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Transcription factor Sp1

 SP1_HUMAN               Reviewed;         785 AA.
P08047; E4Z9M7; G5E9M8; Q86TN8; Q9H3Q5; Q9NR51; Q9NY21; Q9NYE7;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 3.
30-AUG-2017, entry version 216.
RecName: Full=Transcription factor Sp1;
Name=SP1; Synonyms=TSFP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=21798247; DOI=10.1016/j.bbrc.2011.07.047;
Infantino V., Convertini P., Iacobazzi F., Pisano I., Scarcia P.,
Iacobazzi V.;
"Identification of a novel Sp1 splice variant as a strong
transcriptional activator.";
Biochem. Biophys. Res. Commun. 412:86-91(2011).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-785 (ISOFORM 1).
TISSUE=Cervix carcinoma;
Haggart M.H., Ladurner A.G.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-558 (ISOFORM 1), AND
TRANS-SPLICING.
PubMed=10973950; DOI=10.1074/jbc.M002010200;
Takahara T., Kanazu S., Yanagisawa S., Akanuma H.;
"Heterogeneous Sp1 mRNAs in human HepG2 cells include a product of
homotypic trans-splicing.";
J. Biol. Chem. 275:38067-38072(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 90-785 (ISOFORM 1/2), AND PROTEIN
SEQUENCE OF 359-375 AND 670-675.
PubMed=3319186; DOI=10.1016/0092-8674(87)90594-0;
Kadonaga J.T., Carner K.R., Masiarz F.R., Tjian R.;
"Isolation of cDNA encoding transcription factor Sp1 and functional
analysis of the DNA binding domain.";
Cell 51:1079-1090(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-109 (ISOFORM 1).
Nicolas M., Noe V., Ciudad C.J.;
"Expression of transcription factor Sp1 mRNA in mammalian cells.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 1).
Handschug K., Huebner A.;
"Sequencing of the 5' end of human transcription factor SP1 mRNA.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[10]
GLYCOSYLATION.
PubMed=3139301; DOI=10.1016/0092-8674(88)90015-3;
Jackson S.P., Tjian R.;
"O-glycosylation of eukaryotic transcription factors: implications for
mechanisms of transcriptional regulation.";
Cell 55:125-133(1988).
[11]
TRANSACTIVATION DOMAINS.
PubMed=3142690; DOI=10.1016/0092-8674(88)90144-4;
Courey A.J., Tjian R.;
"Analysis of Sp1 in vivo reveals multiple transcriptional domains,
including a novel glutamine-rich activation motif.";
Cell 55:887-898(1988).
[12]
INTERACTION WITH HIV-1 VPR.
PubMed=7592727; DOI=10.1074/jbc.270.43.25564;
Wang L., Mukherjee S., Jia F., Narayan O., Zhao L.J.;
"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. 270:25564-25569(1995).
[13]
IDENTIFICATION OF SEROTONIN 1A RECEPTOR PROMOTER BINDING SITES.
PubMed=8626793; DOI=10.1074/jbc.271.8.4417;
Parks C.L., Shenk T.;
"The serotonin 1a receptor gene contains a TATA-less promoter that
responds to MAZ and Sp1.";
J. Biol. Chem. 271:4417-4430(1996).
[14]
GLYCOSYLATION AT SER-491, MUTAGENESIS OF SER-491, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=9343410; DOI=10.1128/MCB.17.11.6472;
Roos M.D., Su K., Baker J.R., Kudlow J.E.;
"O glycosylation of an Sp1-derived peptide blocks known Sp1 protein
interactions.";
Mol. Cell. Biol. 17:6472-6480(1997).
[15]
INTERACTION WITH SV40 VP2/3.
PubMed=9466902; DOI=10.1006/jmbi.1997.1461;
Gordon-Shaag A., Ben-Nun-Shaul O., Kasamatsu H., Oppenheim A.B.,
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. 275:187-195(1998).
[16]
FUNCTION, AND INTERACTION WITH HLTF.
PubMed=10391891; DOI=10.1074/jbc.274.28.19573;
Ding H., Benotmane A.M., 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. 274:19573-19580(1999).
[17]
INTERACTION WITH ATF7IP; PHC2; POGZ AND HCFC1.
TISSUE=Colon;
PubMed=10976766; DOI=10.1023/A:1007177623283;
Gunther M., Laithier M., Brison O.;
"A set of proteins interacting with transcription factor Sp1
identified in a two-hybrid screening.";
Mol. Cell. Biochem. 210:131-142(2000).
[18]
GLYCOSYLATION AT SER-491, FUNCTION, AND MUTAGENESIS OF SER-491.
PubMed=11371615; DOI=10.1073/pnas.111099998;
Yang X., Su K., Roos M.D., Chang Q., Paterson A.J., Kudlow J.E.;
"O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits
its transcriptional capability.";
Proc. Natl. Acad. Sci. U.S.A. 98:6611-6616(2001).
[19]
PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, AND MUTAGENESIS OF
THR-355; THR-453 AND THR-739.
