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Protein

Cyclic AMP-dependent transcription factor ATF-2

Gene

Atf2

Organism
Rattus norvegicus (Rat)
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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C2H2-typePROSITE-ProRule annotationAdd
BLAST

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-RNO-3214847. HATs acetylate histones.
R-RNO-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
cAMP response element-binding protein CRE-BP1
Gene namesi
Name:Atf2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi621862. 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
  • mitochondrial outer membrane Source: UniProtKB
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
  • 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_0000076579Add
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 – 511PhosphothreonineCombined sources
Modified residuei53 – 531PhosphothreonineCombined sources
Modified residuei55 – 551Phosphothreonine; by VRK1By similarity
Modified residuei72 – 721PhosphoserineBy similarity
Modified residuei94 – 941PhosphoserineCombined sources
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 residuei424 – 4241PhosphoserineBy similarity
Modified residuei428 – 4281PhosphoserineBy 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). 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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ00969.

PTM databases

iPTMnetiQ00969.
PhosphoSiteiQ00969.

Expressioni

Gene expression databases

GenevisibleiQ00969. RN.

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. 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, MRE11A, XPO1, KAT5 and CUL3 (By similarity).By similarity

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi249547. 2 interactions.
STRINGi10116.ENSRNOP00000002174.

Structurei

3D structure databases

ProteinModelPortaliQ00969.
SMRiQ00969. 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

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiQ00969.
KOiK04450.
OMAiHPESTTN.
OrthoDBiEOG741Z31.
PhylomeDBiQ00969.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q00969-1) [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 PHPESTTNDE KEIPLAQTAQ 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 GSGLVRAQSE 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
TEAGATSVLT QMADQSTEPA LSQIVMAPSS QAQPSGS
Length:487
Mass (Da):52,287
Last modified:May 30, 2000 - v2
Checksum:i4ED95B106DF5F9EE
GO
Isoform 2 (identifier: Q00969-2) [UniParc]FASTAAdd to basket

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

Show »
Length:389
Mass (Da):42,320
Checksum:i7E7185C4B1030F40
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei132 – 22998Missing in isoform 2. 1 PublicationVSP_000591Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65148 mRNA. Translation: AAA42013.1.
U38938 mRNA. Translation: AAA93263.1.
PIRiA39429.
RefSeqiNP_112280.1. NM_031018.1. [Q00969-1]
UniGeneiRn.9825.

Genome annotation databases

EnsembliENSRNOT00000002174; ENSRNOP00000002174; ENSRNOG00000001597. [Q00969-1]
ENSRNOT00000050513; ENSRNOP00000046001; ENSRNOG00000001597. [Q00969-2]
GeneIDi81647.
KEGGirno:81647.
UCSCiRGD:621862. rat. [Q00969-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65148 mRNA. Translation: AAA42013.1.
U38938 mRNA. Translation: AAA93263.1.
PIRiA39429.
RefSeqiNP_112280.1. NM_031018.1. [Q00969-1]
UniGeneiRn.9825.

3D structure databases

ProteinModelPortaliQ00969.
SMRiQ00969. Positions 1-38, 336-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249547. 2 interactions.
STRINGi10116.ENSRNOP00000002174.

PTM databases

iPTMnetiQ00969.
PhosphoSiteiQ00969.

Proteomic databases

PaxDbiQ00969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002174; ENSRNOP00000002174; ENSRNOG00000001597. [Q00969-1]
ENSRNOT00000050513; ENSRNOP00000046001; ENSRNOG00000001597. [Q00969-2]
GeneIDi81647.
KEGGirno:81647.
UCSCiRGD:621862. rat. [Q00969-1]

Organism-specific databases

CTDi1386.
RGDi621862. Atf2.

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiQ00969.
KOiK04450.
OMAiHPESTTN.
OrthoDBiEOG741Z31.
PhylomeDBiQ00969.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ00969.

Gene expression databases

GenevisibleiQ00969. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Kageyama R., Sasai Y., Nakanishi S.
    J. Biol. Chem. 266:15525-15531(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. Muramatsu S.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53 AND SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATF2_RAT
AccessioniPrimary (citable) accession number: Q00969
Secondary accession number(s): Q62870
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: June 8, 2016
This is version 132 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. 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.