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Protein

Cyclic AMP-dependent transcription factor ATF-2

Gene

ATF2

Organism
Homo sapiens (Human)
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.4 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri25 – 49C2H2-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • cAMP response element binding Source: BHF-UCL
  • cAMP response element binding protein binding Source: BHF-UCL
  • chromatin binding Source: Ensembl
  • enhancer sequence-specific DNA binding Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein kinase binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: BHF-UCL
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: Ensembl
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB
  • transcription coactivator activity Source: ProtInc
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: BHF-UCL
  • transcription factor activity, RNA polymerase II transcription factor binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: MGI

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

BioCyciZFISH:ENSG00000115966-MONOMER.
ReactomeiR-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-3214847. HATs acetylate histones.
R-HSA-400253. Circadian Clock.
R-HSA-450341. Activation of the AP-1 family of transcription factors.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
SignaLinkiP15336.
SIGNORiP15336.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic AMP-dependent transcription factor ATF-2 (EC:2.3.1.481 Publication)
Short name:
cAMP-dependent transcription factor ATF-2
Alternative name(s):
Activating transcription factor 2
Cyclic AMP-responsive element-binding protein 2
Short name:
CREB-2
Short name:
cAMP-responsive element-binding protein 2
HB16
Histone acetyltransferase ATF2
cAMP response element-binding protein CRE-BP1
Gene namesi
Name:ATF2
Synonyms:CREB2, CREBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:784. ATF2.

Subcellular locationi

  • Nucleus
  • Cytoplasm
  • Mitochondrion outer membrane

  • 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-52 is required for its nuclear localization and negatively regulates its mitochondrial localization. Co-localizes with the MRN complex in the IR-induced foci (IRIF).

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi69T → A: Weak histone acetyltransferase activity. 1 Publication1
Mutagenesisi71T → A: Impairs phosphorylation by PLK3. Weak histone acetyltransferase activity. 2 Publications1
Mutagenesisi121S → A: Reduced phosphorylation and repression of c-Jun-mediated activation of transcription. 1

Organism-specific databases

DisGeNETi1386.
OpenTargetsiENSG00000115966.
PharmGKBiPA25084.

Chemistry databases

DrugBankiDB00852. Pseudoephedrine.

Polymorphism and mutation databases

BioMutaiATF2.
DMDMi215274241.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000765771 – 505Cyclic AMP-dependent transcription factor ATF-2Add BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52Phosphothreonine; by PKC/PRKCH1 Publication1
Modified residuei62Phosphoserine; by VRK1Combined sources1 Publication1
Modified residuei69Phosphothreonine; by MAPK11 and MAPK14Combined sources3 Publications1
Modified residuei71Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK3Combined sources4 Publications1
Modified residuei73Phosphothreonine; by VRK11 Publication1
Modified residuei90PhosphoserineCombined sources1
Modified residuei112PhosphoserineCombined sources1
Modified residuei116PhosphothreonineCombined sources1
Modified residuei121Phosphoserine; by PKC/PRKCA and PKC/PRKCB1 Publication1
Modified residuei136PhosphoserineCombined sources1
Modified residuei328PhosphoserineCombined sources1
Modified residuei340Phosphoserine; by PKC/PRKCA and PKC/PRKCB1 Publication1
Modified residuei357N6-acetyllysine1 Publication1
Modified residuei367Phosphoserine; by PKC/PRKCA and PKC/PRKCB1 Publication1
Modified residuei374N6-acetyllysine1 Publication1
Modified residuei442PhosphoserineCombined sources1
Modified residuei446PhosphoserineCombined sources1
Modified residuei490Phosphoserine; by ATM1 Publication1
Modified residuei498Phosphoserine; by ATM1 Publication1

Post-translational modificationi

Phosphorylation of Thr-69 by MAPK14 and MAPK11, and at Thr-71 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity. Phosphorylated by PLK3 following hyperosmotic stress. Also phosphorylated and activated by JNK and CaMK4. ATM-mediated phosphorylation at Ser-490 and Ser-498 stimulates its function in DNA damage response. Phosphorylation at Ser-62, Thr-73 and Ser-121 activates its transcriptional activity. Phosphorylation at Thr-69 or Thr-71 enhances its histone acetyltransferase (HAT) activity.9 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP15336.
MaxQBiP15336.
PaxDbiP15336.
PeptideAtlasiP15336.
PRIDEiP15336.

PTM databases

iPTMnetiP15336.
PhosphoSitePlusiP15336.

Expressioni

Tissue specificityi

Ubiquitously expressed, with more abundant expression in the brain.

Gene expression databases

BgeeiENSG00000115966.
CleanExiHS_ATF2.
ExpressionAtlasiP15336. baseline and differential.
GenevisibleiP15336. HS.

Organism-specific databases

HPAiCAB003769.
HPA022134.

