SQSTM_MOUSE
ID SQSTM_MOUSE Reviewed; 442 AA.
AC Q64337; Q99JM8;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Sequestosome-1;
DE AltName: Full=STONE14;
DE AltName: Full=Ubiquitin-binding protein p62;
GN Name=Sqstm1; Synonyms=A170, STAP;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC STRAIN=ddY; TISSUE=Macrophage;
RX PubMed=8806656; DOI=10.1006/bbrc.1996.1377;
RA Ishii T., Yanagawa T., Kawane T., Yuki K., Seita J., Yoshida H., Bannai S.;
RT "Murine peritoneal macrophages induce a novel 60-kDa protein with
RT structural similarity to a tyrosine kinase p56lck-associated protein in
RT response to oxidative stress.";
RL Biochem. Biophys. Res. Commun. 226:456-460(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Morris J.C., Long A., Finnerty H., Fitz L., Towler P., Turner K.,
RA Wood C.R.;
RT "Murine cDNA similar to EBI3-associated protein p60 mRNA.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INDUCTION.
RX PubMed=9125146; DOI=10.1006/bbrc.1997.6221;
RA Ishii T., Yanagawa T., Yuki K., Kawane T., Yoshida H., Bannai S.;
RT "Low micromolar levels of hydrogen peroxide and proteasome inhibitors
RT induce the 60-kDa A170 stress protein in murine peritoneal macrophages.";
RL Biochem. Biophys. Res. Commun. 232:33-37(1997).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=9405250; DOI=10.1006/bbrc.1997.7783;
RA Yanagawa T., Yuki K., Yoshida H., Bannai S., Ishii T.;
RT "Phosphorylation of A170 stress protein by casein kinase II-like activity
RT in macrophages.";
RL Biochem. Biophys. Res. Commun. 241:157-163(1997).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10458914; DOI=10.1006/geno.1999.5902;
RA Okazaki M., Ito S., Kawakita K., Takeshita S., Kawai S., Makishima F.,
RA Oda H., Kakinuma A.;
RT "Cloning, expression profile, and genomic organization of the mouse
RT STAP/A170 gene.";
RL Genomics 60:87-95(1999).
RN [9]
RP INDUCTION.
RX PubMed=11162503; DOI=10.1006/bbrc.2000.4107;
RA Kuusisto E., Suuronen T., Salminen A.;
RT "Ubiquitin-binding protein p62 expression is induced during apoptosis and
RT proteasomal inhibition in neuronal cells.";
RL Biochem. Biophys. Res. Commun. 280:223-228(2001).
RN [10]
RP INDUCTION.
RX PubMed=12745069; DOI=10.1016/s0006-291x(03)00728-9;
RA Aono J., Yanagawa T., Itoh K., Li B., Yoshida H., Kumagai Y., Yamamoto M.,
RA Ishii T.;
RT "Activation of Nrf2 and accumulation of ubiquitinated A170 by arsenic in
RT osteoblasts.";
RL Biochem. Biophys. Res. Commun. 305:271-277(2003).
RN [11]
RP FUNCTION, INDUCTION, INTERACTION WITH TRAF6, AND DISRUPTION PHENOTYPE.
RX PubMed=14960283; DOI=10.1016/s1534-5807(03)00403-9;
RA Duran A., Serrano M., Leitges M., Flores J.M., Picard S., Brown J.P.,
RA Moscat J., Diaz-Meco M.T.;
RT "The atypical PKC-interacting protein p62 is an important mediator of RANK-
RT activated osteoclastogenesis.";
RL Dev. Cell 6:303-309(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [13]
RP INDUCTION.
