[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 345-361 AND 394-411, AND INTERACTION WITH EBI3.
TISSUE=B-cell;
PubMed=8551575 [NCBI, ExPASy, EBI, Israel, Japan]
Devergne O.,
Hummel M.,
Koeppen H.,
Le Beau M.M.,
Nathanson E.C.,
Kieff E.,
Birkenbach M.;
"A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes.";
J. Virol. 70:1143-1153(1996).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 51-96; 184-187; 213-217; 239-264 AND 268-281, TISSUE SPECIFICITY, INTERACTION WITH LCK, AND MUTAGENESIS OF TYR-9.
TISSUE=Cervix carcinoma;
DOI=10.1073/pnas.93.12.5991; PubMed=8650207 [NCBI, ExPASy, EBI, Israel, Japan]
Joung I.,
Strominger J.L.,
Shin J.;
"Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 wdomain.";
Proc. Natl. Acad. Sci. U.S.A. 93:5991-5995(1996).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Pancreas, Placenta, Skin, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72, AND INDUCTION.
DOI=10.1016/S0014-5793(98)01021-7; PubMed=9762895 [NCBI, ExPASy, EBI, Israel, Japan]
Vadlamudi R.K.,
Shin J.;
"Genomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding protein.";
FEBS Lett. 435:138-142(1998).
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[5]
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PROTEIN SEQUENCE OF 51-60; 166-174 AND 379-388, AND SUBCELLULAR LOCATION.
PubMed=10362795 [NCBI, ExPASy, EBI, Israel, Japan]
Stumptner C.,
Heid H.,
Fuchsbichler A.,
Hauser H.,
Mischinger H.-J.,
Zatloukal K.,
Denk H.;
"Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent.";
Am. J. Pathol. 154:1701-1710(1999).
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[6]
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INTERACTION WITH LCK AND RASA1.
PubMed=8618896 [NCBI, ExPASy, EBI, Israel, Japan]
Park I.,
Chung J.,
Walsh C.T.,
Yun Y.,
Strominger J.L.,
Shin J.;
"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. 92:12338-12342(1995).
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[7]
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INTERACTION WITH UBIQUITIN.
DOI=10.1074/jbc.271.34.20235; PubMed=8702753 [NCBI, ExPASy, EBI, Israel, Japan]
Vadlamudi R.K.,
Joung I.,
Strominger J.L.,
Shin J.;
"p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins.";
J. Biol. Chem. 271:20235-20237(1996).
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[8]
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INTERACTION WITH NR2F2.
DOI=10.1074/jbc.271.44.27197; PubMed=8910285 [NCBI, ExPASy, EBI, Israel, Japan]
Marcus S.L.,
Winrow C.J.,
Capone J.P.,
Rachubinski R.A.;
"A p56(lck) ligand serves as a coactivator of an orphan nuclear hormone receptor.";
J. Biol. Chem. 271:27197-27200(1996).
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[9]
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INTERACTION WITH PRKCI AND PRKCZ, AND SUBCELLULAR LOCATION.
PubMed=9566925 [NCBI, ExPASy, EBI, Israel, Japan]
Sanchez P.,
De Carcer G.,
Sandoval I.V.,
Moscat J.,
Diaz-Meco M.T.;
"Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62.";
Mol. Cell. Biol. 18:3069-3080(1998).
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[10]
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INTERACTION WITH RIPK1; PRKCZ; PRKCI; IKBKB; TRADD AND TNFRSF1A, AND FUNCTION.
DOI=10.1093/emboj/18.11.3044; PubMed=10356400 [NCBI, ExPASy, EBI, Israel, Japan]
Sanz L.,
Sanchez P.,
Lallena M.-J.,
Diaz-Meco M.T.,
Moscat J.;
"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation.";
EMBO J. 18:3044-3053(1999).
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[11]
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INTERACTION WITH MAPKAPK5, AND SUBCELLULAR LOCATION.
DOI=10.1006/bbrc.2000.2333; PubMed=10708586 [NCBI, ExPASy, EBI, Israel, Japan]
Sudo T.,
Maruyama M.,
Osada H.;
"p62 functions as a p38 MAP kinase regulator.";
Biochem. Biophys. Res. Commun. 269:521-525(2000).
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[12]
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INTERACTION WITH TRAF6 AND RIPK1, DOMAIN, AND FUNCTION.
