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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Midline-2''' is a [[protein]] that in humans is encoded by the ''MID2'' [[gene]].<ref name="pmid10400986">{{cite journal | vauthors = Buchner G, Montini E, Andolfi G, Quaderi N, Cainarca S, Messali S, Bassi MT, Ballabio A, Meroni G, Franco B | title = MID2, a homologue of the Opitz syndrome gene MID1: similarities in subcellular localization and differences in expression during development | journal = Hum Mol Genet | volume = 8 | issue = 8 | pages = 1397–407 | date = Sep 1999 | pmid = 10400986 | pmc =  | doi = 10.1093/hmg/8.8.1397 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MID2 midline 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11043| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MID2_image.jpg
| image_source = [[Protein Data Bank|PDB]] rendering based on 2dja.
| PDB = {{PDB2|2dja}}, {{PDB2|2dmk}}
| Name = Midline 2
| HGNCid = 7096
| Symbol = MID2
| AltSymbols =; MID1; FXY2; RNF60; TRIM1
| OMIM = 300204
| ECnumber = 
| Homologene = 8028
| MGIid = 1344333
| GeneAtlas_image1 = PBB_GE_MID2_208384_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0005875 |text = microtubule associated complex}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 11043
    | Hs_Ensembl = ENSG00000080561
    | Hs_RefseqProtein = NP_036348
    | Hs_RefseqmRNA = NM_012216
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 106955765
    | Hs_GenLoc_end = 107057079
    | Hs_Uniprot = Q9UJV3
    | Mm_EntrezGene = 23947
    | Mm_Ensembl = ENSMUSG00000000266
    | Mm_RefseqmRNA = XM_976732
    | Mm_RefseqProtein = XP_981826
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 136011320
    | Mm_GenLoc_end = 136114080
    | Mm_Uniprot = Q9QUS6
  }}
}}
'''Midline 2''', also known as '''MID2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MID2 midline 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11043| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: MID2 midline 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11043| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
MID2 has been shown to [[Protein-protein interaction|interact]] with [[MID1]].<ref name=pmid11331580>{{cite journal | vauthors = 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 | title = The tripartite motif family identifies cell compartments | journal = EMBO J. | volume = 20 | issue = 9 | pages = 2140–51 | date = May 2001 | pmid = 11331580 | pmc = 125245 | doi = 10.1093/emboj/20.9.2140 }}</ref><ref name=pmid11806752>{{cite journal | vauthors = Short KM, Hopwood B, Yi Z, Cox TC | title = 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 | journal = BMC Cell Biol. | volume = 3 | pages = 1 | year = 2002 | pmid = 11806752 | pmc = 64779 | doi = 10.1186/1471-2121-3-1 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal|authorlink13=Huda Zoghbi | vauthors = 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 | title = A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. | journal = Cell | volume = 125 | issue = 4 | pages = 801–14 | year = 2006 | pmid = 16713569 | doi = 10.1016/j.cell.2006.03.032 }}
| citations =
* {{cite journal | vauthors = Jehee FS, Rosenberg C, Krepischi-Santos AC, Kok F, Knijnenburg J, Froyen G, Vianna-Morgante AM, Opitz JM, Passos-Bueno MR | title = An Xq22.3 duplication detected by comparative genomic hybridization microarray (Array-CGH) defines a new locus (FGS5) for FG syndrome. | journal = Am. J. Med. Genet. A | volume = 139 | issue = 3 | pages = 221–6 | year = 2006 | pmid = 16283679 | doi = 10.1002/ajmg.a.30991 }}
*{{cite journal | author=Lim J, Hao T, Shaw C, ''et al.'' |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801-14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
* {{cite journal | vauthors = 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 | title = Towards a proteome-scale map of the human protein-protein interaction network. | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | year = 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R }}
