VPS28

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Vacuolar protein sorting 28 homolog (S. cerevisiae)
PDB rendering based on 2j9w.
Available structures: 2j9w
Identifiers
Symbol(s) VPS28; MGC60323
External IDs MGI: 1914164 HomoloGene: 69205
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 51160 66914
Ensembl ENSG00000160948 ENSMUSG00000062381
Uniprot Q9UK41 Q8BMZ7
Refseq NM_016208 (mRNA)
NP_057292 (protein)		 NM_025842 (mRNA)
NP_080118 (protein)
Location Chr 8: 145.62 - 145.62 Mb Chr 15: 76.45 - 76.45 Mb
Pubmed search [1] [2]

Vacuolar protein sorting 28 homolog (S. cerevisiae), also known as VPS28, is a human gene.[1]

This gene encodes a protein involved in endosomal sorting of cell surface receptors via a multivesicular body/late endosome pathway. The encoded protein is one of the three subunits of the ESCRT-I complex (endosomal complexes required for transport) involved in the sorting of ubiquitinated proteins. The two other subunits of ESCRT-I are vesicular protein sorting 23, also known as tumor susceptibility gene 101 (TSG101), and vesicular protein sorting 37. Two alternative transcripts encoding different isoforms have been described. Additional alternative transcripts may exist but the proteins encoded by these transcripts have not been verified experimentally.[1]

[edit] References

  1. ^ a b Entrez Gene: VPS28 vacuolar protein sorting 28 homolog (S. cerevisiae).

[edit] Further reading

  • Raiborg C, Rusten TE, Stenmark H (2004). "Protein sorting into multivesicular endosomes.". Curr. Opin. Cell Biol. 15 (4): 446-55. PMID 12892785. 
  • Bishop N, Woodman P (2001). "TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes.". J. Biol. Chem. 276 (15): 11735-42. doi:10.1074/jbc.M009863200. PMID 11134028. 
  • Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs.". Genome Res. 11 (10): 1758-65. doi:10.1101/gr.180101. PMID 11591653. 
  • Bishop N, Horman A, Woodman P (2002). "Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates.". J. Cell Biol. 157 (1): 91-101. doi:10.1083/jcb.200112080. PMID 11916981. 
  • 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. 
  • Martin-Serrano J, Zang T, Bieniasz PD (2003). "Role of ESCRT-I in retroviral budding.". J. Virol. 77 (8): 4794-804. PMID 12663786. 
  • Tanzi GO, Piefer AJ, Bates P (2003). "Equine infectious anemia virus utilizes host vesicular protein sorting machinery during particle release.". J. Virol. 77 (15): 8440-7. PMID 12857913. 
  • Martin-Serrano J, Yarovoy A, Perez-Caballero D, et al. (2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins.". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414-9. doi:10.1073/pnas.2133846100. PMID 14519844. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Stuchell MD, Garrus JE, Müller B, et al. (2005). "The human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 budding.". J. Biol. Chem. 279 (34): 36059-71. doi:10.1074/jbc.M405226200. PMID 15218037. 
  • Bache KG, Slagsvold T, Cabezas A, et al. (2005). "The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian ESCRT-I and mediates receptor down-regulation.". Mol. Biol. Cell 15 (9): 4337-46. doi:10.1091/mbc.E04-03-0250. PMID 15240819. 
  • 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. 
  • Eastman SW, Martin-Serrano J, Chung W, et al. (2005). "Identification of human VPS37C, a component of endosomal sorting complex required for transport-I important for viral budding.". J. Biol. Chem. 280 (1): 628-36. doi:10.1074/jbc.M410384200. PMID 15509564. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514. 
  • Hui EK, Barman S, Tang DH, et al. (2006). "YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42.". J. Virol. 80 (5): 2291-308. doi:10.1128/JVI.80.5.2291-2308.2006. PMID 16474136. 
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