The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Arih2  -  ariadne homolog 2 (Drosophila)

Mus musculus

Synonyms: AI843547, ARI-2, ARI2, Ari2, E3 ubiquitin-protein ligase ARIH2, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Arih2

  • We investigated whether in vivo vaccination with lymphoma cells infected with a recombinant, nonreplicating fowlpox (FP) virus encoding this triad of costimulatory molecules (TRICOM) could stimulate lymphoma-specific immunity [1].
  • Antitumor immunity after vaccination with B lymphoma cells overexpressing a triad of costimulatory molecules [1].
  • CONCLUSIONS: The ability of dendritic cells to activate both naive and effector T cells in vitro and in vivo can be enhanced with the use of poxvirus vectors that potentiate the hyperexpression of a triad of costimulatory molecules [2].
  • These results suggest that His-57, Asp-113, and Ser-194 are the three constituents of the catalytic triad in Achromobacter protease I and that Asp-225 plays a critical role in restricted substrate specificity as a lysyl endopeptidase [3].
  • Wiskott-Aldrich syndrome (WAS) is an X-linked recessive disorder originally characterized by the clinical triad eczema, thrombocytopenia, and severe immunodeficieny, with recurrent bacterial and viral infections, indicating a profound immune cell defect [4].

Psychiatry related information on Arih2


High impact information on Arih2

  • This paper shows that co-culture of mdg/mdg myotubes with normal spinal cord neurons re-establishes Ca2+ channel activity, contraction and normal triad organization [7].
  • The predicted protein resembles serine proteases in that it includes all the residues that form the catalytic triad of the active site of serine proteases [8].
  • The proprotein convertases are all dependent on calcium for activity and all possess highly conserved subtilisin-like domains with the characteristic catalytic triad of this serine protease (ordered Asp, His, and Ser along the polypeptide chain) [9].
  • The pattern resembled that seen with anti-MHC class II antibodies, with the striking exception that BMAC-5+ cells were rare or absent in the portal triad, the islets of Langerhans, and the kidney [10].
  • Enhanced activation of T cells by dendritic cells engineered to hyperexpress a triad of costimulatory molecules [2].

Chemical compound and disease context of Arih2


Biological context of Arih2

  • The biologic function of Triad1 in myelopoiesis was studied by performing granulocyte-macrophage colony-forming unit (CFU-GM) assays using retrovirally transduced primary murine bone marrow cells [11].
  • The structure, in combination with mutagenesis, shows that SpPgdA is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively, somewhat similar to other zinc deacetylases such as LpxC [12].
  • These findings suggest that multiple injections of streptozotocin induce, in susceptible hosts, the triad of direct beta cell cytotoxicity, virus induction within beta cells, and cell-mediated autoimmune reaction [13].
  • Enhancers I and II are most active in hepatocytes surrounding the central vein, with a gradual decrease in activity along the hepatic plates toward the portal triad [14].
  • A seven-bladed beta-propeller domain is situated on top of the catalytic triad and may serve as a "gate" to selectively filter protein access to the catalytic site [15].

Anatomical context of Arih2

  • We conclude that proteasomal degradation of proteins that are ubiquitinated by Triad1 affects the clonogenic growth of primary myeloid progenitor cells [11].
  • Two recombinant poxvirus vectors (replication-defective avipox [fowlpox; rF] and a replication-competent vaccinia [rV]) have been engineered to express a triad of costimulatory molecules (B7-1, intercellular adhesion molecule-1, and leukocyte function-associated antigen-3; designated TRICOM) [2].
  • Ultrastructural analysis demonstrated that triad junctions were reduced in number, and that the SR was often structurally abnormal in the skeletal muscles of the mutant mice [16].
  • The DHP receptor-rich domains may represent the sites where triad junctions with the sarcoplasmic reticulum are being formed [17].
  • The signal conversion occurs in the junctional membrane complex known as the triad junction, where the invaginated plasma membrane called the transverse-tubule (T-tubule) is pinched from both sides by SR membranes [16].

