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Gene Review

MORF4L1  -  mortality factor 4 like 1

Homo sapiens

Synonyms: Eaf3, FWP006, HSPC008, HSPC061, HsT17725, ...
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Disease relevance of MORF4L1

  • The C-terminal part of MRG15 forms a conserved MRG domain which is involved in interactions with the tumor suppressor protein retinoblastoma and a nucleoprotein PAM14 during transcriptional regulation [1].
  • Overexpression from the cytomegalovirus promoter eventually resulted in cell death, possibly due to competition with hMRG15 in endogenous nucleoprotein complexes [2].

High impact information on MORF4L1

  • MRG15, a closely related family member, is in a complex with the retinoblastoma tumor suppressor protein Rb and activates the B-myb promoter, which is tightly controlled by Rb/E2F through the E2F binding site [3].
  • In this study, sucrose gradient analysis demonstrated that MRG15 was present in two distinct nuclear protein complexes, MAF1 (MRG15-associated factor 1) and MAF2 [4].
  • Our previous results indicated that MRG15 (MORF-related gene on chromosome 15) could derepress the B-myb promoter by association with Rb [4].
  • MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation [4].
  • Collectively these results suggest that MRG15 regulates transcription through interactions with a cellular protein complex containing Rb and PAM14 [5].

Biological context of MORF4L1


Associations of MORF4L1 with chemical compounds

  • After nucleotide sequencing and the analysis of homology with known genes, five clones were identified; ribosomal protein S27 (MSGen-9), MRG 15 (MSGen-15), androgen-binding protein (MSGen-18), cathepsin H (MSGen-28), and cytochrome c (MSGen-47) [6].

Other interactions of MORF4L1

  • We have further demonstrated that these interactions require the helix-loop-helix and leucine zipper domains of MRG15 [5].


  1. The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14. Zhang, P., Zhao, J., Wang, B., Du, J., Lu, Y., Chen, J., Ding, J. Protein Sci. (2006) [Pubmed]
  2. Functional analysis of MRG-1: the ortholog of human MRG15 in Caenorhabditis elegans. Olgun, A., Aleksenko, T., Pereira-Smith, O.M., Vassilatis, D.K. J. Gerontol. A Biol. Sci. Med. Sci. (2005) [Pubmed]
  3. MRGX is a novel transcriptional regulator that exhibits activation or repression of the B-myb promoter in a cell type-dependent manner. Tominaga, K., Leung, J.K., Rookard, P., Echigo, J., Smith, J.R., Pereira-Smith, O.M. J. Biol. Chem. (2003) [Pubmed]
  4. MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation. Pardo, P.S., Leung, J.K., Lucchesi, J.C., Pereira-Smith, O.M. J. Biol. Chem. (2002) [Pubmed]
  5. MRG15 activates the B-myb promoter through formation of a nuclear complex with the retinoblastoma protein and the novel protein PAM14. Leung, J.K., Berube, N., Venable, S., Ahmed, S., Timchenko, N., Pereira-Smith, O.M. J. Biol. Chem. (2001) [Pubmed]
  6. Unique genes induced by mechanical stress in periodontal ligament cells. Myokai, F., Oyama, M., Nishimura, F., Ohira, T., Yamamoto, T., Arai, H., Takashiba, S., Murayama, Y. J. Periodont. Res. (2003) [Pubmed]
  7. Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3. Zhang, P., Du, J., Sun, B., Dong, X., Xu, G., Zhou, J., Huang, Q., Liu, Q., Hao, Q., Ding, J. Nucleic Acids Res. (2006) [Pubmed]
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