DOI=10.1093/emboj/19.7.1576; PubMed=10747026 [NCBI, ExPASy, EBI, Israel, Japan]
Sanz L.,
Diaz-Meco M.T.,
Nakano H.,
Moscat J.;
"The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway.";
EMBO J. 19:1576-1586(2000).
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[13]
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INTERACTION WITH NTRK1; TRAF6; NGFR AND PRKCZ, AND FUNCTION.
DOI=10.1074/jbc.C000869200; PubMed=11244088 [NCBI, ExPASy, EBI, Israel, Japan]
Wooten M.W.,
Seibenhener M.L.,
Mamidipudi V.,
Diaz-Meco M.T.,
Barker P.A.,
Moscat J.;
"The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor.";
J. Biol. Chem. 276:7709-7712(2001).
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[14]
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SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11786419 [NCBI, ExPASy, EBI, Israel, Japan]
Zatloukal K.,
Stumptner C.,
Fuchsbichler A.,
Heid H.,
Schnoelzer M.,
Kenner L.,
Kleinert R.,
Prinz M.,
Aguzzi A.,
Denk H.;
"p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases.";
Am. J. Pathol. 160:255-263(2002).
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[15]
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INTERACTION WITH PAWR AND PRKCZ.
DOI=10.1016/S0014-5793(01)03224-0; PubMed=11755531 [NCBI, ExPASy, EBI, Israel, Japan]
Chang S.,
Kim J.H.,
Shin J.;
"p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition.";
FEBS Lett. 510:57-61(2002).
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[16]
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SUBCELLULAR LOCATION.
DOI=10.1053/jhep.2002.32674; PubMed=11981755 [NCBI, ExPASy, EBI, Israel, Japan]
Stumptner C.,
Fuchsbichler A.,
Heid H.,
Zatloukal K.,
Denk H.;
"Mallory body -- a disease-associated type of sequestosome.";
Hepatology 35:1053-1062(2002).
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[17]
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INTERACTION WITH NTRK1; NTRK2 AND NTRK3, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1074/jbc.M208468200; PubMed=12471037 [NCBI, ExPASy, EBI, Israel, Japan]
Geetha T.,
Wooten M.W.;
"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. 278:4730-4739(2003).
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[18]
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INTERACTION WITH PRKCI; PRKCZ; MAP2K5 AND NBR1, DOMAIN, MUTAGENESIS OF LYS-7; LYS-13; 21-ARG-ARG-22; TYR-67; ASP-69; ASP-71; ASP-73; ASP-80 AND GLU-82, AND DIMERIZATION.
DOI=10.1074/jbc.M303221200; PubMed=12813044 [NCBI, ExPASy, EBI, Israel, Japan]
Lamark T.,
Perander M.,
Outzen H.,
Kristiansen K.,
Oevervatn A.,
Michaelsen E.,
Bjoerkoey G.,
Johansen T.;
"Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins.";
J. Biol. Chem. 278:34568-34581(2003).
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[19]
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INTERACTION WITH PRKCZ, DOMAIN, OLIGOMERIZATION, AND MUTAGENESIS OF LYS-7; ASP-69 AND ASP-73.
DOI=10.1016/S1097-2765(03)00246-6; PubMed=12887891 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson M.I.,
Gill D.J.,
Perisic O.,
Quinn M.T.,
Williams R.L.;
"PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62.";
Mol. Cell 12:39-50(2003).
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[20]
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INDUCTION.
DOI=10.1038/sj.onc.1206325; PubMed=12700667 [NCBI, ExPASy, EBI, Israel, Japan]
Thompson H.G.R.,
Harris J.W.,
Wold B.J.,
Lin F.,
Brody J.P.;
"p62 overexpression in breast tumors and regulation by prostate-derived Ets factor in breast cancer cells.";
Oncogene 22:2322-2333(2003).
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[21]
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SUBCELLULAR LOCATION.
DOI=10.1016/j.brainres.2004.03.029; PubMed=15158159 [NCBI, ExPASy, EBI, Israel, Japan]
Nakaso K.,
Yoshimoto Y.,
Nakano T.,
Takeshima T.,
Fukuhara Y.,
Yasui K.,
Araga S.,
Yanagawa T.,
Ishii T.,
Nakashima K.;
"Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson's disease.";
Brain Res. 1012:42-51(2004).
