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Gene Review

MID2  -  midline 2

Homo sapiens

Synonyms: FXY2, MRX101, Midin-2, Midline defect 2, Midline-2, ...
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Disease relevance of MID2


High impact information on MID2

  • MID1 encodes a member of the B-box family of proteins, which contain protein-protein interaction domains, including a RING finger, and are implicated in fundamental processes such as body axis patterning and control of cell proliferation [6].
  • These results suggest that Mid2p influences septin ring organization at the site of cell division and its turnover might normally be required to permit septin ring disassembly [7].
  • An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation [7].
  • In the presence of a nondegradable Mid2p fragment, the septin ring is stabilized and cell cycle progression is delayed [7].
  • We hypothesize that the Trim family of proteins plays a widespread role in innate immunity to viral infection [8].

Biological context of MID2


Anatomical context of MID2

  • A protein highly related to MID1, called MID2, has also been described that similarly associates with microtubules [10].
  • Mid1 could recruit alpha4 onto microtubules, and high levels of alpha4 could displace Mid1 into the cytosol [12].

Associations of MID2 with chemical compounds

  • On the basis of our results, the mutation in the tripartite-motif-containing gene (TRIM32) that replaces aspartate with asparagine at position 487 appears to be the causative mutation of LGMD2H [13].
  • A tripartite motif located in the centre of the 7.5 kb exon 26 of apolipoprotein B (apoB) mRNA directs editosome assembly and site-specific cytidine-to-uridine editing at nucleotide 6666. apoB mRNA editing is a post-transcriptional event, occurring primarily at the time exon 26 is spliced or at a time after splicing, but before nuclear export [14].
  • Rfp becomes oncogenic when its tripartite motif is recombined with the tyrosine kinase domain from the c-ret proto-oncogene [15].
  • A monoclonal antibody, MID 2, which reacts with an epitope common to all human leucocytes, was used to show that the leucocyte common antigen can be resolved into four glycoprotein components with molecular weights of 220 K, 200 K, 180 K and 160 K [16].
  • The effective barrier properties were investigated following treatment for 15 min with one of: acid etchant, Trim, cavity varnish, Hibiscrub, Hydrex and Vitremer using a dye permeability test [17].

Regulatory relationships of MID2

  • Candidate yeast mRNA substrates were identified based on their homology with the mooring sequence-containing tripartite motif at the editing site of apoB mRNA and their ability to be edited by ectopically expressed APOBEC-1 [18].

Other interactions of MID2

  • Together, these data suggest that midin and MID2 have a similar biochemical function but a different physiological role during development [9].
  • The critical interaction between CA and Trim-CypA appears to take place soon after viral entry [19].
  • The exceptions were TRIM1, TRIM5 and TRIM34 proteins [20].
  • Since FG and Opitz G/BBB syndromes share many manifestations we considered MID2 a candidate gene for FG syndrome [21].
  • Mutations in TRIM37 encoding a tripartite motif (TRIM, RING-B-box-coiled-coil)-family protein underlie mulibrey nanism [22].

Analytical, diagnostic and therapeutic context of MID2

  • The expression pattern studied by RNA in situ hybridization in mouse revealed that Mid2 is expressed early in development and the highest level of expression is detected in the heart, unlike Mid1 for which no expression was detected in the developing heart [9].
  • Immunoprecipitation experiments demonstrated the ability of the tripartite motif to mediate midin homodimerization, consistent with the evidence, obtained by gel filtration analysis, that midin exists in the form of large protein complexes [11].
  • We confirmed by immunoprecipitation that this interaction occurs in vivo and that it is mediated by the Mid1 coiled-coil domain [23].
  • Accordingly, we observed differential MID1 transcript patterns in a tissue-specific manner by Northern blot and RT-PCR [24].
  • Gene mapping has identified OS mutations within a protein called Mid1 [12].