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. Interacts with the HK1/VDAC1 complex. Interacts with NBN, MRE11A, XPO1, KAT5 and CUL3.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATF3P188472EBI-1170906,EBI-712767
CITED1Q999662EBI-1170906,EBI-2624951
EXOSC8Q96B263EBI-1170906,EBI-371922
FOSP011007EBI-1170906,EBI-852851
FOSQ6FG413EBI-1170906,EBI-10198738
FOSL2P154084EBI-1170906,EBI-3893419
HBZP0C7463EBI-1170906,EBI-10890294From a different organism.
HDAC4P565242EBI-1170906,EBI-308629
JUNP0541214EBI-1170906,EBI-852823
JUNBP172752EBI-1170906,EBI-748062
JUNDP175352EBI-1170906,EBI-2682803
KIFC3Q9BVG83EBI-1170906,EBI-2125614
MAPK9P459845EBI-1170906,EBI-713568
MDV005Q9DGW52EBI-1170906,EBI-10889526From a different organism.
NFATC1O956442EBI-1170906,EBI-6907210
SS18Q155322EBI-1170906,EBI-2560599
SUMO1P631653EBI-1170906,EBI-80140
SYT-SSX2A4PIW011EBI-1170906,EBI-6050533
VRK1Q999865EBI-1170906,EBI-1769146
ZDHHC17Q8IUH53EBI-1170906,EBI-524753

GO - Molecular functioni

  • cAMP response element binding protein binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107776. 213 interactors.
DIPiDIP-632N.
IntActiP15336. 206 interactors.
MINTiMINT-1788434.
STRINGi9606.ENSP00000264110.

Structurei

Secondary structure

1505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni30 – 32Combined sources3
Beta strandi35 – 38Combined sources4
Helixi39 – 50Combined sources12
Turni51 – 55Combined sources5
Helixi355 – 412Combined sources58

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BHINMR-A19-56[»]
1T2KX-ray3.00D354-414[»]
4H36X-ray3.00B48-55[»]
ProteinModelPortaliP15336.
SMRiP15336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15336.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini352 – 415bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni296 – 299Essential for its histone acetyltransferase activity4
Regioni354 – 374Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni380 – 408Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1 – 7Nuclear export signal 1 (N-NES)7
Motifi405 – 414Nuclear export signal 2 (C-NES)10

Domaini

The nuclear export signal 1 (N-NES) negatively regulates its nuclear localization and transcriptional activity.

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 fingeri25 – 49C2H2-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiP15336.
KOiK04450.
OMAiHPESTTN.
OrthoDBiEOG091G0AO8.
PhylomeDBiP15336.

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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P15336-1) [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
MKFKLHVNSA RQYKDLWNMS DDKPFLCTAP GCGQRFTNED HLAVHKHKHE
60 70 80 90 100
MTLKFGPARN DSVIVADQTP TPTRFLKNCE EVGLFNELAS PFENEFKKAS
110 120 130 140 150
EDDIKKMPLD LSPLATPIIR SKIEEPSVVE TTHQDSPLPH PESTTSDEKE
160 170 180 190 200
VPLAQTAQPT SAIVRPASLQ VPNVLLTSSD SSVIIQQAVP SPTSSTVITQ
210 220 230 240 250
APSSNRPIVP VPGPFPLLLH LPNGQTMPVA IPASITSSNV HVPAAVPLVR
260 270 280 290 300
PVTMVPSVPG IPGPSSPQPV QSEAKMRLKA ALTQQHPPVT NGDTVKGHGS
310 320 330 340 350
GLVRTQSEES RPQSLQQPAT STTETPASPA HTTPQTQSTS GRRRRAANED
360 370 380 390 400
PDEKRRKFLE RNRAAASRCR QKRKVWVQSL EKKAEDLSSL NGQLQSEVTL
410 420 430 440 450
LRNEVAQLKQ LLLAHKDCPV TAMQKKSGYH TADKDDSSED ISVPSSPHTE
460 470 480 490 500
AIQHSSVSTS NGVSSTSKAE AVATSVLTQM ADQSTEPALS QIVMAPSSQS

QPSGS
Length:505
Mass (Da):54,537
Last modified:November 25, 2008 - v4
Checksum:i0190EEFAEC8891A7
GO
Isoform 2 (identifier: P15336-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: Missing.
     177-185: TSSDSSVII → MSTAYFQMM

Show »
Length:329
Mass (Da):35,044
Checksum:iFA37EF544698FEFA
GO
Isoform 3 (identifier: P15336-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     210-505: Missing.

Show »
Length:209
Mass (Da):23,050
Checksum:iA26AF07CA5D8D5E7
GO
Isoform 4 (identifier: P15336-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MKFKLHVNSARQYKDLWNMSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVA → MYCAWMWP

Show »
Length:447
Mass (Da):48,013
Checksum:i344628FF8F94AAED
GO
Isoform 5 (identifier: P15336-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.