Associations of Arih2 with chemical compounds

  • Triad1 was recently identified as a nuclear RING finger protein, which is up-regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells [18].
  • MG29 is expressed in the junctional membrane complex between the cell surface transverse (T) tubule and the sarcoplasmic reticulum (SR), called the triad junction, where the depolarization signal is converted to Ca(2+) release from the SR [19].
  • The first three-dimensional structure of the unique NAT family shows the active-site cysteine to be aligned with conserved histidine and aspartate residues to form a catalytic triad, thus providing an activation mechanism for transfer of the acetyl group from acetyl CoA to cysteine [20].
  • The structural aspects necessary for the protease to function were investigated by means of site-directed mutagenesis to identify the constituents of the catalytic triad and the amino acid residue responsible for lysine specificity [3].
  • The deduced 371-amino-acid sequence shares 68% identity with human CtsW and includes the conserved catalytic triad cysteine, histidine, and asparagine found in all members of this family [21].

Physical interactions of Arih2


Other interactions of Arih2


Analytical, diagnostic and therapeutic context of Arih2


  1. Antitumor immunity after vaccination with B lymphoma cells overexpressing a triad of costimulatory molecules. Briones, J., Timmerman, J.M., Panicalli, D.L., Levy, R. J. Natl. Cancer Inst. (2003) [Pubmed]
  2. Enhanced activation of T cells by dendritic cells engineered to hyperexpress a triad of costimulatory molecules. Hodge, J.W., Rad, A.N., Grosenbach, D.W., Sabzevari, H., Yafal, A.G., Gritz, L., Schlom, J. J. Natl. Cancer Inst. (2000) [Pubmed]
  3. Identification of three catalytic triad constituents and Asp-225 essential for function of lysine-specific serine protease, Achromobacter protease I. Norioka, S., Ohta, S., Ohara, T., Lim, S.I., Sakiyama, F. J. Biol. Chem. (1994) [Pubmed]
  4. The polarization defect of Wiskott-Aldrich syndrome macrophages is linked to dislocalization of the Arp2/3 complex. Linder, S., Higgs, H., Hüfner, K., Schwarz, K., Pannicke, U., Aepfelbacher, M. J. Immunol. (2000) [Pubmed]
  5. Progressive alterations in the hypothalamic-pituitary-adrenal axis in the R6/2 transgenic mouse model of Huntington's disease. Björkqvist, M., Petersén, A., Bacos, K., Isaacs, J., Norlén, P., Gil, J., Popovic, N., Sundler, F., Bates, G.P., Tabrizi, S.J., Brundin, P., Mulder, H. Hum. Mol. Genet. (2006) [Pubmed]
  6. Neuroprotection in Huntington's disease: a 2-year study on minocycline. Bonelli, R.M., Hödl, A.K., Hofmann, P., Kapfhammer, H.P. International clinical psychopharmacology. (2004) [Pubmed]
  7. Restoration of dysgenic muscle contraction and calcium channel function by co-culture with normal spinal cord neurons. Rieger, F., Bournaud, R., Shimahara, T., Garcia, L., Pinçon-Raymond, M., Romey, G., Lazdunski, M. Nature (1987) [Pubmed]
  8. Novel serine proteases encoded by two cytotoxic T lymphocyte-specific genes. Lobe, C.G., Finlay, B.B., Paranchych, W., Paetkau, V.H., Bleackley, R.C. Science (1986) [Pubmed]
  9. Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases. Rouillé, Y., Duguay, S.J., Lund, K., Furuta, M., Gong, Q., Lipkind, G., Oliva, A.A., Chan, S.J., Steiner, D.F. Frontiers in neuroendocrinology. (1995) [Pubmed]
  10. Characterization of the tissue macrophage and the interstitial dendritic cell as distinct leukocytes normally resident in the connective tissue of rat heart. Spencer, S.C., Fabre, J.W. J. Exp. Med. (1990) [Pubmed]
  11. The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells. Marteijn, J.A., van Emst, L., Erpelinck-Verschueren, C.A., Nikoloski, G., Menke, A., de Witte, T., Löwenberg, B., Jansen, J.H., van der Reijden, B.A. Blood (2005) [Pubmed]
