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Gene Review

GLIPR2  -  GLI pathogenesis-related 2

Homo sapiens

Synonyms: C9orf19, GAPR-1, GAPR1, GliPR 2, Glioma pathogenesis-related protein 2, ...
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Disease relevance of C9orf19

  • A novel human transcript, C9orf19, mapped to the genomic region involved in hereditary inclusion body myopathy (IBM2) at chromosome 9p12-p13, has been cloned and characterized [1].
  • We propose that increased GLIPR-2 expression in kidney contributes to development of fibrosis by increasing the pool of activated fibroblasts, possibly through the induction of EMT [2].

High impact information on C9orf19


Biological context of C9orf19

  • Mutation analysis of C9orf19 in IBM2 patients excluded it as the disease causing gene and revealed four single nucleotide polymorphisms within and in the vicinity of the gene, which will certainly be useful tools to study its potential role in several human diseases mapped to chromosome 9p12-p13 [1].
  • Genomic characterization of the C9orf19 gene identified five exons extending over 27.2 kb of genomic DNA, located 12 kb centromeric to the tumor suppressor RECK gene [1].

Anatomical context of C9orf19

  • C9orf19 mRNA is expressed in a wide range of adult tissues as a single transcript, most abundantly in lung and peripheral blood leukocytes [1].
  • Examination of the expression pattern of GLIPR-2 indicated that the protein is selectively expressed in epithelial cells [2].
  • GAPR-1 is tightly anchored to membranes and absent from the cytosol, although it does not possess a membrane-spanning domain [5].

Analytical, diagnostic and therapeutic context of C9orf19


  1. Cloning and characterization of a human novel gene C9orf19 encoding a conserved putative protein with an SCP-like extracellular protein domain. Eisenberg, I., Barash, M., Kahan, T., Mitrani-Rosenbaum, S. Gene (2002) [Pubmed]
  2. The plant pathogenesis related protein GLIPR-2 is highly expressed in fibrotic kidney and promotes epithelial to mesenchymal transition in vitro. Baxter, R.M., Crowell, T.P., George, J.A., Getman, M.E., Gardner, H. Matrix Biol. (2007) [Pubmed]
  3. Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex. Eberle, H.B., Serrano, R.L., Füllekrug, J., Schlosser, A., Lehmann, W.D., Lottspeich, F., Kaloyanova, D., Wieland, F.T., Helms, J.B. J. Cell. Sci. (2002) [Pubmed]
  4. Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism. Serrano, R.L., Kuhn, A., Hendricks, A., Helms, J.B., Sinning, I., Groves, M.R. J. Mol. Biol. (2004) [Pubmed]
  5. Crystallization of a Golgi-associated PR-1-related protein (GAPR-1) that localizes to lipid-enriched microdomains. Groves, M.R., Kuhn, A., Hendricks, A., Radke, S., Serrano, R.L., Helms, J.B., Sinning, I. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
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