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Protein

Cyclic AMP-dependent transcription factor ATF-2

Gene

Atf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri7 – 31C2H2-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Transferase

Keywords - Biological processi

DNA damage, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.
R-MMU-450341. Activation of the AP-1 family of transcription factors.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic AMP-dependent transcription factor ATF-2 (EC:2.3.1.48By similarity)
Short name:
cAMP-dependent transcription factor ATF-2
Alternative name(s):
Activating transcription factor 2
MXBP protein
cAMP response element-binding protein CRE-BP1
Gene namesi
Name:Atf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:109349. Atf2.

Subcellular locationi

  • Nucleus
  • Cytoplasm By similarity
  • Mitochondrion outer membrane By similarity

  • 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).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: MGI
  • mitochondrial outer membrane Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176797.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000765781 – 487Cyclic AMP-dependent transcription factor ATF-2Add BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34Phosphothreonine; by PKC/PRKCHBy similarity1
Modified residuei44PhosphoserineCombined sources1
Modified residuei51Phosphothreonine; by MAPK11 and MAPK14Combined sources1
Modified residuei53Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK3Combined sources1
Modified residuei55Phosphothreonine; by VRK1By similarity1
Modified residuei72PhosphoserineCombined sources1
Modified residuei94PhosphoserineCombined sources1
Modified residuei98PhosphothreonineBy similarity1
Modified residuei103Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity1
Modified residuei118PhosphoserineBy similarity1
Modified residuei310PhosphoserineBy similarity1
Modified residuei322Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity1
Modified residuei339N6-acetyllysineBy similarity1
Modified residuei349Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity1
Modified residuei356N6-acetyllysineBy similarity1
Modified residuei424PhosphoserineBy similarity1
Modified residuei428PhosphoserineBy similarity1
Modified residuei472Phosphoserine; by ATMBy similarity1
Modified residuei480Phosphoserine; by ATMBy similarity1

Post-translational modificationi

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). Phosphorylation at Ser-44, Thr-55 and Ser-103 activates its transcriptional activity (By similarity). ATM-mediated phosphorylation at Ser-472 and Ser-480 stimulates its function in DNA damage response. Phosphorylation at Thr-51 or Thr-53 enhances its histone acetyltransferase (HAT) activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP16951.
PaxDbiP16951.
PeptideAtlasiP16951.
PRIDEiP16951.

PTM databases

iPTMnetiP16951.
PhosphoSitePlusiP16951.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027104.
CleanExiMM_ATF2.
ExpressionAtlasiP16951. baseline and differential.
GenevisibleiP16951. MM.

Interactioni

Subunit structurei

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. Interacts with the HK1/VDAC1 complex. Interacts with NBN, MRE11A, XPO1, KAT5 and CUL3 (By similarity). Binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198233. 15 interactors.
IntActiP16951. 5 interactors.
MINTiMINT-189465.
STRINGi10090.ENSMUSP00000058521.

Structurei

3D structure databases

ProteinModelPortaliP16951.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini334 – 397bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni278 – 281Essential for its histone acetyltransferase activityBy similarity4
Regioni336 – 356Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni362 – 390Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi387 – 396Nuclear export signalBy similarity10

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation
Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri7 – 31C2H2-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiP16951.
KOiK04450.
OMAiHPESTTN.
OrthoDBiEOG091G0AO8.
PhylomeDBiP16951.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR029836. ATF-2.
IPR004827. bZIP.
IPR016378. TF_CRE-BP1-typ.
IPR007087. Znf_C2H2.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR19304:SF9. PTHR19304:SF9. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16951-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ
60 70 80 90 100
TPTPTRFLKN CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI
110 120 130 140 150
IRSKIEEPSV VETTHQDSPL PHPESTTSDE KEVPLAQTAQ PTSAIVRPAS
160 170 180 190 200
LQVPNVLLTS SDSSVIIQQA VPSPTSSTVI TQAPSSNRPI VPVPGPFPLL
210 220 230 240 250
LHLPNGQTMP VAIPASITSS NVHVPAAVPL VRPVTMVPSV PGIPGPSSPQ
260 270 280 290 300
PVQSEAKMRL KAALTQQHPP VTNGDTVKGH GSGLVRTQSE ESRPQSLQQP
310 320 330 340 350
ATSTTETPAS PAHTTPQTQN TSGRRRRAAN EDPDEKRRKF LERNRAAASR
360 370 380 390 400
CRQKRKVWVQ SLEKKAEDLS SLNGQLQSEV TLLRNEVAQL KQLLLAHKDC
410 420 430 440 450
PVTAMQKKSG YHTADKDDSS EDLSVPSSPH TEAIQHSSVS TSNGVSSTSK
460 470 480
AEAVATSVLT QMADQSTEPA LSQIVMAPPS QAQPSGS
Length:487
Mass (Da):52,298
Last modified:May 30, 2000 - v2
Checksum:iF9CDEC3BC3119ACB
GO
Isoform 2 (identifier: P16951-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-229: Missing.

