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P15336

- ATF2_HUMAN

UniProt

P15336 - ATF2_HUMAN

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Protein

Cyclic AMP-dependent transcription factor ATF-2

Gene
ATF2, CREB2, CREBP1
Organism
Homo sapiens (Human)
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.4 Publications

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri25 – 4925C2H2-typeAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. adipose tissue development Source: Ensembl
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. chromatin organization Source: Reactome
  4. fat cell differentiation Source: Ensembl
  5. histone acetylation Source: GOC
  6. innate immune response Source: Reactome
  7. intra-S DNA damage checkpoint Source: UniProtKB
  8. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  9. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  10. outflow tract morphogenesis Source: Ensembl
  11. positive regulation of mitochondrial membrane permeability involved in apoptotic process Source: UniProtKB
  12. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  13. positive regulation of transforming growth factor beta2 production Source: Ensembl
  14. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  15. regulation of transcription, DNA-templated Source: UniProtKB
  16. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  17. response to osmotic stress Source: UniProtKB
  18. stress-activated MAPK cascade Source: Reactome
  19. toll-like receptor 10 signaling pathway Source: Reactome
  20. toll-like receptor 2 signaling pathway Source: Reactome
  21. toll-like receptor 3 signaling pathway Source: Reactome
  22. toll-like receptor 4 signaling pathway Source: Reactome
  23. toll-like receptor 5 signaling pathway Source: Reactome
  24. toll-like receptor 9 signaling pathway Source: Reactome
  25. toll-like receptor signaling pathway Source: Reactome
  26. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  27. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  28. transcription from RNA polymerase II promoter Source: GOC
  29. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
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_172610. HATs acetylate histones.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_24941. Circadian Clock.
SignaLinkiP15336.

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
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
ProteomesiUP000005640: 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).7 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. mitochondrial outer membrane Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691T → A: Weak histone acetyltransferase activity. 1 Publication
Mutagenesisi71 – 711T → A: Impairs phosphorylation by PLK3. Weak histone acetyltransferase activity. 2 Publications
Mutagenesisi121 – 1211S → A: Reduced phosphorylation and repression of c-Jun-mediated activation of transcription.

Organism-specific databases

PharmGKBiPA25084.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Cyclic AMP-dependent transcription factor ATF-2PRO_0000076577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphothreonine; by PKC/PRKCH1 Publication
Modified residuei62 – 621Phosphoserine; by VRK11 Publication
Modified residuei69 – 691Phosphothreonine; by MAPK11 and MAPK147 Publications
Modified residuei71 – 711Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK37 Publications
Modified residuei73 – 731Phosphothreonine; by VRK11 Publication
Modified residuei90 – 901Phosphoserine1 Publication
Modified residuei112 – 1121Phosphoserine4 Publications
Modified residuei116 – 1161Phosphothreonine1 Publication
Modified residuei121 – 1211Phosphoserine; by PKC/PRKCA and PKC/PRKCB1 Publication
Modified residuei328 – 3281Phosphoserine1 Publication
Modified residuei340 – 3401Phosphoserine; by PKC/PRKCA and PKC/PRKCB1 Publication
Modified residuei357 – 3571N6-acetyllysine1 Publication
Modified residuei367 – 3671Phosphoserine; by PKC/PRKCA and PKC/PRKCB1 Publication
Modified residuei374 – 3741N6-acetyllysine1 Publication
Modified residuei490 – 4901Phosphoserine; by ATM1 Publication
Modified residuei498 – 4981Phosphoserine; by ATM1 Publication

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

MaxQBiP15336.
PaxDbiP15336.
PRIDEiP15336.

PTM databases

PhosphoSiteiP15336.

Expressioni

Tissue specificityi

Ubiquitously expressed, with more abundant expression in the brain.

Gene expression databases

ArrayExpressiP15336.
BgeeiP15336.
CleanExiHS_ATF2.
GenevestigatoriP15336.

