(data stored in SCRATCH zone)

SWISSPROT: SP1_HUMAN

ID   SP1_HUMAN               Reviewed;         785 AA.
AC   P08047; E4Z9M7; G5E9M8; Q86TN8; Q9H3Q5; Q9NR51; Q9NY21; Q9NYE7;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   11-DEC-2019, entry version 239.
DE   RecName: Full=Transcription factor Sp1;
GN   Name=SP1; Synonyms=TSFP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=21798247; DOI=10.1016/j.bbrc.2011.07.047;
RA   Infantino V., Convertini P., Iacobazzi F., Pisano I., Scarcia P.,
RA   Iacobazzi V.;
RT   "Identification of a novel Sp1 splice variant as a strong transcriptional
RT   activator.";
RL   Biochem. Biophys. Res. Commun. 412:86-91(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-785 (ISOFORM 1).
RC   TISSUE=Cervix carcinoma;
RA   Haggart M.H., Ladurner A.G.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-558 (ISOFORM 1), AND TRANS-SPLICING.
RX   PubMed=10973950; DOI=10.1074/jbc.m002010200;
RA   Takahara T., Kanazu S., Yanagisawa S., Akanuma H.;
RT   "Heterogeneous Sp1 mRNAs in human HepG2 cells include a product of
RT   homotypic trans-splicing.";
RL   J. Biol. Chem. 275:38067-38072(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 90-785 (ISOFORM 1/2), AND PROTEIN SEQUENCE OF
RP   359-375 AND 670-675.
RX   PubMed=3319186; DOI=10.1016/0092-8674(87)90594-0;
RA   Kadonaga J.T., Carner K.R., Masiarz F.R., Tjian R.;
RT   "Isolation of cDNA encoding transcription factor Sp1 and functional
RT   analysis of the DNA binding domain.";
RL   Cell 51:1079-1090(1987).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-109 (ISOFORM 1).
RA   Nicolas M., Noe V., Ciudad C.J.;
RT   "Expression of transcription factor Sp1 mRNA in mammalian cells.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 1).
RA   Handschug K., Huebner A.;
RT   "Sequencing of the 5' end of human transcription factor SP1 mRNA.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   GLYCOSYLATION.
RX   PubMed=3139301; DOI=10.1016/0092-8674(88)90015-3;
RA   Jackson S.P., Tjian R.;
RT   "O-glycosylation of eukaryotic transcription factors: implications for
RT   mechanisms of transcriptional regulation.";
RL   Cell 55:125-133(1988).
RN   [11]
RP   TRANSACTIVATION DOMAINS.
RX   PubMed=3142690; DOI=10.1016/0092-8674(88)90144-4;
RA   Courey A.J., Tjian R.;
RT   "Analysis of Sp1 in vivo reveals multiple transcriptional domains,
RT   including a novel glutamine-rich activation motif.";
RL   Cell 55:887-898(1988).
RN   [12]
RP   INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION).
RX   PubMed=7592727; DOI=10.1074/jbc.270.43.25564;
RA   Wang L., Mukherjee S., Jia F., Narayan O., Zhao L.J.;
RT   "Interaction of virion protein Vpr of human immunodeficiency virus type 1
RT   with cellular transcription factor Sp1 and trans-activation of viral long
RT   terminal repeat.";
RL   J. Biol. Chem. 270:25564-25569(1995).
RN   [13]
RP   IDENTIFICATION OF SEROTONIN 1A RECEPTOR PROMOTER BINDING SITES.
RX   PubMed=8626793; DOI=10.1074/jbc.271.8.4417;
RA   Parks C.L., Shenk T.;
RT   "The serotonin 1a receptor gene contains a TATA-less promoter that responds
RT   to MAZ and Sp1.";
RL   J. Biol. Chem. 271:4417-4430(1996).
RN   [14]
RP   GLYCOSYLATION AT SER-491, MUTAGENESIS OF SER-491, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=9343410; DOI=10.1128/mcb.17.11.6472;
RA   Roos M.D., Su K., Baker J.R., Kudlow J.E.;
RT   "O glycosylation of an Sp1-derived peptide blocks known Sp1 protein
RT   interactions.";
RL   Mol. Cell. Biol. 17:6472-6480(1997).
RN   [15]
RP   INTERACTION WITH SV40 VP2/3 (MICROBIAL INFECTION).
RX   PubMed=9466902; DOI=10.1006/jmbi.1997.1461;
RA   Gordon-Shaag A., Ben-Nun-Shaul O., Kasamatsu H., Oppenheim A.B.,
RA   Oppenheim A.;
RT   "The SV40 capsid protein VP3 cooperates with the cellular transcription
RT   factor Sp1 in DNA-binding and in regulating viral promoter activity.";
RL   J. Mol. Biol. 275:187-195(1998).
RN   [16]
RP   FUNCTION, AND INTERACTION WITH HLTF.
RX   PubMed=10391891; DOI=10.1074/jbc.274.28.19573;
RA   Ding H., Benotmane A.M., Suske G., Collen D., Belayew A.;
RT   "Functional interactions between Sp1 or Sp3 and the helicase-like
RT   transcription factor mediate basal expression from the human plasminogen
RT   activator inhibitor-1 gene.";
RL   J. Biol. Chem. 274:19573-19580(1999).
RN   [17]
RP   INTERACTION WITH ATF7IP; PHC2; POGZ AND HCFC1.
RC   TISSUE=Colon;
RX   PubMed=10976766; DOI=10.1023/a:1007177623283;
RA   Gunther M., Laithier M., Brison O.;
RT   "A set of proteins interacting with transcription factor Sp1 identified in
RT   a two-hybrid screening.";
RL   Mol. Cell. Biochem. 210:131-142(2000).
RN   [18]
RP   GLYCOSYLATION AT SER-491, FUNCTION, AND MUTAGENESIS OF SER-491.
RX   PubMed=11371615; DOI=10.1073/pnas.111099998;
RA   Yang X., Su K., Roos M.D., Chang Q., Paterson A.J., Kudlow J.E.;
RT   "O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its
RT   transcriptional capability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6611-6616(2001).
RN   [19]
RP   PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, AND MUTAGENESIS OF
RP   THR-355; THR-453 AND THR-739.
