ATF7_HUMAN
ID ATF7_HUMAN Reviewed; 483 AA.
AC P17544; A5D6Y4; B2RMP1; B4DQL4; Q13814; Q8IVR8; Q9UD83;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-7;
DE Short=cAMP-dependent transcription factor ATF-7;
DE AltName: Full=Activating transcription factor 7;
DE AltName: Full=Transcription factor ATF-A;
GN Name=ATF7; Synonyms=ATFA;
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] (ISOFORMS 2 AND 3).
RC TISSUE=Cervix carcinoma;
RX PubMed=1694576; DOI=10.1093/nar/18.12.3467;
RA Gaire M., Chatton B., Kedinger C.;
RT "Isolation and characterization of two novel, closely related ATF cDNA
RT clones from HeLa cells.";
RL Nucleic Acids Res. 18:3467-3473(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RA Chatton B., Gaire M., Goetz J., Hauss C., Kedinger C.;
RT "ATF-a1, a new member of the human ATF family.";
RL Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBUNIT.
RC TISSUE=Cervix carcinoma;
RX PubMed=8288576; DOI=10.1016/s0021-9258(17)42236-8;
RA Pescini R., Kaszubska W., Whelan J., DeLamarter J.F.,
RA Hooft van Huijsduijnen R.;
RT "ATF-a0, a novel variant of the ATF/CREB transcription factor family, forms
RT a dominant transcription inhibitor in ATF-a heterodimers.";
RL J. Biol. Chem. 269:1159-1165(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain, and Colon;
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 [8]
RP SUBUNIT, AND FUNCTION.
RX PubMed=1827203; DOI=10.1073/pnas.88.9.3720;
RA Hai T., Curran T.;
RT "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB
RT alters DNA binding specificity.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3720-3724(1991).
RN [9]
RP INTERACTION WITH HUMAN ADENOVIRUS 2 E1A (MICROBIAL INFECTION),
RP ZINC-BINDING, AND MUTAGENESIS OF ASP-22 AND HIS-27.
RX PubMed=8417352; DOI=10.1128/mcb.13.1.561-570.1993;
RA Chatton B., Bocco J.L., Gaire M., Hauss C., Reimund B., Goetz J.,
RA Kedinger C.;
RT "Transcriptional activation by the adenovirus larger E1a product is
RT mediated by members of the cellular transcription factor ATF family which
RT can directly associate with E1a.";
RL Mol. Cell. Biol. 13:561-570(1993).
RN [10]
RP SUBUNIT.
RX PubMed=8290251;
RA Chatton B., Bocco J.L., Goetz J., Gaire M., Lutz Y., Kedinger C.;
RT "Jun and Fos heterodimerize with ATFa, a member of the ATF/CREB family and
RT modulate its transcriptional activity.";
RL Oncogene 9:375-385(1994).
RN [11]
RP INTERACTION WITH JUN; MAPK9 AND HUMAN ADENOVIRUS 2 E1A (MICROBIAL
RP INFECTION), SUBUNIT, AND MUTAGENESIS OF CYS-14; THR-51; THR-53; THR-101;
RP THR-145 AND THR-147.
RX PubMed=10376527; DOI=10.1038/sj.onc.1202723;
RA De Graeve F., Bahr A., Sabapathy K.T., Hauss C., Wagner E.F., Kedinger C.,
RA Chatton B.;
RT "Role of the ATFa/JNK2 complex in Jun activation.";
RL Oncogene 18:3491-3500(1999).
RN [12]
RP INTERACTION WITH TAF4 AND TAF12, TRANSACTIVATION DOMAIN, AND MUTAGENESIS OF
RP CYS-9; MET-33; LEU-35; THR-51 AND THR-53.
RX PubMed=15735663; DOI=10.1038/sj.onc.1208565;
RA Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C.,
RA Chatton B.;
RT "A functional interaction between ATF7 and TAF12 that is modulated by
RT TAF4.";
RL Oncogene 24:3472-3483(2005).
RN [13]
RP SUMOYLATION AT LYS-107, SUBCELLULAR LOCATION, AND INTERACTION WITH TAF12.
