Hmdb loader
Survey
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP02299
Secondary Accession Numbers
  • 7784
Name Transcription factor Sp1
Synonyms Not Available
Gene Name SP1
Protein Type Unknown
Biological Properties
General Function Involved in zinc ion binding
Specific Function Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR- alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
zinc ion binding
nucleic acid binding
Cellular Location
  1. Nucleus
  2. Cytoplasm
Gene Properties
Chromosome Location Chromosome:1
Locus 12q13.1
SNPs SP1
Gene Sequence
>2358 bp
ATGAGCGACCAAGATCACTCCATGGATGAAATGACAGCTGTGGTGAAAATTGAAAAAGGA
GTTGGTGGCAATAATGGGGGCAATGGTAATGGTGGTGGTGCCTTTTCACAGGCTCGAAGT
AGCAGCACAGGCAGTAGCAGCAGCACTGGAGGAGGAGGGCAGGAGTCCCAGCCATCCCCT
TTGGCTCTGCTGGCAGCAACTTGCAGCAGAATTGAGTCACCCAATGAGAACAGCAACAAC
TCCCAGGGCCCGAGTCAGTCAGGGGGAACAGGTGAGCTTGACCTCACAGCCACACAACTT
TCACAGGGTGCCAATGGCTGGCAGATCATCTCTTCCTCCTCTGGGGCTACCCCTACCTCA
AAGGAACAGAGTGGCAGCAGTACCAATGGCAGCAATGGCAGTGAGTCTTCCAAGAATCGC
ACAGTCTCTGGTGGGCAGTATGTTGTGGCTGCCGCTCCCAACTTACAGAACCAGCAAGTT
CTGACAGGACTACCTGGAGTGATGCCTAATATTCAGTATCAAGTAATCCCACAGTTCCAG
ACCGTTGATGGGCAACAGCTGCAGTTTGCTGCCACTGGGGCCCAAGTGCAGCAGGATGGT
TCTGGTCAAATACAGATCATACCAGGTGCAAACCAACAGATTATCACAAATCGAGGAAGT
GGAGGCAACATCATTGCTGCTATGCCAAACCTACTCCAGCAGGCTGTCCCCCTCCAAGGC
CTGGCTAATAATGTACTCTCAGGACAGACTCAGTATGTGACCAATGTACCAGTGGCCCTG
AATGGGAACATCACCTTGCTACCTGTCAACAGCGTTTCTGCAGCTACCTTGACTCCCAGC
TCTCAGGCAGTCACGATCAGCAGCTCTGGGTCCCAGGAGAGTGGCTCACAGCCTGTCACC
TCAGGGACTACCATCAGTTCTGCCAGCTTGGTATCATCACAAGCCAGTTCCAGCTCCTTT
TTCACCAATGCCAATAGCTACTCAACTACTACTACCACCAGCAACATGGGAATTATGAAC
TTTACTACCAGTGGATCATCAGGGACCAACTCTCAAGGCCAGACACCCCAGAGGGTCAGT
GGGCTACAGGGGTCTGATGCTCTGAACATCCAGCAAAACCAGACATCTGGAGGCTCATTG
CAAGCAGGCCAGCAAAAAGAAGGAGAGCAAAACCAGCAGACACAGCAGCAACAAATTCTT
ATCCAGCCTCAGCTAGTTCAAGGGGGACAGGCCCTCCAGGCCCTCCAAGCAGCACCATTG
TCAGGGCAGACCTTTACAACTCAAGCCATCTCCCAGGAAACCCTCCAGAACCTCCAGCTT
CAGGCTGTTCCAAACTCTGGTCCCATCATCATCCGGACACCAACAGTGGGGCCCAATGGA
CAGGTCAGTTGGCAGACTCTACAGCTGCAGAACCTCCAAGTTCAGAACCCACAAGCCCAA
ACAATCACCTTAGCCCCAATGCAGGGTGTTTCCTTGGGGCAGACCAGCAGCAGCAACACC
ACTCTCACACCCATTGCCTCAGCTGCTTCCATTCCTGCTGGCACAGTCACTGTGAATGCT
GCTCAACTCTCCTCCATGCCAGGCCTCCAGACCATTAACCTCAGTGCATTGGGTACTTCA
GGAATCCAGGTGCACCCAATTCAAGGCCTGCCGTTGGCTATAGCAAATGCCCCAGGTGAT
CATGGAGCTCAGCTTGGTCTCCATGGGGCTGGTGGTGATGGAATACATGATGACACAGCA
GGTGGAGAGGAAGGAGAAAACAGCCCAGATGCCCAACCCCAAGCCGGTCGGAGGACCCGG
CGGGAAGCATGCACCTGCCCCTACTGTAAAGACAGTGAAGGAAGGGGCTCGGGGGATCCT
GGCAAAAAGAAACAGCATATTTGCCACATCCAAGGCTGTGGGAAAGTGTATGGCAAGACC
TCTCACCTGCGGGCACACTTGCGCTGGCATACAGGCGAGAGGCCATTTATGTGTACCTGG
TCATACTGTGGGAAACGCTTCACACGTTCGGATGAGCTACAGAGGCACAAACGTACACAC
ACAGGTGAGAAGAAATTTGCCTGCCCTGAGTGTCCTAAGCGCTTCATGAGGAGTGACCAC
CTGTCAAAACATATCAAGACCCACCAGAATAAGAAGGGAGGCCCAGGTGTAGCTCTGAGT
GTGGGCACTTTGCCCCTGGACAGTGGGGCAGGTTCAGAAGGCAGTGGCACTGCCACTCCT
TCAGCCCTTATTACCACCAATATGGTAGCCATGGAGGCCATCTGTCCAGAGGGCATTGCC
CGTCTTGCCAACAGTGGCATCAACGTCATGCAGGTGGCAGATCTGCAGTCCATTAATATC
AGTGGCAATGGCTTCTGA
Protein Properties
Number of Residues 785
Molecular Weight 80692.7
Theoretical pI 7.36