RX   PubMed=11904305; DOI=10.1074/jbc.m201753200;
RA   Milanini-Mongiat J., Pouyssegur J., Pages G.;
RT   "Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-
RT   activated protein kinases: their implication in vascular endothelial growth
RT   factor gene transcription.";
RL   J. Biol. Chem. 277:20631-20639(2002).
RN   [20]
RP   INTERACTION WITH ZBTB7A.
RX   PubMed=12004059; DOI=10.1074/jbc.m202078200;
RA   Lee D.K., Suh D., Edenberg H.J., Hur M.W.;
RT   "POZ domain transcription factor, FBI-1, represses transcription of
RT   ADH5/FDH by interacting with the zinc finger and interfering with DNA
RT   binding activity of Sp1.";
RL   J. Biol. Chem. 277:26761-26768(2002).
RN   [21]
RP   INTERACTION WITH SV40 VP1 (MICROBIAL INFECTION).
RX   PubMed=12021324; DOI=10.1128/jvi.76.12.5915-5924.2002;
RA   Gordon-Shaag A., Ben-Nun-Shaul O., Roitman V., Yosef Y., Oppenheim A.;
RT   "Cellular transcription factor Sp1 recruits simian virus 40 capsid proteins
RT   to the viral packaging signal, ses.";
RL   J. Virol. 76:5915-5924(2002).
RN   [22]
RP   INTERACTION WITH AATF.
RX   PubMed=12847090; DOI=10.1074/jbc.m306694200;
RA   Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R.,
RA   Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., Fanciulli M.;
RT   "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1
RT   from the p21WAF1/CIP1 promoter.";
RL   J. Biol. Chem. 278:36496-36504(2003).
RN   [23]
RP   INTERACTION WITH VARICELLA-ZOSTER VIRUS IE62 PROTEIN (MICROBIAL INFECTION).
RX   PubMed=12855699; DOI=10.1074/jbc.m302259200;
RA   Peng H., He H., Hay J., Ruyechan W.T.;
RT   "Interaction between the varicella zoster virus IE62 major transactivator
RT   and cellular transcription factor Sp1.";
RL   J. Biol. Chem. 278:38068-38075(2003).
RN   [24]
RP   PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, AND MUTAGENESIS OF
RP   THR-453 AND THR-739.
RX   PubMed=14593115; DOI=10.1074/jbc.m308254200;
RA   Bonello M.R., Khachigian L.M.;
RT   "Fibroblast growth factor-2 represses platelet-derived growth factor
RT   receptor-alpha (PDGFR-alpha) transcription via ERK1/2-dependent Sp1
RT   phosphorylation and an atypical cis-acting element in the proximal PDGFR-
RT   alpha promoter.";
RL   J. Biol. Chem. 279:2377-2382(2004).
RN   [25]
RP   INTERACTION WITH ATF7IP AND ATF7IP2.
RX   PubMed=15691849; DOI=10.1074/jbc.m413654200;
RA   Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.;
RT   "Transcriptional repression and heterochromatin formation by MBD1 and
RT   MCAF/AM family proteins.";
RL   J. Biol. Chem. 280:13928-13935(2005).
RN   [26]
RP   GLYCOSYLATION AT SER-612; THR-640; SER-641; SER-698 AND SER-702,
RP   PHOSPHORYLATION AT SER-612; THR-640; SER-641; SER-698 AND SER-702,
RP   INDUCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16332679; DOI=10.1074/jbc.m511223200;
RA   Majumdar G., Harrington A., Hungerford J., Martinez-Hernandez A.,
RA   Gerling I.C., Raghow R., Solomon S.;
RT   "Insulin dynamically regulates calmodulin gene expression by sequential O-
RT   glycosylation and phosphorylation of SP1 and its subcellular
RT   compartmentalization in liver cells.";
RL   J. Biol. Chem. 281:3642-3650(2006).
RN   [27]
RP   PHOSPHORYLATION AT THR-453 AND THR-739, AND FUNCTION.
RX   PubMed=16377629; DOI=10.1074/jbc.m510937200;
RA   Hsu M.C., Chang H.C., Hung W.C.;
RT   "HER-2/neu represses the metastasis suppressor RECK via ERK and Sp
RT   transcription factors to promote cell invasion.";
RL   J. Biol. Chem. 281:4718-4725(2006).
RN   [28]
RP   SUMOYLATION AT LYS-16, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF LYS-16;
RP   GLU-18 AND LYS-19.
RX   PubMed=16407261; DOI=10.1074/jbc.m600035200;
RA   Spengler M.L., Brattain M.G.;
RT   "Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain
RT   and inhibits Sp1-dependent transcription.";
RL   J. Biol. Chem. 281:5567-5574(2006).
RN   [29]
RP   PHOSPHORYLATION AT SER-59 AND THR-681, DEPHOSPHORYLATION, GLYCOSYLATION,
RP   FUNCTION, AND MUTAGENESIS OF SER-59; SER-220; THR-355; THR-453; THR-651;
RP   THR-681 AND THR-739.
RX   PubMed=17049555; DOI=10.1016/j.jmb.2006.09.036;
RA   Vicart A., Lefebvre T., Imbert J., Fernandez A., Kahn-Perles B.;
RT   "Increased chromatin association of Sp1 in interphase cells by PP2A-
RT   mediated dephosphorylations.";
RL   J. Mol. Biol. 364:897-908(2006).
RN   [30]
RP   ACETYLATION AT LYS-703, INTERACTION WITH HDAC1; EP300 AND JUN, FUNCTION,
RP   AND MUTAGENESIS OF LYS-703.
RX   PubMed=16478997; DOI=10.1128/mcb.26.5.1770-1785.2006;
RA   Hung J.J., Wang Y.T., Chang W.C.;
RT   "Sp1 deacetylation induced by phorbol ester recruits p300 to activate
RT   12(S)-lipoxygenase gene transcription.";
RL   Mol. Cell. Biol. 26:1770-1785(2006).
RN   [31]
RP   PHOSPHORYLATION AT SER-641, FUNCTION, AND MUTAGENESIS OF SER-641.
RX   PubMed=16943418; DOI=10.1128/mcb.00560-06;
RA   Zhang Y., Liao M., Dufau M.L.;
RT   "Phosphatidylinositol 3-kinase/protein kinase Czeta-induced phosphorylation
RT   of Sp1 and p107 repressor release have a critical role in histone
RT   deacetylase inhibitor-mediated derepression of transcription of the
RT   luteinizing hormone receptor gene.";
RL   Mol. Cell. Biol. 26:6748-6761(2006).