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
CITED1Q999662EBI-1170906,EBI-2624951
FOSP011004EBI-1170906,EBI-852851
HDAC4P565242EBI-1170906,EBI-308629
JUNP054125EBI-1170906,EBI-852823
SS18Q155322EBI-1170906,EBI-2560599
SYT-SSX2A4PIW011EBI-1170906,EBI-6050533
VRK1Q999865EBI-1170906,EBI-1769146
ZDHHC17Q8IUH53EBI-1170906,EBI-524753

Protein-protein interaction databases

BioGridi107776. 190 interactions.
DIPiDIP-632N.
IntActiP15336. 183 interactions.
MINTiMINT-1788434.
STRINGi9606.ENSP00000264110.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni30 – 323
Beta strandi35 – 384
Helixi39 – 5012
Turni51 – 555
Helixi355 – 41258

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHINMR-A19-56[»]
1T2KX-ray3.00D354-414[»]
4H36X-ray3.00B48-55[»]
ProteinModelPortaliP15336.
SMRiP15336. Positions 19-56, 354-414.

Miscellaneous databases

EvolutionaryTraceiP15336.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini352 – 41564bZIPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni296 – 2994Essential for its histone acetyltransferase activity
Regioni354 – 37421Basic motif By similarityAdd
BLAST
Regioni380 – 40829Leucine-zipper By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1 – 77Nuclear export signal 1 (N-NES)
Motifi405 – 41410Nuclear export signal 2 (C-NES)

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.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG306955.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiP15336.
KOiK04450.
OMAiTPIIRNK.
OrthoDBiEOG741Z31.
PhylomeDBiP15336.

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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

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

MKFKLHVNSA RQYKDLWNMS DDKPFLCTAP GCGQRFTNED HLAVHKHKHE    50
MTLKFGPARN DSVIVADQTP TPTRFLKNCE EVGLFNELAS PFENEFKKAS 100
EDDIKKMPLD LSPLATPIIR SKIEEPSVVE TTHQDSPLPH PESTTSDEKE 150
VPLAQTAQPT SAIVRPASLQ VPNVLLTSSD SSVIIQQAVP SPTSSTVITQ 200
APSSNRPIVP VPGPFPLLLH LPNGQTMPVA IPASITSSNV HVPAAVPLVR 250
PVTMVPSVPG IPGPSSPQPV QSEAKMRLKA ALTQQHPPVT NGDTVKGHGS 300
GLVRTQSEES RPQSLQQPAT STTETPASPA HTTPQTQSTS GRRRRAANED 350
PDEKRRKFLE RNRAAASRCR QKRKVWVQSL EKKAEDLSSL NGQLQSEVTL 400
LRNEVAQLKQ LLLAHKDCPV TAMQKKSGYH TADKDDSSED ISVPSSPHTE 450
AIQHSSVSTS NGVSSTSKAE AVATSVLTQM ADQSTEPALS QIVMAPSSQS 500
QPSGS 505
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 AAY17203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAY17207.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti352 – 3521D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_035999

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 176176Missing in isoform 2. VSP_000587Add
BLAST
Alternative sequencei1 – 6666MKFKL…SVIVA → MYCAWMWP in isoform 4. VSP_046959Add
BLAST
Alternative sequencei1 – 1818Missing in isoform 5, isoform 6 and isoform 7. VSP_046960Add
BLAST
Alternative sequencei34 – 394361Missing in isoform 6 and isoform 8. VSP_047593Add
BLAST
Alternative sequencei177 – 1859TSSDSSVII → MSTAYFQMM in isoform 2. VSP_000588
Alternative sequencei210 – 505296Missing in isoform 3. VSP_045161Add
BLAST
Alternative sequencei210 – 23728PVPGP…ASITS → SFDQSPWCLVFQESQVLPLP NQYSQKQK in isoform 7. VSP_047594Add
BLAST
Alternative sequencei238 – 505268Missing in isoform 7. VSP_047595Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091V → L in AAB64017. 1 Publication
Sequence conflicti223 – 2231N → S in CAA33886. 1 Publication
Sequence conflicti223 – 2231N → S in AAY17203. 1 Publication
Sequence conflicti223 – 2231N → S in AAY17207. 1 Publication
Sequence conflicti223 – 2231N → S in AAY17215. 1 Publication
Sequence conflicti311 – 3111R → L in AAB64017. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000392543; ENSP00000376326; ENSG00000115966. [P15336-6]
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]
ENST00000487334; ENSP00000443513; ENSG00000115966. [P15336-7]
GeneIDi1386.
KEGGihsa:1386.
UCSCiuc002ujk.4. human.
uc002ujl.4. human. [P15336-1]
uc002ujm.4. human.
uc002ujv.4. human. [P15336-2]
uc002ujy.2. human.