RX PubMed=17264123; DOI=10.1093/nar/gkl1168;
RA Hamard P.J., Boyer-Guittaut M., Camuzeaux B., Dujardin D., Hauss C.,
RA Oelgeschlager T., Vigneron M., Kedinger C., Chatton B.;
RT "Sumoylation delays the ATF7 transcription factor subcellular localization
RT and inhibits its transcriptional activity.";
RL Nucleic Acids Res. 35:1134-1144(2007).
RN [14]
RP PHOSPHORYLATION AT THR-51; THR-53 AND THR-101, SUMOYLATION AT LYS-107,
RP MUTAGENESIS OF THR-51; THR-53; THR-101 AND LYS-107, AND FUNCTION.
RX PubMed=18950637; DOI=10.1016/j.jmb.2008.10.008;
RA Camuzeaux B., Diring J., Hamard P.J., Oulad-Abdelghani M., Donzeau M.,
RA Vigneron M., Kedinger C., Chatton B.;
RT "p38beta2-mediated phosphorylation and sumoylation of ATF7 are mutually
RT exclusive.";
RL J. Mol. Biol. 384:980-991(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, 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 [16]
RP FUNCTION (ISOFORM 5), AND SUBCELLULAR LOCATION (ISOFORM 5).
RX PubMed=21858082; DOI=10.1371/journal.pone.0023351;
RA Diring J., Camuzeaux B., Donzeau M., Vigneron M., Rosa-Calatrava M.,
RA Kedinger C., Chatton B.;
RT "A cytoplasmic negative regulator isoform of ATF7 impairs ATF7 and ATF2
RT phosphorylation and transcriptional activity.";
RL PLoS ONE 6:E23351-E23351(2011).
RN [17]
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP FUNCTION, INTERACTION WITH XRCC6; XRCC7 AND TERT, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=29490055; DOI=10.1093/nar/gky155;
RA Maekawa T., Liu B., Nakai D., Yoshida K., Nakamura K.I., Yasukawa M.,
RA Koike M., Takubo K., Chatton B., Ishikawa F., Masutomi K., Ishii S.;
RT "ATF7 mediates TNF-alpha-induced telomere shortening.";
RL Nucleic Acids Res. 46:4487-4504(2018).
CC -!- FUNCTION: Stress-responsive chromatin regulator that plays a role in
CC various biological processes including innate immunological memory,
CC adipocyte differentiation or telomerase regulation (PubMed:29490055).
CC In absence of stress, contributes to the formation of heterochromatin
CC and heterochromatin-like structure by recruiting histone H3K9 tri- and
CC di-methyltransferases thus silencing the transcription of target genes
CC such as STAT1 in adipocytes, or genes involved in innate immunity in
CC macrophages and adipocytes (By similarity). Stress induces ATF7
CC phosphorylation that disrupts interactions with histone
CC methyltransferase and enhances the association with coactivators
CC containing histone acetyltransferase and/or histone demethylase,
CC leading to disruption of the heterochromatin-like structure and
CC subsequently transcriptional activation (By similarity). In response to
CC TNF-alpha, which is induced by various stresses, phosphorylated ATF7
CC and telomerase are released from telomeres leading to telomere
CC shortening (PubMed:29490055). Also plays a role in maintaining
CC epithelial regenerative capacity and protecting against cell death
CC during intestinal epithelial damage and repair (By similarity).
CC {ECO:0000250|UniProtKB:Q8R0S1, ECO:0000269|PubMed:29490055}.
CC -!- FUNCTION: [Isoform 4]: Acts as a dominant repressor of the E-
CC selectin/NF-ELAM1/delta-A promoter.
CC -!- FUNCTION: [Isoform 5]: Acts as a negative regulator, inhibiting both
CC ATF2 and ATF7 transcriptional activities. It may exert these effects by
CC sequestrating in the cytoplasm the Thr-53 phosphorylating kinase,
CC preventing activation. {ECO:0000269|PubMed:21858082}.