RN   [32]
RP   ERRATUM.
RA   Zhang Y., Liao M., Dufau M.L.;
RL   Mol. Cell. Biol. 26:8214-8214(2006).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [34]
RP   PHOSPHORYLATION AT SER-101, FUNCTION, AND MUTAGENESIS OF SER-101.
RX   PubMed=18171990; DOI=10.1158/1541-7786.mcr-07-0374;
RA   Olofsson B.A., Kelly C.M., Kim J., Hornsby S.M., Azizkhan-Clifford J.;
RT   "Phosphorylation of Sp1 in response to DNA damage by ataxia telangiectasia-
RT   mutated kinase.";
RL   Mol. Cancer Res. 5:1319-1330(2007).
RN   [35]
RP   GLYCOSYLATION, FUNCTION, AND MUTAGENESIS OF SER-612; THR-640; SER-641;
RP   SER-698 AND SER-702.
RX   PubMed=18513490; DOI=10.1016/j.bbrc.2008.05.096;
RA   Chung S.S., Kim J.H., Park H.S., Choi H.H., Lee K.W., Cho Y.M., Lee H.K.,
RA   Park K.S.;
RT   "Activation of PPARgamma negatively regulates O-GlcNAcylation of Sp1.";
RL   Biochem. Biophys. Res. Commun. 372:713-718(2008).
RN   [36]
RP   PHOSPHORYLATION AT SER-7 AND SER-59, SUMOYLATION AT LYS-16, PROTEOLYTIC
RP   PROCESSING, UBIQUITINATION, FUNCTION, AND MUTAGENESIS OF SER-7; SER-59;
RP   SER-728 AND SER-732.
RX   PubMed=18239466; DOI=10.4161/cc.7.5.5402;
RA   Spengler M.L., Guo L.W., Brattain M.G.;
RT   "Phosphorylation mediates Sp1 coupled activities of proteolytic processing,
RT   desumoylation and degradation.";
RL   Cell Cycle 7:623-630(2008).
RN   [37]
RP   PHOSPHORYLATION AT SER-101, FUNCTION, AND MUTAGENESIS OF SER-36; SER-56;
RP   SER-81; SER-85; THR-98; SER-101; THR-250; SER-281; SER-291; SER-296;
RP   SER-313; SER-351; THR-394; THR-427 AND SER-431.
RX   PubMed=18619531; DOI=10.1016/j.cellsig.2008.06.007;
RA   Iwahori S., Yasui Y., Kudoh A., Sato Y., Nakayama S., Murata T.,
RA   Isomura H., Tsurumi T.;
RT   "Identification of phosphorylation sites on transcription factor Sp1 in
RT   response to DNA damage and its accumulation at damaged sites.";
RL   Cell. Signal. 20:1795-1803(2008).
RN   [38]
RP   PHOSPHORYLATION AT THR-668; SER-670 AND THR-681, AND MUTAGENESIS OF
RP   THR-668; SER-670 AND THR-681.
RX   PubMed=18258854; DOI=10.1161/circresaha.107.167395;
RA   Tan N.Y., Midgley V.C., Kavurma M.M., Santiago F.S., Luo X., Peden R.,
RA   Fahmy R.G., Berndt M.C., Molloy M.P., Khachigian L.M.;
RT   "Angiotensin II-inducible platelet-derived growth factor-D transcription
RT   requires specific Ser/Thr residues in the second zinc finger region of
RT   Sp1.";
RL   Circ. Res. 102:38-51(2008).
RN   [39]
RP   PHOSPHORYLATION AT SER-59 AND THR-278, FUNCTION, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF SER-59; SER-73; THR-117; THR-278 AND THR-739.
RX   PubMed=18199680; DOI=10.1091/mbc.e07-09-0881;
RA   Chuang J.-Y., Wang Y.-T., Yeh S.-H., Liu Y.-W., Chang W.-C., Hung J.-J.;
RT   "Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the stability of
RT   transcription factor Sp1 during mitosis.";
RL   Mol. Biol. Cell 19:1139-1151(2008).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-651, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [41]
RP   GLYCOSYLATION, AND INTERACTION WITH ELF1.
RX   PubMed=19285002; DOI=10.1016/j.bbrc.2009.01.121;
RA   Lim K., Chang H.I.;
RT   "O-GlcNAc inhibits interaction between Sp1 and Elf-1 transcription
RT   factors.";
RL   Biochem. Biophys. Res. Commun. 380:569-574(2009).
RN   [42]
RP   GLYCOSYLATION, AND INTERACTION WITH NFYA.
RX   PubMed=19302979; DOI=10.1016/j.bbrc.2009.03.075;
RA   Lim K., Chang H.I.;
RT   "O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.";
RL   Biochem. Biophys. Res. Commun. 382:593-597(2009).
RN   [43]
RP   INTERACTION WITH ATF7IP AND TBP.
RX   PubMed=19106100; DOI=10.1074/jbc.m807098200;
RA   Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
RA   Watanabe S., Saitoh N., Ito T., Nakao M.;
RT   "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
RT   telomerase activity.";
RL   J. Biol. Chem. 284:5165-5174(2009).
RN   [44]
RP   GLYCOSYLATION, AND FUNCTION.
RX   PubMed=19193796; DOI=10.1128/jvi.01384-08;
RA   Jochmann R., Thurau M., Jung S., Hofmann C., Naschberger E., Kremmer E.,
RA   Harrer T., Miller M., Schaft N., Stuerzl M.;
RT   "O-linked N-acetylglucosaminylation of Sp1 inhibits the human
RT   immunodeficiency virus type 1 promoter.";
RL   J. Virol. 83:3704-3718(2009).
RN   [45]
RP   INTERACTION WITH BAHD1.
RX   PubMed=19666599; DOI=10.1073/pnas.0901259106;
RA   Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
RA   Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J.,
RA   Cossart P.;
RT   "Human BAHD1 promotes heterochromatic gene silencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
RN   [46]
RP   INTERACTION WITH EGR1.
RX   PubMed=20121949; DOI=10.1111/j.1742-4658.2009.07553.x;
RA   Hu C.T., Chang T.Y., Cheng C.C., Liu C.S., Wu J.R., Li M.C., Wu W.S.;
RT   "Snail associates with EGR-1 and SP-1 to upregulate transcriptional
RT   activation of p15INK4b.";
RL   FEBS J. 277:1202-1218(2010).