PubMed=11904305; DOI=10.1074/jbc.M201753200;
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. 277:20631-20639(2002).
[20]
INTERACTION WITH SV40 VP1.
PubMed=12021324; DOI=10.1128/JVI.76.12.5915-5924.2002;
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. 76:5915-5924(2002).
[21]
INTERACTION WITH AATF.
PubMed=12847090; DOI=10.1074/jbc.M306694200;
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. 278:36496-36504(2003).
[22]
INTERACTION WITH VARICELLA-ZOSTER VIRUS IE62 PROTEIN.
PubMed=12855699; DOI=10.1074/jbc.M302259200;
Peng H., He H., Hay J., Ruyechan W.T.;
"Interaction between the varicella zoster virus IE62 major
transactivator and cellular transcription factor Sp1.";
J. Biol. Chem. 278:38068-38075(2003).
[23]
PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, AND MUTAGENESIS OF
THR-453 AND THR-739.
PubMed=14593115; DOI=10.1074/jbc.M308254200;
Bonello M.R., Khachigian L.M.;
"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. 279:2377-2382(2004).
[24]
INTERACTION WITH ATF7IP AND ATF7IP2.
PubMed=15691849; DOI=10.1074/jbc.M413654200;
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. 280:13928-13935(2005).
[25]
GLYCOSYLATION AT SER-612; THR-640; SER-641; SER-698 AND SER-702,
PHOSPHORYLATION, INDUCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=16332679; DOI=10.1074/jbc.M511223200;
Majumdar G., Harrington A., Hungerford J., Martinez-Hernandez A.,
Gerling I.C., 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. 281:3642-3650(2006).
[26]
PHOSPHORYLATION AT THR-453 AND THR-739, AND FUNCTION.
PubMed=16377629; DOI=10.1074/jbc.M510937200;
Hsu M.C., Chang H.C., Hung W.C.;
"HER-2/neu represses the metastasis suppressor RECK via ERK and Sp
transcription factors to promote cell invasion.";
J. Biol. Chem. 281:4718-4725(2006).
[27]
SUMOYLATION AT LYS-16, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
LYS-16; GLU-18 AND LYS-19.
PubMed=16407261; DOI=10.1074/jbc.M600035200;
Spengler M.L., Brattain M.G.;
"Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory
domain and inhibits Sp1-dependent transcription.";
J. Biol. Chem. 281:5567-5574(2006).
[28]
PHOSPHORYLATION AT SER-59 AND THR-681, DEPHOSPHORYLATION,
GLYCOSYLATION, FUNCTION, AND MUTAGENESIS OF SER-59; SER-220; THR-355;
THR-453; THR-651; THR-681 AND THR-739.
PubMed=17049555; DOI=10.1016/j.jmb.2006.09.036;
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. 364:897-908(2006).
[29]
ACETYLATION AT LYS-703, INTERACTION WITH HDAC1; EP300 AND JUN,
FUNCTION, AND MUTAGENESIS OF LYS-703.
PubMed=16478997; DOI=10.1128/MCB.26.5.1770-1785.2006;
Hung J.J., Wang Y.T., Chang W.C.;
"Sp1 deacetylation induced by phorbol ester recruits p300 to activate
12(S)-lipoxygenase gene transcription.";
Mol. Cell. Biol. 26:1770-1785(2006).
[30]
PHOSPHORYLATION AT SER-641, FUNCTION, AND MUTAGENESIS OF SER-641.
PubMed=16943418; DOI=10.1128/MCB.00560-06;
Zhang Y., Liao M., Dufau M.L.;
"Phosphatidylinositol 3-kinase/protein kinase Czeta-induced
phosphorylation of Sp1 and p107 repressor release have a critical role
in histone deacetylase inhibitor-mediated derepression of
transcription of the luteinizing hormone receptor gene.";
Mol. Cell. Biol. 26:6748-6761(2006).
[31]
ERRATUM.
Zhang Y., Liao M., Dufau M.L.;
Mol. Cell. Biol. 26:8214-8214(2006).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[33]
PHOSPHORYLATION AT SER-101, FUNCTION, AND MUTAGENESIS OF SER-101.
PubMed=18171990; DOI=10.1158/1541-7786.MCR-07-0374;
Olofsson B.A., Kelly C.M., Kim J., Hornsby S.M., Azizkhan-Clifford J.;
"Phosphorylation of Sp1 in response to DNA damage by ataxia
telangiectasia-mutated kinase.";
Mol. Cancer Res. 5:1319-1330(2007).
[34]
GLYCOSYLATION, FUNCTION, AND MUTAGENESIS OF SER-612; THR-640; SER-641;
SER-698 AND SER-702.
PubMed=18513490; DOI=10.1016/j.bbrc.2008.05.096;
Chung S.S., Kim J.H., Park H.S., Choi H.H., Lee K.W., Cho Y.M.,
Lee H.K., Park K.S.;
"Activation of PPARgamma negatively regulates O-GlcNAcylation of
Sp1.";
Biochem. Biophys. Res. Commun. 372:713-718(2008).