Polymorphism databases

DMDMi215274241.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2262.1. [P15336-1 ]
CCDS58737.1. [P15336-4 ]
CCDS58738.1. [P15336-5 ]
CCDS58739.1. [P15336-3 ]
PIRi S05380.
RefSeqi NP_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 ]
UniGenei Hs.592510.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BHI NMR - A 19-56 [» ]
1T2K X-ray 3.00 D 354-414 [» ]
4H36 X-ray 3.00 B 48-55 [» ]
ProteinModelPortali P15336.
SMRi P15336. Positions 19-56, 354-414.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107776. 190 interactions.
DIPi DIP-632N.
IntActi P15336. 183 interactions.
MINTi MINT-1788434.
STRINGi 9606.ENSP00000264110.

PTM databases

PhosphoSitei P15336.

Polymorphism databases

DMDMi 215274241.

Proteomic databases

MaxQBi P15336.
PaxDbi P15336.
PRIDEi P15336.

Protocols and materials databases

DNASUi 1386.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264110 ; ENSP00000264110 ; ENSG00000115966 . [P15336-1 ]
ENST00000345739 ; ENSP00000340576 ; ENSG00000115966 . [P15336-4 ]
ENST00000392543 ; ENSP00000376326 ; ENSG00000115966 . [P15336-6 ]
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 ]
ENST00000487334 ; ENSP00000443513 ; ENSG00000115966 . [P15336-7 ]
GeneIDi 1386.
KEGGi hsa:1386.
UCSCi uc002ujk.4. human.
uc002ujl.4. human. [P15336-1 ]
uc002ujm.4. human.
uc002ujv.4. human. [P15336-2 ]
uc002ujy.2. human.

Organism-specific databases

CTDi 1386.
GeneCardsi GC02M175937.
HGNCi HGNC:784. ATF2.
HPAi CAB003769.
HPA022134.
MIMi 123811. gene.
neXtProti NX_P15336.
PharmGKBi PA25084.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306955.
HOGENOMi HOG000220894.
HOVERGENi HBG004300.
InParanoidi P15336.
KOi K04450.
OMAi TPIIRNK.
OrthoDBi EOG741Z31.
PhylomeDBi P15336.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_24941. Circadian Clock.
SignaLinki P15336.

Miscellaneous databases

ChiTaRSi ATF2. human.
EvolutionaryTracei P15336.
GeneWikii Activating_transcription_factor_2.
GenomeRNAii 1386.
NextBioi 35461711.
PROi P15336.
SOURCEi Search...

Gene expression databases

ArrayExpressi P15336.
Bgeei P15336.
CleanExi HS_ATF2.
Genevestigatori P15336.