RN   [47]
RP   FUNCTION.
RX   PubMed=20091743; DOI=10.1002/jcb.22457;
RA   Yu H.T., Chan W.W., Chai K.H., Lee C.W., Chang R.C., Yu M.S.,
RA   McLoughlin D.M., Miller C.C., Lau K.F.;
RT   "Transcriptional regulation of human FE65, a ligand of Alzheimer's disease
RT   amyloid precursor protein, by Sp1.";
RL   J. Cell. Biochem. 109:782-793(2010).
RN   [48]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-2 AND SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [49]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [50]
RP   PHOSPHORYLATION AT SER-702.
RX   PubMed=20953893; DOI=10.1007/s00018-010-0541-1;
RA   Alemu E.A., Sjoettem E., Outzen H., Larsen K.B., Holm T., Bjoerkoey G.,
RA   Johansen T.;
RT   "Transforming growth factor-beta-inducible early response gene 1 is a novel
RT   substrate for atypical protein kinase Cs.";
RL   Cell. Mol. Life Sci. 68:1953-1968(2011).
RN   [51]
RP   INTERACTION WITH MEIS2 AND PBX1.
RX   PubMed=21746878; DOI=10.1128/mcb.01456-10;
RA   Bjerke G.A., Hyman-Walsh C., Wotton D.;
RT   "Cooperative transcriptional activation by Klf4, Meis2, and Pbx1.";
RL   Mol. Cell. Biol. 31:3723-3733(2011).
RN   [52]
RP   FUNCTION.
RX   PubMed=21046154; DOI=10.1007/s00438-010-0586-8;
RA   Sachrajda I., Ratajewski M.;
RT   "Mithramycin A suppresses expression of the human melanoma-associated gene
RT   ABCB8.";
RL   Mol. Genet. Genomics 285:57-65(2011).
RN   [53]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [54]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-7 AND SER-59, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [55]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [56]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [57]
RP   9AATAD MOTIF.
RX   PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA   Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT   "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT   valines and intron reservoirs.";
RL   Cell. Mol. Life Sci. 0:0-0(2019).
RN   [58]
RP   STRUCTURE BY NMR OF 654-684 AND 684-712.
RX   PubMed=9065444; DOI=10.1074/jbc.272.12.7801;
RA   Narayan V.A., Kriwacki R.W., Caradonna J.P.;
RT   "Structures of zinc finger domains from transcription factor Sp1. Insights
RT   into sequence-specific protein-DNA recognition.";
RL   J. Biol. Chem. 272:7801-7809(1997).
CC   -!- FUNCTION: Transcription factor that can activate or repress
CC       transcription in response to physiological and pathological stimuli.
CC       Binds with high affinity to GC-rich motifs and regulates the expression
CC       of a large number of genes involved in a variety of processes such as
CC       cell growth, apoptosis, differentiation and immune responses. Highly
CC       regulated by post-translational modifications (phosphorylations,
CC       sumoylation, proteolytic cleavage, glycosylation and acetylation).
CC       Binds also the PDGFR-alpha G-box promoter. May have a role in
CC       modulating the cellular response to DNA damage. Implicated in chromatin
CC       remodeling. Plays an essential role in the regulation of FE65 gene
CC       expression. In complex with ATF7IP, maintains telomerase activity in
CC       cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a
CC       stronger activator of transcription than isoform 1. Positively
CC       regulates the transcription of the core clock component ARNTL/BMAL1
CC       (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115,
CC       PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555,
CC       PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490,
CC       PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21798247,
CC       PubMed:21046154). Plays a role in the recruitment of SMARCA4/BRG1 on
CC       the c-FOS promoter. Plays a role in protecting cells against oxidative
CC       stress following brain injury by regulating the expression of RNF112
CC       (By similarity). {ECO:0000250|UniProtKB:O89090,
CC       ECO:0000250|UniProtKB:Q01714, ECO:0000269|PubMed:10391891,
CC       ECO:0000269|PubMed:11371615, ECO:0000269|PubMed:11904305,
CC       ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629,
CC       ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16943418,
CC       ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990,
CC       ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466,
CC       ECO:0000269|PubMed:18513490, ECO:0000269|PubMed:18619531,
CC       ECO:0000269|PubMed:19193796, ECO:0000269|PubMed:20091743,
CC       ECO:0000269|PubMed:21046154, ECO:0000269|PubMed:21798247}.
CC   -!- SUBUNIT: Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and
CC       PHC2. Interacts with HLTF; the interaction may be required for basal
CC       transcriptional activity of HLTF. Interacts (deacetylated form) with
CC       EP300; the interaction enhances gene expression. Interacts with HDAC1
CC       and JUN. Interacts with ELF1; the interaction is inhibited by
CC       glycosylation of SP1. Interaction with NFYA; the interaction is
CC       inhibited by glycosylation of SP1. Interacts with ATF7IP and TBP.
CC       Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a. Interacts with
CC       EGR1 (PubMed:10391891, PubMed:10976766, PubMed:12021324,
CC       PubMed:12847090, PubMed:12855699, PubMed:15691849, PubMed:16478997,
CC       PubMed:19106100, PubMed:19285002, PubMed:19302979, PubMed:19666599,
CC       PubMed:20121949, PubMed:21746878, PubMed:7592727, PubMed:9466902).
CC       Interacts with SMARCA4/BRG1. Interacts with RNF112 in an oxidative
CC       stress-regulated manner (By similarity). Interacts with ZBTB7A; ZBTB7A
CC       prevents the binding to GC-rich motifs in promoters and represses the
CC       transcriptional activity of SP1 (PubMed:12004059).
CC       {ECO:0000250|UniProtKB:O89090, ECO:0000250|UniProtKB:Q01714,
CC       ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:10976766,
CC       ECO:0000269|PubMed:12004059, ECO:0000269|PubMed:12847090,
CC       ECO:0000269|PubMed:15691849, ECO:0000269|PubMed:16478997,
CC       ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:19285002,
CC       ECO:0000269|PubMed:19302979, ECO:0000269|PubMed:19666599,
CC       ECO:0000269|PubMed:20121949, ECO:0000269|PubMed:21746878}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with varicella-zoster virus
CC       IE62 protein. {ECO:0000269|PubMed:12855699}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with SV40 VP2/3 proteins.
