MID2

Midline 2

PDB rendering based on 2dja.

Available structures
PDB	2DJA, 2DMK

Identifiers

Symbols

MID2; FLJ37715; FLJ41813; FXY2; RNF60; TRIM1

External IDs

OMIM: 300204 MGI: 1344333 HomoloGene: 8028 GeneCards: MID2 Gene

Gene Ontology
Molecular function	• molecular_function • zinc ion binding • ligase activity • metal ion binding
Cellular component	• intracellular • cytoplasm • centrosome • cytoskeleton • microtubule
Biological process	• biological_process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
107.07 – 107.17 Mb

Chr X:
137.2 – 137.3 Mb

PubMed search

[1]

[2]

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

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

^ 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.
^ ^a ^b "Entrez Gene: MID2 midline 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11043.
^ 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 P G, Ballabio A (May. 2001). "The tripartite motif family identifies cell compartments". EMBO J. (England) 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. ISSN 0261-4189. PMC 125245. PMID 11331580. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125245.
^ Short, Kieran M; Hopwood Blair, Yi Zou, Cox Timothy C (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. (England) 3: 1. doi:10.1186/1471-2121-3-1. PMC 64779. PMID 11806752. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=64779.

Lim J, Hao T, Shaw C, et al. (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, et al. (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, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome.". Nature 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2665286.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=490012.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=64779.
Reymond A, Meroni G, Fantozzi A, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125245.
Perry J, Short KM, Romer JT, et al. (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.

PDB gallery

2dmk: The solution structure of the FN3 domain of human Midline 2 protein

MID2

Interactions

References

Further reading