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Cyclic AMP-dependent transcription factor ATF-2 (cAMP-dependent transcription factor ATF-2) (EC 2.3.1.48) (Activating transcription factor 2) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2) (HB16) (Histone acetyltransferase ATF2) (cAMP response element-binding protein CRE-BP1)

 ATF2_HUMAN              Reviewed;         505 AA.
P15336; A1L3Z2; A4D7U4; A4D7U5; A4D7V1; D3DPE9; G8JLM5; Q13000;
Q3B7B7; Q4ZFU9; Q53RY2; Q8TAR1; Q96JT8;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
10-MAY-2017, entry version 194.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-2;
Short=cAMP-dependent transcription factor ATF-2;
EC=2.3.1.48 {ECO:0000269|PubMed:10821277};
AltName: Full=Activating transcription factor 2;
AltName: Full=Cyclic AMP-responsive element-binding protein 2;
Short=CREB-2;
Short=cAMP-responsive element-binding protein 2;
AltName: Full=HB16;
AltName: Full=Histone acetyltransferase ATF2;
AltName: Full=cAMP response element-binding protein CRE-BP1;
Name=ATF2; Synonyms=CREB2, CREBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=2529117;
Maekawa T., Sakura H., Kanei-Ishii C., Sudo T., Yoshimura T.,
Fujisawa J., Yoshida M., Ishii S.;
"Leucine zipper structure of the protein CRE-BP1 binding to the cyclic
AMP response element in brain.";
EMBO J. 8:2023-2028(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=9058782;
Yang L., Lanier E.R., Kraig E.;
"Identification of a novel, spliced variant of CREB that is
preferentially expressed in the thymus.";
J. Immunol. 158:2522-2525(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
TISSUE=Myometrium;
PubMed=11932306; DOI=10.1210/jcem.87.4.8360;
Bailey J., Phillips R.J., Pollard A.J., Gilmore K., Robson S.C.,
Europe-Finner G.N.;
"Characterization and functional analysis of cAMP response element
modulator protein and activating transcription factor 2 (ATF2)
isoforms in the human myometrium during pregnancy and labor:
identification of a novel ATF2 species with potent transactivation
properties.";
J. Clin. Endocrinol. Metab. 87:1717-1728(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 5; 6 AND 7).
von Hippel A.C.;
"Homo sapiens activating transcription factor 2 (ATF2) mRNA splice
variant.";
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 211-505 (ISOFORMS 1/2).
PubMed=2320002; DOI=10.1128/MCB.10.4.1347;
Kara C.J., Liou H.-C., Ivashkiv L.B., Glimcher L.H.;
"A cDNA for a human cyclic AMP response element-binding protein which
is distinct from CREB and expressed preferentially in brain.";
Mol. Cell. Biol. 10:1347-1357(1990).
[9]
PHOSPHORYLATION BY CAMK4.
PubMed=8855261; DOI=10.1073/pnas.93.20.10803;
Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.;
"Regulation of mitogen-activated protein kinases by a
calcium/calmodulin-dependent protein kinase cascade.";
Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996).
[10]
PHOSPHORYLATION AT THR-69 AND THR-71.
PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
Enslen H., Raingeaud J., Davis R.J.;
"Selective activation of p38 mitogen-activated protein (MAP) kinase
isoforms by the MAP kinase kinases MKK3 and MKK6.";
J. Biol. Chem. 273:1741-1748(1998).
[11]
INTERACTION WITH UTF1.
PubMed=9748258; DOI=10.1074/jbc.273.40.25840;
Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A.,
Muramatsu M.;
"Characterization of functional domains of an embryonic stem cell
coactivator UTF1 which are conserved and essential for potentiation of
ATF-2 activity.";
J. Biol. Chem. 273:25840-25849(1998).
[12]
FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, AND MUTAGENESIS OF
THR-69 AND THR-71.
PubMed=10821277; DOI=10.1038/35012097;
Kawasaki H., Schiltz L., Chiu R., Itakura K., Taira K., Nakatani Y.,
Yokoyama K.K.;
"ATF-2 has intrinsic histone acetyltransferase activity which is
modulated by phosphorylation.";
Nature 405:195-200(2000).
[13]
PHOSPHORYLATION AT THR-69 AND THR-71.
PubMed=12110590; DOI=10.1093/emboj/cdf361;
Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P.,
Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A.,
van Dam H.;
"Growth factors can activate ATF2 via a two-step mechanism:
phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69
through RalGDS-Src-p38.";
EMBO J. 21:3782-3793(2002).
