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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) (cAMP response element-binding protein CRE-BP1)

 ATF2_RAT                Reviewed;         487 AA.
Q00969; Q62870;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
25-OCT-2017, entry version 144.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-2;
Short=cAMP-dependent transcription factor ATF-2;
EC=2.3.1.48 {ECO:0000250|UniProtKB:P15336};
AltName: Full=Activating transcription factor 2;
AltName: Full=cAMP response element-binding protein CRE-BP1;
Name=Atf2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=1714459;
Kageyama R., Sasai Y., Nakanishi S.;
"Molecular characterization of transcription factors that bind to the
cAMP responsive region of the substance P precursor gene. cDNA cloning
of a novel C/EBP-related factor.";
J. Biol. Chem. 266:15525-15531(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Brain;
Muramatsu S.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53 AND SER-94,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:P15336}.
-!- 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 (By similarity). Interacts with the HK1/VDAC1 complex.
Interacts with NBN, MRE11, XPO1, KAT5 and CUL3 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
Mitochondrion outer membrane {ECO:0000250}. 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-34 is
required for its nuclear localization and negatively regulates its
mitochondrial localization. Colocalizes with the MRN complex in
the IR-induced foci (IRIF) (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q00969-1; Sequence=Displayed;
Name=2;
IsoId=Q00969-2; Sequence=VSP_000591;
-!- PTM: Phosphorylation of Thr-51 by MAPK14 and MAPK11, and at Thr-53
by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response
to external stimulus like insulin causes increased transcriptional
activity (By similarity). Phosphorylated by PLK3 following
hyperosmotic stress. Also phosphorylated and activated by JNK and
CaMK4 (By similarity). ATM-mediated phosphorylation at Ser-472 and
Ser-480 stimulates its function in DNA damage response.
Phosphorylation at Ser-44, Thr-55 and Ser-103 activates its
transcriptional activity. Phosphorylation at Thr-51 or Thr-53
enhances its histone acetyltransferase (HAT) activity (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M65148; AAA42013.1; -; mRNA.
EMBL; U38938; AAA93263.1; -; mRNA.
PIR; A39429; A39429.
RefSeq; NP_112280.1; NM_031018.1. [Q00969-1]
UniGene; Rn.9825; -.
ProteinModelPortal; Q00969; -.
SMR; Q00969; -.
BioGrid; 249547; 3.
CORUM; Q00969; -.
STRING; 10116.ENSRNOP00000002174; -.
iPTMnet; Q00969; -.
PhosphoSitePlus; Q00969; -.
PaxDb; Q00969; -.
PRIDE; Q00969; -.
Ensembl; ENSRNOT00000002174; ENSRNOP00000002174; ENSRNOG00000001597. [Q00969-1]
Ensembl; ENSRNOT00000050513; ENSRNOP00000046001; ENSRNOG00000001597. [Q00969-2]
GeneID; 81647; -.
KEGG; rno:81647; -.
UCSC; RGD:621862; rat. [Q00969-1]
CTD; 1386; -.
RGD; 621862; Atf2.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00390000020106; -.
HOGENOM; HOG000220894; -.
HOVERGEN; HBG004300; -.
InParanoid; Q00969; -.
KO; K04450; -.
OMA; HPESTTN; -.
OrthoDB; EOG091G0AO8; -.
PhylomeDB; Q00969; -.
Reactome; R-RNO-3214847; HATs acetylate histones.
Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors.
PRO; PR:Q00969; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000001597; -.
Genevisible; Q00969; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0035497; F:cAMP response element binding; IDA:RGD.
GO; GO:0008140; F:cAMP response element binding protein binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0097186; P:amelogenesis; IDA:RGD.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
GO; GO:0031573; P:intra-S DNA damage checkpoint; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0110024; P:positive regulation of cardiac muscle myoblast proliferation; IEA:Ensembl.
GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; ISS:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:RGD.
GO; GO:0032915; P:positive regulation of transforming growth factor beta2 production; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; ISS:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEP:RGD.
InterPro; IPR029836; ATF-2.
InterPro; IPR004827; bZIP.
InterPro; IPR016378; TF_CRE-BP1-typ.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR19304:SF9; PTHR19304:SF9; 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;
Acetylation; Activator; Alternative splicing; Complete proteome;
Cytoplasm; DNA damage; DNA-binding; Membrane; Metal-binding;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Transferase; Zinc; Zinc-finger.
CHAIN 1 487 Cyclic AMP-dependent transcription factor
ATF-2.
/FTId=PRO_0000076579.
DOMAIN 334 397 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
ZN_FING 7 31 C2H2-type. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 278 281 Essential for its histone
acetyltransferase activity.
{ECO:0000250}.
REGION 336 356 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 362 390 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 387 396 Nuclear export signal. {ECO:0000250}.
MOD_RES 34 34 Phosphothreonine; by PKC/PRKCH.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 44 44 Phosphoserine; by VRK1.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 51 51 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 55 55 Phosphothreonine; by VRK1.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 98 98 Phosphothreonine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 103 103 Phosphoserine; by PKC/PRKCA and
PKC/PRKCB.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 322 322 Phosphoserine; by PKC/PRKCA and
PKC/PRKCB.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 339 339 N6-acetyllysine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 349 349 Phosphoserine; by PKC/PRKCA and
PKC/PRKCB.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 356 356 N6-acetyllysine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 472 472 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:P15336}.
MOD_RES 480 480 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:P15336}.
VAR_SEQ 132 229 Missing (in isoform 2).
{ECO:0000303|PubMed:1714459}.
/FTId=VSP_000591.
SEQUENCE 487 AA; 52287 MW; 4ED95B106DF5F9EE CRC64;
MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ TPTPTRFLKN
CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI IRSKIEEPSV VETTHQDSPL
PHPESTTNDE KEIPLAQTAQ PTSAIVRPAS LQVPNVLLTS SDSSVIIQQA VPSPTSSTVI
TQAPSSNRPI VPVPGPFPLL LHLPNGQTMP VAIPASITSS NVHVPAAVPL VRPVTMVPSV
PGIPGPSSPQ PVQSEAKMRL KAALTQQHPP VTNGDTVKGH GSGLVRAQSE ESRPQSLQQP
ATSTTETPAS PAHTTPQTQN TSGRRRRAAN EDPDEKRRKF LERNRAAASR CRQKRKVWVQ
SLEKKAEDLS SLNGQLQSEV TLLRNEVAQL KQLLLAHKDC PVTAMQKKSG YHTADKDDSS
EDLSVPSSPH TEAIQHSSVS TSNGVSSTSK TEAGATSVLT QMADQSTEPA LSQIVMAPSS
QAQPSGS


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