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Nucleoporin 210kDa

From Wikipedia, the free encyclopedia
(Redirected fromGP210)
Protein-coding gene in the species Homo sapiens
Nucleoporin 210kDa
Identifiers
AliasesNUP210, Nup210, GP210, POM210, nucleoporin 210kDa, nucleoporin 210
External IDsOMIM:607703;MGI:1859555;HomoloGene:41286;GeneCards:NUP210;OMA:NUP210 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for Nucleoporin 210kDa
Genomic location for Nucleoporin 210kDa
Band3p25.1Start13,316,235bp[1]
End13,420,309bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for Nucleoporin 210kDa
Genomic location for Nucleoporin 210kDa
Band6 D1|6 40.3 cMStart90,990,050bp[2]
End91,093,811bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • lymph node

  • bone marrow cells

  • buccal mucosa cell

  • thymus

  • spleen

  • blood

  • appendix

  • parotid gland

  • mononuclear cell
Top expressed in
  • mesenteric lymph nodes

  • fetal liver hematopoietic progenitor cell

  • tibiofemoral joint

  • spleen

  • blood

  • thymus

  • human fetus

  • hair follicle

  • bone marrow

  • Paneth cell
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23225

54563

Ensembl

ENSG00000132182

ENSMUSG00000030091

UniProt

Q8TEM1

Q9QY81

RefSeq (mRNA)

NM_024923

NM_018815

RefSeq (protein)

NP_079199

NP_061285

Location (UCSC)Chr 3: 13.32 – 13.42 MbChr 6: 90.99 – 91.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Nuclear pore glycoprotein-210 (gp210) is an essential trafficking regulator in the eukaryoticnuclear pore complex. Gp-210 anchors the pore complex to the nuclear membrane.[5] and protein tagging reveals its primarily located on the luminal side of double layer membrane at the pore. A single polypeptide motif of gp210 is responsible for sorting to nuclear membrane,[6] and indicate the carboxyl tail of the protein is oriented toward the cytoplasmic side of the membrane.

Disassembly and Assembly

[edit]

Duringeukaryoticmitosis thenuclear envelope disintegrates intovesicles dispersingnuclear lamina proteins andnuclear pore complexes. Nup210 is specificallyphosphorylated on the C-terminal (cytoplasmic) domain in mitosis at Ser1880[7] and is dispersed throughout theendoplasmic reticulum during mitosis ashomodimers.[8] Nuclear lamins begin to reassemble around chromosomes at the end of mitosis.[9] Nup210 lags the reassembly process relative to other Nups.[10] and while much of the assembly process can occur without it, the final assembly and dilation of the complexes require Nup210.[11] The replacement ofserine at position 1880 with a phosphorylated 'looking'glutamate results in Nup210 complexes that fail to reassemble indicating thatdephosphorylation of Nup210 within the final phases of proper assembly is required.[12]

Pathology

[edit]

Recognized byanti-nuclear antibodies found inprimary biliary cirrhosis (PBC)anti-Nup210 antibodies correlate with progression toward end stage liver disease. Nup210 is possibly a destructive autoimmune target of the disease. One idea for the loss of tolerance is the increased or abnormal expression of Nup210 in patients with PBC.[13]

Anti-mitochondrial,anti-centromere andanti-nup62 are also found inPBC.

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000132182Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000030091Ensembl, 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. ^Greber UF, Senior A, Gerace L (1990)."A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail".EMBO J.9 (5):1495–502.doi:10.1002/j.1460-2075.1990.tb08267.x.PMC 551841.PMID 2184032.
  6. ^Wozniak RW, Blobel G (1992)."The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope".J. Cell Biol.119 (6):1441–9.doi:10.1083/jcb.119.6.1441.PMC 2289754.PMID 1281815.
  7. ^Favreau C, Worman HJ, Wozniak RW, Frappier T, Courvalin JC (1996). "Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210".Biochemistry.35 (24):8035–44.doi:10.1021/bi9600660.PMID 8672508.
  8. ^Favreau C, Bastos R, Cartaud J, Courvalin JC, Mustonen P (2001)."Biochemical characterization of nuclear pore complex protein gp210 oligomers".Eur. J. Biochem.268 (14):3883–9.doi:10.1046/j.1432-1327.2001.02290.x.PMID 11453980.
  9. ^Yang L, Guan T, Gerace L (1997)."Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis".J. Cell Biol.137 (6):1199–210.doi:10.1083/jcb.137.6.1199.PMC 2132536.PMID 9182656.
  10. ^Bodoor K, Shaikh S, Salina D, et al. (1999). "Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis".J. Cell Sci.112 (13):2253–64.doi:10.1242/jcs.112.13.2253.PMID 10362555.
  11. ^Cohen M, Feinstein N, Wilson KL, Gruenbaum Y (2003)."Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans".Mol. Biol. Cell.14 (10):4230–7.doi:10.1091/mbc.E03-04-0260.PMC 207014.PMID 14517331.
  12. ^Onischenko EA, Crafoord E, Hallberg E (2007). "Phosphomimetic mutation of the mitotically phosphorylated serine 1880 compromises the interaction of the transmembrane nucleoporin gp210 with the nuclear pore complex".Exp. Cell Res.313 (12):2744–51.doi:10.1016/j.yexcr.2007.05.011.hdl:10616/41278.PMID 17559836.
  13. ^Nakamura M, Takii Y, Ito M, et al. (2006). "Increased expression of nuclear envelope gp210 antigen in small bile ducts in primary biliary cirrhosis".J. Autoimmun.26 (2):138–45.doi:10.1016/j.jaut.2005.10.007.PMID 16337775.
Dehydrogenase
Transglutaminase
Nucleoporins
Other
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