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Transcription factor Sp1
MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSP
LALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTS
KEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQ
TVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQG
LANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVT
SGTTISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTTSGSSGTNSQGQTPQRVS
GLQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPL
SGQTFTTQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQ
TITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTS
GIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAGGEEGENSPDAQPQAGRRTR
REACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCTW
SYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALS
VGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVADLQSINI
SGNGF
GenBank ID Protein 38372901
UniProtKB/Swiss-Prot ID P08047
UniProtKB/Swiss-Prot Entry Name SP1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_138473.2
GeneCard ID SP1
GenAtlas ID SP1
HGNC ID HGNC:11205
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  4. Hung JJ, Wang YT, Chang WC: Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription. Mol Cell Biol. 2006 Mar;26(5):1770-85. [PubMed:16478997 ]
  5. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  6. Ichimura T, Watanabe S, Sakamoto Y, Aoto T, Fujita N, Nakao M: Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins. J Biol Chem. 2005 Apr 8;280(14):13928-35. Epub 2005 Feb 2. [PubMed:15691849 ]
  7. Takahara T, Kanazu SI, Yanagisawa S, Akanuma H: Heterogeneous Sp1 mRNAs in human HepG2 cells include a product of homotypic trans-splicing. J Biol Chem. 2000 Dec 1;275(48):38067-72. [PubMed:10973950 ]
  8. Kadonaga JT, Carner KR, Masiarz FR, Tjian R: Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell. 1987 Dec 24;51(6):1079-90. [PubMed:3319186 ]
  9. Jackson SP, Tjian R: O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Cell. 1988 Oct 7;55(1):125-33. [PubMed:3139301 ]
  10. Courey AJ, Tjian R: Analysis of Sp1 in vivo reveals multiple transcriptional domains, including a novel glutamine-rich activation motif. Cell. 1988 Dec 2;55(5):887-98. [PubMed:3142690 ]
  11. Wang L, Mukherjee S, Jia F, Narayan O, Zhao LJ: Interaction of virion protein Vpr of human immunodeficiency virus type 1 with cellular transcription factor Sp1 and trans-activation of viral long terminal repeat. J Biol Chem. 1995 Oct 27;270(43):25564-9. [PubMed:7592727 ]
  12. Parks CL, Shenk T: The serotonin 1a receptor gene contains a TATA-less promoter that responds to MAZ and Sp1. J Biol Chem. 1996 Feb 23;271(8):4417-30. [PubMed:8626793 ]
  13. Roos MD, Su K, Baker JR, Kudlow JE: O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions. Mol Cell Biol. 1997 Nov;17(11):6472-80. [PubMed:9343410 ]
  14. Gordon-Shaag A, Ben-Nun-Shaul O, Kasamatsu H, Oppenheim AB, Oppenheim A: The SV40 capsid protein VP3 cooperates with the cellular transcription factor Sp1 in DNA-binding and in regulating viral promoter activity. J Mol Biol. 1998 Jan 16;275(2):187-95. [PubMed:9466902 ]