CC -!- SUBUNIT: Homodimer; binds DNA as homodimer. Heterodimer;
CC heterodimerizes with other members of ATF family and with JUN family
CC members. Interacts with JNK2; the interaction does not phosphorylate
CC ATF7 but acts as a docking site for other ATF-associated partners such
CC as JUN family members. Interacts (via its transactivation domain) with
CC TAF12 (isoforms TAFII15 and TAFII20); the interaction potentiates the
CC transactivation activity (isoform TAFII20 only) and is inhibited by
CC ATF7 sumoylation. Interacts with TAF4; the interaction inhibits the
CC TAF12-dependent transactivation. Interacts with MAPK9; the interaction
CC does not phosphorylate ATF7 but acts as a docking site for ATF7-
CC associated partners such as JUN. Interacts with Ku complex components
CC XRCC6 and XRCC7 (PubMed:29490055). Interacts with TERT
CC (PubMed:29490055). {ECO:0000269|PubMed:10376527,
CC ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:17264123,
CC ECO:0000269|PubMed:1827203, ECO:0000269|PubMed:29490055,
CC ECO:0000269|PubMed:8288576, ECO:0000269|PubMed:8290251}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus 2 E1A; the
CC interaction enhances the ATF7-mediated viral transactivation activity
CC which requires the zinc-binding domains of both E1A and ATF7.
CC {ECO:0000269|PubMed:10376527, ECO:0000269|PubMed:8417352}.
CC -!- INTERACTION:
CC P17544; P18847: ATF3; NbExp=3; IntAct=EBI-765623, EBI-712767;
CC P17544; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-765623, EBI-10175124;
CC P17544; P06734: FCER2; NbExp=3; IntAct=EBI-765623, EBI-10199985;
CC P17544; P01100: FOS; NbExp=4; IntAct=EBI-765623, EBI-852851;
CC P17544; P15408: FOSL2; NbExp=2; IntAct=EBI-765623, EBI-3893419;
CC P17544; P05412: JUN; NbExp=6; IntAct=EBI-765623, EBI-852823;
CC P17544; P17275: JUNB; NbExp=2; IntAct=EBI-765623, EBI-748062;
CC P17544; P17535: JUND; NbExp=2; IntAct=EBI-765623, EBI-2682803;
CC P17544; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-765623, EBI-749265;
CC P17544; Q9NX40: OCIAD1; NbExp=2; IntAct=EBI-765623, EBI-2683029;
CC P17544; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-765623, EBI-9675724;
CC P17544; P0C746: HBZ; Xeno; NbExp=2; IntAct=EBI-765623, EBI-10890294;
CC P17544; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-765623, EBI-10889526;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:17264123}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17264123}. Chromosome, telomere
CC {ECO:0000269|PubMed:29490055}. Note=Mainly nucleoplasmic. Restricted
CC distribution to the perinuculear region. The sumoylated form locates to
CC the nuclear periphery.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm
CC {ECO:0000269|PubMed:21858082}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P17544-6; Sequence=Displayed;
CC Name=6; Synonyms=ATF-A1;
CC IsoId=P17544-1; Sequence=VSP_060697;
CC Name=2; Synonyms=ATF-A;
CC IsoId=P17544-2; Sequence=VSP_060699;
CC Name=3; Synonyms=ATF-A-delta;
CC IsoId=P17544-3; Sequence=VSP_060697, VSP_060699;
CC Name=4; Synonyms=ATF-A0;
CC IsoId=P17544-4; Sequence=VSP_060701;
CC Name=5; Synonyms=ATF-4;
CC IsoId=P17544-5; Sequence=VSP_060698, VSP_060700;
CC -!- TISSUE SPECIFICITY: Expressed in various tissues including heart,
CC brain, placenta, lung and skeletal muscle. Highest levels in skeletal
CC muscle. Lowest in lung and placenta. {ECO:0000269|PubMed:8288576}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Strongly expressed in skeletal muscle.
CC Also expressed at lower levels in heart and lung.
CC {ECO:0000269|PubMed:8288576}.
CC -!- PTM: On EGF stimulation, phosphorylated first on Thr-53 allowing
CC subsequent phosphorylation on Thr-51. This latter phosphorylation
CC prevents sumoylation, increases binding to TAF12 and enhances
CC transcriptional activity. {ECO:0000269|PubMed:18950637}.
CC -!- PTM: Sumoylation delays nuclear localization and inhibits
CC transactivation activity through preventing binding to TAF12. RANBP2
CC appears to be the specific E3 ligase.
