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Gene Review

ELK3  -  ELK3, ETS-domain protein (SRF accessory...

Homo sapiens

Synonyms: ERP, ETS domain-containing protein Elk-3, ETS-related protein ERP, ETS-related protein NET, NET, ...
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Disease relevance of ELK3


Psychiatry related information on ELK3


High impact information on ELK3

  • The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA) [2].
  • Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10 [2].
  • Net (ERP/SAP2) one of the Ras-inducible TCFs, has a novel inhibitory domain with resemblance to the helix-loop-helix motif [8].
  • However, within the B-cell lineage, ERP is highly expressed primarily at early stages of B-lymphocyte development, and expression declines drastically upon B-cell maturation, correlating with the enhancer activity of the IgH pi site [9].
  • We have cloned the gene for a new ets-related transcription factor, ERP (ets-related protein), from the murine pre-B cell line BASC 6C2 and from mouse lung tissue [9].

Chemical compound and disease context of ELK3


Biological context of ELK3

  • These data suggest that SAP1, SAP2, and SAP3 all contribute to the overall virulence of C. albicans and presumably all play important roles during disseminated infections [10].
  • Removal of the carboxy terminus enables ERP to interact with a variety of ets-binding sites including the E74 site, the IgH enhancer pi site, and the lck promoter ets site, suggesting a carboxy-terminal negative regulatory domain [9].
  • The complete amino acid sequence of the 81 residues in SAP-2 has been determined [11].
  • beta-Glucosidase activator (SAP-2) is a family of heat-stable, acidic glycoproteins which stimulate enzymatic hydrolysis of glucosylceramide [11].
  • The cDNA, designed SAP-1/SAP-2 cDNA, hybridizes with two human mRNA species of approximately 3 kb in length, which most probably arise from polyadenylation at different sites [12].

Anatomical context of ELK3

  • ERP, a new member of the ets transcription factor/oncoprotein family: cloning, characterization, and differential expression during B-lymphocyte development [9].
  • In pulse-chase experiments using antisera raised against SAP-1 or SAP-2, no cross-reacting material could be detected in the patients' fibroblasts [13].
  • Only Sap2 was found to contribute to the ability of C. albicans to damage endothelial cells and stimulate them to express E-selectin [14].
  • Polyclonal anti-SAP-1 and SAP-2 antisera confirmed the tissue-specificity and revealed the subcellular localization of SAPs in large granules concentrated in the apical part of the gut epithelial cells of the parasite [15].
  • Recombinant SAP-2 of F. hepatica has been shown to induce lysis of human erythrocytes and peripheral blood mononuclear cells [15].

Associations of ELK3 with chemical compounds

  • When expressed separately, full length SAP1, SAP2, or the NH2-terminal domain alone, are able to assemble into filaments [16].
  • Secretion of SAP2 was significantly enhanced by addition of AlCl3 but not of KCl, LiCl, CaCl2, MgCl2, mannitol or sucrose to suspension cultures [17].
  • In the absence of T258A and S259A mutations, alanine substitution of all other potential phosphosites within the hNET did not block PKC-induced phosphorylation and down-regulation [18].
  • Saturable concentration- and time-dependent binding of mucin to C. albicans was abrogated by pronase or Sap2p treatment of mucin but was unaffected by beta-mercaptoethanol, sodium periodate, neuraminidase, lectins, or potentially inhibitory sugars [19].
  • Only ritonavir and saquinavir inhibited Sap2p, Sapt1p, Sapp1p, and Saplp in micromolar concentrations [20].

Other interactions of ELK3

  • These data provide further evidence for a crucial role of Sap1 and Sap2 in C. albicans vaginal infections [1].
  • Sap1, Sap2 and Sap3 isoenzymes were found to be related to the vaginopathic potential of C. albicans; Sap4, Sap5 and Sap6 isoenzymes were found to be correlated with systemic infections [21].
  • The amino-terminal amino acid sequences of SAP2 (57 kDa), SAP4 (21 kDa), SAP5 (19 kDa) and SAP6 (17 kDa) were homologous to the sequences of proline-rich proteins, indicating that proline-rich proteins are secreted specifically by these salt-adapted cells [17].
  • Sphingolipid activator protein-2 (SAP-2) has been found to stimulate the enzymatic hydrolysis of at least three sphingolipids, glucosylceramide, galactosylceramide and sphingomyelin [5].

Analytical, diagnostic and therapeutic context of ELK3

  • Colonization of the RHVE by C. albicans SC5314 did not cause any visible epithelial damage 6 h after inoculation, although expression of SAP2, SAP9, and SAP10 was detected by reverse transcriptase PCR [1].
  • ERP differences with vs. without concurrent fMRI [22].
  • Isoelectric focusing followed by electroblotting and immunochemical staining demonstrated no significant difference in the charge of SAP-2 obtained from different cell lines [5].
  • Using monospecific antibodies against SAP-2 the level of SAP-2 was determined in cultured skin fibroblasts by rocket immunoelectrophoresis [5].