  15. Ding H, Benotmane AM, Suske G, Collen D, Belayew A: Functional interactions between Sp1 or Sp3 and the helicase-like transcription factor mediate basal expression from the human plasminogen activator inhibitor-1 gene. J Biol Chem. 1999 Jul 9;274(28):19573-80. [PubMed:10391891 ]
  16. Gunther M, Laithier M, Brison O: A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening. Mol Cell Biochem. 2000 Jul;210(1-2):131-42. [PubMed:10976766 ]
  17. Yang X, Su K, Roos MD, Chang Q, Paterson AJ, Kudlow JE: O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6611-6. Epub 2001 May 22. [PubMed:11371615 ]
  18. Milanini-Mongiat J, Pouyssegur J, Pages G: Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelial growth factor gene transcription. J Biol Chem. 2002 Jun 7;277(23):20631-9. Epub 2002 Mar 19. [PubMed:11904305 ]
  19. Gordon-Shaag A, Ben-Nun-Shaul O, Roitman V, Yosef Y, Oppenheim A: Cellular transcription factor Sp1 recruits simian virus 40 capsid proteins to the viral packaging signal, ses. J Virol. 2002 Jun;76(12):5915-24. [PubMed:12021324 ]
  20. Di Padova M, Bruno T, De Nicola F, Iezzi S, D'Angelo C, Gallo R, Nicosia D, Corbi N, Biroccio A, Floridi A, Passananti C, Fanciulli M: Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter. J Biol Chem. 2003 Sep 19;278(38):36496-504. Epub 2003 Jul 7. [PubMed:12847090 ]
  21. Peng H, He H, Hay J, Ruyechan WT: Interaction between the varicella zoster virus IE62 major transactivator and cellular transcription factor Sp1. J Biol Chem. 2003 Sep 26;278(39):38068-75. Epub 2003 Jul 10. [PubMed:12855699 ]
  22. Bonello MR, Khachigian LM: Fibroblast growth factor-2 represses platelet-derived growth factor receptor-alpha (PDGFR-alpha) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-alpha promoter. J Biol Chem. 2004 Jan 23;279(4):2377-82. Epub 2003 Oct 30. [PubMed:14593115 ]
  23. Majumdar G, Harrington A, Hungerford J, Martinez-Hernandez A, Gerling IC, Raghow R, Solomon S: Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells. J Biol Chem. 2006 Feb 10;281(6):3642-50. Epub 2005 Dec 6. [PubMed:16332679 ]
  24. Hsu MC, Chang HC, Hung WC: HER-2/neu represses the metastasis suppressor RECK via ERK and Sp transcription factors to promote cell invasion. J Biol Chem. 2006 Feb 24;281(8):4718-25. Epub 2005 Dec 23. [PubMed:16377629 ]
  25. Spengler ML, Brattain MG: Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription. J Biol Chem. 2006 Mar 3;281(9):5567-74. Epub 2006 Jan 5. [PubMed:16407261 ]
  26. Vicart A, Lefebvre T, Imbert J, Fernandez A, Kahn-Perles B: Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations. J Mol Biol. 2006 Dec 15;364(5):897-908. Epub 2006 Sep 16. [PubMed:17049555 ]
  27. Zhang Y, Liao M, Dufau ML: Phosphatidylinositol 3-kinase/protein kinase Czeta-induced phosphorylation of Sp1 and p107 repressor release have a critical role in histone deacetylase inhibitor-mediated derepression [corrected] of transcription of the luteinizing hormone receptor gene. Mol Cell Biol. 2006 Sep;26(18):6748-61. [PubMed:16943418 ]