  12. Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Blair, D.E., Schüttelkopf, A.W., MacRae, J.I., van Aalten, D.M. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  13. Studies of streptozotocin-induced insulitis and diabetes. Rossini, A.A., Like, A.A., Chick, W.L., Appel, M.C., Cahill, G.F. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  14. Individual mouse alpha-fetoprotein enhancer elements exhibit different patterns of tissue-specific and hepatic position-dependent activities. Ramesh, T.M., Ellis, A.W., Spear, B.T. Mol. Cell. Biol. (1995) [Pubmed]
  15. Promotion of tumor growth by murine fibroblast activation protein, a serine protease, in an animal model. Cheng, J.D., Dunbrack, R.L., Valianou, M., Rogatko, A., Alpaugh, R.K., Weiner, L.M. Cancer Res. (2002) [Pubmed]
  16. Deficiency of triad junction and contraction in mutant skeletal muscle lacking junctophilin type 1. Ito, K., Komazaki, S., Sasamoto, K., Yoshida, M., Nishi, M., Kitamura, K., Takeshima, H. J. Cell Biol. (2001) [Pubmed]
  17. Dihydropyridine receptor alpha subunits in normal and dysgenic muscle in vitro: expression of alpha 1 is required for proper targeting and distribution of alpha 2. Flucher, B.E., Phillips, J.L., Powell, J.A. J. Cell Biol. (1991) [Pubmed]
  18. TRIADs: a new class of proteins with a novel cysteine-rich signature. van der Reijden, B.A., Erpelinck-Verschueren, C.A., Löwenberg, B., Jansen, J.H. Protein Sci. (1999) [Pubmed]
  19. Abnormal features in skeletal muscle from mice lacking mitsugumin29. Nishi, M., Komazaki, S., Kurebayashi, N., Ogawa, Y., Noda, T., Iino, M., Takeshima, H. J. Cell Biol. (1999) [Pubmed]
  20. Arylamine N-acetyltransferases - of mice, men and microorganisms. Upton, A., Johnson, N., Sandy, J., Sim, E. Trends Pharmacol. Sci. (2001) [Pubmed]
  21. Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity. Ondr, J.K., Pham, C.T. J. Biol. Chem. (2004) [Pubmed]
  22. Extraction of junctional complexes from triad junctions of rabbit skeletal muscle. Motoike, H.K., Caswell, A.H., Smilowitz, H.M., Brandt, N.R. J. Muscle Res. Cell. Motil. (1994) [Pubmed]
  23. Abnormal junctional membrane structures in cardiac myocytes expressing ectopic junctophilin type 1. Komazaki, S., Nishi, M., Takeshima, H. FEBS Lett. (2003) [Pubmed]
  24. Cathepsin-6, a novel cysteine proteinase showing homology with and co-localized expression with cathepsin J/P in the labyrinthine layer of mouse placenta. Nakajima, A., Kataoka, K., Takata, Y., Huh, N.H. Biochem. J. (2000) [Pubmed]
  25. Phosphoacetylcholinesterase: toxicity of phosphorus oxychloride to mammals and insects that can be attributed to selective phosphorylation of acetylcholinesterase by phosphorodichloridic acid. Quistad, G.B., Zhang, N., Sparks, S.E., Casida, J.E. Chem. Res. Toxicol. (2000) [Pubmed]
  26. Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases. David, F., Bernard, A.M., Pierres, M., Marguet, D. J. Biol. Chem. (1993) [Pubmed]
  27. TNF plays an essential role in tumor regression after adoptive transfer of perforin/IFN-gamma double knockout effector T cells. Poehlein, C.H., Hu, H.M., Yamada, J., Assmann, I., Alvord, W.G., Urba, W.J., Fox, B.A. J. Immunol. (2003) [Pubmed]
  28. cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases. Karlsson, M., Contreras, J.A., Hellman, U., Tornqvist, H., Holm, C. J. Biol. Chem. (1997) [Pubmed]
  29. The Ca2+ channel alpha2delta-1 subunit determines Ca2+ current kinetics in skeletal muscle but not targeting of alpha1S or excitation-contraction coupling. Obermair, G.J., Kugler, G., Baumgartner, S., Tuluc, P., Grabner, M., Flucher, B.E. J. Biol. Chem. (2005) [Pubmed]
  30. Over-expression of Microspan, a novel component of the sarcoplasmic reticulum, causes severe muscle pathology with triad abnormalities. Miller, G., Peter, A.K., Espinoza, E., Heighway, J., Crosbie, R.H. J. Muscle Res. Cell. Motil. (2006) [Pubmed]
  31. Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions. Suzuki, T., Park, H., Lennarz, W.J. FASEB J. (2002) [Pubmed]
WikiGenes - Universities