[14]
PHOSPHORYLATION AT SER-62 AND THR-73, AND SUBCELLULAR LOCATION.
PubMed=15105425; DOI=10.1074/jbc.M401009200;
Sevilla A., Santos C.R., Vega F.M., Lazo P.A.;
"Human vaccinia-related kinase 1 (VRK1) activates the ATF2
transcriptional activity by novel phosphorylation on Thr-73 and Ser-62
and cooperates with JNK.";
J. Biol. Chem. 279:27458-27465(2004).
[15]
FUNCTION, INTERACTION WITH NBN AND MRE11, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION AT SER-490 AND SER-498.
PubMed=15916964; DOI=10.1016/j.molcel.2005.04.015;
Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N.,
Ronai Z.;
"ATM-dependent phosphorylation of ATF2 is required for the DNA damage
response.";
Mol. Cell 18:577-587(2005).
[16]
ACETYLATION AT LYS-357 AND LYS-374, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17590016; DOI=10.1021/bi7000054;
Karanam B., Wang L., Wang D., Liu X., Marmorstein R., Cotter R.,
Cole P.A.;
"Multiple roles for acetylation in the interaction of p300 HAT with
ATF-2.";
Biochemistry 46:8207-8216(2007).
[17]
REVIEW.
PubMed=18677098; DOI=10.4161/cc.6388;
Bhoumik A., Ronai Z.;
"ATF2: a transcription factor that elicits oncogenic or tumor
suppressor activities.";
Cell Cycle 7:2341-2345(2008).
[18]
FUNCTION, INTERACTION WITH CUL3 AND KAT5, AND SUBCELLULAR LOCATION.
PubMed=18397884; DOI=10.1074/jbc.M802030200;
Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.;
"Regulation of TIP60 by ATF2 modulates ATM activation.";
J. Biol. Chem. 283:17605-17614(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69 AND SER-112, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
PHOSPHORYLATION AT THR-69; THR-71; SER-121; SER-340 AND SER-367, AND
SUBCELLULAR LOCATION.
PubMed=19176525; DOI=10.1074/jbc.M808719200;
Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.;
"Phosphorylation of activation transcription factor-2 at serine 121 by
protein kinase c controls c-Jun-mediated activation of
transcription.";
J. Biol. Chem. 284:8567-8581(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71 AND SER-112,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71; SER-112 AND
THR-116, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
PHOSPHORYLATION AT THR-71, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
THR-71.
PubMed=21098032; DOI=10.1074/jbc.M110.166009;
Wang L., Payton R., Dai W., Lu L.;
"Hyperosmotic stress-induced ATF-2 activation through Polo-like kinase
3 in human corneal epithelial cells.";
J. Biol. Chem. 286:1951-1958(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71; SER-90 AND
SER-112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HK1/VDAC1 COMPLEX,
AND PHOSPHORYLATION AT THR-52.
PubMed=22304920; DOI=10.1016/j.cell.2012.01.016;
Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L.,
Ideker T., Ronai Z.A.;
"PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while
blocking its apoptotic function at mitochondria.";
Cell 148:543-555(2012).
[28]
SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, INTERACTION WITH XPO1,
AND HETERODIMERIZATION WITH JUN.
PubMed=22275354; DOI=10.1074/jbc.M111.294272;
Hsu C.C., Hu C.D.;
"Critical role of N-terminal end-localized nuclear export signal in
regulation of activating transcription factor 2 (ATF2) subcellular
localization and transcriptional activity.";
J. Biol. Chem. 287:8621-8632(2012).
[29]
REVIEW.
PubMed=22685333; DOI=10.1242/jcs.095000;
Lau E., Ronai Z.A.;
"ATF2-at the crossroad of nuclear and cytosolic functions.";
J. Cell Sci. 125:2815-2824(2012).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; THR-69; THR-71;
SER-112 AND SER-136, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-328; SER-442
AND SER-446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
STRUCTURE BY NMR OF 19-56.
