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P16951

- ATF2_MOUSE

UniProt

P16951 - ATF2_MOUSE

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Protein

Cyclic AMP-dependent transcription factor ATF-2

Gene

Atf2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C2H2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cAMP response element binding Source: Ensembl
  2. cAMP response element binding protein binding Source: Ensembl
  3. chromatin binding Source: MGI
  4. DNA binding Source: MGI
  5. histone acetyltransferase activity Source: UniProtKB
  6. metal ion binding Source: UniProtKB-KW
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  8. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  9. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. adipose tissue development Source: MGI
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. fat cell differentiation Source: MGI
  4. histone acetylation Source: GOC
  5. intra-S DNA damage checkpoint Source: UniProtKB
  6. outflow tract morphogenesis Source: MGI
  7. positive regulation of mitochondrial membrane permeability involved in apoptotic process Source: UniProtKB
  8. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  9. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  10. positive regulation of transforming growth factor beta2 production Source: MGI
  11. regulation of transcription, DNA-templated Source: UniProtKB
  12. response to osmotic stress Source: UniProtKB
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

ReactomeiREACT_204811. Activation of the AP-1 family of transcription factors.
REACT_226917. HATs acetylate histones.

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
ProteomesiUP000000589: 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

  1. cytoplasm Source: UniProtKB
  2. membrane Source: MGI
  3. mitochondrial outer membrane Source: UniProtKB
  4. nucleus Source: MGI
  5. site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Cyclic AMP-dependent transcription factor ATF-2PRO_0000076578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphothreonine; by PKC/PRKCHBy similarity
Modified residuei44 – 441Phosphoserine; by VRK1By similarity
Modified residuei51 – 511Phosphothreonine; by MAPK11 and MAPK141 Publication
Modified residuei53 – 531Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK31 Publication
Modified residuei55 – 551Phosphothreonine; by VRK1By similarity
Modified residuei72 – 721PhosphoserineBy similarity
Modified residuei94 – 941PhosphoserineBy similarity
Modified residuei98 – 981PhosphothreonineBy similarity
Modified residuei103 – 1031Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity
Modified residuei310 – 3101PhosphoserineBy similarity
Modified residuei322 – 3221Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity
Modified residuei339 – 3391N6-acetyllysineBy similarity
Modified residuei349 – 3491Phosphoserine; by PKC/PRKCA and PKC/PRKCBBy similarity
Modified residuei356 – 3561N6-acetyllysineBy similarity
Modified residuei472 – 4721Phosphoserine; by ATMBy similarity
Modified residuei480 – 4801Phosphoserine; by ATMBy similarity

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 similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP16951.
PaxDbiP16951.
PRIDEiP16951.

PTM databases

PhosphoSiteiP16951.

Expressioni

Gene expression databases

BgeeiP16951.
CleanExiMM_ATF2.
ExpressionAtlasiP16951. baseline and differential.
GenevestigatoriP16951.

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

Protein-protein interaction databases

BioGridi198233. 12 interactions.
IntActiP16951. 5 interactions.
MINTiMINT-189465.

Structurei

3D structure databases

ProteinModelPortaliP16951.
SMRiP16951. Positions 1-38, 336-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini334 – 39764bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Essential for its histone acetyltransferase activityBy similarity
Regioni336 – 35621Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni362 – 39029Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi387 – 39610Nuclear export signalBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C2H2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG306955.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiP16951.
KOiK04450.
OMAiTPIIRNK.
PhylomeDBiP16951.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR004827. bZIP.
IPR016378. TF_cAMP-dep.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
SM00355. ZnF_C2H2. 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. Align

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 AAB21128.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAB21129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti482 – 4876AQPSGS → HSPQEVD in AAB21128. (PubMed:11471062)Curated
Sequence conflicti482 – 4876AQPSGS → HSPQEVD in AAB21129. (PubMed:11471062)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848MSDDK…SVIVA → MHCPWVWP in isoform 3. CuratedVSP_000589Add
BLAST
Alternative sequencei132 – 22998Missing in isoform 2. CuratedVSP_000590Add
BLAST