CC -!- PTM: On EGF stimulation, phosphorylated first on Thr-53 allowing
CC subsequent phosphorylation on Thr-51. This latter phosphorylation
CC prevents sumoylation, increases binding to TAF12 and enhances
CC transcriptional activity (PubMed:18950637). Social isolation stress as
CC well as TNF-alpha also induce the phosphorylation of ATF7
CC (PubMed:29490055). Phosphorylated in proliferating colonic and small
CC intestinal epithelial cells (By similarity).
CC {ECO:0000250|UniProtKB:Q8R0S1, ECO:0000269|PubMed:18950637,
CC ECO:0000269|PubMed:29490055}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; X52943; CAA37118.1; -; mRNA.
DR EMBL; X57197; CAA40483.1; -; mRNA.
DR EMBL; AK298853; BAG60976.1; -; mRNA.
DR EMBL; AC023509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96723.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96724.1; -; Genomic_DNA.
DR EMBL; BC042363; AAH42363.1; -; mRNA.
DR EMBL; BC136302; AAI36303.1; -; mRNA.
DR EMBL; BC140006; AAI40007.1; -; mRNA.
DR CCDS; CCDS44906.1; -. [P17544-6]
DR CCDS; CCDS58238.1; -. [P17544-5]
DR PIR; S12741; S12741.
DR RefSeq; NP_001123532.1; NM_001130060.1. [P17544-2]
DR RefSeq; NP_001193611.1; NM_001206682.1. [P17544-5]
DR RefSeq; NP_001193612.1; NM_001206683.1. [P17544-5]
DR RefSeq; NP_006847.1; NM_006856.2. [P17544-6]
DR RefSeq; XP_005268644.1; XM_005268587.3.
DR RefSeq; XP_016874211.1; XM_017018722.1.
DR AlphaFoldDB; P17544; -.
DR SMR; P17544; -.
DR BioGRID; 116206; 80.
DR ComplexPortal; CPX-6409; bZIP transcription factor complex, ATF2-ATF7.
DR ComplexPortal; CPX-6466; bZIP transcription factor complex, ATF3-ATF7.
DR ComplexPortal; CPX-6721; bZIP transcription factor complex, ATF7-ATF7.
DR ComplexPortal; CPX-6781; bZIP transcription factor complex, ATF7-BACH1.
DR ComplexPortal; CPX-6782; bZIP transcription factor complex, ATF7-CEBPG.
DR ComplexPortal; CPX-6783; bZIP transcription factor complex, ATF7-FOS.
DR ComplexPortal; CPX-6784; bZIP transcription factor complex, ATF7-DDIT3.
DR ComplexPortal; CPX-6785; bZIP transcription factor complex, ATF7-FOSL2.
DR ComplexPortal; CPX-6786; bZIP transcription factor complex, ATF7-JUN.
DR ComplexPortal; CPX-6787; bZIP transcription factor complex, ATF7-JUNB.
DR ComplexPortal; CPX-6788; bZIP transcription factor complex, ATF7-JUND.
DR ComplexPortal; CPX-6789; bZIP transcription factor complex, ATF7-NFE2.
DR ComplexPortal; CPX-6790; bZIP transcription factor complex, ATF7-NFE2L1.
DR CORUM; P17544; -.
DR ELM; P17544; -.
DR IntAct; P17544; 38.
DR MINT; P17544; -.
DR STRING; 9606.ENSP00000399465; -.
DR DrugBank; DB00852; Pseudoephedrine.
DR iPTMnet; P17544; -.
DR PhosphoSitePlus; P17544; -.
DR BioMuta; ATF7; -.
DR DMDM; 12643393; -.
DR EPD; P17544; -.
DR jPOST; P17544; -.
DR MassIVE; P17544; -.
DR MaxQB; P17544; -.
DR PaxDb; P17544; -.
DR PeptideAtlas; P17544; -.
DR PRIDE; P17544; -.
DR ProteomicsDB; 53487; -. [P17544-1]
DR ProteomicsDB; 53488; -. [P17544-2]
DR ProteomicsDB; 53489; -. [P17544-3]
DR ProteomicsDB; 53490; -. [P17544-4]
DR ProteomicsDB; 53491; -. [P17544-5]
DR ProteomicsDB; 53492; -. [P17544-6]
DR ABCD; P17544; 6 sequenced antibodies.
