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Mid 1

Midline-1 is a protein that in humans is encoded by the MID1 gene. The protein encoded by this gene is a member of the tripartite motif (TRIM) family

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MID1Available structuresPDBOrtholog search: PDBe RCSB List of PDB id codes

2DQ5, 2FFW, 2JUN, 5IM8

IdentifiersAliasesMID1, BBBG1, FXY, GBBB1, MIDIN, OGS1, OS, OSX, RNF59, TRIM18, XPRF, ZNFXY, midline 1External IDsMGI: 1100537 HomoloGene: 7837 GeneCards: MID1 Gene location (Human)Chr.X chromosome (human)[1]BandXp22.2Start10,445,310 bp[1]End10,833,654 bp[1]Gene location (Mouse)Chr.X chromosome (mouse)[2]BandX F5|X 79.19 cMStart169,685,199 bp[2]End170,005,736 bp[2]RNA expression pattern

More reference expression dataGene ontologyMolecular function• protein homodimerization activity
• microtubule binding
• zinc ion binding
• metal ion binding
• phosphoprotein binding
• protein binding
• identical protein binding
• protein heterodimerization activity
• ubiquitin protein ligase binding
• transferase activity
Cellular component• cytoplasm
• cytosol
• microtubule cytoskeleton
• spindle
• intracellular
• microtubule associated complex
• cytoplasmic microtubule
• microtubule
• cytoskeleton
Biological process• pattern specification process
• interferon-gamma-mediated signaling pathway
• negative regulation of microtubule depolymerization
• protein localization to microtubule
• microtubule cytoskeleton organization
• positive regulation of stress-activated MAPK cascade
Sources:Amigo / QuickGOOrthologsSpeciesHumanMouseEntrezEnsemblUniProtRefSeq (mRNA)NM_000381




RefSeq (protein)NP_000372



Location (UCSC)Chr X: 10.45 – 10.83 MbChr X: 169.69 – 170.01 MbPubMed search[3][4]WikidataView/Edit HumanView/Edit Mouse

Midline-1 is a protein that in humans is encoded by the MID1 gene.[5][6][7]

Contents Function

The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also known as the 'RING-B box-coiled coil' (RBCC) subgroup of RING finger proteins. 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. This protein forms homodimers which associate with microtubules in the cytoplasm. The protein is likely involved in the formation of multiprotein structures acting as anchor points to microtubules. Mutations in this gene have been associated with the X-linked form of Opitz syndrome, which is characterized by midline abnormalities such as cleft lip, laryngeal cleft, heart defects, hypospadias, and agenesis of the corpus callosum. This gene was also the first example of a gene subject to X inactivation in human while escaping it in mouse. Several different transcript variants are generated by alternate splicing; however, the full length nature of two variants has not been determined.[7]


MID1 has been shown to interact with MID2.[8][9]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101871 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035299 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Quaderi NA, Schweiger S, Gaudenz K, Franco B, Rugarli EI, Berger W, Feldman GJ, Volta M, Andolfi G, Gilgenkrantz S, Marion RW, Hennekam RC, Opitz JM, Muenke M, Ropers HH, Ballabio A (Dec 1997). "Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22". Nat Genet. 17 (3): 285–91. doi:10.1038/ng1197-285. PMID 9354791. 
  6. ^ Perry J, Feather S, Smith A, Palmer S, Ashworth A (Mar 1998). "The human FXY gene is located within Xp22.3: implications for evolution of the mammalian X chromosome". Hum Mol Genet. 7 (2): 299–305. doi:10.1093/hmg/7.2.299. PMID 9425238. 
  7. ^ a b "Entrez Gene: MID1 midline 1 (Opitz/BBB syndrome)". 
  8. ^ 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. 
  9. ^ 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 .mw-parser-output .refbegin{font-size:90%;margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{list-style-type:none;margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li,.mw-parser-output .refbegin-hanging-indents>dl>dd{margin-left:0;padding-left:3.2em;text-indent:-3.2em;list-style:none}.mw-parser-output .refbegin-100{font-size:100%} External links PDB gallery@media all and (max-width:720px){.mw-parser-output .mw-module-gallery{display:block!important;float:none!important}.mw-parser-output .mw-module-gallery div{display:inherit!important;float:none!important;width:auto!important}}2ffw: Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING 

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