RX PubMed=15890008; DOI=10.1089/ars.2005.7.639;
RA Holtz W.A., Turetzky J.M., O'Malley K.L.;
RT "Microarray expression profiling identifies early signaling transcripts
RT associated with 6-OHDA-induced dopaminergic cell death.";
RL Antioxid. Redox Signal. 7:639-648(2005).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=16286508; DOI=10.1083/jcb.200507002;
RA Bjorkoy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A.,
RA Stenmark H., Johansen T.;
RT "p62/SQSTM1 forms protein aggregates degraded by autophagy and has a
RT protective effect on huntingtin-induced cell death.";
RL J. Cell Biol. 171:603-614(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [16]
RP FUNCTION, INTERACTION WITH CYLD AND TRAF6, AND IDENTIFICATION IN A COMPLEX
RP WITH CYLD AND TRAF6.
RX PubMed=18382763; DOI=10.1172/jci34257;
RA Jin W., Chang M., Paul E.M., Babu G., Lee A.J., Reiley W., Wright A.,
RA Zhang M., You J., Sun S.C.;
RT "Deubiquitinating enzyme CYLD negatively regulates RANK signaling and
RT osteoclastogenesis in mice.";
RL J. Clin. Invest. 118:1858-1866(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; THR-269 AND THR-272, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [19]
RP INTERACTION WITH KEAP1.
RX PubMed=20495340; DOI=10.4161/auto.6.5.12189;
RA Fan W., Tang Z., Chen D., Moughon D., Ding X., Chen S., Zhu M., Zhong Q.;
RT "Keap1 facilitates p62-mediated ubiquitin aggregate clearance via
RT autophagy.";
RL Autophagy 6:614-621(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-269; THR-272;
RP SER-330; SER-334; SER-363 AND SER-367, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KEAP1, AND MUTAGENESIS OF
RP 349-ASP--GLU-354.
RX PubMed=20421418; DOI=10.1128/mcb.00248-10;
RA Lau A., Wang X.J., Zhao F., Villeneuve N.F., Wu T., Jiang T., Sun Z.,
RA White E., Zhang D.D.;
RT "A noncanonical mechanism of Nrf2 activation by autophagy deficiency:
RT direct interaction between Keap1 and p62.";
RL Mol. Cell. Biol. 30:3275-3285(2010).
RN [22]
RP INTERACTION WITH GBP1.
RX PubMed=21551061; DOI=10.1126/science.1201711;
RA Kim B.H., Shenoy A.R., Kumar P., Das R., Tiwari S., MacMicking J.D.;
RT "A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial
RT infection.";
RL Science 332:717-721(2011).
RN [23]
RP INTERACTION WITH TRIM50, AND SUBCELLULAR LOCATION.
RX PubMed=22792322; DOI=10.1371/journal.pone.0040440;
RA Fusco C., Micale L., Egorov M., Monti M., D'Addetta E.V., Augello B.,
RA Cozzolino F., Calcagni A., Fontana A., Polishchuk R.S., Didelot G.,
RA Reymond A., Pucci P., Merla G.;
RT "The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and promotes
RT the sequestration and clearance of ubiquitinated proteins into the
RT aggresome.";
RL PLoS ONE 7:E40440-E40440(2012).
RN [24]
RP INTERACTION WITH SESN2 AND ULK1.
RX PubMed=25040165; DOI=10.1111/febs.12905;
RA Ro S.H., Semple I.A., Park H., Park H., Park H.W., Kim M., Kim J.S.,
RA Lee J.H.;
RT "Sestrin2 promotes Unc-51-like kinase 1 mediated phosphorylation of
RT p62/sequestosome-1.";
RL FEBS J. 281:3816-3827(2014).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 335-344 IN COMPLEX WITH MAP1LC3B,
RP MUTAGENESIS OF 337-ASP--ASP-339; TRP-340 AND LEU-343, AND INTERACTION WITH
RP GABARAP AND GABARAPL2.
RX PubMed=18524774; DOI=10.1074/jbc.m802182200;
RA Ichimura Y., Kumanomidou T., Sou Y.S., Mizushima T., Ezaki J., Ueno T.,
RA Kominami E., Yamane T., Tanaka K., Komatsu M.;
RT "Structural basis for sorting mechanism of p62 in selective autophagy.";
RL J. Biol. Chem. 283:22847-22857(2008).