Show »
Length:487
Mass (Da):52,277
Checksum:i58ADD6240D6270E8
GO
Isoform 6 (identifier: P15336-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.
     34-394: Missing.

Show »
Length:126
Mass (Da):13,149
Checksum:iB9D2E843EB156412
GO
Isoform 7 (identifier: P15336-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.
     210-237: PVPGPFPLLLHLPNGQTMPVAIPASITS → SFDQSPWCLVFQESQVLPLPNQYSQKQK
     238-505: Missing.

Show »
Length:219
Mass (Da):24,097
Checksum:i6DA3C87FF1008F68
GO
Isoform 8 (identifier: P15336-8) [UniParc]FASTAAdd to basket
Also known as: ATF2-small

The sequence of this isoform differs from the canonical sequence as follows:
     34-394: Missing.

Show »
Length:144
Mass (Da):15,409
Checksum:i8B7F060B955355C7
GO

Sequence cautioni

The sequence AAY17203 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAY17207 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti209V → L in AAB64017 (PubMed:9058782).Curated1
Sequence conflicti223N → S in CAA33886 (PubMed:2529117).Curated1
Sequence conflicti223N → S in AAY17203 (Ref. 4) Curated1
Sequence conflicti223N → S in AAY17207 (Ref. 4) Curated1
Sequence conflicti223N → S in AAY17215 (Ref. 4) Curated1
Sequence conflicti311R → L in AAB64017 (PubMed:9058782).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035999352D → H in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0005871 – 176Missing in isoform 2. 1 PublicationAdd BLAST176
Alternative sequenceiVSP_0469591 – 66MKFKL…SVIVA → MYCAWMWP in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0469601 – 18Missing in isoform 5, isoform 6 and isoform 7. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_04759334 – 394Missing in isoform 6 and isoform 8. 2 PublicationsAdd BLAST361
Alternative sequenceiVSP_000588177 – 185TSSDSSVII → MSTAYFQMM in isoform 2. 1 Publication9
Alternative sequenceiVSP_045161210 – 505Missing in isoform 3. 1 PublicationAdd BLAST296
Alternative sequenceiVSP_047594210 – 237PVPGP…ASITS → SFDQSPWCLVFQESQVLPLP NQYSQKQK in isoform 7. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_047595238 – 505Missing in isoform 7. 1 PublicationAdd BLAST268

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15875 mRNA. Translation: CAA33886.1.
U16028 mRNA. Translation: AAB64017.1.
AY029364 mRNA. Translation: AAK55760.1.
DQ003037 mRNA. Translation: AAY17203.1. Different initiation.
DQ003038 mRNA. Translation: AAY17204.1.
DQ003041 mRNA. Translation: AAY17207.1. Different initiation.
DQ003044 mRNA. Translation: AAY17210.1.
DQ003047 mRNA. Translation: AAY17213.1.
DQ003049 mRNA. Translation: AAY17215.1.
AC131958 Genomic DNA. Translation: AAX88876.1.
AC074291 Genomic DNA. Translation: AAY15004.1.
AC007435 Genomic DNA. No translation available.
AC096649 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11111.1.
CH471058 Genomic DNA. Translation: EAX11112.1.
CH471058 Genomic DNA. Translation: EAX11113.1.
BC026175 mRNA. Translation: AAH26175.1.
BC107698 mRNA. Translation: AAI07699.1.
BC130335 mRNA. Translation: AAI30336.1.
BC130337 mRNA. Translation: AAI30338.1.
M31630 mRNA. Translation: AAA35951.1.
CCDSiCCDS2262.1. [P15336-1]
CCDS58737.1. [P15336-4]
CCDS58738.1. [P15336-5]
CCDS58739.1. [P15336-3]
PIRiS05380.
RefSeqiNP_001243019.1. NM_001256090.1. [P15336-1]
NP_001243020.1. NM_001256091.1. [P15336-5]
NP_001243021.1. NM_001256092.1. [P15336-4]
NP_001243022.1. NM_001256093.1.
NP_001243023.1. NM_001256094.1. [P15336-3]
NP_001871.2. NM_001880.3. [P15336-1]
UniGeneiHs.592510.

