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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.

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C2H2-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  3. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  4. cAMP response element binding Source: Ensembl
  5. cAMP response element binding protein binding Source: Ensembl
  6. chromatin binding Source: MGI
  7. histone acetyltransferase activity Source: UniProtKB
  8. metal ion binding Source: UniProtKB-KW
  9. protein binding Source: UniProtKB
  10. 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. intra-S DNA damage checkpoint Source: UniProtKB
  5. outflow tract morphogenesis Source: MGI
  6. positive regulation of mitochondrial membrane permeability involved in apoptotic process Source: UniProtKB
  7. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  9. positive regulation of transforming growth factor beta2 production Source: MGI
  10. regulation of transcription, DNA-templated Source: UniProtKB
  11. 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:2.3.1.48)
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.

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-2
PRO_0000076578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphothreonine; by PKC/PRKCH By similarity
Modified residuei44 – 441Phosphoserine; by VRK1 By 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 VRK1 By similarity
Modified residuei72 – 721Phosphoserine By similarity
Modified residuei94 – 941Phosphoserine By similarity
Modified residuei98 – 981Phosphothreonine By similarity
Modified residuei103 – 1031Phosphoserine; by PKC/PRKCA and PKC/PRKCB By similarity
Modified residuei310 – 3101Phosphoserine By similarity
Modified residuei322 – 3221Phosphoserine; by PKC/PRKCA and PKC/PRKCB By similarity
Modified residuei339 – 3391N6-acetyllysine By similarity
Modified residuei349 – 3491Phosphoserine; by PKC/PRKCA and PKC/PRKCB By similarity
Modified residuei356 – 3561N6-acetyllysine By similarity
Modified residuei472 – 4721Phosphoserine; by ATM By similarity
Modified residuei480 – 4801Phosphoserine; by ATM By 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.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP16951.
PaxDbiP16951.
PRIDEiP16951.

PTM databases

PhosphoSiteiP16951.

Expressioni

Gene expression databases

ArrayExpressiP16951.
BgeeiP16951.
CleanExiMM_ATF2.
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.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini334 – 39764bZIP
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Essential for its histone acetyltransferase activity By similarity
Regioni336 – 35621Basic motif By similarity
Add
BLAST
Regioni362 – 39029Leucine-zipper By similarity
Add
BLAST

Motif

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

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.

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

MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ    50
TPTPTRFLKN CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI 100
IRSKIEEPSV VETTHQDSPL PHPESTTSDE KEVPLAQTAQ PTSAIVRPAS 150
LQVPNVLLTS SDSSVIIQQA VPSPTSSTVI TQAPSSNRPI VPVPGPFPLL 200
LHLPNGQTMP VAIPASITSS NVHVPAAVPL VRPVTMVPSV PGIPGPSSPQ 250
PVQSEAKMRL KAALTQQHPP VTNGDTVKGH GSGLVRTQSE ESRPQSLQQP 300
ATSTTETPAS PAHTTPQTQN TSGRRRRAAN EDPDEKRRKF LERNRAAASR 350
CRQKRKVWVQ SLEKKAEDLS SLNGQLQSEV TLLRNEVAQL KQLLLAHKDC 400
PVTAMQKKSG YHTADKDDSS EDLSVPSSPH TEAIQHSSVS TSNGVSSTSK 450
AEAVATSVLT QMADQSTEPA LSQIVMAPPS QAQPSGS 487
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.
The sequence AAB21129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848MSDDK…SVIVA → MHCPWVWP in isoform 3.
VSP_000589Add
BLAST
Alternative sequencei132 – 22998Missing in isoform 2.
VSP_000590Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti482 – 4876AQPSGS → HSPQEVD in AAB21128. 1 Publication
Sequence conflicti482 – 4876AQPSGS → HSPQEVD in AAB21129. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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

ArrayExpressi P16951.
Bgeei P16951.
CleanExi MM_ATF2.
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: September 3, 2014
This is version 141 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

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