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Homo sapiens
Homo sapiens
Mus musculus
Homo sapiens
Mus musculus
Homo sapiens
Mus musculus
Mus musculus
Homo sapiens
Mus musculus
Transcription Factor Encyclopedia  BETA
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No annotation is available in this section for this article. The content below is taken from a related TF, FOSL1 (Homo sapiens).

FOSL1 encodes for 271 amino acid protein with an expected molecular weight of 29.4 kDa. However, in protein extracts isolated from cells stimulated with growth factors or from cancer cells, FOSL1 exhibits multiple bands ranging from 30-40 kDa on immunoblots. Although the appearance of these multiple forms is mainly attributed to post-translational modifications of this protein, FOSL1 exhibits several alternatively spliced variants and one un-spliced form with different transcripts encoding for proteins with different functional domains ( The nature of formation of these alternatively spliced variants of FOSL1 and their functional significance in physiologic and pathologic processes is unclear.

Covalent modifications
No annotation is available in this section for this article. The content below is taken from a related TF, FOSL1 (Homo sapiens).

FOSL1 is covalently modified by posttranslational modifications via phosphorylation at serine and threonine residues, mainly through Rsk and ERK1/2/5 MAP kinases.[1][2][3][4][5][2][6][7]These modifications are known to affect both the protein stability and the transactivation potential of FOSL1.[8] FOSL1 also contains several cysteine residues. The cysteine residues of JUN (a dimeric partner of FOSL1) have been shown to undergo oxidation and glutathionylation as well as sumoylation, which affect its DNA binding activity.[9] [10][11] Whether such modification(s) affects FOSL1 functions, such as its DNA binding activity and transactivation potential, remains to be investigated. FOSL1 contains a nuclear localization signal and is mostly localized in the nucleus. However, immunolocalization studies revealed the presence of a FOSL1 antigen in the cytoplasm in certain situations, such as in the presence of oxidative stress [3] and in cancerous tissues.[12] Although the exact nature of this nuclear-cytoplasmic localization in regulating various cellular processes is unclear, it appears that this trafficking affects the gene expression as well as the stability of this transcription factor.[3]

  1. Young MR et al. Transactivation of Fra-1 and consequent activation of AP-1 occur extracellular signal-regulated kinase dependently. Mol. Cell. Biol., 22(2):587-98. (PMID 11756554)
  2. Basbous J et al. Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer. Mol. Cell. Biol., 27(11):3936-50. (PMID 17371847)
  3. Burch PM et al. An extracellular signal-regulated kinase 1- and 2-dependent program of chromatin trafficking of c-Fos and Fra-1 is required for cyclin D1 expression during cell cycle reentry. Mol. Cell. Biol., 24(11):4696-709. (PMID 15143165)
  4. Casalino L et al. Accumulation of Fra-1 in ras-transformed cells depends on both transcriptional autoregulation and MEK-dependent posttranslational stabilization. Mol. Cell. Biol., 23(12):4401-15. (PMID 12773579)
  5. Vial E et al. ERK-MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility. Cancer Cell, 4(1):67-79. (PMID 12892714)
  6. Gruda MC et al. Regulation of Fra-1 and Fra-2 phosphorylation differs during the cell cycle of fibroblasts and phosphorylation in vitro by MAP kinase affects DNA binding activity. Oncogene, 9(9):2537-47. (PMID 8058317)
  1. Murphy LO et al. A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration. Mol. Cell. Biol., 24(1):144-53. (PMID 14673150)
  2. Gomard T et al. Fos family protein degradation by the proteasome. Biochem. Soc. Trans., 36(Pt 5):858-63. (PMID 18793151)
  3. Abate C et al. Redox regulation of fos and jun DNA-binding activity in vitro. Science, 249(4973):1157-61. (PMID 2118682)
  4. Klatt P et al. Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation. J. Biol. Chem., 274(22):15857-64. (PMID 10336489)
  5. Bossis G et al. Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation. Mol. Cell. Biol., 25(16):6964-79. (PMID 16055710)
  6. Song Y et al. An association of a simultaneous nuclear and cytoplasmic localization of Fra-1 with breast malignancy. BMC Cancer, 6:298. (PMID 17192200)