ID   ATF2_HUMAN              Reviewed;         487 AA.
AC   P15336; Q13000;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 3.
DT   10-JUL-2007, entry version 84.
DE   Cyclic AMP-dependent transcription factor ATF-2 (Activating
DE   transcription factor 2) (cAMP response element-binding protein CRE-
DE   BP1) (HB16).
GN   Name=ATF2; Synonyms=CREB2, CREBP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   MEDLINE=90005408; PubMed=2529117;
RA   Maekawa T., Sakura H., Kanei-Ishii C., Sudo T., Yoshimura T.,
RA   Fujisawa J., Yoshida M., Ishii S.;
RT   "Leucine zipper structure of the protein CRE-BP1 binding to the cyclic
RT   AMP response element in brain.";
RL   EMBO J. 8:2023-2028(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
RX   MEDLINE=97211815; PubMed=9058782;
RA   Yang L., Lanier E.R., Kraig E.;
RT   "Identification of a novel, spliced variant of CREB that is
RT   preferentially expressed in the thymus.";
RL   J. Immunol. 158:2522-2525(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 193-487.
RX   MEDLINE=90205810; PubMed=2320002;
RA   Kara C.J., Liou H.-C., Ivashkiv L.B., Glimcher L.H.;
RT   "A cDNA for a human cyclic AMP response element-binding protein which
RT   is distinct from CREB and expressed preferentially in brain.";
RL   Mol. Cell. Biol. 10:1347-1357(1990).
RN   [4]
RP   INTERACTION WITH UTF1.
RX   MEDLINE=98421505; PubMed=9748258; DOI=10.1074/jbc.273.40.25840;
RA   Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A.,
RA   Muramatsu M.;
RT   "Characterization of functional domains of an embryonic stem cell
RT   coactivator UTF1 which are conserved and essential for potentiation of
RT   ATF-2 activity.";
RL   J. Biol. Chem. 273:25840-25849(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53 AND SER-94,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
CC   -!- FUNCTION: Transcriptional activator, probably constitutive, which
CC       binds to the cAMP-responsive element (CRE) (consensus: 5'-
CC       GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular
CC       promoters. Interaction with JUN redirects JUN to bind to CRES
CC       preferentially over the 12-O-tetradecanoylphorbol-13-acetate
CC       response elements (TRES) as part of an ATF2-c-Jun complex.
CC   -!- SUBUNIT: Binds DNA as a dimer and can form a homodimer in the
CC       absence of DNA. Can form a heterodimer with JUN. Interacts with
CC       SMAD3 and SMAD4. Binds through its N-terminal region to UTF1 which
CC       acts as a coactivator of ATF2 transcriptional activity.
CC   -!- INTERACTION:
CC       Q15759:MAPK11; NbExp=1; IntAct=EBI-1170906, EBI-298304;
CC       P45983-1:MAPK8; NbExp=1; IntAct=EBI-1170906, EBI-288687;
CC       P45984-1:MAPK9; NbExp=1; IntAct=EBI-1170906, EBI-713586;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P15336-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15336-2; Sequence=VSP_000587, VSP_000588;
CC   -!- TISSUE SPECIFICITY: Abundant expression seen in the brain.
CC   -!- PTM: Phosphorylation of Thr-51 and Thr-53 by MAPK14 causes
CC       increased transcriptional activity. Also phosphorylated and
CC       activated by JNK.
CC   -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
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DR   EMBL; X15875; CAA33886.1; ALT_INIT; mRNA.
DR   EMBL; U16028; AAB64017.1; -; mRNA.
DR   EMBL; M31630; AAA35951.1; -; mRNA.
DR   PIR; S05380; S05380.
DR   UniGene; Hs.592510; -.
DR   PDB; 1BHI; NMR; @=1-38.
DR   PDB; 1T2K; X-ray; D=336-396.
DR   DIP; DIP:632N; -.
DR   IntAct; P15336; -.
DR   TRANSFAC; T00167; -.
DR   Ensembl; ENSG00000115966; Homo sapiens.
DR   KEGG; hsa:1386; -.
DR   HGNC; HGNC:784; ATF2.
DR   HPA; CAB003769; -.
DR   MIM; 123811; gene.
DR   PharmGKB; PA25084; -.
DR   Reactome; REACT_6900.2; Immune System signaling.
DR   ArrayExpress; P15336; -.
DR   GermOnline; ENSG00000115966; Homo sapiens.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor acti...; TAS:ProtInc.
DR   GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR004827; TF_bZIP.
DR   InterPro; IPR007087; Znf_C2H2.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SMART; SM00355; ZnF_C2H2; 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.
KW   3D-structure; Activator; Alternative splicing; DNA-binding;
KW   Metal-binding; Nucleus; Phosphorylation; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    487       Cyclic AMP-dependent transcription factor
FT                                ATF-2.
FT                                /FTId=PRO_0000076577.
FT   DOMAIN      362    390       Leucine-zipper.
FT   ZN_FING       7     31       C2H2-type.
FT   DNA_BIND    333    356       Basic motif.
FT   MOD_RES      51     51       Phosphothreonine; by MAPK14.
FT   MOD_RES      53     53       Phosphothreonine; by MAPK14.
FT   MOD_RES      94     94       Phosphoserine.
FT   VAR_SEQ       1    158       Missing (in isoform 2).
FT                                /FTId=VSP_000587.
FT   VAR_SEQ     159    167       TSSDSSVII -> MSTAYFQMM (in isoform 2).
FT                                /FTId=VSP_000588.
FT   CONFLICT    191    191       V -> L (in Ref. 2).
FT   CONFLICT    205    205       N -> S (in Ref. 1).
FT   CONFLICT    293    293       R -> L (in Ref. 2).
FT   TURN         12     14
FT   STRAND       17     20
FT   HELIX        21     32
FT   TURN         33     37
FT   HELIX       337    394
SQ   SEQUENCE   487 AA;  52277 MW;  58ADD6240D6270E8 CRC64;
     MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ TPTPTRFLKN
     CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI IRSKIEEPSV VETTHQDSPL
     PHPESTTSDE KEVPLAQTAQ PTSAIVRPAS LQVPNVLLTS SDSSVIIQQA VPSPTSSTVI
     TQAPSSNRPI VPVPGPFPLL LHLPNGQTMP VAIPASITSS NVHVPAAVPL VRPVTMVPSV
     PGIPGPSSPQ PVQSEAKMRL KAALTQQHPP VTNGDTVKGH GSGLVRTQSE ESRPQSLQQP
     ATSTTETPAS PAHTTPQTQS TSGRRRRAAN EDPDEKRRKF LERNRAAASR CRQKRKVWVQ
     SLEKKAEDLS SLNGQLQSEV TLLRNEVAQL KQLLLAHKDC PVTAMQKKSG YHTADKDDSS
     EDISVPSSPH TEAIQHSSVS TSNGVSSTSK AEAVATSVLT QMADQSTEPA LSQIVMAPSS
     QSQPSGS
//