Genome annotation databases

EnsembliENST00000264110; ENSP00000264110; ENSG00000115966. [P15336-1]
ENST00000345739; ENSP00000340576; ENSG00000115966. [P15336-4]
ENST00000392544; ENSP00000376327; ENSG00000115966. [P15336-1]
ENST00000409499; ENSP00000386282; ENSG00000115966. [P15336-8]
ENST00000409635; ENSP00000387093; ENSG00000115966. [P15336-4]
ENST00000409833; ENSP00000386526; ENSG00000115966. [P15336-3]
ENST00000426833; ENSP00000407911; ENSG00000115966. [P15336-5]
GeneIDi1386.
KEGGihsa:1386.
UCSCiuc002ujk.5. human. [P15336-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15875 mRNA. Translation: CAA33886.1.
U16028 mRNA. Translation: AAB64017.1.
AY029364 mRNA. Translation: AAK55760.1.
DQ003037 mRNA. Translation: AAY17203.1. Different initiation.
DQ003038 mRNA. Translation: AAY17204.1.
DQ003041 mRNA. Translation: AAY17207.1. Different initiation.
DQ003044 mRNA. Translation: AAY17210.1.
DQ003047 mRNA. Translation: AAY17213.1.
DQ003049 mRNA. Translation: AAY17215.1.
AC131958 Genomic DNA. Translation: AAX88876.1.
AC074291 Genomic DNA. Translation: AAY15004.1.
AC007435 Genomic DNA. No translation available.
AC096649 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11111.1.
CH471058 Genomic DNA. Translation: EAX11112.1.
CH471058 Genomic DNA. Translation: EAX11113.1.
BC026175 mRNA. Translation: AAH26175.1.
BC107698 mRNA. Translation: AAI07699.1.
BC130335 mRNA. Translation: AAI30336.1.
BC130337 mRNA. Translation: AAI30338.1.
M31630 mRNA. Translation: AAA35951.1.
CCDSiCCDS2262.1. [P15336-1]
CCDS58737.1. [P15336-4]
CCDS58738.1. [P15336-5]
CCDS58739.1. [P15336-3]
PIRiS05380.
RefSeqiNP_001243019.1. NM_001256090.1. [P15336-1]
NP_001243020.1. NM_001256091.1. [P15336-5]
NP_001243021.1. NM_001256092.1. [P15336-4]
NP_001243022.1. NM_001256093.1.
NP_001243023.1. NM_001256094.1. [P15336-3]
NP_001871.2. NM_001880.3. [P15336-1]
UniGeneiHs.592510.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BHINMR-A19-56[»]
1T2KX-ray3.00D354-414[»]
4H36X-ray3.00B48-55[»]
ProteinModelPortaliP15336.
SMRiP15336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107776. 213 interactors.
DIPiDIP-632N.
IntActiP15336. 206 interactors.
MINTiMINT-1788434.
STRINGi9606.ENSP00000264110.

Chemistry databases

DrugBankiDB00852. Pseudoephedrine.

PTM databases

iPTMnetiP15336.
PhosphoSitePlusiP15336.

Polymorphism and mutation databases

BioMutaiATF2.
DMDMi215274241.

Proteomic databases

EPDiP15336.
MaxQBiP15336.
PaxDbiP15336.
PeptideAtlasiP15336.
PRIDEiP15336.

Protocols and materials databases

DNASUi1386.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264110; ENSP00000264110; ENSG00000115966. [P15336-1]
ENST00000345739; ENSP00000340576; ENSG00000115966. [P15336-4]
ENST00000392544; ENSP00000376327; ENSG00000115966. [P15336-1]
ENST00000409499; ENSP00000386282; ENSG00000115966. [P15336-8]
ENST00000409635; ENSP00000387093; ENSG00000115966. [P15336-4]
ENST00000409833; ENSP00000386526; ENSG00000115966. [P15336-3]
ENST00000426833; ENSP00000407911; ENSG00000115966. [P15336-5]
GeneIDi1386.
KEGGihsa:1386.
UCSCiuc002ujk.5. human. [P15336-1]

Organism-specific databases

CTDi1386.
DisGeNETi1386.
GeneCardsiATF2.
HGNCiHGNC:784. ATF2.
HPAiCAB003769.
HPA022134.
MIMi123811. gene.
neXtProtiNX_P15336.
OpenTargetsiENSG00000115966.
PharmGKBiPA25084.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiP15336.
KOiK04450.
OMAiHPESTTN.
OrthoDBiEOG091G0AO8.
PhylomeDBiP15336.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115966-MONOMER.
ReactomeiR-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-3214847. HATs acetylate histones.
R-HSA-400253. Circadian Clock.
R-HSA-450341. Activation of the AP-1 family of transcription factors.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
SignaLinkiP15336.
SIGNORiP15336.

Miscellaneous databases

ChiTaRSiATF2. human.
EvolutionaryTraceiP15336.
GeneWikiiActivating_transcription_factor_2.
GenomeRNAii1386.
PROiP15336.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115966.
CleanExiHS_ATF2.
ExpressionAtlasiP15336. baseline and differential.
GenevisibleiP15336. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P15336
Secondary accession number(s): A1L3Z2
, A4D7U4, A4D7U5, A4D7V1, D3DPE9, G8JLM5, Q13000, Q3B7B7, Q4ZFU9, Q53RY2, Q8TAR1, Q96JT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 189 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.