[35]
PHOSPHORYLATION AT SER-7 AND SER-59, SUMOYLATION AT LYS-16,
PROTEOLYTIC PROCESSING, UBIQUITINATION, FUNCTION, AND MUTAGENESIS OF
SER-7; SER-59; SER-728 AND SER-732.
PubMed=18239466; DOI=10.4161/cc.7.5.5402;
Spengler M.L., Guo L.W., Brattain M.G.;
"Phosphorylation mediates Sp1 coupled activities of proteolytic
processing, desumoylation and degradation.";
Cell Cycle 7:623-630(2008).
[36]
PHOSPHORYLATION AT SER-101, FUNCTION, AND MUTAGENESIS OF SER-36;
SER-56; SER-81; SER-85; THR-98; SER-101; THR-250; SER-281; SER-291;
SER-296; SER-313; SER-351; THR-394; THR-427 AND SER-431.
PubMed=18619531; DOI=10.1016/j.cellsig.2008.06.007;
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. 20:1795-1803(2008).
[37]
PHOSPHORYLATION AT THR-668; SER-670 AND THR-681, AND MUTAGENESIS OF
THR-668; SER-670 AND THR-681.
PubMed=18258854; DOI=10.1161/CIRCRESAHA.107.167395;
Tan N.Y., Midgley V.C., Kavurma M.M., Santiago F.S., Luo X., Peden R.,
Fahmy R.G., Berndt M.C., Molloy M.P., Khachigian L.M.;
"Angiotensin II-inducible platelet-derived growth factor-D
transcription requires specific Ser/Thr residues in the second zinc
finger region of Sp1.";
Circ. Res. 102:38-51(2008).
[38]
PHOSPHORYLATION AT SER-59 AND THR-278, FUNCTION, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF SER-59; SER-73; THR-117; THR-278 AND THR-739.
PubMed=18199680; DOI=10.1091/mbc.E07-09-0881;
Chuang J.-Y., Wang Y.-T., Yeh S.-H., Liu Y.-W., Chang W.-C.,
Hung J.-J.;
"Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the
stability of transcription factor Sp1 during mitosis.";
Mol. Biol. Cell 19:1139-1151(2008).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-651, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[40]
GLYCOSYLATION, AND INTERACTION WITH ELF1.
PubMed=19285002; DOI=10.1016/j.bbrc.2009.01.121;
Lim K., Chang H.I.;
"O-GlcNAc inhibits interaction between Sp1 and Elf-1 transcription
factors.";
Biochem. Biophys. Res. Commun. 380:569-574(2009).
[41]
GLYCOSYLATION, AND INTERACTION WITH NFYA.
PubMed=19302979; DOI=10.1016/j.bbrc.2009.03.075;
Lim K., Chang H.I.;
"O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.";
Biochem. Biophys. Res. Commun. 382:593-597(2009).
[42]
INTERACTION WITH ATF7IP AND TBP.
PubMed=19106100; DOI=10.1074/jbc.M807098200;
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
Watanabe S., Saitoh N., Ito T., Nakao M.;
"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
telomerase activity.";
J. Biol. Chem. 284:5165-5174(2009).
[43]
GLYCOSYLATION, AND FUNCTION.
PubMed=19193796; DOI=10.1128/JVI.01384-08;
Jochmann R., Thurau M., Jung S., Hofmann C., Naschberger E.,
Kremmer E., Harrer T., Miller M., Schaft N., Stuerzl M.;
"O-linked N-acetylglucosaminylation of Sp1 inhibits the human
immunodeficiency virus type 1 promoter.";
J. Virol. 83:3704-3718(2009).
[44]
INTERACTION WITH BAHD1.
PubMed=19666599; DOI=10.1073/pnas.0901259106;
Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C.,
Feunteun J., Cossart P.;
"Human BAHD1 promotes heterochromatic gene silencing.";
Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
[45]
INTERACTION WITH EGR1.
PubMed=20121949; DOI=10.1111/j.1742-4658.2009.07553.x;
Hu C.T., Chang T.Y., Cheng C.C., Liu C.S., Wu J.R., Li M.C., Wu W.S.;
"Snail associates with EGR-1 and SP-1 to upregulate transcriptional
activation of p15INK4b.";
FEBS J. 277:1202-1218(2010).
[46]
FUNCTION.
PubMed=20091743; DOI=10.1002/jcb.22457;
Yu H.T., Chan W.W., Chai K.H., Lee C.W., Chang R.C., Yu M.S.,
McLoughlin D.M., Miller C.C., Lau K.F.;
"Transcriptional regulation of human FE65, a ligand of Alzheimer's
disease amyloid precursor protein, by Sp1.";
J. Cell. Biochem. 109:782-793(2010).
[47]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2 AND SER-7, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[49]
PHOSPHORYLATION AT SER-702.
PubMed=20953893; DOI=10.1007/s00018-010-0541-1;
Alemu E.A., Sjoettem E., Outzen H., Larsen K.B., Holm T.,
Bjoerkoey G., Johansen T.;
"Transforming growth factor-beta-inducible early response gene 1 is a
novel substrate for atypical protein kinase Cs.";
Cell. Mol. Life Sci. 68:1953-1968(2011).
