Menu
Home
People
Places
Arts
History
Plants & Animals
Science
Life & Culture
Technology
Reference.org
Activating transcription factor 2
open-in-new
<h2 id="function">Function</h2> <p>This gene encodes a <a href="/facts/Transcription_factor/wro0DPHe">transcription factor</a> that is a member of the <a href="/facts/Leucine_zipper/tlAMv6Ul">leucine zipper</a> family of DNA-binding proteins. This protein binds to the <a href="/facts/CREB/ug1kE9j0">cAMP-responsive element</a> (CRE), an octameric palindrome. The protein forms a homodimer or heterodimer with <a href="/facts/C-Jun/Cbvb15yT">c-Jun</a>. The protein is also a <a href="/facts/Histone_acetyltransferase/gIzJY5fn">histone acetyltransferase</a> (HAT) that specifically acetylates histones H2B and H4 in vitro; thus, it may represent a class of sequence-specific factors that activate transcription by direct effects on <a href="/facts/Chromatin/ha0TJheJ">chromatin</a> components. Additional transcript variants have been identified but their biological validity has not been determined.<a class="footnote-ref" id="fnref:2" href="#fn:2"><sup>2</sup></a> </p><p>The gene atf2 is located at human chromosome 2q32.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> The protein ATF-2 has 505 amino acids. Studies in mice indicate a role for ATF-2 in the development of nervous system and the skeleton.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> ATF-2 is normally activated in response to signals that converge on <a href="/facts/P38_mitogen-activated_protein_kinases/oodDxsQK">stress-activated protein kinases p38</a> and <a href="/facts/JNK/Ckax9edE">JNK</a>.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> ATF-2 phosphorylation in response to treatment of cells with tumor promoter <a href="/facts/Phorbol/u8Su5FTc">phorbol</a> ester has been demonstrated.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p><p>Several studies implicate abnormal activation of ATF-2 in growth and progression of mammalian skin tumors.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a><a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> ATF-2 may mediate oncogenesis caused by mutant <a href="/facts/Ras_protein/JB883YoM">Ras protein</a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> and regulate maintenance of the aggressive cancer phenotype of some types of epithelial cells. </p><p>ATF2 has also been shown to be <a href="/facts/Phosphorylation/LXUEEeIL">phosphorylated</a> at its <a href="/facts/C-terminus/ws4scHgT">C-terminal</a> (serine 472 and 480 in mouse; serine 490 and 498 in human) by <a href="/facts/Ataxia_telangiectasia_mutated/oBMxx2Y7">ATM</a> upon <a href="/facts/DNA_repair/hsURuYYq">double-stranded breaks</a>.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> Mice with mutations of these two serines are sensitive to irradiation and easier to tumorigenesis under p53 knockout background. </p> <h2 id="interactions">Interactions</h2> <p>Activating transcription factor 2 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with </p> <ul><li><a href="/facts/C-jun/Cbvb15yT">C-jun</a>,<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a><a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a></li> <li><a href="/facts/Casein_kinase_2%2c_alpha_1/kfnSXaUM">Casein kinase 2, alpha 1</a>,<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a></li> <li><a href="/facts/CREB_binding_protein/F4p9VIV7">CREB binding protein</a>,<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a></li> <li><a href="/facts/CSNK2A2/sJRy4olM">CSNK2A2</a>,<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a></li> <li><a href="/facts/JDP2_(gene)/kEqc5r1e">JDP2</a>,<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a></li> <li><a href="/facts/MAPK14/uMXodaVC">MAPK14</a>,<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a><a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a><a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a></li> <li><a href="/facts/MAPK8/fbUM7qyf">MAPK8</a>,<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a><a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a><a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a><a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a></li> <li><a href="/facts/Mothers_against_decapentaplegic_homolog_3/6j6Go6va">Mothers against decapentaplegic homolog 3</a><a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a></li> <li><a href="/facts/NCOA6/zqUpCwbH">NCOA6</a>,<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a></li> <li><a href="/facts/RUVBL2/nhIUsckX">RUVBL2</a>,<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a></li> <li><a href="/facts/UBE2I/tJYXLkrl">UBE2I</a>.