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[22]
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INTERACTION WITH TRAF6; PSMC2 AND PSMD4, DOMAIN, MUTAGENESIS OF LEU-398; PHE-406; LEU-413; LEU-417 AND ILE-431, AND FUNCTION.
DOI=10.1128/MCB.24.18.8055-8068.2004; PubMed=15340068 [NCBI, ExPASy, EBI, Israel, Japan]
Seibenhener M.L.,
Babu J.R.,
Geetha T.,
Wong H.C.,
Krishna N.R.,
Wooten M.W.;
"Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation.";
Mol. Cell. Biol. 24:8055-8068(2004).
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[23]
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INTERACTION WITH MAPT, DOMAIN, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1111/j.1471-4159.2005.03181.x; PubMed=15953362 [NCBI, ExPASy, EBI, Israel, Japan]
Babu J.R.,
Geetha T.,
Wooten M.W.;
"Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation.";
J. Neurochem. 94:192-203(2005).
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[24]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E.,
Tannenbaum S.R.,
White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
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[25]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-148, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J.,
Moritz A.,
Lee K.A.,
Guo A.,
Goss V.L.,
Spek E.J.,
Zhang H.,
Zha X.-M.,
Polakiewicz R.D.,
Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
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[26]
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FUNCTION.
DOI=10.1074/jbc.C500237200; PubMed=16079148 [NCBI, ExPASy, EBI, Israel, Japan]
Wooten M.W.,
Geetha T.,
Seibenhener M.L.,
Babu J.R.,
Diaz-Meco M.T.,
Moscat J.;
"The p62 scaffold regulates nerve growth factor-induced NF-kappaB activation by influencing TRAF6 polyubiquitination.";
J. Biol. Chem. 280:35625-35629(2005).
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[27]
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INTERACTION WITH JUB AND LIMD1.
DOI=10.1128/MCB.25.10.4010-4022.2005; PubMed=15870274 [NCBI, ExPASy, EBI, Israel, Japan]
Feng Y.,
Longmore G.D.;
"The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex.";
Mol. Cell. Biol. 25:4010-4022(2005).
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[28]
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INDUCTION, AND FUNCTION.
DOI=10.1016/j.mcn.2005.02.011; PubMed=15911346 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Z.,
Figueiredo-Pereira M.E.;
"Inhibition of sequestosome 1/p62 up-regulation prevents aggregation of ubiquitinated proteins induced by prostaglandin J2 without reducing its neurotoxicity.";
Mol. Cell. Neurosci. 29:222-231(2005).
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[29]
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INTERACTION WITH NBR1 AND TRIM55, PHOSPHORYLATION, DOMAINS, AND FUNCTION.
DOI=10.1126/science.1110463; PubMed=15802564 [NCBI, ExPASy, EBI, Israel, Japan]
Lange S.,
Xiang F.,
Yakovenko A.,
Vihola A.,
Hackman P.,
Rostkova E.,
Kristensen J.,
Brandmeier B.,
Franzen G.,
Hedberg B.,
Gunnarsson L.G.,
Hughes S.M.,
Marchand S.,
Sejersen T.,
Richard I.,
Edstroem L.,
Ehler E.,
Udd B.,
Gautel M.;
"The kinase domain of titin controls muscle gene expression and protein turnover.";
Science 308:1599-1603(2005).
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[30]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269; SER-272 AND SER-332, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V.,
Blagoev B.,
Gnad F.,
Macek B.,
Kumar C.,
Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
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[31]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A.,
Villen J.,
Gerber S.A.,
Rush J.,
Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
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[32]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M.,
Sillje H.H.W.,
Sauer G.,
Nigg E.A.,
Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
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[33]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R.,
Zhu Z.,
Chan K.C.,
Issaq H.J.,
Dimitrov D.S.,
Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
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[34]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269; SER-361; SER-365 AND SER-366, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H.,
Horn D.M.,
Tang N.,
Mathivanan S.,
Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
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[35]
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STRUCTURE BY NMR OF 387-436, CHARACTERIZATION OF VARIANT LEU-392, AND DOMAIN.
DOI=10.1074/jbc.M307416200; PubMed=12857745 [NCBI, ExPASy, EBI, Israel, Japan]
Ciani B.,
Layfield R.,
Cavey J.R.,
Sheppard P.W.,
Searle M.S.;
"Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone.";
J. Biol. Chem. 278:37409-37412(2003).
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[36]
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VARIANT PDB LEU-392, AND VARIANTS VAL-117 AND GLN-274.