[50]
INTERACTION WITH MEIS2 AND PBX1.
PubMed=21746878; DOI=10.1128/MCB.01456-10;
Bjerke G.A., Hyman-Walsh C., Wotton D.;
"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1.";
Mol. Cell. Biol. 31:3723-3733(2011).
[51]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-7 AND SER-59, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[53]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[54]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[55]
STRUCTURE BY NMR OF 654-684 AND 684-712.
PubMed=9065444; DOI=10.1074/jbc.272.12.7801;
Narayan V.A., Kriwacki R.W., Caradonna J.P.;
"Structures of zinc finger domains from transcription factor Sp1.
Insights into sequence-specific protein-DNA recognition.";
J. Biol. Chem. 272:7801-7809(1997).
-!- 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.
In complex with ATF7IP, maintains telomerase activity in cancer
cells by inducing TERT and TERC gene expression. Isoform 3 is a
stronger activator of transcription than isoform 1. Positively
regulates the transcription of the core clock component
ARNTL/BMAL1. {ECO:0000269|PubMed:10391891,
ECO:0000269|PubMed:11371615, ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629,
ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16943418,
ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990,
ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466,
ECO:0000269|PubMed:18513490, ECO:0000269|PubMed:18619531,
ECO:0000269|PubMed:19193796, ECO:0000269|PubMed:20091743,
ECO:0000269|PubMed:21798247}.
-!- SUBUNIT: Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF
and PHC2. Interacts with varicella-zoster virus IE62 protein.
Interacts with HIV-1 Vpr; the interaction is inhibited by SP1 O-
glycosylation. Interacts with SV40 VP2/3 proteins. Interacts with
SV40 major capsid protein VP1; this interaction leads to a
cooperativity between the 2 proteins in DNA binding. Interacts
with HLTF; the interaction may be required for basal
transcriptional activity of HLTF. Interacts (deacetylated form)
with EP300; the interaction enhances gene expression. Interacts
with HDAC1 and JUN. Interacts with ELF1; the interaction is
inhibited by glycosylation of SP1. Interaction with NFYA; the
interaction is inhibited by glycosylation of SP1. Interacts with
SMARCA4/BRG1 (By similarity). Interacts with ATF7IP and TBP.
Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a. Interacts
with EGR1. {ECO:0000250, ECO:0000269|PubMed:10391891,
ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:12021324,
ECO:0000269|PubMed:12847090, ECO:0000269|PubMed:12855699,
ECO:0000269|PubMed:15691849, ECO:0000269|PubMed:16478997,
ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:19285002,
ECO:0000269|PubMed:19302979, ECO:0000269|PubMed:19666599,
ECO:0000269|PubMed:20121949, ECO:0000269|PubMed:21746878,
ECO:0000269|PubMed:7592727, ECO:0000269|PubMed:9466902}.
-!- INTERACTION:
Q9NY61:AATF; NbExp=2; IntAct=EBI-298336, EBI-372428;
Q92988:DLX4; NbExp=4; IntAct=EBI-298336, EBI-1752755;
Q01094:E2F1; NbExp=2; IntAct=EBI-298336, EBI-448924;
P32519:ELF1; NbExp=2; IntAct=EBI-298336, EBI-765526;
Q99814:EPAS1; NbExp=2; IntAct=EBI-298336, EBI-447470;
P03372:ESR1; NbExp=2; IntAct=EBI-298336, EBI-78473;
P51610:HCFC1; NbExp=4; IntAct=EBI-298336, EBI-396176;
Q16665:HIF1A; NbExp=3; IntAct=EBI-298336, EBI-447269;
Q13118:KLF10; NbExp=2; IntAct=EBI-298336, EBI-1389509;
P01106:MYC; NbExp=4; IntAct=EBI-298336, EBI-447544;
P16333:NCK1; NbExp=2; IntAct=EBI-298336, EBI-389883;
P23708:Nfya (xeno); NbExp=18; IntAct=EBI-298336, EBI-862337;
Q8IXK0:PHC2; NbExp=2; IntAct=EBI-298336, EBI-713786;
Q7Z3K3:POGZ; NbExp=2; IntAct=EBI-298336, EBI-1389308;
P14859:POU2F1; NbExp=7; IntAct=EBI-298336, EBI-624770;
Q06455:RUNX1T1; NbExp=2; IntAct=EBI-298336, EBI-743342;
Q15459:SF3A1; NbExp=2; IntAct=EBI-298336, EBI-1054743;
Q13485:SMAD4; NbExp=2; IntAct=EBI-298336, EBI-347263;
Q12772:SREBF2; NbExp=3; IntAct=EBI-298336, EBI-465059;
P40763:STAT3; NbExp=4; IntAct=EBI-298336, EBI-518675;
Q8N680:ZBTB2; NbExp=4; IntAct=EBI-298336, EBI-2515601;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear location is
governed by glycosylated/phosphorylated states. Insulin promotes
nuclear location, while glucagon favors cytoplasmic location.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Sp1a;
IsoId=P08047-1; Sequence=Displayed;
Name=2; Synonyms=Sp1b;
IsoId=P08047-2; Sequence=VSP_053934;
Name=3; Synonyms=Sp1c;
IsoId=P08047-3; Sequence=VSP_053935;
-!- TISSUE SPECIFICITY: Up-regulated in adenocarcinomas of the stomach
(at protein level). Isoform 3 is ubiquitously expressed at low
levels. {ECO:0000269|PubMed:21798247}.
