v
* t
* e

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
* GCN4
* 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)|

| Group A|

* AS-C
* ASCL1
* ASCL2
* ATOH1
* HAND
* 1
* 2
* MESP2
* Myogenic regulatory factors
* MyoD
* Myogenin
* MYF5
* MYF6
* NeuroD
* 1
* 2
* Neurogenins
* 1
* 2
* 3
* OLIG
* 1
* 2
* Paraxis
* TCF15
* Scleraxis
* SLC
* LYL1
* TAL
* 1
* 2
* Twist

|

Group B|

* FIGLA
* Myc
* c-Myc
* l-Myc
* n-Myc
* MXD4
* TCF4

Group C
bHLH-PAS|

* AhR
* AHRR
* ARNT
* ARNTL
* ARNTL2
* CLOCK
* HIF
* 1A
* EPAS1
* 3A
* NPAS
* 1
* 2
* 3
* PER
* 1
* 2
* 3
* Period
* SIM
* 1
* 2

Group D|

* BHLH
* 2
* 3
* 9
* Pho4
* ID
* 1
* 2
* 3
* 4

Group E|

* HES
* 1
* 2
* 3
* 4
* 5
* 6
* 7
* HEY
* 1
* 2
* L

Group F
bHLH-COE|

* EBF1

(1.3) bHLH-ZIP|

* AP-4
* MAX
* MXD1
* MXD3
* MITF
* MNT
* MLX
* MLXIPL
* MXI1
* Myc
* SREBP
* 1
* 2
* USF1

(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
* S1
* S2
* YY1
* HIC
* 1
* 2
* HIVEP
* 1
* 2
* 3
* IKZF
* 1
* 2
* 3
* ILF
* 2
* 3
* KLF
* 1
* 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
* 21
* 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
* 300
* 318
* 330
* 346
* 350
* 365
* 366
* 384
* 423
* 451
* 452
* 471
* 593
* 638
* 644
* 649
* 655
* 804A

(2.4) Cys6|

* HIVEP1

(2.5) Alternating composition|

* AIRE
* DIDO1
* GRLF1
* ING
* 1
* 2
* 4
* JARID
* 1A
* 1B
* 1C
* 1D
* 2
* JMJD1B

(2.6) WRKY|

* WRKY

(3) Helix-turn-helix domains

| (3.1) Homeodomain|

| Antennapedia
ANTP class|

| protoHOX
Hox-like|

* ParaHox
* Gsx
* 1
* 2
* Xlox
* PDX1
* Cdx
* 1
* 2
* 4
* extended Hox: Evx1
* Evx2
* MEOX1
* MEOX2
* 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
* GBX1
* GBX2
* MNX1

|

metaHOX
NK-like|

* BARHL1
* BARHL2
* BARX1
* BARX2
* BSX
* DBX
* 1
* 2
* DLX
* 1
* 2
* 3
* 4
* 5
* 6
* EMX
* 1
* 2
* EN
* 1
* 2
* HHEX
* HLX
* LBX1
* LBX2
* MSX
* 1
* 2
* NANOG
* NKX
* 2-1
* 2-2
* 2-3
* 2-5
* 3-1
* 3-2
* HMX1
* HMX2
* HMX3
* 6-1
* 6-2
* NATO
* TLX1
* TLX2
* TLX3
* VAX1
* VAX2

other|

* ARX
* CRX
* CUTL1
* FHL
* 1
* 2
* 3
* HESX1
* HOPX
* LMX
* 1A
* 1B
* NOBOX
* TALE
* IRX
* 1
* 2
* 3
* 4
* 5
* 6
* MKX
* MEIS
* 1
* 2
* PBX
* 1
* 2
* 3
* PKNOX
* 1
* 2
* SIX
* 1
* 2
* 3
* 4
* 5
* PHF
* 1
* 3
* 6
* 8
* 10
* 16
* 17
* 20
* 21A
* POU domain
* PIT-1
* BRN-3: A
* B
* C
* Octamer transcription factor: 1
* 2
* 3/4
* 6
* 7
* 11
* SATB2
* ZEB
* 1
* 2

(3.2) Paired box|

* PAX
* 1
* 2
* 3
* 4
* 5
* 6
* 7
* 8
* 9
* PRRX
* 1
* 2
* PROP1
* PHOX
* 2A
* 2B
* RAX
* SHOX
* SHOX2
* VSX1
* VSX2
* Bicoid
* GSC
* BICD2
* OTX
* 1
* 2
* PITX
* 1
* 2
* 3

(3.3) Fork head / winged helix|

* E2F
* 1
* 2
* 3
* 4
* 5
* FOX proteins
* A1
* A2
* A3
* B1
* B2
* C1
* C2
* D1
* D2
* D3
* D4
* D4L1
* D4L3
* D4L4
* D4L5
* D4L6
* E1
* E3
* F1
* F2
* G1
* H1
* I1
* I2
* I3
* J1
* J2
* J3
* K1
* K2
* L1
* L2
* M1
* N1
* N2
* N3
* N4
* O1
* O3
* O4
* O6
* P1
* P2
* P3
* P4
* Q1
* R1
* R2
* S1

(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-like|

* p53 p63 p73 family
* p53
* TP63
* p73
* TBX
* 1
* 2
* 3
* 5
* 19
* 21
* 22
* TBR1
* TBR2
* TFT
* MYRF

(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
* SOX
* 1
* 2
* 3
* 4
* 5
* 6
* 8
* 9
* 10
* 11
* 12
* 13
* 14
* 15
* 18
* 21
* SRY
* SSRP1
* TCF/LEF
* TCF
* 1
* 3
* 4
* LEF1
* 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

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