Sequestosome 1

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Sequestosome 1
Protein SQSTM1 PDB 1q02.png
PDB rendering based on 1q02.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols SQSTM1 ; A170; OSIL; PDB3; ZIP3; p60; p62; p62B
External IDs OMIM601530 MGI107931 HomoloGene31202 GeneCards: SQSTM1 Gene
RNA expression pattern
PBB GE SQSTM1 201471 s at tn.png
PBB GE SQSTM1 213112 s at tn.png
More reference expression data
Species Human Mouse
Entrez 8878 18412
Ensembl ENSG00000161011 ENSMUSG00000015837
UniProt Q13501 Q64337
RefSeq (mRNA) NM_001142298 NM_001290769
RefSeq (protein) NP_001135770 NP_001277698
Location (UCSC) Chr 5:
179.23 – 179.27 Mb
Chr 11:
50.2 – 50.21 Mb
PubMed search [1] [2]

Sequestosome-1 is a protein that in humans is encoded by the SQSTM1 gene.[1][2][3]

Model organisms[edit]

Model organisms have been used in the study of SQSTM1 function. A conditional knockout mouse line, called Sqstm1tm1a(KOMP)Wtsi[9][10] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[11][12][13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[7][14] Twenty two tests were carried out on homozygous mutant mice and one significant abnormality was observed: females had abnormal complete blood count parameters, including an increased red blood cell distribution width and increased mean platelet volume.[7]


Sequestosome 1 has been shown to interact with:


  1. ^ Joung I, Strominger JL, Shin J (July 1996). "Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain". Proc Natl Acad Sci U S A 93 (12): 5991–5. doi:10.1073/pnas.93.12.5991. PMC 39176. PMID 8650207. 
  2. ^ Devergne O, Hummel M, Koeppen H, Le Beau MM, Nathanson EC, Kieff E et al. (February 1996). "A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes". J Virol 70 (2): 1143–53. PMC 189923. PMID 8551575. 
  3. ^ "Entrez Gene: SQSTM1 sequestosome 1". 
  4. ^ "Haematology data for Sqstm1". Wellcome Trust Sanger Institute. 
  5. ^ "Salmonella infection data for Sqstm1". Wellcome Trust Sanger Institute. 
  6. ^ "Citrobacter infection data for Sqstm1". Wellcome Trust Sanger Institute. 
  7. ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  8. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  9. ^ "International Knockout Mouse Consortium". 
  10. ^ "Mouse Genome Informatics". 
  11. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V et al. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750. 
  12. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  13. ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  14. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. 
  15. ^ Shvets E, Fass E, Scherz-Shouval R, Elazar Z. "The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes". J. Cell. Sci. 121 (Pt 16): 2685–95. doi:10.1242/jcs.026005. PMID 18653543. 
  16. ^ Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (May 1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Mol. Cell. Biol. 18 (5): 3069–80. PMC 110686. PMID 9566925. 
  17. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  18. ^ Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J. "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation". EMBO J. 18 (11): 3044–53. doi:10.1093/emboj/18.11.3044. PMC 1171386. PMID 10356400. 
  19. ^ Sanz L, Diaz-Meco MT, Nakano H, Moscat J (April 2000). "The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway". EMBO J. 19 (7): 1576–86. doi:10.1093/emboj/19.7.1576. PMC 310227. PMID 10747026. 
  20. ^ Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J (March 2001). "The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor". J. Biol. Chem. 276 (11): 7709–12. doi:10.1074/jbc.C000869200. PMID 11244088. 
  21. ^ a b Geetha T, Wooten MW. "Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling". J. Biol. Chem. 278 (7): 4730–9. doi:10.1074/jbc.M208468200. PMID 12471037. 
  22. ^ a b Jadhav T, Geetha T, Jiang J, Wooten MW. "Identification of a consensus site for TRAF6/p62 polyubiquitination". Biochem. Biophys. Res. Commun. 371 (3): 521–4. doi:10.1016/j.bbrc.2008.04.138. PMC 2474794. PMID 18457658. 
  23. ^ Wooten MW, Geetha T, Babu JR, Seibenhener ML, Peng J, Cox N et al. "Essential role of sequestosome 1/p62 in regulating accumulation of Lys63-ubiquitinated proteins". J. Biol. Chem. 283 (11): 6783–9. doi:10.1074/jbc.M709496200. PMID 18174161. 

Further reading[edit]