RN [26] {ECO:0007744|PDB:3ADE}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 346-359 IN COMPLEX WITH KEAP1,
RP FUNCTION, SUBUNIT, INTERACTION WITH KEAP1, AND MUTAGENESIS OF LYS-7;
RP ASP-69; ASP-349; PRO-350; SER-351; THR-352; GLY-353 AND GLU-354.
RX PubMed=20173742; DOI=10.1038/ncb2021;
RA Komatsu M., Kurokawa H., Waguri S., Taguchi K., Kobayashi A., Ichimura Y.,
RA Sou Y.S., Ueno I., Sakamoto A., Tong K.I., Kim M., Nishito Y., Iemura S.,
RA Natsume T., Ueno T., Kominami E., Motohashi H., Tanaka K., Yamamoto M.;
RT "The selective autophagy substrate p62 activates the stress responsive
RT transcription factor Nrf2 through inactivation of Keap1.";
RL Nat. Cell Biol. 12:213-223(2010).
RN [27] {ECO:0007744|PDB:3WDZ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 346-359 IN COMPLEX WITH KEAP1,
RP FUNCTION, SUBUNIT, INTERACTION WITH KEAP1, PHOSPHORYLATION AT SER-351, AND
RP MUTAGENESIS OF SER-351.
RX PubMed=24011591; DOI=10.1016/j.molcel.2013.08.003;
RA Ichimura Y., Waguri S., Sou Y.S., Kageyama S., Hasegawa J., Ishimura R.,
RA Saito T., Yang Y., Kouno T., Fukutomi T., Hoshii T., Hirao A., Takagi K.,
RA Mizushima T., Motohashi H., Lee M.S., Yoshimori T., Tanaka K., Yamamoto M.,
RA Komatsu M.;
RT "Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective
RT autophagy.";
RL Mol. Cell 51:618-631(2013).
CC -!- FUNCTION: Autophagy receptor required for selective macroautophagy
CC (aggrephagy). Functions as a bridge between polyubiquitinated cargo and
CC autophagosomes. Interacts directly with both the cargo to become
CC degraded and an autophagy modifier of the MAP1 LC3 family. Required
CC both for the formation and autophagic degradation of polyubiquitin-
CC containing bodies, called ALIS (aggresome-like induced structures) and
CC links ALIS to the autophagic machinery. Involved in midbody ring
CC degradation (By similarity). May regulate the activation of NFKB1 by
CC TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role
CC in titin/TTN downstream signaling in muscle cells. May regulate
CC signaling cascades through ubiquitination. Adapter that mediates the
CC interaction between TRAF6 and CYLD (PubMed:14960283, PubMed:18382763).
CC May be involved in cell differentiation, apoptosis, immune response and
CC regulation of K(+) channels. Involved in endosome organization by
CC retaining vesicles in the perinuclear cloud: following ubiquitination
CC by RNF26, attracts specific vesicle-associated adapters, forming a
CC molecular bridge that restrains cognate vesicles in the perinuclear
CC region and organizes the endosomal pathway for efficient cargo
CC transport (By similarity). Promotes relocalization of 'Lys-63'-linked
CC ubiquitinated STING1 to autophagosomes (By similarity). Acts as an
CC activator of the NFE2L2/NRF2 pathway via interaction with KEAP1:
CC interaction inactivates the BCR(KEAP1) complex, promoting nuclear
CC accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective
CC genes (PubMed:20421418, PubMed:20173742).
CC {ECO:0000250|UniProtKB:O08623, ECO:0000250|UniProtKB:Q13501,
CC ECO:0000269|PubMed:14960283, ECO:0000269|PubMed:18382763,
CC ECO:0000269|PubMed:20173742, ECO:0000269|PubMed:20421418}.