  28. Olofsson BA, Kelly CM, Kim J, Hornsby SM, Azizkhan-Clifford J: Phosphorylation of Sp1 in response to DNA damage by ataxia telangiectasia-mutated kinase. Mol Cancer Res. 2007 Dec;5(12):1319-30. doi: 10.1158/1541-7786.MCR-07-0374. [PubMed:18171990 ]
  29. Chung SS, Kim JH, Park HS, Choi HH, Lee KW, Cho YM, Lee HK, Park KS: Activation of PPARgamma negatively regulates O-GlcNAcylation of Sp1. Biochem Biophys Res Commun. 2008 Aug 8;372(4):713-8. doi: 10.1016/j.bbrc.2008.05.096. Epub 2008 May 28. [PubMed:18513490 ]
  30. Spengler ML, Guo LW, Brattain MG: Phosphorylation mediates Sp1 coupled activities of proteolytic processing, desumoylation and degradation. Cell Cycle. 2008 Mar 1;7(5):623-30. Epub 2007 Dec 4. [PubMed:18239466 ]
  31. Iwahori S, Yasui Y, Kudoh A, Sato Y, Nakayama S, Murata T, Isomura H, Tsurumi T: Identification of phosphorylation sites on transcription factor Sp1 in response to DNA damage and its accumulation at damaged sites. Cell Signal. 2008 Oct;20(10):1795-803. doi: 10.1016/j.cellsig.2008.06.007. Epub 2008 Jun 19. [PubMed:18619531 ]
  32. Tan NY, Midgley VC, Kavurma MM, Santiago FS, Luo X, Peden R, Fahmy RG, Berndt MC, Molloy MP, Khachigian LM: Angiotensin II-inducible platelet-derived growth factor-D transcription requires specific Ser/Thr residues in the second zinc finger region of Sp1. Circ Res. 2008 Feb 29;102(4):e38-51. doi: 10.1161/CIRCRESAHA.107.167395. Epub 2008 Feb 7. [PubMed:18258854 ]
  33. Chuang JY, Wang YT, Yeh SH, Liu YW, Chang WC, Hung JJ: Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the stability of transcription factor Sp1 during mitosis. Mol Biol Cell. 2008 Mar;19(3):1139-51. doi: 10.1091/mbc.E07-09-0881. Epub 2008 Jan 16. [PubMed:18199680 ]
  34. Lim K, Chang HI: O-GlcNAc inhibits interaction between Sp1 and Elf-1 transcription factors. Biochem Biophys Res Commun. 2009 Mar 13;380(3):569-74. doi: 10.1016/j.bbrc.2009.01.121. Epub 2009 Jan 25. [PubMed:19285002 ]
  35. Lim K, Chang HI: O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y. Biochem Biophys Res Commun. 2009 May 8;382(3):593-7. doi: 10.1016/j.bbrc.2009.03.075. Epub 2009 Mar 18. [PubMed:19302979 ]
  36. Jochmann R, Thurau M, Jung S, Hofmann C, Naschberger E, Kremmer E, Harrer T, Miller M, Schaft N, Sturzl M: O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter. J Virol. 2009 Apr;83(8):3704-18. doi: 10.1128/JVI.01384-08. Epub 2009 Feb 4. [PubMed:19193796 ]
  37. Bierne H, Tham TN, Batsche E, Dumay A, Leguillou M, Kerneis-Golsteyn S, Regnault B, Seeler JS, Muchardt C, Feunteun J, Cossart P: Human BAHD1 promotes heterochromatic gene silencing. Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13826-31. doi: 10.1073/pnas.0901259106. Epub 2009 Aug 3. [PubMed:19666599 ]
  38. Yu HT, Chan WW, Chai KH, Lee CW, Chang RC, Yu MS, McLoughlin DM, Miller CC, Lau KF: Transcriptional regulation of human FE65, a ligand of Alzheimer's disease amyloid precursor protein, by Sp1. J Cell Biochem. 2010 Mar 1;109(4):782-93. doi: 10.1002/jcb.22457. [PubMed:20091743 ]
  39. Narayan VA, Kriwacki RW, Caradonna JP: Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition. J Biol Chem. 1997 Mar 21;272(12):7801-9. [PubMed:9065444 ]