PubMed=10092462; DOI=10.1006/jmbi.1999.2620;
Nagadoi A., Nakazawa K., Uda H., Okuno K., Maekawa T., Ishii S.,
Nishimura Y.;
"Solution structure of the transactivation domain of ATF-2 comprising
a zinc finger-like subdomain and a flexible subdomain.";
J. Mol. Biol. 287:593-607(1999).
[33]
VARIANT [LARGE SCALE ANALYSIS] HIS-352.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Transcriptional activator which regulates the
transcription of various genes, including those involved in anti-
apoptosis, cell growth, and DNA damage response. Dependent on its
binding partner, binds to CRE (cAMP response element) consensus
sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1)
consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes
to global transcription and the DNA damage response, in addition
to specific transcriptional activities that are related to cell
development, proliferation and death. In the cytoplasm, interacts
with and perturbs HK1- and VDAC1-containing complexes at the
mitochondrial outer membrane, thereby impairing mitochondrial
membrane potential, inducing mitochondrial leakage and promoting
cell death. The phosphorylated form (mediated by ATM) plays a role
in the DNA damage response and is involved in the ionizing
radiation (IR)-induced S phase checkpoint control and in the
recruitment of the MRN complex into the IR-induced foci (IRIF).
Exhibits histone acetyltransferase (HAT) activity which
specifically acetylates histones H2B and H4 in vitro. In concert
with CUL3 and RBX1, promotes the degradation of KAT5 thereby
attenuating its ability to acetylate and activate ATM. Can elicit
oncogenic or tumor suppressor activities depending on the tissue
or cell type. {ECO:0000269|PubMed:10821277,
ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:18397884,
ECO:0000269|PubMed:22304920}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:10821277}.
-!- SUBUNIT: Binds DNA as a dimer and can form a homodimer in the
absence of DNA. Can form a heterodimer with JUN.
Heterodimerization is essential for its transcriptional activity.
Interacts with SMAD3 and SMAD4. Binds through its N-terminal
region to UTF1 which acts as a coactivator of ATF2 transcriptional
activity. Interacts with the HK1/VDAC1 complex. Interacts with
NBN, MRE11, XPO1, KAT5 and CUL3. {ECO:0000269|PubMed:15916964,
ECO:0000269|PubMed:18397884, ECO:0000269|PubMed:22275354,
ECO:0000269|PubMed:22304920, ECO:0000269|PubMed:9748258}.
-!- INTERACTION:
P18847:ATF3; NbExp=2; IntAct=EBI-1170906, EBI-712767;
Q99966:CITED1; NbExp=2; IntAct=EBI-1170906, EBI-2624951;
Q96B26:EXOSC8; NbExp=3; IntAct=EBI-1170906, EBI-371922;
P01100:FOS; NbExp=9; IntAct=EBI-1170906, EBI-852851;
Q6FG41:FOS; NbExp=3; IntAct=EBI-1170906, EBI-10198738;
P15408:FOSL2; NbExp=4; IntAct=EBI-1170906, EBI-3893419;
P0C746:HBZ (xeno); NbExp=3; IntAct=EBI-1170906, EBI-10890294;
P56524:HDAC4; NbExp=2; IntAct=EBI-1170906, EBI-308629;
P05412:JUN; NbExp=14; IntAct=EBI-1170906, EBI-852823;
P17275:JUNB; NbExp=2; IntAct=EBI-1170906, EBI-748062;
P17535:JUND; NbExp=2; IntAct=EBI-1170906, EBI-2682803;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-1170906, EBI-2125614;
P45984:MAPK9; NbExp=5; IntAct=EBI-1170906, EBI-713568;
Q9DGW5:MDV005 (xeno); NbExp=2; IntAct=EBI-1170906, EBI-10889526;
O95644:NFATC1; NbExp=2; IntAct=EBI-1170906, EBI-6907210;
Q15532:SS18; NbExp=2; IntAct=EBI-1170906, EBI-2560599;
P63165:SUMO1; NbExp=5; IntAct=EBI-1170906, EBI-80140;
A4PIW0:SYT-SSX2; NbExp=11; IntAct=EBI-1170906, EBI-6050533;
Q99986:VRK1; NbExp=5; IntAct=EBI-1170906, EBI-1769146;
Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-1170906, EBI-524753;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion outer
membrane. Note=Shuttles between the cytoplasm and the nucleus and
heterodimerization with JUN is essential for the nuclear
localization. Localization to the cytoplasm is observed under
conditions of cellular stress and in disease states. Localizes at
the mitochondrial outer membrane in response to genotoxic stress.
Phosphorylation at Thr-52 is required for its nuclear localization
and negatively regulates its mitochondrial localization. Co-
localizes with the MRN complex in the IR-induced foci (IRIF).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=P15336-1; Sequence=Displayed;
Name=2;
IsoId=P15336-2; Sequence=VSP_000587, VSP_000588;
Name=3;
IsoId=P15336-3; Sequence=VSP_045161;
Name=4;
IsoId=P15336-4; Sequence=VSP_046959;
Name=5;
IsoId=P15336-5; Sequence=VSP_046960;
Name=6;
IsoId=P15336-6; Sequence=VSP_046960, VSP_047593;
Name=7;
IsoId=P15336-7; Sequence=VSP_046960, VSP_047594, VSP_047595;
Name=8; Synonyms=ATF2-small;
IsoId=P15336-8; Sequence=VSP_047593;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with more abundant
expression in the brain.