CC       Interacts with SV40 major capsid protein VP1; this interaction leads to
CC       a cooperativity between the 2 proteins in DNA binding.
CC       {ECO:0000269|PubMed:12021324, ECO:0000269|PubMed:9466902}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr; the
CC       interaction is inhibited by SP1 O-glycosylation.
CC       {ECO:0000269|PubMed:7592727}.
CC   -!- INTERACTION:
CC       Q9NY61:AATF; NbExp=2; IntAct=EBI-298336, EBI-372428;
CC       Q8N726:CDKN2A; NbExp=4; IntAct=EBI-298336, EBI-625922;
CC       Q92988:DLX4; NbExp=4; IntAct=EBI-298336, EBI-1752755;
CC       Q01094:E2F1; NbExp=2; IntAct=EBI-298336, EBI-448924;
CC       P32519:ELF1; NbExp=2; IntAct=EBI-298336, EBI-765526;
CC       Q99814:EPAS1; NbExp=2; IntAct=EBI-298336, EBI-447470;
CC       P03372:ESR1; NbExp=2; IntAct=EBI-298336, EBI-78473;
CC       P51610:HCFC1; NbExp=4; IntAct=EBI-298336, EBI-396176;
CC       Q13547:HDAC1; NbExp=2; IntAct=EBI-298336, EBI-301834;
CC       Q16665:HIF1A; NbExp=3; IntAct=EBI-298336, EBI-447269;
CC       Q13118:KLF10; NbExp=2; IntAct=EBI-298336, EBI-1389509;
CC       P01106:MYC; NbExp=4; IntAct=EBI-298336, EBI-447544;
CC       P16333:NCK1; NbExp=2; IntAct=EBI-298336, EBI-389883;
CC       P23708:Nfya (xeno); NbExp=18; IntAct=EBI-298336, EBI-862337;
CC       Q8IXK0:PHC2; NbExp=2; IntAct=EBI-298336, EBI-713786;
CC       Q7Z3K3:POGZ; NbExp=2; IntAct=EBI-298336, EBI-1389308;
CC       P14859:POU2F1; NbExp=7; IntAct=EBI-298336, EBI-624770;
CC       Q06455:RUNX1T1; NbExp=2; IntAct=EBI-298336, EBI-743342;
CC       Q15459:SF3A1; NbExp=2; IntAct=EBI-298336, EBI-1054743;
CC       Q13485:SMAD4; NbExp=2; IntAct=EBI-298336, EBI-347263;
CC       Q12772:SREBF2; NbExp=3; IntAct=EBI-298336, EBI-465059;
CC       P40763:STAT3; NbExp=4; IntAct=EBI-298336, EBI-518675;
CC       Q9UL17:TBX21; NbExp=4; IntAct=EBI-298336, EBI-3922312;
CC       P04637:TP53; NbExp=3; IntAct=EBI-298336, EBI-366083;
CC       Q8N680:ZBTB2; NbExp=4; IntAct=EBI-298336, EBI-2515601;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear location is
CC       governed by glycosylated/phosphorylated states. Insulin promotes
CC       nuclear location, while glucagon favors cytoplasmic location.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Sp1a;
CC         IsoId=P08047-1; Sequence=Displayed;
CC       Name=2; Synonyms=Sp1b;
CC         IsoId=P08047-2; Sequence=VSP_053934;
CC       Name=3; Synonyms=Sp1c;
CC         IsoId=P08047-3; Sequence=VSP_053935;
CC   -!- TISSUE SPECIFICITY: Up-regulated in adenocarcinomas of the stomach (at
CC       protein level). Isoform 3 is ubiquitously expressed at low levels.
CC       {ECO:0000269|PubMed:21798247}.
CC   -!- INDUCTION: By insulin. {ECO:0000269|PubMed:16332679}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000269|PubMed:31375868}.
CC   -!- PTM: Phosphorylated on multiple serine and threonine residues.
CC       Phosphorylation is coupled to ubiquitination, sumoylation and
CC       proteolytic processing. Phosphorylation on Ser-59 enhances proteolytic
CC       cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein
CC       degradation. Hyperphosphorylation on Ser-101 in response to DNA damage
CC       has no effect on transcriptional activity. MAPK1/MAPK3-mediated
CC       phosphorylation on Thr-453 and Thr-739 enhances VEGF transcription but,
CC       represses FGF2-triggered PDGFR-alpha transcription. Also implicated in
CC       the repression of RECK by ERBB2. Hyperphosphorylated on Thr-278 and
CC       Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the
CC       ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain
CC       by calmodulin-activated PKCzeta. Phosphorylation on Ser-641 by PKCzeta
CC       is critical for TSA-activated LHR gene expression through release of
CC       its repressor, p107. Phosphorylation on Thr-668, Ser-670 and Thr-681 is
CC       stimulated by angiotensin II via the AT1 receptor inducing increased
CC       binding to the PDGF-D promoter. This phosphorylation is increased in
CC       injured artey wall. Ser-59 and Thr-681 can both be dephosphorylated by
CC       PP2A during cell-cycle interphase. Dephosphorylation on Ser-59 leads to
CC       increased chromatin association during interphase and increases the
CC       transcriptional activity. On insulin stimulation, sequentially
CC       glycosylated and phosphorylated on several C-terminal serine and
CC       threonine residues. {ECO:0000269|PubMed:11904305,
CC       ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16332679,
CC       ECO:0000269|PubMed:16377629, ECO:0000269|PubMed:16943418,
CC       ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990,
CC       ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466,
CC       ECO:0000269|PubMed:18258854, ECO:0000269|PubMed:18619531}.
CC   -!- PTM: Acetylated. Acetylation/deacetylation events affect
CC       transcriptional activity. Deacetylation leads to an increase in the
CC       expression the 12(s)-lipooxygenase gene though recruitment of p300 to
CC       the promoter. {ECO:0000269|PubMed:16478997}.
CC   -!- PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal
CC       proteolytically-cleaved peptide and is triggered by phosphorylation.
CC       {ECO:0000269|PubMed:18239466}.
CC   -!- PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage
CC       of the N-terminal repressor domain. Sumoylation levels are attenuated
CC       during tumorigenesis. Phosphorylation mediates SP1 desumoylation.
CC   -!- PTM: Proteolytic cleavage in the N-terminal repressor domain is
CC       prevented by sumoylation. The C-terminal cleaved product is susceptible
CC       to degradation.
