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 24-JAN-2024, entry version 260.
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 INTERACTION WITH DDX3X.
RX PubMed=16818630; DOI=10.1158/0008-5472.can-05-2415;
RA Chao C.H., Chen C.M., Cheng P.L., Shih J.W., Tsou A.P., Lee Y.H.;
RT "DDX3, a DEAD box RNA helicase with tumor growth-suppressive property and
RT transcriptional regulation activity of the p21waf1/cip1 promoter, is a
RT candidate tumor suppressor.";
RL Cancer Res. 66:6579-6588(2006).
RN [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
RP ERRATUM OF PUBMED:16943418.
RA Zhang Y., Liao M., Dufau M.L.;
RL Mol. Cell. Biol. 26:8214-8214(2006).
RN [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
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. 77:1793-1810(2020).
RN [59]
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 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). Interacts with
CC DDX3X; this interaction potentiates SP1-induced CDKN1A/WAF1/CIP1
CC transcription (PubMed:16818630). Interacts with MSX1; the interaction
CC may inhibit MSX1 autoinactivation (By similarity).
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:16818630, ECO:0000269|PubMed:19106100,
CC ECO:0000269|PubMed:19285002, ECO:0000269|PubMed:19302979,
CC ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:20121949,
CC 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 P08047; Q9NY61: AATF; NbExp=2; IntAct=EBI-298336, EBI-372428;
CC P08047; Q8N726: CDKN2A; NbExp=4; IntAct=EBI-298336, EBI-625922;
CC P08047; Q92988: DLX4; NbExp=4; IntAct=EBI-298336, EBI-1752755;
CC P08047; Q01094: E2F1; NbExp=2; IntAct=EBI-298336, EBI-448924;
CC P08047; P32519: ELF1; NbExp=2; IntAct=EBI-298336, EBI-765526;
CC P08047; Q99814: EPAS1; NbExp=2; IntAct=EBI-298336, EBI-447470;
CC P08047; P03372: ESR1; NbExp=2; IntAct=EBI-298336, EBI-78473;
CC P08047; P51610: HCFC1; NbExp=4; IntAct=EBI-298336, EBI-396176;
CC P08047; Q13547: HDAC1; NbExp=2; IntAct=EBI-298336, EBI-301834;
CC P08047; Q16665: HIF1A; NbExp=3; IntAct=EBI-298336, EBI-447269;
CC P08047; Q13118: KLF10; NbExp=2; IntAct=EBI-298336, EBI-1389509;
CC P08047; P01106: MYC; NbExp=4; IntAct=EBI-298336, EBI-447544;
CC P08047; P16333: NCK1; NbExp=2; IntAct=EBI-298336, EBI-389883;
CC P08047; Q8IXK0: PHC2; NbExp=2; IntAct=EBI-298336, EBI-713786;
CC P08047; Q7Z3K3: POGZ; NbExp=2; IntAct=EBI-298336, EBI-1389308;
CC P08047; P14859: POU2F1; NbExp=7; IntAct=EBI-298336, EBI-624770;
CC P08047; Q06455: RUNX1T1; NbExp=2; IntAct=EBI-298336, EBI-743342;
CC P08047; Q15459: SF3A1; NbExp=2; IntAct=EBI-298336, EBI-1054743;
CC P08047; Q13485: SMAD4; NbExp=2; IntAct=EBI-298336, EBI-347263;
CC P08047; P08047: SP1; NbExp=2; IntAct=EBI-298336, EBI-298336;
CC P08047; Q12772: SREBF2; NbExp=3; IntAct=EBI-298336, EBI-465059;
CC P08047; P40763: STAT3; NbExp=4; IntAct=EBI-298336, EBI-518675;
CC P08047; Q9UL17: TBX21; NbExp=4; IntAct=EBI-298336, EBI-3922312;
CC P08047; P04637: TP53; NbExp=3; IntAct=EBI-298336, EBI-366083;
CC P08047; Q8N680: ZBTB2; NbExp=4; IntAct=EBI-298336, EBI-2515601;
CC P08047; P23708: Nfya; Xeno; NbExp=18; IntAct=EBI-298336, EBI-862337;
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDB; 6PV0; NMR; -; A=654-684.
DR PDB; 6PV1; NMR; -; A=654-684.
DR PDB; 6PV2; NMR; -; A=654-684.
DR PDB; 6PV3; NMR; -; A=655-684.
DR PDB; 6UCO; NMR; -; A=654-684.
DR PDB; 6UCP; NMR; -; A=654-684.
DR PDBsum; 1SP1; -.
DR PDBsum; 1SP2; -.
DR PDBsum; 1VA1; -.
DR PDBsum; 1VA2; -.
DR PDBsum; 1VA3; -.
DR PDBsum; 6PV0; -.
DR PDBsum; 6PV1; -.
DR PDBsum; 6PV2; -.
DR PDBsum; 6PV3; -.
DR PDBsum; 6UCO; -.
DR PDBsum; 6UCP; -.
DR AlphaFoldDB; P08047; -.
DR BMRB; P08047; -.