<a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a></li></ul> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Activating_transcription_factor/csSC8Q5S">Activating transcription factor</a></li></ul> <h2 id="external-links">External links</h2> <ul><li>Human <a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=ATF2"><i>ATF2</i></a> genome location and <a href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=ATF2"><i>ATF2</i></a> gene details page in the <a href="/facts/UCSC_Genome_Browser/kwumPyLb">UCSC Genome Browser</a>.</li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Denys H, Desmet R, Stragier M, Vergison R, Lemahieu SF (1977). "Cystitis emphysematosa". <i>Acta Urol Belg</i>. 45 (4): 327–31. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/602896">602896</a>.</li> <li>Kim SJ, Wagner S, Liu F, O'Reilly MA, Robbins PD, Green MR (1992). "Retinoblastoma gene product activates expression of the human TGF-beta 2 gene through transcription factor ATF-2". <i>Nature</i>. 358 (6384): 331–4. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1992Natur.358..331K">1992Natur.358..331K</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F358331a0">10.1038/358331a0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1641004">1641004</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:9770957">9770957</a>.</li> <li>Hai T, Curran T (1991). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC51524">"Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 88 (9): 3720–4. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1991PNAS...88.3720H">1991PNAS...88.3720H</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.88.9.3720">10.1073/pnas.88.9.3720</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC51524">51524</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1827203">1827203</a>.</li> <li>Hoeffler JP, Lustbader JW, Chen CY (1991). <a href="https://doi.org/10.1210%2Fmend-5-2-256">"Identification of multiple nuclear factors that interact with cyclic adenosine 3',5'-monophosphate response element-binding protein and activating transcription factor-2 by protein-protein interactions"</a>. <i>Mol. Endocrinol</i>. 5 (2): 256–66. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1210%2Fmend-5-2-256">10.1210/mend-5-2-256</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1828107">1828107</a>.</li> <li>Ozawa K, Sudo T, Soeda E, Yoshida MC, Ishii S (1991). "Assignment of the human CREB2 (CRE-BP1) gene to 2q32". <i>Genomics</i>. 10 (4): 1103–4. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0888-7543%2891%2990210-6">10.1016/0888-7543(91)90210-6</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1833307">1833307</a>.</li> <li>Diep A, Li C, Klisak I, Mohandas T, Sparkes RS, Gaynor R, Lusis AJ (1991). "Assignment of the gene for cyclic AMP-response element binding protein 2 (CREB2) to human chromosome 2q24.1-q32". <i>Genomics</i>. 11 (4): 1161–3. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0888-7543%2891%2990047-I">10.1016/0888-7543(91)90047-I</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1838349">1838349</a>.</li> <li>Kara CJ, Liou HC, Ivashkiv LB, Glimcher LH (1990). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362236">"A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain"</a>. <i>Mol. Cell. Biol</i>. 10 (4): 1347–57. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FMCB.10.4.1347">10.1128/MCB.10.4.1347</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362236">362236</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2320002">2320002</a>.</li> <li>Gonzalez GA, Yamamoto KK, Fischer WH, Karr D, Menzel P, Biggs W, Vale WW, Montminy MR (1989). "A cluster of phosphorylation sites on the cyclic AMP-regulated nuclear factor CREB predicted by its sequence". <i>Nature</i>. 