DR Antibodypedia; 931; 286 antibodies from 35 providers.
DR DNASU; 11016; -.
DR Ensembl; ENST00000420353.7; ENSP00000399465.1; ENSG00000170653.19. [P17544-6]
DR Ensembl; ENST00000456903.8; ENSP00000387406.3; ENSG00000170653.19. [P17544-6]
DR Ensembl; ENST00000548118.6; ENSP00000456858.1; ENSG00000170653.19. [P17544-5]
DR Ensembl; ENST00000548446.6; ENSP00000449938.1; ENSG00000170653.19. [P17544-1]
DR Ensembl; ENST00000591397.1; ENSP00000465192.1; ENSG00000170653.19. [P17544-5]
DR GeneID; 11016; -.
DR KEGG; hsa:11016; -.
DR MANE-Select; ENST00000420353.7; ENSP00000399465.1; NM_006856.3; NP_006847.1.
DR UCSC; uc001sdz.4; human. [P17544-6]
DR CTD; 11016; -.
DR DisGeNET; 11016; -.
DR GeneCards; ATF7; -.
DR HGNC; HGNC:792; ATF7.
DR HPA; ENSG00000170653; Low tissue specificity.
DR MIM; 606371; gene.
DR neXtProt; NX_P17544; -.
DR OpenTargets; ENSG00000170653; -.
DR PharmGKB; PA25092; -.
DR VEuPathDB; HostDB:ENSG00000170653; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000155261; -.
DR HOGENOM; CLU_021564_0_0_1; -.
DR InParanoid; P17544; -.
DR OMA; ANNDHLE; -.
DR OrthoDB; 978850at2759; -.
DR PhylomeDB; P17544; -.
DR PathwayCommons; P17544; -.
DR SignaLink; P17544; -.
DR SIGNOR; P17544; -.
DR BioGRID-ORCS; 11016; 33 hits in 1099 CRISPR screens.
DR ChiTaRS; ATF7; human.
DR GeneWiki; ATF7; -.
DR GenomeRNAi; 11016; -.
DR Pharos; P17544; Tbio.
DR PRO; PR:P17544; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P17544; protein.
DR Bgee; ENSG00000170653; Expressed in popliteal artery and 166 other tissues.
DR ExpressionAtlas; P17544; baseline and differential.
DR Genevisible; P17544; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0035497; F:cAMP response element binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
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:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
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 InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016378; TF_CRE-BP1-typ.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00170; bZIP_1; 1.
DR PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromosome; Cytoplasm; DNA-binding;
KW Host-virus interaction; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..483
FT /note="Cyclic AMP-dependent transcription factor ATF-7"
FT /id="PRO_0000076592"
FT DOMAIN 332..395
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT ZN_FING 7..31
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..285
FT /note="Transactivation domain"
FT REGION 110..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..483
FT /note="Essential for binding adenovirus 2 E1A"
FT REGION 334..354
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 360..388
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 407..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphothreonine; by MAPK11"
FT /evidence="ECO:0000269|PubMed:18950637"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18950637"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18950637"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:17264123,
FT ECO:0000269|PubMed:18950637"
FT VAR_SEQ 88
FT /note="K -> KARSRTVAKKLV (in isoform 6 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_060697"
FT VAR_SEQ 89..117
FT /note="AAAGPLDMSLPSTPDIKIKEEEPVEVDSS -> ARSRTVAKKLVVFRPRLFL
FT LCFGIIFLIG (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_060698"
FT VAR_SEQ 114..134
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_060699"
FT VAR_SEQ 118..483
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_060700"
FT VAR_SEQ 135..310
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_060701"
FT MUTAGEN 9
FT /note="C->A: Severely reduced TAF12-mediated enhancement of
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:15735663"
FT MUTAGEN 14
FT /note="C->A: Greatly reduced JNK2- or adenovirus E1A-
FT mediated transactivation. Abolishes adenovirus 2 E1A-
FT mediated transactivation; when associated with A-51; A-53
FT and G-101."
FT /evidence="ECO:0000269|PubMed:10376527"
FT MUTAGEN 22
FT /note="D->K: No effect on binding adenovirus 2 E1A.
