Sequestosome 1

From Wikipedia, the free encyclopedia

Sequestosome 1

PDB rendering based on 1q02.

Available structures: 1q02

Identifiers

Symbol(s)

SQSTM1; p60; A170; OSIL; PDB3; ZIP3; p62; p62B

External IDs

OMIM: 601530 MGI: 107931 HomoloGene: 31202

Gene ontology
Molecular Function:	• protein binding • zinc ion binding • protein kinase binding • receptor tyrosine kinase binding • SH2 domain binding • ubiquitin binding • metal ion binding
Cellular Component:	• nucleus • cytosol
Biological Process:	• ubiquitin-dependent protein catabolic process • apoptosis • response to stress • immune response • intracellular signaling cascade • protein localization • endosome transport • cell differentiation • regulation of I-kappaB kinase/NF-kappaB cascade • positive regulation of transcription from RNA polymerase II promoter

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003900 (mRNA)
NP_003891 (protein)

NM_011018 (mRNA)
NP_035148 (protein)

Location

Chr 5: 179.18 - 179.2 Mb

Chr 11: 50.04 - 50.05 Mb

Pubmed search

[1]

[2]

Sequestosome 1, also known as SQSTM1, is a human gene.^[1]

[edit] References

^ Entrez Gene: SQSTM1 sequestosome 1.

[edit] Further reading

Geetha T, Wooten MW (2002). "Structure and functional properties of the ubiquitin binding protein p62.". FEBS Lett. 512 (1-3): 19–24. PMID 11852044.
Layfield R, Ciani B, Ralston SH, et al. (2005). "Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone.". Biochem. Soc. Trans. 32 (Pt 5): 728–30. doi:10.1042/BST0320728. PMID 15493999.
Michou L, Collet C, Laplanche JL, et al. (2006). "Genetics of Paget's disease of bone.". Joint Bone Spine 73 (3): 243–8. doi:10.1016/j.jbspin.2005.05.009. PMID 16574459.
Devergne O, Hummel M, Koeppen H, et al. (1996). "A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes.". J. Virol. 70 (2): 1143–53. PMID 8551575.
Park I, Chung J, Walsh CT, et al. (1996). "Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region.". Proc. Natl. Acad. Sci. U.S.A. 92 (26): 12338–42. PMID 8618896.
Joung I, Strominger JL, Shin J (1996). "Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain.". Proc. Natl. Acad. Sci. U.S.A. 93 (12): 5991–5. PMID 8650207.
Iyer N, Reagan MS, Wu KJ, et al. (1996). "Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein.". Biochemistry 35 (7): 2157–67. doi:10.1021/bi9524124. PMID 8652557.
Vadlamudi RK, Joung I, Strominger JL, Shin J (1996). "p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins.". J. Biol. Chem. 271 (34): 20235–7. PMID 8702753.
Marcus SL, Winrow CJ, Capone JP, Rachubinski RA (1996). "A p56(lck) ligand serves as a coactivator of an orphan nuclear hormone receptor.". J. Biol. Chem. 271 (44): 27197–200. PMID 8910285.
Jallal B, Mossie K, Vasiloudis G, et al. (1997). "The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase.". J. Biol. Chem. 272 (18): 12158–63. PMID 9115287.
Sanchez P, De Carcer G, Sandoval IV, et al. (1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62.". Mol. Cell. Biol. 18 (5): 3069–80. PMID 9566925.
Vadlamudi RK, Shin J (1998). "Genomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding protein.". FEBS Lett. 435 (2-3): 138–42. PMID 9762895.
Sanz L, Sanchez P, Lallena MJ, et al. (1999). "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. PMID 10356400.
Stumptner C, Heid H, Fuchsbichler A, et al. (1999). "Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent.". Am. J. Pathol. 154 (6): 1701–10. PMID 10362795.
Sudo T, Maruyama M, Osada H (2000). "p62 functions as a p38 MAP kinase regulator.". Biochem. Biophys. Res. Commun. 269 (2): 521–5. doi:10.1006/bbrc.2000.2333. PMID 10708586.
Sanz L, Diaz-Meco MT, Nakano H, Moscat J (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. PMID 10747026.
Wooten MW, Seibenhener ML, Mamidipudi V, et al. (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.
Kuusisto E, Salminen A, Alafuzoff I (2001). "Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies.". Neuroreport 12 (10): 2085–90. PMID 11447312.
Laurin N, Brown JP, Lemainque A, et al. (2001). "Paget disease of bone: mapping of two loci at 5q35-qter and 5q31.". Am. J. Hum. Genet. 69 (3): 528–43. PMID 11473345.
Chang S, Kim JH, Shin J (2002). "p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition.". FEBS Lett. 510 (1-2): 57–61. PMID 11755531.