-!- INDUCTION: By insulin. {ECO:0000269|PubMed:16332679}.
-!- PTM: Phosphorylated on multiple serine and threonine residues.
Phosphorylation is coupled to ubiquitination, sumoylation and
proteolytic processing. Phosphorylation on Ser-59 enhances
proteolytic cleavage. Phosphorylation on Ser-7 enhances
ubiquitination and protein degradation. Hyperphosphorylation on
Ser-101 in response to DNA damage has no effect on transcriptional
activity. MAPK1/MAPK3-mediated phosphorylation on Thr-453 and Thr-
739 enhances VEGF transcription but, represses FGF2-triggered
PDGFR-alpha transcription. Also implicated in the repression of
RECK by ERBB2. Hyperphosphorylated on Thr-278 and Thr-739 during
mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-
dependent pathway. Phosphorylated in the zinc-finger domain by
calmodulin-activated PKCzeta. Phosphorylation on Ser-641 by
PKCzeta is critical for TSA-activated LHR gene expression through
release of its repressor, p107. Phosphorylation on Thr-668, Ser-
670 and Thr-681 is stimulated by angiotensin II via the AT1
receptor inducing increased binding to the PDGF-D promoter. This
phosphorylation is increased in injured artey wall. Ser-59 and
Thr-681 can both be dephosphorylated by PP2A during cell-cycle
interphase. Dephosphorylation on Ser-59 leads to increased
chromatin association during interphase and increases the
transcriptional activity. On insulin stimulation, sequentially
glycosylated and phosphorylated on several C-terminal serine and
threonine residues. {ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16332679,
ECO:0000269|PubMed:16377629, ECO:0000269|PubMed:16943418,
ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990,
ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466,
ECO:0000269|PubMed:18258854, ECO:0000269|PubMed:18619531}.
-!- PTM: Acetylated. Acetylation/deacetylation events affect
transcriptional activity. Deacetylation leads to an increase in
the expression the 12(s)-lipooxygenase gene though recruitment of
p300 to the promoter. {ECO:0000269|PubMed:16478997}.
-!- PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal
proteolytically-cleaved peptide and is triggered by
phosphorylation. {ECO:0000269|PubMed:18239466}.
-!- PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic
cleavage of the N-terminal repressor domain. Sumoylation levels
are attenuated during tumorigenesis. Phosphorylation mediates SP1
desumoylation.
-!- PTM: Proteolytic cleavage in the N-terminal repressor domain is
prevented by sumoylation. The C-terminal cleaved product is
susceptible to degradation.
-!- PTM: O-glycosylated; Contains 8 N-acetylglucosamine side chains.
Levels are controlled by insulin and the SP1 phosphorylation
states. Insulin-mediated O-glycosylation locates SP1 to the
nucleus, where it is sequentially deglycosylated and
phosphorylated. O-glycosylation affects transcriptional activity
through disrupting the interaction with a number of transcription
factors including ELF1 and NFYA. Also inhibits interaction with
the HIV1 promoter. Inhibited by peroxisomome proliferator receptor
gamma (PPARgamma).
-!- MISCELLANEOUS: In the hepatoma cell line Hep-G2, SP1 precursor
mRNA may undergo homotype trans-splicing leading to the
duplication of exons 2 and 3.
-!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH43224.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; FN908228; CBM42955.1; -; mRNA.
EMBL; AC068889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96699.1; -; Genomic_DNA.
EMBL; BC043224; AAH43224.1; ALT_INIT; mRNA.
EMBL; BC062539; AAH62539.1; -; mRNA.
EMBL; AF252284; AAF67726.1; -; mRNA.
EMBL; AB039286; BAB13476.1; -; Genomic_DNA.
EMBL; J03133; AAA61154.1; -; mRNA.
EMBL; AF255682; AAF78781.1; -; mRNA.
EMBL; AJ272134; CAB75345.1; -; mRNA.
CCDS; CCDS44898.1; -. [P08047-2]
CCDS; CCDS8857.1; -. [P08047-1]
PIR; A29635; A29635.
RefSeq; NP_001238754.1; NM_001251825.1. [P08047-3]
RefSeq; NP_003100.1; NM_003109.1. [P08047-2]
RefSeq; NP_612482.2; NM_138473.2. [P08047-1]
RefSeq; XP_011536998.1; XM_011538696.2. [P08047-2]
UniGene; Hs.620754; -.
UniGene; Hs.649191; -.
PDB; 1SP1; NMR; -; A=684-712.
PDB; 1SP2; NMR; -; A=654-684.
