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Gene Review

UBQLN2  -  ubiquilin 2

Homo sapiens

Synonyms: ALS15, CHAP1, CHAP1/DSK2, Chap1, DSK2, ...
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Disease relevance of UBQLN2


High impact information on UBQLN2

  • PLIC-1, a newly described ubiquitin-related protein, inhibited both Jurkat migration toward SDF-1alpha and A431 wound healing, but the closely related PLIC-2 did not [3].
  • Cyclic hydroxamic-acid-containing peptide 1 (CHAP1), designed as a hybrid of trichostatin A and trapoxin, is a lead compound for the development of potent inhibitors of histone deacetylase (HDAC) [4].
  • The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome [5].
  • We have shown previously that ADP released upon platelet adhesion mediated by alphaIIb beta3 integrin triggers accumulation of phosphatidylinositol 3',4'-bisphosphate (PtdIns-3,4-P2) (Gironcel, D. , Racaud-Sultan, C., Payrastre, B., Haricot, M., Borchert, G., Kieffer, N., Breton, M., and Chap, H. (1996) FEBS Lett. 389, 253-256) [6].
  • We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces [7].

Biological context of UBQLN2


Anatomical context of UBQLN2

  • Using a fractionation procedure on Percoll gradient (Perret, B., Chap, H. and Douste-Blazy, L. (1979) Biochim. Biophys. Acta 556, 434-446), the enzyme activity displayed the same profile as that of [3H]concanavalin A, a plasma membrane marker [11].

Associations of UBQLN2 with chemical compounds

  • These results are discussed in the light of our former hypothesis that arachidonic acid release from platelet phospholipids might occur through the sequential action of a phosphatidylinositol-specific phospholipase C coupled to a diacylglycerol lipase (Mauco, G., Chap, H., Simon, M.F. and Douste-Blazy, L. (1978) Biochimie 60, 553-561) [11].

Regulatory relationships of UBQLN2

  • Expression of genes encoding antioxidant proteins was induced in the wild type but not in chap1 mutants [10].


  1. Interhemispheric suppression: a test of central auditory function. Bergman, M., Hirsch, S., Solzi, P. Ear and hearing. (1987) [Pubmed]
  2. Extreme hyperkalemia induced by drugs. Rigolin, V.H., Chap, L. Postgraduate medicine. (1991) [Pubmed]
  3. The ubiquitin-related protein PLIC-1 regulates heterotrimeric G protein function through association with Gbetagamma. N'Diaye, E.N., Brown, E.J. J. Cell Biol. (2003) [Pubmed]
  4. Cyclic hydroxamic-acid-containing peptide 31, a potent synthetic histone deacetylase inhibitor with antitumor activity. Komatsu, Y., Tomizaki, K.Y., Tsukamoto, M., Kato, T., Nishino, N., Sato, S., Yamori, T., Tsuruo, T., Furumai, R., Yoshida, M., Horinouchi, S., Hayashi, H. Cancer Res. (2001) [Pubmed]
  5. The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome. Kleijnen, M.F., Alarcon, R.M., Howley, P.M. Mol. Biol. Cell (2003) [Pubmed]
  6. Lipid products of phosphoinositide 3-kinase and phosphatidylinositol 4',5'-bisphosphate are both required for ADP-dependent platelet spreading. Heraud, J.M., Racaud-Sultan, C., Gironcel, D., Albigès-Rizo, C., Giacomini, T., Roques, S., Martel, V., Breton-Douillon, M., Perret, B., Chap, H. J. Biol. Chem. (1998) [Pubmed]
  7. Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a. Walters, K.J., Kleijnen, M.F., Goh, A.M., Wagner, G., Howley, P.M. Biochemistry (2002) [Pubmed]
  8. Assignment of ubiquilin2 (UBQLN2) to human chromosome xp11. 23-->p11.1 by GeneBridge radiation hybrids. Kaye, F.J., Shows, T.B. Cytogenet. Cell Genet. (2000) [Pubmed]
  9. A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. Kaye, F.J., Modi, S., Ivanovska, I., Koonin, E.V., Thress, K., Kubo, A., Kornbluth, S., Rose, M.D. FEBS Lett. (2000) [Pubmed]
  10. Activation of an AP1-like transcription factor of the maize pathogen Cochliobolus heterostrophus in response to oxidative stress and plant signals. Lev, S., Hadar, R., Amedeo, P., Baker, S.E., Yoder, O.C., Horwitz, B.A. Eukaryotic Cell (2005) [Pubmed]
  11. Studies on enzymes related to diacylglycerol production in activated platelets. II. Subcellular distribution, enzymatic properties and positional specificity of diacylglycerol- and monoacylglycerol-lipases. Mauco, G., Fauvel, J., Chap, H., Douste-Blazy, L. Biochim. Biophys. Acta (1984) [Pubmed]
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