  1. Evolution of a cytoplasmic tripartite motif (TRIM) protein in cows that restricts retroviral infection. Si, Z., Vandegraaff, N., O'huigin, C., Song, B., Yuan, W., Xu, C., Perron, M., Li, X., Marasco, W.A., Engelman, A., Dean, M., Sodroski, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Trim5{alpha} Accelerates Degradation of Cytosolic Capsid Associated with Productive HIV-1 Entry. Chatterji, U., Bobardt, M.D., Gaskill, P., Sheeter, D., Fox, H., Gallay, P.A. J. Biol. Chem. (2006) [Pubmed]
  3. Species-specific variation in the B30.2(SPRY) domain of TRIM5alpha determines the potency of human immunodeficiency virus restriction. Stremlau, M., Perron, M., Welikala, S., Sodroski, J. J. Virol. (2005) [Pubmed]
  4. Cyclophilin A Renders Human Immunodeficiency Virus Type 1 Sensitive to Old World Monkey but Not Human TRIM5{alpha} Antiviral Activity. Keckesova, Z., Ylinen, L.M., Towers, G.J. J. Virol. (2006) [Pubmed]
  5. X-linked Opitz syndrome: novel mutations in the MID1 gene and redefinition of the clinical spectrum. De Falco, F., Cainarca, S., Andolfi, G., Ferrentino, R., Berti, C., Rodríguez Criado, G., Rittinger, O., Dennis, N., Odent, S., Rastogi, A., Liebelt, J., Chitayat, D., Winter, R., Jawanda, H., Ballabio, A., Franco, B., Meroni, G. Am. J. Med. Genet. A (2003) [Pubmed]
  6. Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22. Quaderi, N.A., Schweiger, S., Gaudenz, K., Franco, B., Rugarli, E.I., Berger, W., Feldman, G.J., Volta, M., Andolfi, G., Gilgenkrantz, S., Marion, R.W., Hennekam, R.C., Opitz, J.M., Muenke, M., Ropers, H.H., Ballabio, A. Nat. Genet. (1997) [Pubmed]
  7. An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation. Tasto, J.J., Morrell, J.L., Gould, K.L. J. Cell Biol. (2003) [Pubmed]
  8. Trim5alpha protein restricts both HIV-1 and murine leukemia virus. Yap, M.W., Nisole, S., Lynch, C., Stoye, J.P. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  9. MID2, a homologue of the Opitz syndrome gene MID1: similarities in subcellular localization and differences in expression during development. Buchner, G., Montini, E., Andolfi, G., Quaderi, N., Cainarca, S., Messali, S., Bassi, M.T., Ballabio, A., Meroni, G., Franco, B. Hum. Mol. Genet. (1999) [Pubmed]
  10. MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders. Short, K.M., Hopwood, B., Yi, Z., Cox, T.C. BMC Cell Biol. (2002) [Pubmed]
  11. Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle. Cainarca, S., Messali, S., Ballabio, A., Meroni, G. Hum. Mol. Genet. (1999) [Pubmed]
  12. Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4. Liu, J., Prickett, T.D., Elliott, E., Meroni, G., Brautigan, D.L. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  13. Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene. Frosk, P., Weiler, T., Nylen, E., Sudha, T., Greenberg, C.R., Morgan, K., Fujiwara, T.M., Wrogemann, K. Am. J. Hum. Genet. (2002) [Pubmed]
  14. Commitment of apolipoprotein B RNA to the splicing pathway regulates cytidine-to-uridine editing-site utilization. Sowden, M.P., Smith, H.C. Biochem. J. (2001) [Pubmed]
  15. Mouse ret finger protein (rfp) proto-oncogene is expressed at specific stages of mouse spermatogenesis. Cao, T., Shannon, M., Handel, M.A., Etkin, L.D. Dev. Genet. (1996) [Pubmed]
  16. A common epitope identified by a monoclonal antibody, MID 2, present on all leucocytes and associated with a group of high molecular weight glycopeptides. Banga, J.P., Guarnotta, G., Harte, A., Pryce, G., Campbell, M.A., Quartey-Papafio, R., Lydyard, P.M., Roitt, I.M. Scand. J. Immunol. (1984) [Pubmed]
  17. The permeability of dental gloves following exposure to certain dental materials. Tinsley, D., Chadwick, R.G. Journal of dentistry. (1997) [Pubmed]
  18. Identification of the yeast cytidine deaminase CDD1 as an orphan C-->U RNA editase. Dance, G.S., Beemiller, P., Yang, Y., Mater, D.V., Mian, I.S., Smith, H.C. Nucleic Acids Res. (2001) [Pubmed]
  19. Trim-cyclophilin A fusion proteins can restrict human immunodeficiency virus type 1 infection at two distinct phases in the viral life cycle. Yap, M.W., Dodding, M.P., Stoye, J.P. J. Virol. (2006) [Pubmed]
  20. Antiretroviral potential of human tripartite motif-5 and related proteins. Zhang, F., Hatziioannou, T., Perez-Caballero, D., Derse, D., Bieniasz, P.D. Virology (2006) [Pubmed]
  21. An Xq22.3 duplication detected by comparative genomic hybridization microarray (Array-CGH) defines a new locus (FGS5) for FG syndrome. Jehee, F.S., Rosenberg, C., Krepischi-Santos, A.C., Kok, F., Knijnenburg, J., Froyen, G., Vianna-Morgante, A.M., Opitz, J.M., Passos-Bueno, M.R. Am. J. Med. Genet. A (2005) [Pubmed]
  22. TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase. Kallijärvi, J., Lahtinen, U., Hämäläinen, R., Lipsanen-Nyman, M., Palvimo, J.J., Lehesjoki, A.E. Exp. Cell Res. (2005) [Pubmed]
  23. Mig12, a novel Opitz syndrome gene product partner, is expressed in the embryonic ventral midline and co-operates with Mid1 to bundle and stabilize microtubules. Berti, C., Fontanella, B., Ferrentino, R., Meroni, G. BMC Cell Biol. (2004) [Pubmed]
  24. Regulation of the MID1 protein function is fine-tuned by a complex pattern of alternative splicing. Winter, J., Lehmann, T., Krauss, S., Trockenbacher, A., Kijas, Z., Foerster, J., Suckow, V., Yaspo, M.L., Kulozik, A., Kalscheuer, V., Schneider, R., Schweiger, S. Hum. Genet. (2004) [Pubmed]
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