337 (6209): 749–52. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1989Natur.337..749G">1989Natur.337..749G</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F337749a0">10.1038/337749a0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2521922">2521922</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4345950">4345950</a>.</li> <li>Maekawa T, Sakura H, Kanei-Ishii C, Sudo T, Yoshimura T, Fujisawa J, Yoshida M, Ishii S (1989). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC401081">"Leucine zipper structure of the protein CRE-BP1 binding to the cyclic AMP response element in brain"</a>. <i>EMBO J</i>. 8 (7): 2023–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fj.1460-2075.1989.tb03610.x">10.1002/j.1460-2075.1989.tb03610.x</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC401081">401081</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2529117">2529117</a>.</li> <li>Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ (1995). <a href="https://doi.org/10.1074%2Fjbc.270.13.7420">"Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine"</a>. <i>J. Biol. Chem</i>. 270 (13): 7420–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.270.13.7420">10.1074/jbc.270.13.7420</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7535770">7535770</a>.</li> <li>Livingstone C, Patel G, Jones N (1995). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398272">"ATF-2 contains a phosphorylation-dependent transcriptional activation domain"</a>. <i>EMBO J</i>. 14 (8): 1785–97. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fj.1460-2075.1995.tb07167.x">10.1002/j.1460-2075.1995.tb07167.x</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398272">398272</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7737129">7737129</a>.</li> <li>van Dam H, Wilhelm D, Herr I, Steffen A, Herrlich P, Angel P (1995). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398273">"ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents"</a>. <i>EMBO J</i>. 14 (8): 1798–811. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fj.1460-2075.1995.tb07168.x">10.1002/j.1460-2075.1995.tb07168.x</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398273">398273</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7737130">7737130</a>.</li> <li>Zhou Q, Gedrich RW, Engel DA (1995). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC189172">"Transcriptional repression of the c-fos gene by YY1 is mediated by a direct interaction with ATF/CREB"</a>. <i>J. Virol</i>. 69 (7): 4323–30. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FJVI.69.7.4323-4330.1995">10.1128/JVI.69.7.4323-4330.1995</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC189172">189172</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7769693">7769693</a>.</li> <li>Newell CL, Deisseroth AB, Lopez-Berestein G (1994). "Interaction of nuclear proteins with an AP-1/CRE-like promoter sequence in the human TNF-alpha gene". <i>J. Leukoc. Biol</i>. 56 (1): 27–35. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fjlb.56.1.27">10.1002/jlb.56.1.27</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8027667">8027667</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:85570533">85570533</a>.</li> <li>Nomura N, Zu YL, Maekawa T, Tabata S, Akiyama T, Ishii S (1993). <a href="https://doi.org/10.1016%2FS0021-9258%2818%2953604-8">"Isolation and characterization of a novel member of the gene family encoding the cAMP response element-binding protein CRE-BP1"</a>. <i>J. Biol. Chem</i>. 268 (6): 4259–66. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2818%2953604-8">10.1016/S0021-9258(18)53604-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8440710">8440710</a>.</li> <li>Martin ML, Lieberman PM, Curran T (1996). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231198">"Fos-Jun dimerization promotes interaction of the basic region with TFIIE-34 and TFIIF"</a>. <i>Mol. Cell. Biol</i>. 16 (5): 2110–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2Fmcb.16.5.2110">10.1128/mcb.16.5.2110</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC231198">231198</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8628277">8628277</a>.