PDB; 1VA1; NMR; -; A=619-654.
PDB; 1VA2; NMR; -; A=654-684.
PDB; 1VA3; NMR; -; A=684-712.
PDBsum; 1SP1; -.
PDBsum; 1SP2; -.
PDBsum; 1VA1; -.
PDBsum; 1VA2; -.
PDBsum; 1VA3; -.
DisProt; DP00378; -.
ProteinModelPortal; P08047; -.
SMR; P08047; -.
BioGrid; 112550; 229.
DIP; DIP-36N; -.
ELM; P08047; -.
IntAct; P08047; 67.
MINT; MINT-98326; -.
STRING; 9606.ENSP00000329357; -.
ChEMBL; CHEMBL6103; -.
iPTMnet; P08047; -.
PhosphoSitePlus; P08047; -.
UniCarbKB; P08047; -.
BioMuta; SP1; -.
DMDM; 13638437; -.
EPD; P08047; -.
MaxQB; P08047; -.
PaxDb; P08047; -.
PeptideAtlas; P08047; -.
PRIDE; P08047; -.
Ensembl; ENST00000327443; ENSP00000329357; ENSG00000185591. [P08047-1]
Ensembl; ENST00000426431; ENSP00000404263; ENSG00000185591. [P08047-2]
GeneID; 6667; -.
KEGG; hsa:6667; -.
UCSC; uc001scw.4; human. [P08047-1]
CTD; 6667; -.
DisGeNET; 6667; -.
GeneCards; SP1; -.
HGNC; HGNC:11205; SP1.
HPA; CAB000330; -.
HPA; HPA001853; -.
HPA; HPA012292; -.
MIM; 189906; gene.
neXtProt; NX_P08047; -.
OpenTargets; ENSG00000185591; -.
PharmGKB; PA36042; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118984; -.
HOGENOM; HOG000234295; -.
HOVERGEN; HBG008933; -.
InParanoid; P08047; -.
KO; K04684; -.
OMA; CSRIESP; -.
OrthoDB; EOG091G0HX6; -.
PhylomeDB; P08047; -.
TreeFam; TF350150; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
SignaLink; P08047; -.
SIGNOR; P08047; -.
ChiTaRS; SP1; human.
EvolutionaryTrace; P08047; -.
GeneWiki; Sp1_transcription_factor; -.
GenomeRNAi; 6667; -.
PMAP-CutDB; P08047; -.
PRO; PR:P08047; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000185591; -.
CleanEx; HS_SP1; -.
ExpressionAtlas; P08047; baseline and differential.
Genevisible; P08047; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
GO; GO:0017053; C:transcriptional repressor complex; IDA:CAFA.
GO; GO:0043425; F:bHLH transcription factor binding; ISS:BHF-UCL.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:BHF-UCL.
GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:CAFA.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:CAFA.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISS:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:HGNC.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:CAFA.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:1904828; P:positive regulation of hydrogen sulfide biosynthetic process; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0100057; P:regulation of phenotypic switching by transcription from RNA polymerase II promoter; IC:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Biological rhythms; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Glycoprotein;
Host-virus interaction; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CHAIN 2 785 Transcription factor Sp1.
/FTId=PRO_0000047137.
ZN_FING 626 650 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 656 680 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 686 708 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 2 82 Repressor domain.
REGION 146 251 Transactivation domain A (Gln-rich).
REGION 261 495 Transactivation domain B (Gln-rich).
REGION 496 610 Transactivation domain C (highly
charged).
REGION 619 785 VZV IE62-binding.
REGION 708 785 Domain D.
COMPBIAS 36 143 Ser/Thr-rich.
COMPBIAS 271 379 Ser/Thr-rich.
SITE 63 64 Cleavage. {ECO:0000305}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18239466}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17049555,
ECO:0000269|PubMed:18199680,
ECO:0000269|PubMed:18239466}.
MOD_RES 101 101 Phosphoserine; by ATM.
{ECO:0000269|PubMed:18171990,
ECO:0000269|PubMed:18619531}.
MOD_RES 278 278 Phosphothreonine; by MAPK8.
{ECO:0000305|PubMed:18199680}.
MOD_RES 453 453 Phosphothreonine; by MAPK1 AND MAPK3.
{ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:14593115,
ECO:0000269|PubMed:16377629}.
MOD_RES 612 612 Phosphoserine; alternate.
{ECO:0000269|PubMed:16332679}.
MOD_RES 640 640 Phosphothreonine; alternate.
{ECO:0000269|PubMed:16332679}.
MOD_RES 641 641 Phosphoserine; by PKC/PRKCZ; alternate.
{ECO:0000269|PubMed:16943418}.
MOD_RES 651 651 Phosphothreonine; by PKC/PRKCZ.
{ECO:0000244|PubMed:18669648}.
MOD_RES 668 668 Phosphothreonine.
{ECO:0000269|PubMed:18258854}.
MOD_RES 670 670 Phosphoserine; by PKC/PRKCZ.
{ECO:0000269|PubMed:18258854}.
