RefSeq (protein)


Location (UCSC) Chr 1: 212.57 – 212.62 Mb Chr 1: 191.17 – 191.22 Mb PubMed search [3] [4] Wikidata
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Cyclic AMP-dependent transcription factor ATF-3 is a protein that, in humans, is encoded by the ATF3 gene.[5]


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 in Pain Research.[8]

See also


ATF3 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000162772 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026628 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Chen BP, Liang G, Whelan J, Hai T (June 1994). "ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by alternatively spliced isoforms". J Biol Chem. 269 (22): 15819–26. PMID 7515060. 
  6. ^ "Entrez Gene: ATF3 activating transcription factor 3". 
  7. ^ Chen BP, Wolfgang CD, Hai T (Mar 1996). "Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10". Molecular and Cellular Biology. 16 (3): 1157–68. doi:10.1128/MCB.16.3.1157. PMC 231098Freely accessible. PMID 8622660. 
  8. ^ Lindå H, Sköld MK, Ochsmann T (2011). "Activating transcription factor 3, a useful marker for regenerative response after nerve root injury". Front Neurol. 2: 30. doi:10.3389/fneur.2011.00030. PMC 3099310Freely accessible. PMID 21629765. 
  9. ^ Pearson AG, Gray CW, Pearson JF, Greenwood JM, During MJ, Dragunow M (December 2003). "ATF3 enhances c-Jun-mediated neurite sprouting". Brain Res. Mol. Brain Res. 120 (1): 38–45. doi:10.1016/j.molbrainres.2003.09.014. PMID 14667575. 
  10. ^ a b Chen BP, Wolfgang CD, Hai T (March 1996). "Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10". Mol. Cell. Biol. 16 (3): 1157–68. doi:10.1128/MCB.16.3.1157. PMC 231098Freely accessible. PMID 8622660. 
  11. ^ Hai T, Curran T (May 1991). "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity". Proc. Natl. Acad. Sci. U.S.A. 88 (9): 3720–4. doi:10.1073/pnas.88.9.3720. PMC 51524Freely accessible. PMID 1827203. 
  12. ^ Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (January 1994). "Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression". Mol. Endocrinol. 8 (1): 59–68. doi:10.1210/mend.8.1.8152431. PMID 8152431. 
  13. ^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070. 
  14. ^ Yan C, Wang H, Boyd DD (March 2002). "ATF3 represses 72-kDa type IV collagenase (MMP-2) expression by antagonizing p53-dependent trans-activation of the collagenase promoter". J. Biol. Chem. 277 (13): 10804–12. doi:10.1074/jbc.M112069200. PMID 11792711. 
  15. ^ Kang Y, Chen CR, Massagué J (April 2003). "A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells". Mol. Cell. 11 (4): 915–26. doi:10.1016/s1097-2765(03)00109-6. PMID 12718878. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

  1. ^ Koh EH, Park JY, Park HS, Jeon MJ, Ryu JW, Kim M, Kim SY, Kim MS, Kim SW, Park IS, Youn JH, Lee KU (December 2007). "Essential role of mitochondrial function in adiponectin synthesis in adipocytes". Diabetes. 56 (12): 2973–81. doi:10.2337/db07-0510. PMID 17827403.