-!- DOMAIN: The nuclear export signal 1 (N-NES) negatively regulates
its nuclear localization and transcriptional activity.
-!- PTM: Phosphorylation of Thr-69 by MAPK14 and MAPK11, and at Thr-71
by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response
to external stimulus like insulin causes increased transcriptional
activity. Phosphorylated by PLK3 following hyperosmotic stress.
Also phosphorylated and activated by JNK and CaMK4. ATM-mediated
phosphorylation at Ser-490 and Ser-498 stimulates its function in
DNA damage response. Phosphorylation at Ser-62, Thr-73 and Ser-121
activates its transcriptional activity. Phosphorylation at Thr-69
or Thr-71 enhances its histone acetyltransferase (HAT) activity.
{ECO:0000269|PubMed:10821277, ECO:0000269|PubMed:12110590,
ECO:0000269|PubMed:15105425, ECO:0000269|PubMed:15916964,
ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:21098032,
ECO:0000269|PubMed:22304920, ECO:0000269|PubMed:8855261,
ECO:0000269|PubMed:9430721}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAY17203.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAY17207.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ATF2ID718ch2q31.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X15875; CAA33886.1; -; mRNA.
EMBL; U16028; AAB64017.1; -; mRNA.
EMBL; AY029364; AAK55760.1; -; mRNA.
EMBL; DQ003037; AAY17203.1; ALT_INIT; mRNA.
EMBL; DQ003038; AAY17204.1; -; mRNA.
EMBL; DQ003041; AAY17207.1; ALT_INIT; mRNA.
EMBL; DQ003044; AAY17210.1; -; mRNA.
EMBL; DQ003047; AAY17213.1; -; mRNA.
EMBL; DQ003049; AAY17215.1; -; mRNA.
EMBL; AC131958; AAX88876.1; -; Genomic_DNA.
EMBL; AC074291; AAY15004.1; -; Genomic_DNA.
EMBL; AC007435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471058; EAX11111.1; -; Genomic_DNA.
EMBL; CH471058; EAX11112.1; -; Genomic_DNA.
EMBL; CH471058; EAX11113.1; -; Genomic_DNA.
EMBL; BC026175; AAH26175.1; -; mRNA.
EMBL; BC107698; AAI07699.1; -; mRNA.
EMBL; BC130335; AAI30336.1; -; mRNA.
EMBL; BC130337; AAI30338.1; -; mRNA.
EMBL; M31630; AAA35951.1; -; mRNA.
CCDS; CCDS2262.1; -. [P15336-1]
CCDS; CCDS58737.1; -. [P15336-4]
CCDS; CCDS58738.1; -. [P15336-5]
CCDS; CCDS58739.1; -. [P15336-3]
PIR; S05380; S05380.
RefSeq; NP_001243019.1; NM_001256090.1. [P15336-1]
RefSeq; NP_001243020.1; NM_001256091.1. [P15336-5]
RefSeq; NP_001243021.1; NM_001256092.1. [P15336-4]
RefSeq; NP_001243022.1; NM_001256093.1.
RefSeq; NP_001243023.1; NM_001256094.1. [P15336-3]
RefSeq; NP_001871.2; NM_001880.3. [P15336-1]
UniGene; Hs.592510; -.
PDB; 1BHI; NMR; -; A=19-56.
PDB; 1T2K; X-ray; 3.00 A; D=354-414.
PDB; 4H36; X-ray; 3.00 A; B=48-55.
PDBsum; 1BHI; -.
PDBsum; 1T2K; -.
PDBsum; 4H36; -.
ProteinModelPortal; P15336; -.
SMR; P15336; -.
BioGrid; 107776; 213.
DIP; DIP-632N; -.
IntAct; P15336; 208.
MINT; MINT-1788434; -.
STRING; 9606.ENSP00000264110; -.
DrugBank; DB00852; Pseudoephedrine.
iPTMnet; P15336; -.
PhosphoSitePlus; P15336; -.
BioMuta; ATF2; -.
DMDM; 215274241; -.
EPD; P15336; -.
MaxQB; P15336; -.
PaxDb; P15336; -.
