ATF3

Cyclic AMP-dependent transcription factor ATF-3 is a protein that, in humans, is encoded by the ATF3 gene.^[5]

ATF3
Identifiers
Aliases	ATF3, activating transcription factor 3
External IDs	OMIM: 603148; MGI: 109384; HomoloGene: 1265; GeneCards: ATF3; OMA:ATF3 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q32.3 Start 212,565,334 bp[1] End 212,620,777 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 H6|1 96.28 cM Start 190,902,493 bp[2] End 190,950,236 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in vena cava gastric mucosa gallbladder saphenous vein trachea urethra pericardium skin of thigh left uterine tube cardia Top expressed in granulocyte plantaris muscle lumbar spinal ganglion islet of Langerhans intestinal villus jejunum muscle of thigh stroma of bone marrow sciatic nerve endocardial cushion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transcription cis-regulatory region binding protein homodimerization activity protein binding RNA polymerase II transcription regulatory region sequence-specific DNA binding DNA-binding transcription repressor activity, RNA polymerase II-specific protein heterodimerization activity identical protein binding DNA-binding transcription activator activity, RNA polymerase II-specific DNA binding transcription corepressor activity DNA-binding transcription factor activity RNA polymerase II cis-regulatory region sequence-specific DNA binding DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component nucleolus nucleoplasm CHOP-ATF3 complex nucleus Biological process regulation of transcription by RNA polymerase II positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress positive regulation of cell population proliferation skeletal muscle cell differentiation regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance gluconeogenesis cellular response to amino acid starvation negative regulation of transcription, DNA-templated regulation of transcription, DNA-templated positive regulation of TRAIL-activated apoptotic signaling pathway transcription, DNA-templated positive regulation of gene expression PERK-mediated unfolded protein response positive regulation of transcription by RNA polymerase II negative regulation of ERK1 and ERK2 cascade negative regulation of transcription by RNA polymerase II endoplasmic reticulum unfolded protein response transcription by RNA polymerase II positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 467 11910 Ensembl ENSG00000162772 ENSMUSG00000026628 UniProt P18847 Q60765 RefSeq (mRNA) NM_001030287 NM_001040619 NM_001206484 NM_001206485 NM_001206486 NM_001206488 NM_001674 NM_004024 NM_007498 RefSeq (protein) NP_001025458 NP_001035709 NP_001193413 NP_001193415 NP_001193417 NP_001665 NP_031524 Location (UCSC) Chr 1: 212.57 – 212.62 Mb Chr 1: 190.9 – 190.95 Mb PubMed search [3] [4]
Wikidata
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Function

Activating transcription factor 3 is a member of the mammalian activation transcription factor/cAMP responsive element-binding (CREB) protein family of transcription factors. Multiple transcript variants encoding two different isoforms have been found for this gene. The longer isoform represses rather than activates transcription from promoters with ATF binding elements. The shorter isoform (deltaZip2) lacks the leucine zipper protein-dimerization motif and does not bind to DNA, and it stimulates transcription, it is presumed, by sequestering inhibitory co-factors away from the promoter. It is possible that alternative splicing of the ATF3 gene may be physiologically important in the regulation of target genes.^[6]

Clinical significance

ATF-3 is induced upon physiological stress in various tissues.^[7] It is also a marker of regeneration following injury of dorsal root ganglion neurons, as injured regenerating neurons activate this transcription factor. ^[8] Functional validation studies have shown that ATF3 can promote regeneration of peripheral neurons, but is not capable of promoting regeneration of central nervous system neurons. ^[9]

See also

• Activating transcription factor

Interactions

ATF3 has been shown to interact with:

• C-jun,^[10][11][12]
• DDIT3^[11]
• JunD,^[13]
• P53,^[14][15] and
• SMAD3.^[16]