MOD_RES 681 681 Phosphothreonine; by PKC/PRKCZ.
{ECO:0000269|PubMed:17049555,
ECO:0000269|PubMed:18258854}.
MOD_RES 702 702 Phosphoserine; alternate.
{ECO:0000305|PubMed:20953893}.
MOD_RES 703 703 N6-acetyllysine.
{ECO:0000269|PubMed:16478997}.
MOD_RES 739 739 Phosphothreonine; by MAPK1, MAPK3 AND
MAPK8. {ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:14593115,
ECO:0000269|PubMed:16377629}.
CARBOHYD 491 491 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:11371615,
ECO:0000269|PubMed:9343410}.
CARBOHYD 612 612 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:16332679}.
CARBOHYD 640 640 O-linked (GlcNAc) threonine; alternate.
{ECO:0000269|PubMed:16332679}.
CARBOHYD 641 641 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:16332679}.
CARBOHYD 698 698 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:16332679}.
CARBOHYD 702 702 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:16332679}.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 7 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_053934.
VAR_SEQ 54 101 Missing (in isoform 3).
{ECO:0000303|PubMed:21798247}.
/FTId=VSP_053935.
VARIANT 737 737 T -> A (in dbSNP:rs3741665).
/FTId=VAR_019971.
MUTAGEN 7 7 S->A: Increase in protein stability. No
change in sumoylation.
{ECO:0000269|PubMed:18239466}.
MUTAGEN 15 15 V->R: Enhanced transcriptional activity.
MUTAGEN 16 16 K->R: Loss of sumoylation. No cleavage
and reduced transcriptional activity.
{ECO:0000269|PubMed:16407261}.
MUTAGEN 18 18 E->A: Loss of sumoylation. Increased
cleavage and enhanced transcriptional
activity. {ECO:0000269|PubMed:16407261}.
MUTAGEN 19 19 K->R: No effect on sumoylation nor on
proteolytic cleavage.
{ECO:0000269|PubMed:16407261}.
MUTAGEN 36 36 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 56 56 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 59 59 S->A: Loss of phosphorylation. No effect
on activated MAPK8-mediated
phosphorylation. Similar loss of
phosphorylation as by dephosphorylation
by PP2AC. Reduced proteolytic processing.
{ECO:0000269|PubMed:17049555,
ECO:0000269|PubMed:18199680,
ECO:0000269|PubMed:18239466}.
MUTAGEN 59 59 S->E: Some association with chromatin,
increased phosphorylation levels and
decreased glycosylation.
{ECO:0000269|PubMed:17049555,
ECO:0000269|PubMed:18199680,
ECO:0000269|PubMed:18239466}.
MUTAGEN 73 73 S->A: Little effect on activated MAPK8-
mediated phosphorylation.
{ECO:0000269|PubMed:18199680}.
MUTAGEN 81 81 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 85 85 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 98 98 T->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 101 101 S->A: Significant reduction of
phosphorylation on DNA damage.
{ECO:0000269|PubMed:18171990,
ECO:0000269|PubMed:18619531}.
MUTAGEN 101 101 S->D: Increase in phosphorylation on DNA
damage. {ECO:0000269|PubMed:18171990,
ECO:0000269|PubMed:18619531}.
MUTAGEN 117 117 T->A: No effect on activated MAPK8-
mediated phosphorylation.
{ECO:0000269|PubMed:18199680}.
MUTAGEN 220 220 S->A: No effect on dephosphorylation by
PP2A. {ECO:0000269|PubMed:17049555}.
MUTAGEN 250 250 T->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 278 278 T->A: Almost complete abolition of
activated MAPK8-mediated phosphorylation
and 40% reduction in protein levels
during mitosis. Protein levels reduced by
70% during mitosis; when associated with
A-739. {ECO:0000269|PubMed:18199680}.
MUTAGEN 278 278 T->D: Increased protein stability during
mitosis; when associated with D-739.
{ECO:0000269|PubMed:18199680}.
MUTAGEN 281 281 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 291 291 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 296 296 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 313 313 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 351 351 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 355 355 T->A: No effect on dephosphorylation by
PP2A. {ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:17049555}.
MUTAGEN 394 394 T->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 427 427 T->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 431 431 S->A: No effect on phosphorylation on DNA
damage. {ECO:0000269|PubMed:18619531}.
MUTAGEN 453 453 T->A: Abolishes MAPK-mediated
phosphorylation, 50% reduction in
MAPK1/MAPK3-mediated activity on VEGF
promoter and no effect on
dephosphorylation by PP2A. Greatly
reduced MAPK1-mediated activity on VEGF
promoter; when associated with A-739.
{ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:14593115,
ECO:0000269|PubMed:17049555}.
MUTAGEN 491 491 S->A: Loss of O-glycosylation. Increase
in transcriptional activity.
{ECO:0000269|PubMed:11371615,
ECO:0000269|PubMed:9343410}.
MUTAGEN 612 612 S->A: Diminished glycosylation. Inhibits
transcriptional activity; when associated
with A-640; A-641; A-698 and A-702.