CC   -!- PTM: O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels
CC       are controlled by insulin and the SP1 phosphorylation states. Insulin-
CC       mediated O-glycosylation locates SP1 to the nucleus, where it is
CC       sequentially deglycosylated and phosphorylated. O-glycosylation affects
CC       transcriptional activity through disrupting the interaction with a
CC       number of transcription factors including ELF1 and NFYA. Also inhibits
CC       interaction with the HIV1 promoter. Inhibited by peroxisomome
CC       proliferator receptor gamma (PPARgamma).
CC   -!- MISCELLANEOUS: In the hepatoma cell line Hep-G2, SP1 precursor mRNA may
CC       undergo homotype trans-splicing leading to the duplication of exons 2
CC       and 3.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43224.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; FN908228; CBM42955.1; -; mRNA.
DR   EMBL; AC068889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW96699.1; -; Genomic_DNA.
DR   EMBL; BC043224; AAH43224.1; ALT_INIT; mRNA.
DR   EMBL; BC062539; AAH62539.1; -; mRNA.
DR   EMBL; AF252284; AAF67726.1; -; mRNA.
DR   EMBL; AB039286; BAB13476.1; -; Genomic_DNA.
DR   EMBL; J03133; AAA61154.1; -; mRNA.
DR   EMBL; AF255682; AAF78781.1; -; mRNA.
DR   EMBL; AJ272134; CAB75345.1; -; mRNA.
DR   CCDS; CCDS44898.1; -. [P08047-2]
DR   CCDS; CCDS8857.1; -. [P08047-1]
DR   PIR; A29635; A29635.
DR   RefSeq; NP_001238754.1; NM_001251825.1. [P08047-3]
DR   RefSeq; NP_003100.1; NM_003109.1. [P08047-2]
DR   RefSeq; NP_612482.2; NM_138473.2. [P08047-1]
DR   RefSeq; XP_011536998.1; XM_011538696.2.
DR   PDB; 1SP1; NMR; -; A=684-712.
DR   PDB; 1SP2; NMR; -; A=654-684.
DR   PDB; 1VA1; NMR; -; A=619-654.
DR   PDB; 1VA2; NMR; -; A=654-684.
DR   PDB; 1VA3; NMR; -; A=684-712.
DR   PDBsum; 1SP1; -.
DR   PDBsum; 1SP2; -.
DR   PDBsum; 1VA1; -.
DR   PDBsum; 1VA2; -.
DR   PDBsum; 1VA3; -.
DR   SMR; P08047; -.
DR   BioGrid; 112550; 243.
DR   CORUM; P08047; -.
DR   DIP; DIP-36N; -.
DR   ELM; P08047; -.
DR   IntAct; P08047; 73.
DR   MINT; P08047; -.
DR   STRING; 9606.ENSP00000329357; -.
DR   ChEMBL; CHEMBL6103; -.
DR   GlyConnect; 605; -.
DR   iPTMnet; P08047; -.
DR   PhosphoSitePlus; P08047; -.
DR   UniCarbKB; P08047; -.
DR   BioMuta; SP1; -.
DR   DMDM; 13638437; -.
DR   EPD; P08047; -.
DR   jPOST; P08047; -.
DR   MassIVE; P08047; -.
DR   MaxQB; P08047; -.
DR   PaxDb; P08047; -.
DR   PeptideAtlas; P08047; -.
DR   PRIDE; P08047; -.
DR   ProteomicsDB; 33987; -.
DR   ProteomicsDB; 52061; -. [P08047-1]
DR   Ensembl; ENST00000327443; ENSP00000329357; ENSG00000185591. [P08047-1]
DR   Ensembl; ENST00000426431; ENSP00000404263; ENSG00000185591. [P08047-2]
DR   GeneID; 6667; -.
DR   KEGG; hsa:6667; -.
DR   UCSC; uc001scw.4; human. [P08047-1]
DR   CTD; 6667; -.
DR   DisGeNET; 6667; -.
DR   EuPathDB; HostDB:ENSG00000185591.9; -.
DR   GeneCards; SP1; -.
DR   HGNC; HGNC:11205; SP1.
DR   HPA; CAB000330; -.
DR   HPA; HPA001853; -.
DR   HPA; HPA012292; -.
DR   MIM; 189906; gene.
DR   neXtProt; NX_P08047; -.
DR   OpenTargets; ENSG00000185591; -.
DR   PharmGKB; PA36042; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000157804; -.
DR   HOGENOM; HOG000234295; -.
DR   InParanoid; P08047; -.
DR   KO; K04684; -.
DR   OMA; MGIMNFS; -.
DR   OrthoDB; 1085860at2759; -.
DR   PhylomeDB; P08047; -.
DR   TreeFam; TF350150; -.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR   Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   SignaLink; P08047; -.
DR   SIGNOR; P08047; -.
DR   ChiTaRS; SP1; human.
DR   EvolutionaryTrace; P08047; -.
DR   GeneWiki; Sp1_transcription_factor; -.
DR   GenomeRNAi; 6667; -.
DR   Pharos; P08047; Tbio.
DR   PRO; PR:P08047; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P08047; protein.
DR   Bgee; ENSG00000185591; Expressed in 208 organ(s), highest expression level in nipple.
DR   ExpressionAtlas; P08047; baseline and differential.
DR   Genevisible; P08047; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032993; C:protein-DNA complex; ISS:ARUK-UCL.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:CAFA.
DR   GO; GO:0043425; F:bHLH transcription factor binding; ISS:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:CAFA.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:BHF-UCL.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0000987; F:proximal promoter sequence-specific DNA binding; ISS:ARUK-UCL.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:CAFA.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:CAFA.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISS:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:HGNC-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:1904828; P:positive regulation of hydrogen sulfide biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0033194; P:response to hydroperoxide; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0042795; P:snRNA transcription by RNA polymerase II; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   DisProt; DP00378; -.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
DR   PRODOM; P08047.
DR   SWISS-2DPAGE; P08047.
