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Gene Review

SERTAD2  -  SERTA domain containing 2

Homo sapiens

Synonyms: KIAA0127, SERTA domain-containing protein 2, Sei-2, TRIP-Br2, Transcriptional regulator interacting with the PHD-bromodomain 2
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High impact information on SERTAD2

  • Ablation of TRIP-Br2, a regulator of fat lipolysis, thermogenesis and oxidative metabolism, prevents diet-induced obesity and insulin resistance [1].
    1. TRIP-Br2-null mice are resistant to obesity and obesity-related insulin resistance.
    2. Adipocytes of these knockout mice showed greater stimulated lipolysis secondary to enhanced expression of hormone sensitive lipase (HSL) and β3-adrenergic (Adrb3) receptors.
    3. The knockout mice also have higher energy expenditure because of increased adipocyte thermogenesis and oxidative metabolism caused by upregulating key enzymes in their respective processes.
    4. Collectively, TRIP-Br2, modulates fat storage through simultaneous regulation of lipolysis, thermogenesis and oxidative metabolism.
    5. TRIP-Br2 expression is selectively elevated in visceral fat in obese humans , suggests that this transcriptional co-regulator is a new therapeutic target for counteracting the development of obesity, insulin resistance and hyperlipidemia.
  • Overexpression of TRIP-Br2 is sufficient to transform murine fibroblasts and promotes tumorigenesis in nude mice. The transformed phenotype is characterized by deregulation of the E2F/DP-transcriptional pathway through upregulation of the key E2F-responsive genes CYCLIN E, CYCLIN A2, CDC6 and DHFR [2].
  • TRIP-Br2 is frequently overexpressed in both cancer cell lines and multiple human tumors TRIP [2].
  • Clinicopathologic correlation indicates that overexpression of TRIP-Br2 in hepatocellular carcinoma is associated with a worse clinical outcome by Kaplan-Meier survival analysis. Small interfering RNAmediated (siRNA) knockdown of TRIP-Br2 was sufficient to inhibit cellautonomous growth of HCT-116 cells in vitro [2].
  • Overexpression of the proto-oncogene TRIP-Br2 (SERTAD2) has been shown to induce E2F activity and [3] promote tumorigenesis [2], whereas ablation of TRIP-Br2 arrests cell proliferation [4].
  • TRIP-Br2 was observed to be a short-lived protein in which the expression level peaks at theG1/S boundary [5].
  • Co-immunoprecipitation studies revealed that TRIP-Br1 and TRIP-Br2 forms ubiquitin conjugates [5].
  • In silico analysis identified a putative leucine-rich nuclear export signal (NES) motif that overlaps with the PHD-Bromo interaction domain in the acidic C-terminal transactivation domain (TAD) of TRIP-Br2. This NES motif is highly conserved

    in widely divergent species and in all TRIP-Br family members [5].


  • Mutation of leucine residue 238 of this NES motif abolished the interaction between CRM1 and TRIP-Br2, as well as the nuclear export of TRIP-Br2 and its subsequent 26 S proteasome-dependent degradation [5].
  • To characterize the TRIP-Br "integrator" function(s), decoy peptides (*Br1 and *Br2) have been used to antagonize the interaction between TRIP-Br1 or TRIP-Br2 and the PHD zinc finger and/or bromodomain of other transcription factors [8].
  • I-mfa domain proteins specifically interact with SERTA domain proteins and repress their transactivating functions [9].




  1. Ablation of TRIP-Br2, a regulator of fat lipolysis, thermogenesis and oxidative metabolism, prevents diet-induced obesity and insulin resistance. Liew, C.W., Boucher, J., Cheong, J.K., Vernochet, C., Koh, H.J., Mallol, C., Townsend, K., Langin, D., Kawamori, D., Hu, J., Tseng, Y.H., Hellerstein, M.K., Farmer, S.R., Goodyear, L., Doria, A., Blüher, M., Hsu, S.I., Kulkarni, R.N. Nat. Med. (2013) [Pubmed]
  2. TRIP-Br2 promotes oncogenesis in nude mice and is frequently overexpressed in multiple human tumors. Cheong, J.K., Gunaratnam, L., Zang, Z.J., Yang, C.M., Sun, X., Nasr, S.L., Sim, K.G., Peh, B.K., Rashid, S.B., Bonventre, J.V., Salto-Tellez, M., Hsu, S.I. J. Transl. Med. (2009) [Pubmed]
  3. TRIP-Br: a novel family of PHD zinc finger- and bromodomain-interacting proteins that regulate the transcriptional activity of E2F-1/DP-1. Hsu, S.I., Yang, C.M., Sim, K.G., Hentschel, D.M., O'Leary, E., Bonventre, J.V. EMBO. J. (2001) [Pubmed]
  4. The TRIP-Br family of transcriptional regulators is essential for the execution of cyclin E-mediated cell cycle progression. Sim, K.G., Cheong, J.K., Hsu, S.I. Cell. Cycle. (2006) [Pubmed]
  5. CRM1-mediated nuclear export is required for 26 S proteasome-dependent degradation of the TRIP-Br2 proto-oncoprotein. Cheong, J.K., Gunaratnam, L., Hsu, S.I. J. Biol. Chem. (2008) [Pubmed]
  6. CDCA4 Is an E2F Transcription Factor Family-induced Nuclear Factor That Regulates E2F-dependent Transcriptional Activation and Cell Proliferation. Hayashi, R., Goto, Y., Ikeda, R., Yokoyama, K.K., Yoshida, K. J. Biol. Chem. (2006) [Pubmed]
  7. Celecoxib reduces microvessel density in patients treated with nasopharyngeal carcinoma and induces changes in gene expression. Soo, R., Wu, J., Aggarwal, A., Tao, Q., Hsieh, W., Putti, T., Tan, K., Soon, W., Lai, Y., Mow, B., Hsu, S., Loh, K., Tan, L., Tan, P., Goh, B.C. Ann. Oncol. (2006) [Pubmed]
  8. TRIP-Br links E2F to novel functions in the regulation of cyclin E expression during cell cycle progression and in the maintenance of genomic stability. Sim, K.G., Zang, Z., Yang, C.M., Bonventre, J.V., Hsu, S.I. Cell Cycle (2004) [Pubmed]
  9. I-mfa domain proteins specifically interact with SERTA domain proteins and repress their transactivating functions. Kusano, S., Shiimura, Y., Eizuru, Y. Biochimie. (2011) [Pubmed]
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