P16951 · ATF2_MOUSE
- ProteinCyclic AMP-dependent transcription factor ATF-2
- GeneAtf2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids487 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCyclic AMP-dependent transcription factor ATF-2
- Short namescAMP-dependent transcription factor ATF-2
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP16951
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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).
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000076578 | 1-487 | Cyclic AMP-dependent transcription factor ATF-2 | |||
Sequence: MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDLSVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQMADQSTEPALSQIVMAPPSQAQPSGS | ||||||
Modified residue | 34 | Phosphothreonine; by PKC/PRKCH | ||||
Sequence: T | ||||||
Modified residue | 44 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 51 | Phosphothreonine; by MAPK11 and MAPK14 | ||||
Sequence: T | ||||||
Modified residue | 53 | Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK3 | ||||
Sequence: T | ||||||
Modified residue | 55 | Phosphothreonine; by VRK1 | ||||
Sequence: T | ||||||
Modified residue | 72 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 94 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 98 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 103 | Phosphoserine; by PKC/PRKCA and PKC/PRKCB | ||||
Sequence: S | ||||||
Modified residue | 118 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 310 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 322 | Phosphoserine; by PKC/PRKCA and PKC/PRKCB | ||||
Sequence: S | ||||||
Modified residue | 339 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 349 | Phosphoserine; by PKC/PRKCA and PKC/PRKCB | ||||
Sequence: S | ||||||
Modified residue | 356 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 424 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 428 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 472 | Phosphoserine; by ATM | ||||
Sequence: S | ||||||
Modified residue | 480 | Phosphoserine; by ATM | ||||
Sequence: S |
Post-translational modification
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. Phosphorylated by PLK3 following hyperosmotic stress. Also phosphorylated and activated by JNK and CaMK4. 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 acetylation of histones H2B and H4.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
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, MRE11, XPO1, KAT5 and CUL3 (By similarity).
Binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity
Binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 7-31 | C2H2-type | ||||
Sequence: FLCTAPGCGQRFTNEDHLAVHKHKH | ||||||
Region | 106-137 | Disordered | ||||
Sequence: EEPSVVETTHQDSPLPHPESTTSDEKEVPLAQ | ||||||
Region | 241-355 | Disordered | ||||
Sequence: PGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKR | ||||||
Region | 278-281 | Essential for its histone acetyltransferase activity | ||||
Sequence: KGHG | ||||||
Compositional bias | 282-324 | Polar residues | ||||
Sequence: SGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGR | ||||||
Compositional bias | 325-348 | Basic and acidic residues | ||||
Sequence: RRRAANEDPDEKRRKFLERNRAAA | ||||||
Domain | 334-397 | bZIP | ||||
Sequence: DEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAH | ||||||
Region | 336-356 | Basic motif | ||||
Sequence: KRRKFLERNRAAASRCRQKRK | ||||||
Region | 362-390 | Leucine-zipper | ||||
Sequence: LEKKAEDLSSLNGQLQSEVTLLRNEVAQL | ||||||
Motif | 387-396 | Nuclear export signal | ||||
Sequence: VAQLKQLLLA | ||||||
Region | 407-453 | Disordered | ||||
Sequence: KKSGYHTADKDDSSEDLSVPSSPHTEAIQHSSVSTSNGVSSTSKAEA | ||||||
Compositional bias | 424-453 | Polar residues | ||||
Sequence: SVPSSPHTEAIQHSSVSTSNGVSSTSKAEA |
Sequence similarities
Belongs to the bZIP family. ATF subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P16951-1
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.
- Name1
- Length487
- Mass (Da)52,298
- Last updated2000-05-30 v2
- ChecksumF9CDEC3BC3119ACB
P16951-2
- Name2
- Differences from canonical
- 132-229: Missing
P16951-3
- Name3
- Differences from canonical
- 1-48: MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVA → MHCPWVWP
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_000589 | 1-48 | in isoform 3 | |||
Sequence: MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVA → MHCPWVWP | ||||||
Alternative sequence | VSP_000590 | 132-229 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 282-324 | Polar residues | ||||
Sequence: SGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQNTSGR | ||||||
Compositional bias | 325-348 | Basic and acidic residues | ||||
Sequence: RRRAANEDPDEKRRKFLERNRAAA | ||||||
Compositional bias | 424-453 | Polar residues | ||||
Sequence: SVPSSPHTEAIQHSSVSTSNGVSSTSKAEA | ||||||
Sequence conflict | 482-487 | in Ref. 1; AAB21128/AAB21129 | ||||
Sequence: AQPSGS → HSPQEVD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF483482 EMBL· GenBank· DDBJ | AAL90756.1 EMBL· GenBank· DDBJ | mRNA | ||
AF483483 EMBL· GenBank· DDBJ | AAL90757.1 EMBL· GenBank· DDBJ | mRNA | ||
S76657 EMBL· GenBank· DDBJ | AAB21128.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
S76659 EMBL· GenBank· DDBJ | AAB21129.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
S76655 EMBL· GenBank· DDBJ | AAB21127.1 EMBL· GenBank· DDBJ | mRNA | ||
M31629 EMBL· GenBank· DDBJ | AAA39780.1 EMBL· GenBank· DDBJ | mRNA |