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   Biological rhythms; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Glycoprotein; Host-virus interaction; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692"
FT   CHAIN           2..785
FT                   /note="Transcription factor Sp1"
FT                   /id="PRO_0000047137"
FT   ZN_FING         626..650
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         656..680
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         686..708
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          2..82
FT                   /note="Repressor domain"
FT   REGION          146..251
FT                   /note="Transactivation domain A (Gln-rich)"
FT   REGION          261..495
FT                   /note="Transactivation domain B (Gln-rich)"
FT   REGION          496..610
FT                   /note="Transactivation domain C (highly charged)"
FT   REGION          619..785
FT                   /note="VZV IE62-binding"
FT   REGION          708..785
FT                   /note="Domain D"
FT   MOTIF           462..470
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000269|PubMed:31375868"
FT   COMPBIAS        36..143
FT                   /note="Ser/Thr-rich"
FT   COMPBIAS        271..379
FT                   /note="Ser/Thr-rich"
FT   SITE            63..64
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:18239466"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:16964243,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:17049555,
FT                   ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466"
FT   MOD_RES         101
FT                   /note="Phosphoserine; by ATM"
FT                   /evidence="ECO:0000269|PubMed:18171990,
FT                   ECO:0000269|PubMed:18619531"
FT   MOD_RES         278
FT                   /note="Phosphothreonine; by MAPK8"
FT                   /evidence="ECO:0000305|PubMed:18199680"
FT   MOD_RES         453
FT                   /note="Phosphothreonine; by MAPK1 and MAPK3"
FT                   /evidence="ECO:0000269|PubMed:11904305,
FT                   ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629"
FT   MOD_RES         612
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   MOD_RES         640
FT                   /note="Phosphothreonine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   MOD_RES         641
FT                   /note="Phosphoserine; by PKC/PRKCZ; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679,
FT                   ECO:0000269|PubMed:16943418"
FT   MOD_RES         651
FT                   /note="Phosphothreonine; by PKC/PRKCZ"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         668
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18258854"
FT   MOD_RES         670
FT                   /note="Phosphoserine; by PKC/PRKCZ"
FT                   /evidence="ECO:0000269|PubMed:18258854"
FT   MOD_RES         681
FT                   /note="Phosphothreonine; by PKC/PRKCZ"
FT                   /evidence="ECO:0000269|PubMed:17049555,
FT                   ECO:0000269|PubMed:18258854"
FT   MOD_RES         698
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   MOD_RES         702
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679,
FT                   ECO:0000305|PubMed:20953893"
FT   MOD_RES         703
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:16478997"
FT   MOD_RES         739
FT                   /note="Phosphothreonine; by MAPK1, MAPK3 and MAPK8"
FT                   /evidence="ECO:0000269|PubMed:11904305,
FT                   ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629"
FT   CARBOHYD        491
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000269|PubMed:11371615,
FT                   ECO:0000269|PubMed:9343410"
FT   CARBOHYD        612
FT                   /note="O-linked (GlcNAc) serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   CARBOHYD        640
FT                   /note="O-linked (GlcNAc) threonine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   CARBOHYD        641
FT                   /note="O-linked (GlcNAc) serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   CARBOHYD        698
FT                   /note="O-linked (GlcNAc) serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   CARBOHYD        702
FT                   /note="O-linked (GlcNAc) serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16332679"
FT   CROSSLNK        16
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT   CROSSLNK        16
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         1..7
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053934"
FT   VAR_SEQ         54..101
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:21798247"
FT                   /id="VSP_053935"
FT   VARIANT         737
FT                   /note="T -> A (in dbSNP:rs3741665)"
FT                   /id="VAR_019971"
FT   MUTAGEN         7
FT                   /note="S->A: Increase in protein stability. No change in
FT                   sumoylation."
FT                   /evidence="ECO:0000269|PubMed:18239466"
FT   MUTAGEN         15
FT                   /note="V->R: Enhanced transcriptional activity."
FT   MUTAGEN         16
FT                   /note="K->R: Loss of sumoylation. No cleavage and reduced
FT                   transcriptional activity."
FT                   /evidence="ECO:0000269|PubMed:16407261"
FT   MUTAGEN         18
FT                   /note="E->A: Loss of sumoylation. Increased cleavage and
FT                   enhanced transcriptional activity."
FT                   /evidence="ECO:0000269|PubMed:16407261"
FT   MUTAGEN         19
FT                   /note="K->R: No effect on sumoylation nor on proteolytic
FT                   cleavage."
FT                   /evidence="ECO:0000269|PubMed:16407261"
FT   MUTAGEN         36
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         56
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         59
FT                   /note="S->A: Loss of phosphorylation. No effect on
FT                   activated MAPK8-mediated phosphorylation. Similar loss of
FT                   phosphorylation as by dephosphorylation by PP2AC. Reduced
FT                   proteolytic processing."
FT                   /evidence="ECO:0000269|PubMed:17049555,
FT                   ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466"
FT   MUTAGEN         59
FT                   /note="S->E: Some association with chromatin, increased
FT                   phosphorylation levels and decreased glycosylation."
FT                   /evidence="ECO:0000269|PubMed:17049555,
FT                   ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466"
FT   MUTAGEN         73
FT                   /note="S->A: Little effect on activated MAPK8-mediated
FT                   phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:18199680"
FT   MUTAGEN         81
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         85
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         98
FT                   /note="T->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         101
FT                   /note="S->A: Significant reduction of phosphorylation on
FT                   DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18171990,
FT                   ECO:0000269|PubMed:18619531"
FT   MUTAGEN         101
FT                   /note="S->D: Increase in phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18171990,
FT                   ECO:0000269|PubMed:18619531"
FT   MUTAGEN         117
FT                   /note="T->A: No effect on activated MAPK8-mediated
FT                   phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:18199680"
FT   MUTAGEN         220
FT                   /note="S->A: No effect on dephosphorylation by PP2A."
FT                   /evidence="ECO:0000269|PubMed:17049555"
FT   MUTAGEN         250
FT                   /note="T->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         278
FT                   /note="T->A: Almost complete abolition of activated MAPK8-
FT                   mediated phosphorylation and 40% reduction in protein
FT                   levels during mitosis. Protein levels reduced by 70% during
FT                   mitosis; when associated with A-739."
FT                   /evidence="ECO:0000269|PubMed:18199680"
FT   MUTAGEN         278
FT                   /note="T->D: Increased protein stability during mitosis;
FT                   when associated with D-739."
FT                   /evidence="ECO:0000269|PubMed:18199680"
FT   MUTAGEN         281
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         291
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         296
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         313
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         351
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         355
FT                   /note="T->A: No effect on dephosphorylation by PP2A."
