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Gene Review

RBMX  -  RNA binding motif protein, X-linked

Homo sapiens

Synonyms: Glycoprotein p43, HNRNPG, HNRPG, Heterogeneous nuclear ribonucleoprotein G, RBMXP1, ...
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Disease relevance of RBMX


High impact information on RBMX

  • The hnRNP G family comprises three closely related proteins, hnRNP G, RBMY and hnRNP G-T [4].
  • We show here that hnRNP G and hTra2beta have opposite effects upon the incorporation of several exons, both being able to act as either an activator or a repressor [4].
  • Co-transfection with hnRNP G represses incorporation in cardiac myoblasts, whereas hTra2beta increases it in skeletal myoblasts [4].
  • Surprisingly, although this antiserum was raised against human hnRNP G-T protein, it can also detect a similar protein in the testis of several mammals [5].
  • We conclude that the hnRNP G family of proteins is involved in pre-mRNA splicing and infer that RBM may be involved in Tra2beta-dependent splicing in spermatocytes [6].

Chemical compound and disease context of RBMX

  • Its putative RNA-binding domain most closely resembles that of two previously characterized human RNA-binding proteins, YRRM, the gene for which has been implicated in azoospermia, and hnRNP G, a glycoprotein, also identified as an auto-antigen [7].

Biological context of RBMX

  • We have also found that multiple processed copies of RBMX are present in the human genome [8].
  • RBMX-like sequences (RBMXLs) located on human Chrs 1, 4, 6, 9 (9p13 and 9p24), 11, 20, and X lack introns and thus probably result from retroposition events [8].
  • RBMX and RBMY are members of an ancient pair of genes located on the sex chromosomes that encode RNA-binding proteins involved in splicing [8].
  • These genes have differentiated and evolved separately on the X and Y Chromosomes. RBMY has acquired a testis-specific function, whereas, as shown here, RBMX is ubiquitously expressed and is subject to X inactivation [8].
  • This autosomal, testis-specific copy of RBMX could potentially compensate for RBMX that is presumably inactivated in male germ cells, in a manner analogous to autosomal retroposed copies of other X-linked genes [8].

Anatomical context of RBMX

  • RESULTS: In situ immunohistochemical staining showed robust presence of hnRNP G in the basal cell layers of normal oral epithelium but the level of its staining was markedly reduced in dysplastic or cancerous tissues [3].
  • We found that hnRNP G is expressed in normal human oral epithelial cells while frequently not found in the cells derived from human oral squamous cell carcinomas (HOSCC) [3].

Associations of RBMX with chemical compounds


Other interactions of RBMX

  • One canine serum reacting with Sm proteins was observed, and five canine sera presented anti-RNP autoantibodies against the antigens 70K, A, C, and/or B/B'. The autoantigen most frequently recognised was a 43 kDa nuclear protein, previously described as hnRNP G [10].

Analytical, diagnostic and therapeutic context of RBMX


  1. RBMX is a novel hepatic transcriptional regulator of SREBP-1c gene response to high-fructose diet. Takemoto, T., Nishio, Y., Sekine, O., Ikeuchi, C., Nagai, Y., Maeno, Y., Maegawa, H., Kimura, H., Kashiwagi, A. FEBS Lett. (2007) [Pubmed]
  2. Associations of homologous RNA-binding motif gene on the X chromosome (RBMX) and its like sequence on chromosome 9 (RBMXL9) with non-obstructive azoospermia. Tsujimura, A., Fujita, K., Komori, K., Tanjapatkul, P., Miyagawa, Y., Takada, S., Matsumiya, K., Sada, M., Katsuyama, Y., Ota, M., Okuyama, A. Asian J. Androl. (2006) [Pubmed]
  3. Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive effect against oral squamous cell carcinoma cells. Shin, K.H., Kang, M.K., Kim, R.H., Christensen, R., Park, N.H. Clin. Cancer Res. (2006) [Pubmed]
  4. HnRNP G and Tra2beta: opposite effects on splicing matched by antagonism in RNA binding. Nasim, M.T., Chernova, T.K., Chowdhury, H.M., Yue, B.G., Eperon, I.C. Hum. Mol. Genet. (2003) [Pubmed]
  5. An evolutionarily conserved germ cell-specific hnRNP is encoded by a retrotransposed gene. Elliott, D.J., Venables, J.P., Newton, C.S., Lawson, D., Boyle, S., Eperon, I.C., Cooke, H.J. Hum. Mol. Genet. (2000) [Pubmed]
  6. RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing. Venables, J.P., Elliott, D.J., Makarova, O.V., Makarov, E.M., Cooke, H.J., Eperon, I.C. Hum. Mol. Genet. (2000) [Pubmed]
  7. RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain. Derry, J.M., Kerns, J.A., Francke, U. Hum. Mol. Genet. (1995) [Pubmed]
  8. Expression and conservation of processed copies of the RBMX gene. Lingenfelter, P.A., Delbridge, M.L., Thomas, S., Hoekstra, H.E., Mitchell, M.J., Graves, J.A., Disteche, C.M. Mamm. Genome (2001) [Pubmed]
  9. hnRNP G: sequence and characterization of a glycosylated RNA-binding protein. Soulard, M., Della Valle, V., Siomi, M.C., Piñol-Roma, S., Codogno, P., Bauvy, C., Bellini, M., Lacroix, J.C., Monod, G., Dreyfuss, G. Nucleic Acids Res. (1993) [Pubmed]
  10. Autoantibody profiles in canine ANA-positive sera investigated by immunoblot and ELISA. Welin Henriksson, E., Hansson, H., Karlsson-Parra, A., Pettersson, I. Vet. Immunol. Immunopathol. (1998) [Pubmed]
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