Show »
Length:389
Mass (Da):42,345
Checksum:i770AD65EA6114F10
GO
Isoform 3 (identifier: P16951-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVA → MHCPWVWP

Show »
Length:447
Mass (Da):48,002
Checksum:i35A0751C1627D682
GO

Sequence cautioni

The sequence AAB21128 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAB21129 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti482 – 487AQPSGS → HSPQEVD in AAB21128 (PubMed:11471062).Curated6
Sequence conflicti482 – 487AQPSGS → HSPQEVD in AAB21129 (PubMed:11471062).Curated6

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0005891 – 48MSDDK…SVIVA → MHCPWVWP in isoform 3. CuratedAdd BLAST48
Alternative sequenceiVSP_000590132 – 229Missing in isoform 2. CuratedAdd BLAST98

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF483482 mRNA. Translation: AAL90756.1.
AF483483 mRNA. Translation: AAL90757.1.
S76657 mRNA. Translation: AAB21128.1. Different initiation.
S76659 mRNA. Translation: AAB21129.1. Different initiation.
S76655 mRNA. Translation: AAB21127.1.
M31629 mRNA. Translation: AAA39780.1.
CCDSiCCDS16134.1. [P16951-1]
CCDS16135.1. [P16951-3]
CCDS71076.1. [P16951-2]
PIRiA42026.
C42026.
RefSeqiNP_001020264.1. NM_001025093.2. [P16951-1]
UniGeneiMm.209903.

Genome annotation databases

EnsembliENSMUST00000055833; ENSMUSP00000058521; ENSMUSG00000027104. [P16951-1]
ENSMUST00000090802; ENSMUSP00000088311; ENSMUSG00000027104. [P16951-3]
ENSMUST00000100009; ENSMUSP00000097588; ENSMUSG00000027104. [P16951-1]
ENSMUST00000112007; ENSMUSP00000107638; ENSMUSG00000027104. [P16951-3]
ENSMUST00000112010; ENSMUSP00000107641; ENSMUSG00000027104. [P16951-3]
ENSMUST00000112016; ENSMUSP00000107647; ENSMUSG00000027104. [P16951-2]
ENSMUST00000112017; ENSMUSP00000107648; ENSMUSG00000027104. [P16951-1]
GeneIDi11909.
KEGGimmu:11909.
UCSCiuc008kdd.2. mouse. [P16951-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF483482 mRNA. Translation: AAL90756.1.
AF483483 mRNA. Translation: AAL90757.1.
S76657 mRNA. Translation: AAB21128.1. Different initiation.
S76659 mRNA. Translation: AAB21129.1. Different initiation.
S76655 mRNA. Translation: AAB21127.1.
M31629 mRNA. Translation: AAA39780.1.
CCDSiCCDS16134.1. [P16951-1]
CCDS16135.1. [P16951-3]
CCDS71076.1. [P16951-2]
PIRiA42026.
C42026.
RefSeqiNP_001020264.1. NM_001025093.2. [P16951-1]
UniGeneiMm.209903.

3D structure databases

ProteinModelPortaliP16951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198233. 15 interactors.
IntActiP16951. 5 interactors.
MINTiMINT-189465.
STRINGi10090.ENSMUSP00000058521.

Chemistry databases

ChEMBLiCHEMBL2176797.

PTM databases

iPTMnetiP16951.
PhosphoSitePlusiP16951.

Proteomic databases

MaxQBiP16951.
PaxDbiP16951.
PeptideAtlasiP16951.
PRIDEiP16951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055833; ENSMUSP00000058521; ENSMUSG00000027104. [P16951-1]
ENSMUST00000090802; ENSMUSP00000088311; ENSMUSG00000027104. [P16951-3]
ENSMUST00000100009; ENSMUSP00000097588; ENSMUSG00000027104. [P16951-1]
ENSMUST00000112007; ENSMUSP00000107638; ENSMUSG00000027104. [P16951-3]
ENSMUST00000112010; ENSMUSP00000107641; ENSMUSG00000027104. [P16951-3]
ENSMUST00000112016; ENSMUSP00000107647; ENSMUSG00000027104. [P16951-2]
ENSMUST00000112017; ENSMUSP00000107648; ENSMUSG00000027104. [P16951-1]
GeneIDi11909.
KEGGimmu:11909.
UCSCiuc008kdd.2. mouse. [P16951-1]

Organism-specific databases

CTDi1386.
MGIiMGI:109349. Atf2.

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiP16951.
KOiK04450.
OMAiHPESTTN.
OrthoDBiEOG091G0AO8.
PhylomeDBiP16951.

Enzyme and pathway databases

ReactomeiR-MMU-3214847. HATs acetylate histones.
R-MMU-450341. Activation of the AP-1 family of transcription factors.

Miscellaneous databases

ChiTaRSiAtf2. mouse.
PROiP16951.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027104.
CleanExiMM_ATF2.
ExpressionAtlasiP16951. baseline and differential.
GenevisibleiP16951. MM.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR029836. ATF-2.
IPR004827. bZIP.
IPR016378. TF_CRE-BP1-typ.
IPR007087. Znf_C2H2.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR19304:SF9. PTHR19304:SF9. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATF2_MOUSE
AccessioniPrimary (citable) accession number: P16951
Secondary accession number(s): Q64089, Q64090, Q64091
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.