DR SMR; P08047; -.
DR BioGRID; 112550; 341.
DR CORUM; P08047; -.
DR DIP; DIP-36N; -.
DR ELM; P08047; -.
DR IntAct; P08047; 120.
DR MINT; P08047; -.
DR STRING; 9606.ENSP00000329357; -.
DR BindingDB; P08047; -.
DR ChEMBL; CHEMBL6103; -.
DR GlyConnect; 605; 1 O-GlcNAc glycan.
DR GlyCosmos; P08047; 25 sites, 2 glycans.
DR GlyGen; P08047; 26 sites, 2 O-linked glycans (26 sites).
DR iPTMnet; P08047; -.
DR PhosphoSitePlus; P08047; -.
DR BioMuta; SP1; -.
DR DMDM; 13638437; -.
DR EPD; P08047; -.
DR jPOST; P08047; -.
DR MassIVE; P08047; -.
DR MaxQB; P08047; -.
DR PaxDb; 9606-ENSP00000329357; -.
DR PeptideAtlas; P08047; -.
DR ProteomicsDB; 33987; -.
DR ProteomicsDB; 52061; -. [P08047-1]
DR Pumba; P08047; -.
DR Antibodypedia; 892; 1267 antibodies from 47 providers.
DR DNASU; 6667; -.
DR Ensembl; ENST00000327443.9; ENSP00000329357.4; ENSG00000185591.10. [P08047-1]
DR Ensembl; ENST00000426431.2; ENSP00000404263.2; ENSG00000185591.10. [P08047-2]
DR GeneID; 6667; -.
DR KEGG; hsa:6667; -.
DR MANE-Select; ENST00000327443.9; ENSP00000329357.4; NM_138473.3; NP_612482.2.
DR UCSC; uc001scw.4; human. [P08047-1]
DR AGR; HGNC:11205; -.
DR CTD; 6667; -.
DR DisGeNET; 6667; -.
DR GeneCards; SP1; -.
DR HGNC; HGNC:11205; SP1.
DR HPA; ENSG00000185591; Low tissue specificity.
DR MIM; 189906; gene.
DR neXtProt; NX_P08047; -.
DR OpenTargets; ENSG00000185591; -.
DR PharmGKB; PA36042; -.
DR VEuPathDB; HostDB:ENSG00000185591; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157804; -.
DR HOGENOM; CLU_019688_2_0_1; -.
DR InParanoid; P08047; -.
DR OMA; NWSFCGK; -.
DR OrthoDB; 5396935at2759; -.
DR PhylomeDB; P08047; -.
DR TreeFam; TF350150; -.
DR PathwayCommons; P08047; -.
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 Reactome; R-HSA-9735871; SARS-CoV-1 targets host intracellular signalling and regulatory pathways.
DR Reactome; R-HSA-9762293; Regulation of CDH11 gene transcription.
DR Reactome; R-HSA-9818030; NFE2L2 regulating tumorigenic genes.
DR SignaLink; P08047; -.
DR SIGNOR; P08047; -.
DR BioGRID-ORCS; 6667; 167 hits in 1197 CRISPR screens.
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 nipple and 188 other cell types or tissues.
DR ExpressionAtlas; P08047; baseline and differential.
DR Genevisible; P08047; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000791; C:euchromatin; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0032993; C:protein-DNA complex; ISS:ARUK-UCL.
DR GO; GO:0017053; C:transcription 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:ARUK-UCL.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:HGNC-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:1904568; P:cellular response to wortmannin; IEA:Ensembl.
DR GO; GO:0034224; P:cellular response to zinc ion starvation; IEA:Ensembl.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IMP:ARUK-UCL.
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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
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:1905564; P:positive regulation of vascular endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033194; P:response to hydroperoxide; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd22539; SP1_N; 1.
DR DisProt; DP00378; -.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR IDEAL; IID00266; -.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR23235:SF16; TRANSCRIPTION FACTOR SP1; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
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; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|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 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..82
FT /note="Repressor domain"
FT REGION 109..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..251
FT /note="Transactivation domain A (Gln-rich)"
FT REGION 261..495
FT /note="Transactivation domain B (Gln-rich)"
FT REGION 329..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..610
FT /note="Transactivation domain C (highly charged)"
FT REGION 567..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 29..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 63..64
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18239466,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17049555,
FT ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:23186163"
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:0007744|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:0007744|PubMed:25218447,
FT ECO:0007744|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:0007829|PDB:1VA1"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:1VA1"
FT HELIX 640..651
FT /evidence="ECO:0007829|PDB:1VA1"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:6UCO"
FT TURN 661..663
FT /evidence="ECO:0007829|PDB:1VA2"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:1VA2"
FT HELIX 670..677
FT /evidence="ECO:0007829|PDB:1SP2"
FT TURN 678..680
FT /evidence="ECO:0007829|PDB:1SP2"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:6PV0"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:1SP1"
FT HELIX 699..706
FT /evidence="ECO:0007829|PDB:1SP1"
FT HELIX 707..709
FT /evidence="ECO:0007829|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
//
