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Gene Review

RBM17  -  RNA binding motif protein 17

Homo sapiens

Synonyms: 45 kDa-splicing factor, MGC14439, RNA-binding motif protein 17, SPF45, Splicing factor 45
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Disease relevance of RBM17

  • A similar role for SPF45 is demonstrated in the activation of a cryptic 3' ss generated by a mutation that causes human beta-thalassemia [1].
  • Our analyses using tissue microarrays and sausages of tumors indicated that SPF45 is highly expressed in numerous carcinomas including bladder, breast, colon, lung, ovarian, pancreatic, and prostate [2].
  • However, it is questionable as to whether the SPF 45 product provides protection against 45 minimal erythema doses [3].

High impact information on RBM17

  • A detailed examination of the Drosophila Sex-lethal gene has led to two significant discoveries-the role of the splicing factor SPF45 in defining the site of exon ligation, and that alternative splicing can be regulated at the second step [4].
  • Thus, SPF45-mediated drug resistance in A2780 cells may result in part from effects of SPF45 on the transcription or alternate splicing of ERbeta-regulated genes [5].
  • A2780-SPF45 cells accumulated similar levels of doxorubicin as vector-transfected and parental A2780 cells, indicating that drug resistance is not due to differences in drug accumulation [5].
  • The splicing factor SPF45 (RBM17) is frequently overexpressed in many solid tumors, and stable expression in HeLa cells confers resistance to doxorubicin and vincristine [5].
  • We isolated the human homologue and examined the normal human tissue expression, tumor expression, and the phenotype caused by overexpression of human SPF45 [2].

Biological context of RBM17


Anatomical context of RBM17


Associations of RBM17 with chemical compounds

  • Our effort to identify novel drug-resistant genes in cyclophosphamide-resistant EMT6 mouse mammary tumors led us to the identification of SPF45 [2].

Other interactions of RBM17

  • Coimmunoprecipitation experiments suggest that SPF45 and ERbeta physically interact in vivo [5].
  • The parasite Toxoplasma gondii expresses a 55 kDa protein or TgDRE that belongs to a novel family of proteins characterized by the presence of three domains, a human splicing factor 45-like motif (SF), a glycine-rich motif (G-patch), and a RNA recognition motif (RRM) [7].


  1. Splicing regulation at the second catalytic step by Sex-lethal involves 3' splice site recognition by SPF45. Lallena, M.J., Chalmers, K.J., Llamazares, S., Lamond, A.I., Valcárcel, J. Cell (2002) [Pubmed]
  2. Human SPF45, a splicing factor, has limited expression in normal tissues, is overexpressed in many tumors, and can confer a multidrug-resistant phenotype to cells. Sampath, J., Long, P.R., Shepard, R.L., Xia, X., Devanarayan, V., Sandusky, G.E., Perry, W.L., Dantzig, A.H., Williamson, M., Rolfe, M., Moore, R.E. Am. J. Pathol. (2003) [Pubmed]
  3. Simplified method to substantiate SPF labeling for sunscreen products. Sayre, R.M., Stanfield, J., Lott, D.L., Dowdy, J.C. Photodermatology, photoimmunology & photomedicine. (2003) [Pubmed]
  4. Sex, AGility, and the regulation of alternative splicing. Graveley, B.R. Cell (2002) [Pubmed]
  5. Human splicing factor SPF45 (RBM17) confers broad multidrug resistance to anticancer drugs when overexpressed--a phenotype partially reversed by selective estrogen receptor modulators. Perry, W.L., Shepard, R.L., Sampath, J., Yaden, B., Chin, W.W., Iversen, P.W., Jin, S., Lesoon, A., O'Brien, K.A., Peek, V.L., Rolfe, M., Shyjan, A., Tighe, M., Williamson, M., Krishnan, V., Moore, R.E., Dantzig, A.H. Cancer Res. (2005) [Pubmed]
  6. A novel DNA repair enzyme containing RNA recognition, G-patch and specific splicing factor 45-like motifs in the protozoan parasite Toxoplasma gondii. Dendouga, N., Callebaut, I., Tomavo, S. Eur. J. Biochem. (2002) [Pubmed]
  7. Structural and functional characterization of the TgDRE multidomain protein, a DNA repair enzyme from Toxoplasma gondii. Frénal, K., Callebaut, I., Wecker, K., Prochnicka-Chalufour, A., Dendouga, N., Zinn-Justin, S., Delepierre, M., Tomavo, S., Wolff, N. Biochemistry (2006) [Pubmed]
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