</li> <li>Yang L, Lanier ER, Kraig E (1997). <a href="https://doi.org/10.4049%2Fjimmunol.158.6.2522">"Identification of a novel, spliced variant of CREB that is preferentially expressed in the thymus"</a>. <i>J. Immunol</i>. 158 (6): 2522–5. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.4049%2Fjimmunol.158.6.2522">10.4049/jimmunol.158.6.2522</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9058782">9058782</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:29299351">29299351</a>.</li> <li>Shuman JD, Cheong J, Coligan JE (1997). <a href="https://doi.org/10.1074%2Fjbc.272.19.12793">"ATF-2 and C/EBPalpha can form a heterodimeric DNA binding complex in vitro. Functional implications for transcriptional regulation"</a>. <i>J. Biol. Chem</i>. 272 (19): 12793–800. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.272.19.12793">10.1074/jbc.272.19.12793</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9139739">9139739</a>.</li> <li>Fukunaga R, Hunter T (1997). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1169795">"MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates"</a>. <i>EMBO J</i>. 16 (8): 1921–33. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Femboj%2F16.8.1921">10.1093/emboj/16.8.1921</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1169795">1169795</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9155018">9155018</a>.</li> <li>Kumar S, McDonnell PC, Gum RJ, Hand AT, Lee JC, Young PR (1997). "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles". <i>Biochem. Biophys. Res. Commun</i>. 235 (3): 533–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fbbrc.1997.6849">10.1006/bbrc.1997.6849</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9207191">9207191</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P15336">PDBe-KB</a> provides an overview of all the structure information available in the PDB for Human Cyclic AMP-dependent transcription factor ATF-2</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>"Entrez Gene: ATF2 activating transcription factor 2". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1386" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1386</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>"Entrez Gene: ATF2 activating transcription factor 2". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1386" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1386</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Ozawa K, Sudo T, Soeda E, Yoshida MC, Ishii S (1991). "Assignment of the human CREB2 (CRE-BP1) gene to 2q32". Genomics. 10 (4): 1103–4. doi:10.1016/0888-7543(91)90210-6. PMID 1833307. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Reimold AM, Grusby MJ, Kosaras B, Fries JW, Mori R, Maniwa S, Clauss IM, Collins T, Sidman RL, Glimcher MJ, Glimcher LH (1996). "Chondrodysplasia and neurological abnormalities in ATF-2-deficient mice". Nature. 379 (6562): 262–5. Bibcode:1996Natur.379..262R. doi:10.1038/379262a0. PMID 8538792. S2CID 4326412. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Gupta S, Campbell D, Dérijard B, Davis RJ (1995). "Transcription factor ATF2 regulation by the JNK signal transduction pathway". Science. 267 (5196): 389–93. Bibcode:1995Sci...267..389G. doi:10.1126/science.7824938. PMID 7824938. S2CID 40268838. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Yamasaki T, Takahashi A, Pan J, Yamaguchi N, Yokoyama KK (March 2009). "Phosphorylation of Activation Transcription Factor-2 at Serine 121 by Protein Kinase C Controls c-Jun-mediated Activation of Transcription". J. Biol. Chem. 284 (13): 8567–81. doi:10.1074/jbc.M808719200. PMC 2659215. PMID 19176525. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2659215" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2659215</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Leslie MC, Bar-Eli M (2005). "Regulation of gene expression in melanoma: new approaches for treatment". J. Cell. Biochem. 94 (1): 25–38. doi:10.1002/jcb.20296. PMID 15523674. S2CID 23515325. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Papassava P, Gorgoulis VG, Papaevangeliou D, Vlahopoulos S, van Dam H, Zoumpourlis V (2004). "Overexpression of activating transcription factor-2 is required for tumor growth and progression in mouse skin tumors". Cancer Res. 64 (23): 8573–84. doi:10.1158/0008-5472.CAN-03-0955. PMID 15574764. S2CID 14845890. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Vlahopoulos SA, Logotheti S, Mikas D, Giarika A, Gorgoulis V, Zoumpourlis V (17 March 2008). "The role of ATF-2 in oncogenesis". BioEssays. 30 (4): 314–27. doi:10.1002/bies.20734. PMID 18348191. S2CID 678541. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Bhoumik A, Takahashi S, Breitweiser W, Shiloh Y, Jones N, Ronai Z (May 2005). "ATM-dependent phosphorylation of ATF2 is required for the DNA damage response". Mol. Cell. 18 (5): 577–87. doi:10.1016/j.molcel.2005.04.015. PMC 2954254. PMID 15916964. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954254" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954254</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Newell CL, Deisseroth AB, Lopez-Berestein G (July 1994). "Interaction of nuclear proteins with an AP-1/CRE-like promoter sequence in the human TNF-alpha gene". J. Leukoc. Biol. 56 (1): 27–35. doi:10.1002/jlb.56.1.27. PMID 8027667. S2CID 85570533. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>Kara CJ, Liou HC, Ivashkiv LB, Glimcher LH (April 1990). "A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain". Mol. Cell. Biol. 10 (4): 1347–57. doi:10.1128/MCB.10.4.1347. PMC 362236. PMID 2320002. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362236" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC362236</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>Hai T, Curran T (May 1991). "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity". Proc. Natl. Acad. Sci. U.S.A. 88 (9): 3720–4. Bibcode:1991PNAS...88.3720H. doi:10.1073/pnas.88.9.3720. PMC 51524. PMID 1827203. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC51524" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC51524</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> <li id="fn:14"><p>Yamaguchi Y, Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (August 1998). "Casein kinase II interacts with the bZIP domains of several transcription factors". Nucleic Acids Res. 26 (16): 3854–61. doi:10.1093/nar/26.16.3854. PMC 147779. PMID 9685505. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC147779" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC147779</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></p></li> <li id="fn:15"><p>Sano Y, Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (October 1998). "CBP alleviates the intramolecular inhibition of ATF-2 function". J. Biol. Chem. 273 (44): 29098–105. doi:10.1074/jbc.273.44.29098. PMID 9786917. <a href="https://doi.org/10.1074%2Fjbc.273.44.29098" target="_blank">https://doi.org/10.1074%2Fjbc.273.44.29098</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></p></li> <li id="fn:16"><p>Yamaguchi Y, Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (August 1998). "Casein kinase II interacts with the bZIP domains of several transcription factors". Nucleic Acids Res. 26 (16): 3854–61. doi:10.1093/nar/26.16.3854. PMC 147779. PMID 9685505. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC147779" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC147779</a> <a href="#fnref:16" class="footnote-back-ref">↩</a></p></li> <li id="fn:17"><p>Murata T, Shinozuka Y, Obata Y, Yokoyama KK (May 2008). "Phosphorylation of two eukaryotic transcription factors, Jun dimerization protein 2 and activation transcription factor 2, in Escherichia coli by Jun N-terminal kinase 1". Anal. Biochem. 376 (1): 115–21. doi:10.1016/j.ab.2008.01.038. PMID 18307971. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:17" class="footnote-back-ref">↩</a></p></li> <li id="fn:18"><p>Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ (March 1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine". J. Biol. Chem. 270 (13): 7420–6. doi:10.1074/jbc.270.13.7420. PMID 7535770. <a href="https://doi.org/10.1074%2Fjbc.270.13.7420" target="_blank">https://doi.org/10.1074%2Fjbc.270.13.7420</a> <a href="#fnref:18" class="footnote-back-ref">↩</a></p></li> <li id="fn:19"><p>Chen Z, Cobb MH (May 2001). "Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2". J. Biol. Chem. 276 (19): 16070–5. doi:10.1074/jbc.M100681200. PMID 11279118. <a href="https://doi.org/10.1074%2Fjbc.M100681200" target="_blank">https://doi.org/10.1074%2Fjbc.M100681200</a> <a href="#fnref:19" class="footnote-back-ref">↩</a></p></li> <li id="fn:20"><p>Tournier C, Whitmarsh AJ, Cavanagh J, Barrett T, Davis RJ (July 1997). "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase". Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7337–42. Bibcode:1997PNAS...94.7337T. doi:10.1073/pnas.94.14.7337. PMC 23822. PMID 9207092. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23822" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23822</a> <a href="#fnref:20" class="footnote-back-ref">↩</a></p></li> <li id="fn:21"><p>Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ (March 1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine". J. Biol. Chem. 270 (13): 7420–6. doi:10.1074/jbc.270.13.7420. PMID 7535770. <a href="https://doi.org/10.1074%2Fjbc.270.13.7420" target="_blank">https://doi.org/10.1074%2Fjbc.270.13.7420</a> <a href="#fnref:21" class="footnote-back-ref">↩</a></p></li> <li id="fn:22"><p>Chen Z, Cobb MH (May 2001). "Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2". J. Biol. Chem. 276 (19): 16070–5. doi:10.1074/jbc.M100681200. PMID 11279118. <a href="https://doi.org/10.1074%2Fjbc.M100681200" target="_blank">https://doi.org/10.1074%2Fjbc.M100681200</a> <a href="#fnref:22" class="footnote-back-ref">↩</a></p></li> <li id="fn:23"><p>Tournier C, Whitmarsh AJ, Cavanagh J, Barrett T, Davis RJ (July 1997). "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase". Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7337–42. Bibcode:1997PNAS...94.7337T. doi:10.1073/pnas.94.14.7337. PMC 23822. PMID 9207092. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23822" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23822</a> <a href="#fnref:23" class="footnote-back-ref">↩</a></p></li> <li id="fn:24"><p>Fuchs SY, Xie B, Adler V, Fried VA, Davis RJ, Ronai Z (December 1997). "c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors". J. Biol. Chem. 272 (51): 32163–8. doi:10.1074/jbc.272.51.32163. PMID 9405416. <a href="https://doi.org/10.1074%2Fjbc.272.51.32163" target="_blank">https://doi.org/10.1074%2Fjbc.272.51.32163</a> <a href="#fnref:24" class="footnote-back-ref">↩</a></p></li> <li id="fn:25"><p>Sano Y, Harada J, Tashiro S, Gotoh-Mandeville R, Maekawa T, Ishii S (March 1999). "ATF-2 is a common nuclear target of Smad and TAK1 pathways in transforming growth factor-beta signaling". J. Biol. Chem. 274 (13): 8949–57. doi:10.1074/jbc.274.13.8949. PMID 10085140. <a href="https://doi.org/10.1074%2Fjbc.274.13.8949" target="_blank">https://doi.org/10.1074%2Fjbc.274.13.8949</a> <a href="#fnref:25" class="footnote-back-ref">↩</a></p></li> <li id="fn:26"><p>Hong S, Choi HM, Park MJ, Kim YH, Choi YH, Kim HH, Choi YH, Cheong J (April 2004). "Activation and interaction of ATF2 with the coactivator ASC-2 are responsive for granulocytic differentiation by retinoic acid". J. Biol. Chem. 279 (17): 16996–7003. doi:10.1074/jbc.M311752200. PMID 14734562. <a href="https://doi.org/10.1074%2Fjbc.M311752200" target="_blank">https://doi.org/10.1074%2Fjbc.M311752200</a> <a href="#fnref:26" class="footnote-back-ref">↩</a></p></li> <li id="fn:27"><p>Cho SG, Bhoumik A, Broday L, Ivanov V, Rosenstein B, Ronai Z (December 2001). "TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage". Mol. Cell. Biol. 21 (24): 8398–413. doi:10.1128/MCB.21.24.8398-8413.2001. PMC 100004. PMID 11713276. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC100004" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC100004</a> <a href="#fnref:27" class="footnote-back-ref">↩</a></p></li> <li id="fn:28"><p>Firestein R, Feuerstein N (March 1998). "Association of activating transcription factor 2 (ATF2) with the ubiquitin-conjugating enzyme hUBC9. Implication of the ubiquitin/proteasome pathway in regulation of ATF2 in T cells". J. Biol. Chem. 273 (10): 5892–902. doi:10.1074/jbc.273.10.5892. PMID 9488727. <a href="https://doi.org/10.1074%2Fjbc.273.10.5892" target="_blank">https://doi.org/10.1074%2Fjbc.273.10.5892</a> <a href="#fnref:28" class="footnote-back-ref">↩</a></p></li> </ol>