FT                   /evidence="ECO:0000269|PubMed:11904305,
FT                   ECO:0000269|PubMed:17049555"
FT   MUTAGEN         394
FT                   /note="T->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         427
FT                   /note="T->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         431
FT                   /note="S->A: No effect on phosphorylation on DNA damage."
FT                   /evidence="ECO:0000269|PubMed:18619531"
FT   MUTAGEN         453
FT                   /note="T->A: Abolishes MAPK-mediated phosphorylation, 50%
FT                   reduction in MAPK1/MAPK3-mediated activity on VEGF promoter
FT                   and no effect on dephosphorylation by PP2A. Greatly reduced
FT                   MAPK1-mediated activity on VEGF promoter; when associated
FT                   with A-739."
FT                   /evidence="ECO:0000269|PubMed:11904305,
FT                   ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:17049555"
FT   MUTAGEN         491
FT                   /note="S->A: Loss of O-glycosylation. Increase in
FT                   transcriptional activity."
FT                   /evidence="ECO:0000269|PubMed:11371615,
FT                   ECO:0000269|PubMed:9343410"
FT   MUTAGEN         612
FT                   /note="S->A: Diminished glycosylation. Inhibits
FT                   transcriptional activity; when associated with A-640; A-
FT                   641; A-698 and A-702."
FT                   /evidence="ECO:0000269|PubMed:18513490"
FT   MUTAGEN         640
FT                   /note="T->A: Diminished glycosylation. Inhibits
FT                   transcriptional activity; when associated with A-612; A-
FT                   641; A-698 and A-702."
FT                   /evidence="ECO:0000269|PubMed:18513490"
FT   MUTAGEN         641
FT                   /note="S->A: Abolishes PRKCzeta-mediated phosphorylation.
FT                   Diminished glycosylation. Inhibits transcriptional
FT                   activity; when associated with A-612; A-640; A-641 and A-
FT                   702."
FT                   /evidence="ECO:0000269|PubMed:16943418,
FT                   ECO:0000269|PubMed:18513490"
FT   MUTAGEN         651
FT                   /note="T->A: No effect on dephosphorylation by PP2A."
FT                   /evidence="ECO:0000269|PubMed:17049555"
FT   MUTAGEN         668
FT                   /note="T->A: Abolishes PRKCzeta-mediated but not PKCdelta-
FT                   mediated phosphorylation. No effect on DNA binding; when
FT                   associated with A-670 and A-681."
FT                   /evidence="ECO:0000269|PubMed:18258854"
FT   MUTAGEN         670
FT                   /note="S->A: Abolishes PRKCzeta-mediated but not PKCdelta-
FT                   mediated phosphorylation. No effect on DNA binding; when
FT                   associated with A-668 and A-681."
FT                   /evidence="ECO:0000269|PubMed:18258854"
FT   MUTAGEN         681
FT                   /note="T->A: Abolishes PRKCzeta-mediated but not PKCdelta-
FT                   mediated phosphorylation. Some effect on dephosphorylation
FT                   by PP2A. No effect on DNA binding; when associated with A-
FT                   668 and A-681."
FT                   /evidence="ECO:0000269|PubMed:17049555,
FT                   ECO:0000269|PubMed:18258854"
FT   MUTAGEN         698
FT                   /note="S->A: Diminished glycosylation. Inhibits
FT                   transcriptional activity; when associated with A-612; A-
FT                   640; A-641 and A-702."
FT                   /evidence="ECO:0000269|PubMed:18513490"
FT   MUTAGEN         702
FT                   /note="S->A: Diminished glycosylation. Inhibits
FT                   transcriptional activity; when associated with A-612; A-
FT                   640; A-641 and A-698."
FT                   /evidence="ECO:0000269|PubMed:18513490"
FT   MUTAGEN         703
FT                   /note="K->A: Abolishes acetylation. Increases recruitment
FT                   of p300 to the promoter and enhances gene transcription."
FT                   /evidence="ECO:0000269|PubMed:16478997"
FT   MUTAGEN         728
FT                   /note="S->A: Exhibits attenuated endoproteolytic cleavage;
FT                   when associated with A-732."
FT                   /evidence="ECO:0000269|PubMed:18239466"
FT   MUTAGEN         732
FT                   /note="S->A: Exhibits attenuated endoproteolytic cleavage;
FT                   when associated with A-728."
FT                   /evidence="ECO:0000269|PubMed:18239466"
FT   MUTAGEN         739
FT                   /note="T->A: Abolishes MAPK-mediated phosphorylation. 50%
FT                   reduction in MAPK1/MAPK3-mediated activity on VEGF
FT                   promoter, 40% reduction in protein levels during mitosis
FT                   and no effect on dephosphorylation by PP2A. Greatly reduced
FT                   MAPK1-mediated activity on VEGF promoter; when associated
FT                   with A-453. Protein levels during mitosis reduced by 70%;
FT                   when associated with A-278."
FT                   /evidence="ECO:0000269|PubMed:11904305,
FT                   ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:17049555,
FT                   ECO:0000269|PubMed:18199680"
FT   MUTAGEN         739
FT                   /note="T->D: Increased protein stability during mitosis;
FT                   when associated with D-278."
FT                   /evidence="ECO:0000269|PubMed:11904305,
FT                   ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:17049555,
FT                   ECO:0000269|PubMed:18199680"
FT   CONFLICT        366
FT                   /note="D -> G (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        670
FT                   /note="S -> F (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          620..622
FT                   /evidence="ECO:0000244|PDB:1VA1"
FT   STRAND          636..638
FT                   /evidence="ECO:0000244|PDB:1VA1"
FT   HELIX           640..651
FT                   /evidence="ECO:0000244|PDB:1VA1"
FT   TURN            661..663
FT                   /evidence="ECO:0000244|PDB:1VA2"
FT   STRAND          666..668
FT                   /evidence="ECO:0000244|PDB:1VA2"
FT   HELIX           670..677
FT                   /evidence="ECO:0000244|PDB:1SP2"
FT   TURN            678..680
FT                   /evidence="ECO:0000244|PDB:1SP2"
FT   TURN            689..692
FT                   /evidence="ECO:0000244|PDB:1SP1"
FT   HELIX           699..706
FT                   /evidence="ECO:0000244|PDB:1SP1"
FT   HELIX           707..709
FT                   /evidence="ECO:0000244|PDB:1SP1"
SQ   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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