MID2

Midline 2
PDB rendering based on 2dja.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2DJA​, 2DMK​
Identifiers
Symbols	MID2 ; FXY2; MRX101; RNF60; TRIM1
External IDs	OMIM: 300204 MGI: 1344333 HomoloGene: 8028 GeneCards: MID2 Gene
Gene ontology Molecular function • protein binding • microtubule binding • zinc ion binding • ligase activity • protein homodimerization activity • protein heterodimerization activity • phosphoprotein binding Cellular component • cytoplasm • microtubule • extracellular exosome Biological process • protein ubiquitination • negative regulation of viral transcription • protein localization to microtubule • positive regulation of I-kappaB kinase/NF-kappaB signaling • innate immune response • negative regulation of viral entry into host cell • positive regulation of sequence-specific DNA binding transcription factor activity • positive regulation of NF-kappaB transcription factor activity • negative regulation of viral release from host cell Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	11043	23947
Ensembl	ENSG00000080561	ENSMUSG00000000266
UniProt	Q9UJV3	Q9QUS6
RefSeq (mRNA)	NM_012216	NM_011845
RefSeq (protein)	NP_036348	NP_035975
Location (UCSC)	Chr X: 107.83 – 107.93 Mb	Chr X: 140.66 – 140.77 Mb
PubMed search

Midline-2 is a protein that in humans is encoded by the MID2 gene.^[1][2]

Function

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to microtubular structures in the cytoplasm. Its function has not been identified. Alternate splicing of this gene results in two transcript variants encoding different isoforms.^[2]

Interactions

MID2 has been shown to interact with MID1.^[3][4]

References

1. Buchner G, Montini E, Andolfi G, Quaderi N, Cainarca S, Messali S, Bassi MT, Ballabio A, Meroni G, Franco B (Sep 1999). "MID2, a homologue of the Opitz syndrome gene MID1: similarities in subcellular localization and differences in expression during development". Hum Mol Genet 8 (8): 1397–407. doi:10.1093/hmg/8.8.1397. PMID 10400986.
2. "Entrez Gene: MID2 midline 2".
3. Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
4. Short KM, Hopwood B, Yi Z, Cox TC (2002). "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". BMC Cell Biol. 3: 1. doi:10.1186/1471-2121-3-1. PMC 64779. PMID 11806752.

Further reading

• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
• Jehee FS, Rosenberg C, Krepischi-Santos AC, Kok F, Knijnenburg J, Froyen G, Vianna-Morgante AM, Opitz JM, Passos-Bueno MR (2006). "An Xq22.3 duplication detected by comparative genomic hybridization microarray (Array-CGH) defines a new locus (FGS5) for FG syndrome.". Am. J. Med. Genet. A 139 (3): 221–6. doi:10.1002/ajmg.a.30991. PMID 16283679.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Yap MW, Nisole S, Lynch C, Stoye JP (2004). "Trim5alpha protein restricts both HIV-1 and murine leukemia virus.". Proc. Natl. Acad. Sci. U.S.A. 101 (29): 10786–91. doi:10.1073/pnas.0402876101. PMC 490012. PMID 15249690.
• Short KM, Hopwood B, Yi Z, Cox TC (2002). "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.". BMC Cell Biol. 3: 1. doi:10.1186/1471-2121-3-1. PMC 64779. PMID 11806752.
• Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (2001). "The tripartite motif family identifies cell compartments.". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
• Perry J, Short KM, Romer JT, Swift S, Cox TC, Ashworth A (2000). "FXY2/MID2, a gene related to the X-linked Opitz syndrome gene FXY/MID1, maps to Xq22 and encodes an FNIII domain-containing protein that associates with microtubules.". Genomics 62 (3): 385–94. doi:10.1006/geno.1999.6043. PMID 10644436.
• Cainarca S, Messali S, Ballabio A, Meroni G (1999). "Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle.". Hum. Mol. Genet. 8 (8): 1387–96. doi:10.1093/hmg/8.8.1387. PMID 10400985.