FT Abolishes ATF7-mediated E1A responsiveness."
FT /evidence="ECO:0000269|PubMed:8417352"
FT MUTAGEN 27
FT /note="H->N: No effect on binding adenovirus 2 E1A.
FT Abolishes ATF7-mediated E1A responsiveness."
FT /evidence="ECO:0000269|PubMed:8417352"
FT MUTAGEN 33
FT /note="M->D: Severely reduced TAF12-induced transcriptional
FT activity; when associated with S-35."
FT /evidence="ECO:0000269|PubMed:15735663"
FT MUTAGEN 35
FT /note="L->S: Severely reduced TAF12-induced transcriptional
FT activity; when associated with D-33."
FT /evidence="ECO:0000269|PubMed:15735663"
FT MUTAGEN 51
FT /note="T->A: Severely reduced TAF12-induced transcriptional
FT activity. No effect on MAPK9-mediated phosphorylation; when
FT associated with A-53. Greatly reduces MAPK9- and adenovirus
FT E1A-mediated transactivation; when associated with A-53 and
FT G-101. Abolishes adenovirus 2 E1A-mediated transactivation;
FT when associated with A-14; A-53 and G-101."
FT /evidence="ECO:0000269|PubMed:10376527,
FT ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"
FT MUTAGEN 51
FT /note="T->D: Completely abolishes MAPK9- and adenovirus
FT E1A-mediated transactivation; when associated with D-53."
FT /evidence="ECO:0000269|PubMed:10376527,
FT ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"
FT MUTAGEN 53
FT /note="T->A: Severely reduced TAF12-induced transcriptional
FT activity. No effect on MAPK9-mediated phosphorylation; when
FT associated with A-51. Greatly reduces MAPK9- and adenovirus
FT E1A-mediated transactivation; when associated with A-51 and
FT G-101. Abolishes adenovirus 2 E1A-mediated transactivation;
FT when associated with A-14; A-51 and G-101."
FT /evidence="ECO:0000269|PubMed:10376527,
FT ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"
FT MUTAGEN 53
FT /note="T->D: Completely abolishes MAPK9- and adenovirus
FT E1A-mediated transactivation; when associated with D-51."
FT /evidence="ECO:0000269|PubMed:10376527,
FT ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:18950637"
FT MUTAGEN 101
FT /note="T->G: Some reduction in transactivation but,
FT completely abolishes MAPK9-mediated activation. Abolishes
FT MAPK9-mediated and greatly reduces adenovirus E1A-mediated
FT transactivation; when associated with A-51 and A-53.
FT Abolishes adenovirus 2 E1A-mediated transactivation; when
FT associated with A-14; A-51 and A-53."
FT /evidence="ECO:0000269|PubMed:10376527,
FT ECO:0000269|PubMed:18950637"
FT MUTAGEN 107
FT /note="K->R: Abolishes sumoylation. Exclusive nucleoplasmic
FT location. Increase in binding the E-selectin promoter."
FT /evidence="ECO:0000269|PubMed:18950637"
FT MUTAGEN 145
FT /note="T->A: No effect on transactivation; when associated
FT with A-147."
FT /evidence="ECO:0000269|PubMed:10376527"
FT MUTAGEN 147
FT /note="T->A: No effect on transactivation; when associated
FT with A-145."
FT /evidence="ECO:0000269|PubMed:10376527"
FT CONFLICT 12
FT /note="P -> T (in Ref. 7; AAH42363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 51757 MW; 07080BC24FED635B CRC64;
MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ TPTPTRFLKN
CEEVGLFNEL ASSFEHEFKK AADEDEKKAA AGPLDMSLPS TPDIKIKEEE PVEVDSSPPD
SPASSPCSPP LKEKEVTPKP VLISTPTPTI VRPGSLPLHL GYDPLHPTLP SPTSVITQAP
PSNRQMGSPT GSLPLVMHLA NGQTMPVLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN
SSGSISPSGH PIPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQSQILIQHP
DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR QKRKLWVSSL
EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV TALQKKTQGY LESPKESSEP
TGSPAPVIQH SSATAPSNGL SVRSAAEAVA TSVLTQMASQ RTELSMPIQS HVIMTPQSQS
AGR