{ECO:0000269|PubMed:18513490}.
MUTAGEN 640 640 T->A: Diminished glycosylation. Inhibits
transcriptional activity; when associated
with A-612; A-641; A-698 and A-702.
{ECO:0000269|PubMed:18513490}.
MUTAGEN 641 641 S->A: Abolishes PRKCzeta-mediated
phosphorylation. Diminished
glycosylation. Inhibits transcriptional
activity; when associated with A-612; A-
640; A-641 and A-702.
{ECO:0000269|PubMed:16943418,
ECO:0000269|PubMed:18513490}.
MUTAGEN 651 651 T->A: No effect on dephosphorylation by
PP2A. {ECO:0000269|PubMed:17049555}.
MUTAGEN 668 668 T->A: Abolishes PRKCzeta-mediated but not
PKCdelta-mediated phosphorylation. No
effect on DNA binding; when associated
with A-670 and A-681.
{ECO:0000269|PubMed:18258854}.
MUTAGEN 670 670 S->A: Abolishes PRKCzeta-mediated but not
PKCdelta-mediated phosphorylation. No
effect on DNA binding; when associated
with A-668 and A-681.
{ECO:0000269|PubMed:18258854}.
MUTAGEN 681 681 T->A: Abolishes PRKCzeta-mediated but not
PKCdelta-mediated phosphorylation. Some
effect on dephosphorylation by PP2A. No
effect on DNA binding; when associated
with A-668 and A-681.
{ECO:0000269|PubMed:17049555,
ECO:0000269|PubMed:18258854}.
MUTAGEN 698 698 S->A: Diminished glycosylation. Inhibits
transcriptional activity; when associated
with A-612; A-640; A-641 and A-702.
{ECO:0000269|PubMed:18513490}.
MUTAGEN 702 702 S->A: Diminished glycosylation. Inhibits
transcriptional activity; when associated
with A-612; A-640; A-641 and A-698.
{ECO:0000269|PubMed:18513490}.
MUTAGEN 703 703 K->A: Abolishes acetylation. Increases
recruitment of p300 to the promoter and
enhances gene transcription.
{ECO:0000269|PubMed:16478997}.
MUTAGEN 728 728 S->A: Exhibits attenuated endoproteolytic
cleavage; when associated with A-732.
{ECO:0000269|PubMed:18239466}.
MUTAGEN 732 732 S->A: Exhibits attenuated endoproteolytic
cleavage; when associated with A-728.
{ECO:0000269|PubMed:18239466}.
MUTAGEN 739 739 T->A: Abolishes MAPK-mediated
phosphorylation. 50% reduction in
MAPK1/MAPK3-mediated activity on VEGF
promoter, 40% reduction in protein levels
during mitosis and no effect on
dephosphorylation by PP2A. Greatly
reduced MAPK1-mediated activity on VEGF
promoter; when associated with A-453.
Protein levels during mitosis reduced by
70%; when associated with A-278.
{ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:14593115,
ECO:0000269|PubMed:17049555,
ECO:0000269|PubMed:18199680}.
MUTAGEN 739 739 T->D: Increased protein stability during
mitosis; when associated with D-278.
{ECO:0000269|PubMed:11904305,
ECO:0000269|PubMed:14593115,
ECO:0000269|PubMed:17049555,
ECO:0000269|PubMed:18199680}.
CONFLICT 366 366 D -> G (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 670 670 S -> F (in Ref. 7; AA sequence).
{ECO:0000305}.
STRAND 620 622 {ECO:0000244|PDB:1VA1}.
STRAND 636 638 {ECO:0000244|PDB:1VA1}.
HELIX 640 651 {ECO:0000244|PDB:1VA1}.
TURN 661 663 {ECO:0000244|PDB:1VA2}.
STRAND 666 668 {ECO:0000244|PDB:1VA2}.
HELIX 670 677 {ECO:0000244|PDB:1SP2}.
TURN 678 680 {ECO:0000244|PDB:1SP2}.
TURN 689 692 {ECO:0000244|PDB:1SP1}.
HELIX 699 706 {ECO:0000244|PDB:1SP1}.
HELIX 707 709 {ECO:0000244|PDB:1SP1}.
SEQUENCE 785 AA; 80693 MW; 43893DBF6518B9EA CRC64;
MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG GGGQESQPSP
LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL SQGANGWQII SSSSGATPTS
KEQSGSSTNG SNGSESSKNR TVSGGQYVVA AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ
TVDGQQLQFA ATGAQVQQDG SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG
LANNVLSGQT QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT
SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN SQGQTPQRVS
GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL IQPQLVQGGQ ALQALQAAPL
SGQTFTTQAI SQETLQNLQL QAVPNSGPII IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ
TITLAPMQGV SLGQTSSSNT TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS
GIQVHPIQGL PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR
REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH TGERPFMCTW
SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH LSKHIKTHQN KKGGPGVALS
VGTLPLDSGA GSEGSGTATP SALITTNMVA MEAICPEGIA RLANSGINVM QVADLQSINI
SGNGF


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