VPS29

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Vacuolar protein sorting 29 homolog (S. cerevisiae)
File:PBB Protein VPS29 image.jpg
PDB rendering based on 1w24.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols VPS29 ; DC15; DC7; DKFZp564F0223; FLJ20492; PEP11
External IDs Template:OMIM5 Template:MGI HomoloGene9433
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Vacuolar protein sorting 29 homolog (S. cerevisiae), also known as VPS29, is a human gene.[1]

This gene belongs to a group of vacuolar protein sorting (VPS) genes that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases. The protein encoded by this gene is a component of a large multimeric complex, termed the retromer complex, which is involved in retrograde transport of proteins from endosomes to the trans-Golgi network. This VPS protein may be involved in the formation of the inner shell of the retromer coat for retrograde vesicles leaving the prevacuolar compartment. Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.[1]

References

  1. 1.0 1.1 "Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)".

Further reading

  • Seaman MN, McCaffery JM, Emr SD (1998). "A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast". J. Cell Biol. 142 (3): 665–81. PMID 9700157.
  • Edgar AJ, Polak JM (2000). "Human homologues of yeast vacuolar protein sorting 29 and 35". Biochem. Biophys. Res. Commun. 277 (3): 622–30. doi:10.1006/bbrc.2000.3727. PMID 11062004.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. PMID 11076863.
  • Haft CR, de la Luz Sierra M, Bafford R; et al. (2001). "Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes". Mol. Biol. Cell. 11 (12): 4105–16. PMID 11102511.
  • Wiemann S, Weil B, Wellenreuther R; et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
  • Simpson JC, Wellenreuther R, Poustka A; et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614.
  • 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.
  • Vergés M, Luton F, Gruber C; et al. (2004). "The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor". Nat. Cell Biol. 6 (8): 763–9. doi:10.1038/ncb1153. PMID 15247922.
  • Mingot JM, Bohnsack MT, Jäkle U, Görlich D (2005). "Exportin 7 defines a novel general nuclear export pathway". EMBO J. 23 (16): 3227–36. doi:10.1038/sj.emboj.7600338. PMID 15282546.
  • 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.
  • Wiemann S, Arlt D, Huber W; et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMID 15489336.
  • Wang D, Guo M, Liang Z; et al. (2005). "Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites". J. Biol. Chem. 280 (24): 22962–7. doi:10.1074/jbc.M500464200. PMID 15788412.
  • Mehrle A, Rosenfelder H, Schupp I; et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMID 16381901.
  • Damen E, Krieger E, Nielsen JE; et al. (2006). "The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide". Biochem. J. 398 (3): 399–409. doi:10.1042/BJ20060033. PMID 16737443.
  • Rojas R, Kametaka S, Haft CR, Bonifacino JS (2007). "Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors". Mol. Cell. Biol. 27 (3): 1112–24. doi:10.1128/MCB.00156-06. PMID 17101778.
  • Hierro A, Rojas AL, Rojas R; et al. (2007). "Functional architecture of the retromer cargo-recognition complex". Nature. 449 (7165): 1063–7. doi:10.1038/nature06216. PMID 17891154.

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