PeptideAtlas; P15336; -.
PRIDE; P15336; -.
DNASU; 1386; -.
Ensembl; ENST00000264110; ENSP00000264110; ENSG00000115966. [P15336-1]
Ensembl; ENST00000345739; ENSP00000340576; ENSG00000115966. [P15336-4]
Ensembl; ENST00000392544; ENSP00000376327; ENSG00000115966. [P15336-1]
Ensembl; ENST00000409499; ENSP00000386282; ENSG00000115966. [P15336-8]
Ensembl; ENST00000409635; ENSP00000387093; ENSG00000115966. [P15336-4]
Ensembl; ENST00000409833; ENSP00000386526; ENSG00000115966. [P15336-3]
Ensembl; ENST00000426833; ENSP00000407911; ENSG00000115966. [P15336-5]
GeneID; 1386; -.
KEGG; hsa:1386; -.
UCSC; uc002ujk.5; human. [P15336-1]
CTD; 1386; -.
DisGeNET; 1386; -.
GeneCards; ATF2; -.
HGNC; HGNC:784; ATF2.
HPA; CAB003769; -.
HPA; HPA022134; -.
MIM; 123811; gene.
neXtProt; NX_P15336; -.
OpenTargets; ENSG00000115966; -.
PharmGKB; PA25084; -.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00390000020106; -.
HOGENOM; HOG000220894; -.
HOVERGEN; HBG004300; -.
InParanoid; P15336; -.
KO; K04450; -.
OMA; HPESTTN; -.
OrthoDB; EOG091G0AO8; -.
PhylomeDB; P15336; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
SignaLink; P15336; -.
SIGNOR; P15336; -.
ChiTaRS; ATF2; human.
EvolutionaryTrace; P15336; -.
GeneWiki; Activating_transcription_factor_2; -.
GenomeRNAi; 1386; -.
PRO; PR:P15336; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115966; -.
CleanEx; HS_ATF2; -.
ExpressionAtlas; P15336; baseline and differential.
Genevisible; P15336; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0035497; F:cAMP response element binding; IDA:BHF-UCL.
GO; GO:0008140; F:cAMP response element binding protein binding; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IC:BHF-UCL.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IC:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0097186; P:amelogenesis; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
GO; GO:0031573; P:intra-S DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IMP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0032915; P:positive regulation of transforming growth factor beta2 production; IEA:Ensembl.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IC:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEA:Ensembl.
InterPro; IPR029836; ATF-2.
InterPro; IPR004827; bZIP.
InterPro; IPR016378; TF_CRE-BP1-typ.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR19304:SF33; PTHR19304:SF33; 1.
Pfam; PF00170; bZIP_1; 1.
PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; DNA damage; DNA-binding; Membrane;
Metal-binding; Mitochondrion; Mitochondrion outer membrane; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Transferase; Zinc; Zinc-finger.
CHAIN 1 505 Cyclic AMP-dependent transcription factor
ATF-2.
/FTId=PRO_0000076577.
DOMAIN 352 415 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
ZN_FING 25 49 C2H2-type. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 296 299 Essential for its histone
acetyltransferase activity.
REGION 354 374 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 380 408 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 1 7 Nuclear export signal 1 (N-NES).
MOTIF 405 414 Nuclear export signal 2 (C-NES).
MOD_RES 52 52 Phosphothreonine; by PKC/PRKCH.
{ECO:0000269|PubMed:22304920}.
MOD_RES 62 62 Phosphoserine; by VRK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15105425}.
MOD_RES 69 69 Phosphothreonine; by MAPK11 and MAPK14.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12110590,
ECO:0000269|PubMed:19176525,
ECO:0000269|PubMed:9430721}.
MOD_RES 71 71 Phosphothreonine; by MAPK1, MAPK3,
MAPK11, MAPK12, MAPK14 and PLK3.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12110590,
ECO:0000269|PubMed:19176525,
ECO:0000269|PubMed:21098032,
ECO:0000269|PubMed:9430721}.
MOD_RES 73 73 Phosphothreonine; by VRK1.
{ECO:0000269|PubMed:15105425}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 116 116 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 121 121 Phosphoserine; by PKC/PRKCA and
PKC/PRKCB. {ECO:0000269|PubMed:19176525}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:24275569}.
MOD_RES 340 340 Phosphoserine; by PKC/PRKCA and
PKC/PRKCB. {ECO:0000269|PubMed:19176525}.
MOD_RES 357 357 N6-acetyllysine.