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. "Leucine zipper structure of the protein CRE-BP1 binding to the cyclic AMP response element in brain."
    Maekawa T., Sakura H., Kanei-Ishii C., Sudo T., Yoshimura T., Fujisawa J., Yoshida M., Ishii S.
    EMBO J. 8:2023-2028(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "Identification of a novel, spliced variant of CREB that is preferentially expressed in the thymus."
    Yang L., Lanier E.R., Kraig E.
    J. Immunol. 158:2522-2525(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Thymus.
  3. "Characterization and functional analysis of cAMP response element modulator protein and activating transcription factor 2 (ATF2) isoforms in the human myometrium during pregnancy and labor: identification of a novel ATF2 species with potent transactivation properties."
    Bailey J., Phillips R.J., Pollard A.J., Gilmore K., Robson S.C., Europe-Finner G.N.
    J. Clin. Endocrinol. Metab. 87:1717-1728(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
    Tissue: Myometrium.
  4. "Homo sapiens activating transcription factor 2 (ATF2) mRNA splice variant."
    von Hippel A.C.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 5; 6 AND 7).
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Brain.
  8. "A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain."
    Kara C.J., Liou H.-C., Ivashkiv L.B., Glimcher L.H.
    Mol. Cell. Biol. 10:1347-1357(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-505 (ISOFORMS 1/2).
  9. "Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade."
    Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.
    Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CAMK4.
  10. "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6."
    Enslen H., Raingeaud J., Davis R.J.
    J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-69 AND THR-71.
  11. "Characterization of functional domains of an embryonic stem cell coactivator UTF1 which are conserved and essential for potentiation of ATF-2 activity."
    Fukushima A., Okuda A., Nishimoto M., Seki N., Hori T.A., Muramatsu M.
    J. Biol. Chem. 273:25840-25849(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UTF1.
  12. "ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation."
    Kawasaki H., Schiltz L., Chiu R., Itakura K., Taira K., Nakatani Y., Yokoyama K.K.
    Nature 405:195-200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-69 AND THR-71.
  13. "Growth factors can activate ATF2 via a two-step mechanism: phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69 through RalGDS-Src-p38."
    Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P., Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A., van Dam H.
    EMBO J. 21:3782-3793(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-69 AND THR-71.
  14. "Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK."
    Sevilla A., Santos C.R., Vega F.M., Lazo P.A.
    J. Biol. Chem. 279:27458-27465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-62 AND THR-73, SUBCELLULAR LOCATION.
  15. "ATM-dependent phosphorylation of ATF2 is required for the DNA damage response."
    Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N., Ronai Z.
    Mol. Cell 18:577-587(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NBN AND MRE11A, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-490 AND SER-498.
  16. "Multiple roles for acetylation in the interaction of p300 HAT with ATF-2."
    Karanam B., Wang L., Wang D., Liu X., Marmorstein R., Cotter R., Cole P.A.
    Biochemistry 46:8207-8216(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-357 AND LYS-374, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "ATF2: a transcription factor that elicits oncogenic or tumor suppressor activities."
    Bhoumik A., Ronai Z.
    Cell Cycle 7:2341-2345(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  18. "Regulation of TIP60 by ATF2 modulates ATM activation."
    Bhoumik A., Singha N., O'Connell M.J., Ronai Z.A.
    J. Biol. Chem. 283:17605-17614(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL3 AND KAT5, SUBCELLULAR LOCATION.
  19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69 AND SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase c controls c-Jun-mediated activation of transcription."
    Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.
    J. Biol. Chem. 284:8567-8581(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-69; THR-71; SER-121; SER-340 AND SER-367, SUBCELLULAR LOCATION.
  23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71 AND SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71; SER-112 AND THR-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Hyperosmotic stress-induced ATF-2 activation through Polo-like kinase 3 in human corneal epithelial cells."
    Wang L., Payton R., Dai W., Lu L.
    J. Biol. Chem. 286:1951-1958(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-71, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-71.
  26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; THR-71; SER-90 AND SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria."
    Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L., Ideker T., Ronai Z.A.
    Cell 148:543-555(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HK1/VDAC1 COMPLEX, PHOSPHORYLATION AT THR-52.
  28. "Critical role of N-terminal end-localized nuclear export signal in regulation of activating transcription factor 2 (ATF2) subcellular localization and transcriptional activity."
    Hsu C.C., Hu C.D.
    J. Biol. Chem. 287:8621-8632(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, INTERACTION WITH XPO1, HETERODIMERIZATION WITH JUN.
  29. "ATF2-at the crossroad of nuclear and cytosolic functions."
    Lau E., Ronai Z.A.
    J. Cell Sci. 125:2815-2824(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  30. "Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain."
    Nagadoi A., Nakazawa K., Uda H., Okuno K., Maekawa T., Ishii S., Nishimura Y.
    J. Mol. Biol. 287:593-607(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 19-56.
  31. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-352.

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: September 3, 2014
This is version 164 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

External Data

Dasty 3

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