DOI=10.1086/340731; PubMed=11992264 [NCBI, ExPASy, EBI, Israel, Japan]
Laurin N.,
Brown J.P.,
Morissette J.,
Raymond V.;
"Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone.";
Am. J. Hum. Genet. 70:1582-1588(2002).
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[37]
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VARIANT PDB LEU-392.
DOI=10.1093/hmg/11.22.2735; PubMed=12374763 [NCBI, ExPASy, EBI, Israel, Japan]
Hocking L.J.,
Lucas G.J.A.,
Daroszewska A.,
Mangion J.,
Olavesen M.,
Cundy T.,
Nicholson G.C.,
Ward L.,
Bennett S.T.,
Wuyts W.,
Van Hul W.,
Ralston S.H.;
"Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease.";
Hum. Mol. Genet. 11:2735-2739(2002).
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[38]
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VARIANT PDB LEU-387.
PubMed=14584883 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson-Pais T.L.,
Wisdom J.H.,
Weldon K.S.,
Cody J.D.,
Hansen M.F.,
Singer F.R.,
Leach R.J.;
"Three novel mutations in SQSTM1 identified in familial Paget's disease of bone.";
J. Bone Miner. Res. 18:1748-1753(2003).
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[39]
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VARIANTS PDB LEU-392; PRO-399; THR-404 AND ARG-425.
DOI=10.1002/art.20224; PubMed=15146436 [NCBI, ExPASy, EBI, Israel, Japan]
Eekhoff E.W.M.,
Karperien M.,
Houtsma D.,
Zwinderman A.H.,
Dragoiescu C.,
Kneppers A.L.J.,
Papapoulos S.E.;
"Familial Paget's disease in The Netherlands: occurrence, identification of new mutations in the sequestosome 1 gene, and their clinical associations.";
Arthritis Rheum. 50:1650-1654(2004).
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[40]
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VARIANT PDB LEU-392.
DOI=10.1016/j.bone.2004.01.010; PubMed=15207768 [NCBI, ExPASy, EBI, Israel, Japan]
Good D.A.,
Busfield F.,
Fletcher B.H.,
Lovelock P.K.,
Duffy D.L.,
Kesting J.B.,
Andersen J.,
Shaw J.T.E.;
"Identification of SQSTM1 mutations in familial Paget's disease in Australian pedigrees.";
Bone 35:277-282(2004).
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[41]
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VARIANTS PDB LEU-392; VAL-404 AND ARG-425.
DOI=10.1359/JBMR.040203; PubMed=15125799 [NCBI, ExPASy, EBI, Israel, Japan]
Falchetti A.,
Di Stefano M.,
Marini F.,
Del Monte F.,
Mavilia C.,
Strigoli D.,
De Feo M.L.,
Isaia G.,
Masi L.,
Amedei A.,
Cioppi F.,
Ghinoi V.,
Maddali Bongi S.,
Di Fede G.,
Sferrazza C.,
Rini G.B.,
Melchiorre D.,
Matucci-Cerinic M.,
Brandi M.L.;
"Two novel mutations at exon 8 of the Sequestosome 1 (SQSTM1) gene in an Italian series of patients affected by Paget's disease of bone (PDB).";
J. Bone Miner. Res. 19:1013-1017(2004).
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[42]
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VARIANTS PDB VAL-404; SER-411 AND ARG-425, AND CHARACTERIZATION OF VARIANTS VAL-404; SER-411 AND ARG-425.
DOI=10.1359/JBMR.040315; PubMed=15176995 [NCBI, ExPASy, EBI, Israel, Japan]
Hocking L.J.,
Lucas G.J.A.,
Daroszewska A.,
Cundy T.,
Nicholson G.C.,
Donath J.,
Walsh J.P.,
Finlayson C.,
Cavey J.R.,
Ciani B.,
Sheppard P.W.,
Searle M.S.,
Layfield R.,
Ralston S.H.;
"Novel UBA domain mutations of SQSTM1 in Paget's disease of bone: genotype phenotype correlation, functional analysis, and structural consequences.";
J. Bone Miner. Res. 19:1122-1127(2004).
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