MID2

From Wikipedia, the free encyclopedia

Midline 2

PDB rendering based on 2dja.

Available structures: 2dja, 2dmk

Identifiers

Symbol(s)

MID2; MID1; FXY2; RNF60; TRIM1

External IDs

OMIM: 300204 MGI: 1344333 HomoloGene: 8028

Gene ontology
Molecular Function:	• molecular_function • protein binding • zinc ion binding • metal ion binding
Cellular Component:	• intracellular • microtubule • microtubule associated complex
Biological Process:	• biological_process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012216 (mRNA)
NP_036348 (protein)

XM_976732 (mRNA)
XP_981826 (protein)

Location

Chr X: 106.96 - 107.06 Mb

Chr X: 136.01 - 136.11 Mb

Pubmed search

[1]

[2]

Midline 2, also known as MID2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: MID2 midline 2.

[edit] Further reading

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. PMID 15772651.
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. PMID 15489334.
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. PMID 15249690.
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. PMID 12477932.
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. PMID 11806752.
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. PMID 11331580.
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.
Buchner G, Montini E, Andolfi G, et al. (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. PMID 10400986.
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. PMID 10400985.