MID2

Midline-2 is a protein that in humans is encoded by the MID2 gene.[5][6]

MID2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DJA, 2DMK
Identifiers
Aliases	MID2, FXY2, MRX101, RNF60, TRIM1, midline 2
External IDs	OMIM: 300204 MGI: 1344333 HomoloGene: 8028 GeneCards: MID2
Gene location (Human) Chr. X chromosome (human)[1] Band Xq22.3 Start 107,825,755 bp[1] End 107,927,193 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X F1|X 61.35 cM Start 140,664,599 bp[2] End 140,767,715 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein homodimerization activity • microtubule binding • zinc ion binding • metal ion binding • phosphoprotein binding • GO:0001948 protein binding • protein heterodimerization activity • identical protein binding • transferase activity Cellular component • cytoplasm • intracellular • microtubule • extracellular exosome • cytoskeleton Biological process • positive regulation of autophagy • positive regulation of sequence-specific DNA binding transcription factor activity • protein localization to microtubule • positive regulation of NF-kappaB transcription factor activity • protein ubiquitination • positive regulation of I-kappaB kinase/NF-kappaB signaling • innate immune system • negative regulation of viral transcription • negative regulation of viral entry into host cell • negative regulation of viral release from host cell Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11043	23947
Ensembl	ENSG00000080561	ENSMUSG00000000266
UniProt	Q9UJV3	Q9QUS6
RefSeq (mRNA)	NM_012216 NM_052817 NM_001382751 NM_001382752	NM_011845 NM_001358366 NM_001358367
RefSeq (protein)	NP_036348 NP_438112 NP_001369680 NP_001369681	NP_035975 NP_001345295 NP_001345296
Location (UCSC)	Chr X: 107.83 – 107.93 Mb	Chr X: 140.66 – 140.77 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

MID2 has been shown to interact with MID1.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000080561 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000266 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: MID2 midline 2".
7. 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.
8. 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. Bibcode:2005Natur.437.1173R. 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. Bibcode:2004PNAS..10110786Y. 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.