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]
XP_006498655.1. XM_006498592.1. [P16951-1]
XP_006498656.1. XM_006498593.1. [P16951-1]
XP_006498657.1. XM_006498594.1. [P16951-1]
XP_006498658.1. XM_006498595.1. [P16951-1]
XP_006498659.1. XM_006498596.1. [P16951-1]
XP_006543929.1. XM_006543866.1. [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]
GeneIDi102641666.
11909.
KEGGimmu:102641666.
mmu:11909.
UCSCiuc008kdd.1. 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 .
CCDSi CCDS16134.1. [P16951-1 ]
CCDS16135.1. [P16951-3 ]
CCDS71076.1. [P16951-2 ]
PIRi A42026.
C42026.
RefSeqi NP_001020264.1. NM_001025093.2. [P16951-1 ]
XP_006498655.1. XM_006498592.1. [P16951-1 ]
XP_006498656.1. XM_006498593.1. [P16951-1 ]
XP_006498657.1. XM_006498594.1. [P16951-1 ]
XP_006498658.1. XM_006498595.1. [P16951-1 ]
XP_006498659.1. XM_006498596.1. [P16951-1 ]
XP_006543929.1. XM_006543866.1. [P16951-1 ]
UniGenei Mm.209903.

3D structure databases

ProteinModelPortali P16951.
SMRi P16951. Positions 1-38, 336-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198233. 12 interactions.
IntActi P16951. 5 interactions.
MINTi MINT-189465.

Chemistry

ChEMBLi CHEMBL2176797.

PTM databases

PhosphoSitei P16951.

Proteomic databases

MaxQBi P16951.
PaxDbi P16951.
PRIDEi P16951.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055833 ; 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 ]
GeneIDi 102641666.
11909.
KEGGi mmu:102641666.
mmu:11909.
UCSCi uc008kdd.1. mouse. [P16951-1 ]

Organism-specific databases

CTDi 1386.
MGIi MGI:109349. Atf2.

Phylogenomic databases

eggNOGi NOG306955.
GeneTreei ENSGT00390000020106.
HOGENOMi HOG000220894.
HOVERGENi HBG004300.
InParanoidi P16951.
KOi K04450.
OMAi TPIIRNK.
PhylomeDBi P16951.

Enzyme and pathway databases

Reactomei REACT_204811. Activation of the AP-1 family of transcription factors.
REACT_226917. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi Atf2. mouse.
NextBioi 279971.
PROi P16951.
SOURCEi Search...

Gene expression databases

Bgeei P16951.
CleanExi MM_ATF2.
ExpressionAtlasi P16951. baseline and differential.
Genevestigatori P16951.

Family and domain databases

Gene3Di 3.30.160.60. 1 hit.
InterProi IPR004827. bZIP.
IPR016378. TF_cAMP-dep.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00170. bZIP_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTi SM00338. BRLZ. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: ILS and ISS.
  2. "Functionally distinct isoforms of the CRE-BP DNA-binding protein mediate activity of a T-cell-specific enhancer."
    Georgopoulos K., Morgan B.A., Moore D.D.
    Mol. Cell. Biol. 12:747-757(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-487, ALTERNATIVE SPLICING.
  3. "mXBP/CRE-BP2 and c-Jun form a complex which binds to the cyclic AMP, but not to the 12-O-tetradecanoylphorbol-13-acetate, response element."
    Ivashkiv L.B., Liou H.-C., Kara C.J., Lamph W.W., Verma I.M., Glimcher L.H.
    Mol. Cell. Biol. 10:1609-1621(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-487.
  4. "UTF1, a novel transcriptional coactivator expressed in pluripotent embryonic stem cells and extra-embryonic cells."
    Okuda A., Fukushima A., Nishimoto M., Orimo A., Yamagishi T., Nabeshima Y., Kuro-o M., Nabeshima Y., Boon K., Keaveney M., Stunnenberg H.G., Muramatsu M.
    EMBO J. 17:2019-2032(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UTF1.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 AND THR-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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 26, 2014
This is version 144 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

External Data

Dasty 3