*{{cite journal | author=Jehee FS, Rosenberg C, Krepischi-Santos AC, ''et al.'' |title=An Xq22.3 duplication detected by comparative genomic hybridization microarray (Array-CGH) defines a new locus (FGS5) for FG syndrome. |journal=Am. J. Med. Genet. A |volume=139 |issue= 3 |pages= 221-6 |year= 2006 |pmid= 16283679 |doi= 10.1002/ajmg.a.30991 }}
* {{cite journal | vauthors = Yap MW, Nisole S, Lynch C, Stoye JP | title = Trim5alpha protein restricts both HIV-1 and murine leukemia virus. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 101 | issue = 29 | pages = 10786–91 | year = 2004 | pmid = 15249690 | pmc = 490012 | doi = 10.1073/pnas.0402876101 | bibcode = 2004PNAS..10110786Y }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
* {{cite journal | vauthors = Short KM, Hopwood B, Yi Z, Cox TC | title = 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. | journal = BMC Cell Biol. | volume = 3 | pages = 1 | year = 2002 | pmid = 11806752 | pmc = 64779 | doi = 10.1186/1471-2121-3-1 }}
*{{cite journal  | author=Ross MT, Grafham DV, Coffey AJ, ''et al.'' |title=The DNA sequence of the human X chromosome. |journal=Nature |volume=434 |issue= 7031 |pages= 325-37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 }}
* {{cite journal | vauthors = 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 | title = The tripartite motif family identifies cell compartments. | journal = EMBO J. | volume = 20 | issue = 9 | pages = 2140–51 | year = 2001 | pmid = 11331580 | pmc = 125245 | doi = 10.1093/emboj/20.9.2140 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Perry J, Short KM, Romer JT, Swift S, Cox TC, Ashworth A | title = 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. | journal = Genomics | volume = 62 | issue = 3 | pages = 385–94 | year = 2000 | pmid = 10644436 | doi = 10.1006/geno.1999.6043 }}
*{{cite journal | author=Yap MW, Nisole S, Lynch C, Stoye JP |title=Trim5alpha protein restricts both HIV-1 and murine leukemia virus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 29 |pages= 10786-91 |year= 2004 |pmid= 15249690 |doi= 10.1073/pnas.0402876101 }}
* {{cite journal | vauthors = Cainarca S, Messali S, Ballabio A, Meroni G | title = Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle. | journal = Hum. Mol. Genet. | volume = 8 | issue = 8 | pages = 1387–96 | year = 1999 | pmid = 10400985 | doi = 10.1093/hmg/8.8.1387 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Short KM, Hopwood B, Yi Z, Cox TC |title=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. |journal=BMC Cell Biol. |volume=3 |issue=  |pages= 1 |year= 2002 |pmid= 11806752 |doi= }}
*{{cite journal | author=Reymond A, Meroni G, Fantozzi A, ''et al.'' |title=The tripartite motif family identifies cell compartments. |journal=EMBO J. |volume=20 |issue= 9 |pages= 2140-51 |year= 2001 |pmid= 11331580 |doi= 10.1093/emboj/20.9.2140 }}
*{{cite journal | author=Perry J, Short KM, Romer JT, ''et al.'' |title=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. |journal=Genomics |volume=62 |issue= 3 |pages= 385-94 |year= 2000 |pmid= 10644436 |doi= 10.1006/geno.1999.6043 }}
*{{cite journal | author=Buchner G, Montini E, Andolfi G, ''et al.'' |title=MID2, a homologue of the Opitz syndrome gene MID1: similarities in subcellular localization and differences in expression during development. |journal=Hum. Mol. Genet. |volume=8 |issue= 8 |pages= 1397-407 |year= 1999 |pmid= 10400986 |doi=  }}
*{{cite journal  | author=Cainarca S, Messali S, Ballabio A, Meroni G |title=Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle. |journal=Hum. Mol. Genet. |volume=8 |issue= 8 |pages= 1387-96 |year= 1999 |pmid= 10400985 |doi= }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=11043}}
{{WikiDoc Sources}}
 
 
{{gene-X-stub}}

Latest revision as of 03:28, 8 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 2.0 2.1 "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


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