{ECO:0000269|PubMed:17590016}.
MOD_RES 367 367 Phosphoserine; by PKC/PRKCA and
PKC/PRKCB. {ECO:0000269|PubMed:19176525}.
MOD_RES 374 374 N6-acetyllysine.
{ECO:0000269|PubMed:17590016}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 490 490 Phosphoserine; by ATM.
{ECO:0000269|PubMed:15916964}.
MOD_RES 498 498 Phosphoserine; by ATM.
{ECO:0000269|PubMed:15916964}.
VAR_SEQ 1 176 Missing (in isoform 2).
{ECO:0000303|PubMed:9058782}.
/FTId=VSP_000587.
VAR_SEQ 1 66 MKFKLHVNSARQYKDLWNMSDDKPFLCTAPGCGQRFTNEDH
LAVHKHKHEMTLKFGPARNDSVIVA -> MYCAWMWP (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046959.
VAR_SEQ 1 18 Missing (in isoform 5, isoform 6 and
isoform 7). {ECO:0000303|Ref.4}.
/FTId=VSP_046960.
VAR_SEQ 34 394 Missing (in isoform 6 and isoform 8).
{ECO:0000303|PubMed:11932306,
ECO:0000303|Ref.4}.
/FTId=VSP_047593.
VAR_SEQ 177 185 TSSDSSVII -> MSTAYFQMM (in isoform 2).
{ECO:0000303|PubMed:9058782}.
/FTId=VSP_000588.
VAR_SEQ 210 505 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045161.
VAR_SEQ 210 237 PVPGPFPLLLHLPNGQTMPVAIPASITS -> SFDQSPWCL
VFQESQVLPLPNQYSQKQK (in isoform 7).
{ECO:0000303|Ref.4}.
/FTId=VSP_047594.
VAR_SEQ 238 505 Missing (in isoform 7).
{ECO:0000303|Ref.4}.
/FTId=VSP_047595.
VARIANT 352 352 D -> H (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035999.
MUTAGEN 69 69 T->A: Weak histone acetyltransferase
activity. {ECO:0000269|PubMed:10821277}.
MUTAGEN 71 71 T->A: Impairs phosphorylation by PLK3.
Weak histone acetyltransferase activity.
{ECO:0000269|PubMed:10821277,
ECO:0000269|PubMed:21098032}.
MUTAGEN 121 121 S->A: Reduced phosphorylation and
repression of c-Jun-mediated activation
of transcription.
CONFLICT 209 209 V -> L (in Ref. 2; AAB64017).
{ECO:0000305}.
CONFLICT 223 223 N -> S (in Ref. 1; CAA33886 and 4;
AAY17203/AAY17207/AAY17215).
{ECO:0000305}.
CONFLICT 311 311 R -> L (in Ref. 2; AAB64017).
{ECO:0000305}.
TURN 30 32 {ECO:0000244|PDB:1BHI}.
STRAND 35 38 {ECO:0000244|PDB:1BHI}.
HELIX 39 50 {ECO:0000244|PDB:1BHI}.
TURN 51 55 {ECO:0000244|PDB:1BHI}.
HELIX 355 412 {ECO:0000244|PDB:1T2K}.
SEQUENCE 505 AA; 54537 MW; 0190EEFAEC8891A7 CRC64;
MKFKLHVNSA RQYKDLWNMS DDKPFLCTAP GCGQRFTNED HLAVHKHKHE MTLKFGPARN
DSVIVADQTP TPTRFLKNCE EVGLFNELAS PFENEFKKAS EDDIKKMPLD LSPLATPIIR
SKIEEPSVVE TTHQDSPLPH PESTTSDEKE VPLAQTAQPT SAIVRPASLQ VPNVLLTSSD
SSVIIQQAVP SPTSSTVITQ APSSNRPIVP VPGPFPLLLH LPNGQTMPVA IPASITSSNV
HVPAAVPLVR PVTMVPSVPG IPGPSSPQPV QSEAKMRLKA ALTQQHPPVT NGDTVKGHGS
GLVRTQSEES RPQSLQQPAT STTETPASPA HTTPQTQSTS GRRRRAANED PDEKRRKFLE
RNRAAASRCR QKRKVWVQSL EKKAEDLSSL NGQLQSEVTL LRNEVAQLKQ LLLAHKDCPV
TAMQKKSGYH TADKDDSSED ISVPSSPHTE AIQHSSVSTS NGVSSTSKAE AVATSVLTQM
ADQSTEPALS QIVMAPSSQS QPSGS


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