  1. The secreted aspartyl proteinases Sap1 and Sap2 cause tissue damage in an in vitro model of vaginal candidiasis based on reconstituted human vaginal epithelium. Schaller, M., Bein, M., Korting, H.C., Baur, S., Hamm, G., Monod, M., Beinhauer, S., Hube, B. Infect. Immun. (2003) [Pubmed]
  2. Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. O'Brien, J.S., Kretz, K.A., Dewji, N., Wenger, D.A., Esch, F., Fluharty, A.L. Science (1988) [Pubmed]
  3. In vivo analysis of secreted aspartyl proteinase expression in human oral candidiasis. Naglik, J.R., Newport, G., White, T.C., Fernandes-Naglik, L.L., Greenspan, J.S., Greenspan, D., Sweet, S.P., Challacombe, S.J., Agabian, N. Infect. Immun. (1999) [Pubmed]
  4. Invasion of Candida albicans correlates with expression of secreted aspartic proteinases during experimental infection of human epidermis. Schaller, M., Schackert, C., Korting, H.C., Januschke, E., Hube, B. J. Invest. Dermatol. (2000) [Pubmed]
  5. Studies on a sphingolipid activator protein (SAP-2) in fibroblasts from patients with lysosomal storage diseases, including Niemann-Pick disease Type C. Fujibayashi, S., Wenger, D.A. Clin. Chim. Acta (1985) [Pubmed]
  6. Neural correlates of impulsive responding in borderline personality disorder: ERP evidence for reduced action monitoring. de Bruijn, E.R., Grootens, K.P., Verkes, R.J., Buchholz, V., Hummelen, J.W., Hulstijn, W. Journal of psychiatric research. (2006) [Pubmed]
  7. The development of visual- and auditory processing in Rett syndrome: an ERP study. Stauder, J.E., Smeets, E.E., van Mil, S.G., Curfs, L.G. Brain Dev. (2006) [Pubmed]
  8. Net (ERP/SAP2) one of the Ras-inducible TCFs, has a novel inhibitory domain with resemblance to the helix-loop-helix motif. Maira, S.M., Wurtz, J.M., Wasylyk, B. EMBO J. (1996) [Pubmed]
  9. ERP, a new member of the ets transcription factor/oncoprotein family: cloning, characterization, and differential expression during B-lymphocyte development. Lopez, M., Oettgen, P., Akbarali, Y., Dendorfer, U., Libermann, T.A. Mol. Cell. Biol. (1994) [Pubmed]
  10. Disruption of each of the secreted aspartyl proteinase genes SAP1, SAP2, and SAP3 of Candida albicans attenuates virulence. Hube, B., Sanglard, D., Odds, F.C., Hess, D., Monod, M., Schäfer, W., Brown, A.J., Gow, N.A. Infect. Immun. (1997) [Pubmed]
  11. The activator protein for glucosylceramide beta-glucosidase from guinea pig liver. Improved isolation method and complete amino acid sequence. Sano, A., Radin, N.S., Johnson, L.L., Tarr, G.E. J. Biol. Chem. (1988) [Pubmed]
  12. Human sphingolipid activator protein-1 and sphingolipid activator protein-2 are encoded by the same gene. Reiner, O., Dagan, O., Horowitz, M. J. Mol. Neurosci. (1989) [Pubmed]
  13. Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene. Schnabel, D., Schröder, M., Fürst, W., Klein, A., Hurwitz, R., Zenk, T., Weber, J., Harzer, K., Paton, B.C., Poulos, A. J. Biol. Chem. (1992) [Pubmed]
  14. Secreted aspartyl proteinases and interactions of Candida albicans with human endothelial cells. Ibrahim, A.S., Filler, S.G., Sanglard, D., Edwards, J.E., Hube, B. Infect. Immun. (1998) [Pubmed]
  15. The saposin-like proteins 1, 2, and 3 of Fasciola gigantica. Grams, R., Adisakwattana, P., Ritthisunthorn, N., Eursitthichai, V., Vichasri-Grams, S., Viyanant, V. Mol. Biochem. Parasitol. (2006) [Pubmed]
  16. Structure of a filamentous phosphoglycoprotein polymer: the secreted acid phosphatase of Leishmania mexicana. Stierhof, Y.D., Wiese, M., Ilg, T., Overath, P., Häner, M., Aebi, U. J. Mol. Biol. (1998) [Pubmed]
  17. Specific secretion of proline-rich proteins by salt-adapted winged bean cells. Esaka, M., Hayakawa, H. Plant Cell Physiol. (1995) [Pubmed]
  18. Phosphorylation of the norepinephrine transporter at threonine 258 and serine 259 is linked to protein kinase C-mediated transporter internalization. Jayanthi, L.D., Annamalai, B., Samuvel, D.J., Gether, U., Ramamoorthy, S. J. Biol. Chem. (2006) [Pubmed]
  19. Characterization of binding of Candida albicans to small intestinal mucin and its role in adherence to mucosal epithelial cells. de Repentigny, L., Aumont, F., Bernard, K., Belhumeur, P. Infect. Immun. (2000) [Pubmed]
  20. Secreted aspartic proteases of Candida albicans, Candida tropicalis, Candida parapsilosis and Candida lusitaniae. Inhibition with peptidomimetic inhibitors. Pichová, I., Pavlícková, L., Dostál, J., Dolejsí, E., Hrusková-Heidingsfeldová, O., Weber, J., Ruml, T., Soucek, M. Eur. J. Biochem. (2001) [Pubmed]
  21. Distribution of secreted aspartyl proteinases using a polymerase chain reaction assay with SAP specific primers in Candida albicans isolates. Kalkanci, A., Bozdayi, G., Biri, A., Kustimur, S. Folia Microbiol. (Praha) (2005) [Pubmed]
  22. ERP differences with vs. without concurrent fMRI. Bregadze, N., Lavric, A. International journal of psychophysiology : official journal of the International Organization of Psychophysiology. (2006) [Pubmed]
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