CC -!- SUBUNIT: Homooligomer or heterooligomer; may form homotypic arrays
CC (PubMed:20173742). Interacts directly with PRKCI and PRKCZ (Probable).
CC Interacts with EBI3, LCK, RASA1, PRKCZ, PRKCI, NR2F2, NTRK1, NTRK2,
CC NTRK3, NBR1, MAP2K5, TRIM13, TRIM55 and MAPKAPK5. Interacts with the
CC proteasome subunits PSMD4 and PSMC2. Interacts with K63-
CC polyubiquitinated MAPT/TAU. Interacts with IKBKB through PRKCZ and
CC PRKCI. Interacts with NGFR through TRAF6 and bridges that complex to
CC NTRK1. Forms a complex with MAP2K5 and PRKCZ or PRKCI. Component of a
CC ternary complex with PAWR and PRKCZ. Upon TNF-alpha stimulation,
CC interacts with RIPK1 probably bridging IKBKB to the TNF-R1 complex
CC composed of TNF-R1/TNFRSF1A, TRADD and RIPK1. Forms a complex with
CC AJUBA, PRKCZ and TRAF6. Forms ternary complexes with PRKCZ and KCNAB2
CC or PRKCZ and GABBR3. Interacts with KCNAB1, GABRR1, GABRR2 and GABRR3.
CC Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6. Identified in
CC a heterotrimeric complex with ubiquitin and ZFAND5, where ZFAND5 and
CC SQSTM1 both interact with the same ubiquitin molecule (By similarity).
CC Interacts with TRAF6 and CYLD. Identified in a complex with TRAF6 and
CC CYLD. Directly interacts with MAP1LC3A and MAP1LC3B, as well as with
CC other MAP1 LC3 family members, including GABARAP, GABARAPL1 and
CC GABARAPL2; these interactions are necessary for the recruitment MAP1
CC LC3 family members to inclusion bodies containing polyubiquitinated
CC protein aggregates and for their degradation by autophagy (By
CC similarity). Interacts with FHOD3 (By similarity). Interacts with TRMI5
CC (By similarity). Interacts with SESN1 (By similarity). Interacts with
CC SESN2 (PubMed:25040165). Interacts with ULK1 (PubMed:25040165).
CC Interacts with UBD (By similarity). Interacts with WDR81; the
CC interaction is direct and regulates the interaction of SQSTM1 with
CC ubiquitinated proteins (By similarity). Interacts with WDFY3; this
CC interaction is required to recruit WDFY3 to cytoplasmic bodies and to
CC PML bodies (By similarity). Interacts with TRIM23 (By similarity).
CC Interacts with LRRC25. Interacts with TRIM50 (PubMed:22792322).
CC Interacts with TRIM16 (By similarity). Interacts with STING1; leading
CC to relocalization of STING1 to autophagosomes (By similarity).
CC Interacts (when phosphorylated at Ser-351) with KEAP1; the interaction
CC is direct and inactivates the BCR(KEAP1) complex by sequestering KEAP1
CC in inclusion bodies, promoting its degradation (PubMed:20495340,
CC PubMed:20421418, PubMed:20173742). Interacts with GBP1
CC (PubMed:21551061). Interacts with MOAP1; promoting dissociation of
CC SQSTM1 inclusion bodies that sequester KEAP1 (By similarity).
CC {ECO:0000250|UniProtKB:O08623, ECO:0000250|UniProtKB:Q13501,
CC ECO:0000269|PubMed:20173742, ECO:0000269|PubMed:20421418,
CC ECO:0000269|PubMed:20495340, ECO:0000269|PubMed:21551061,
CC ECO:0000269|PubMed:22792322, ECO:0000269|PubMed:25040165, ECO:0000305}.
CC -!- INTERACTION:
CC Q64337; Q9Z2X8: Keap1; NbExp=6; IntAct=EBI-645025, EBI-647110;
CC Q64337; Q9WVS7: Map2k5; NbExp=3; IntAct=EBI-645025, EBI-446144;
CC Q64337; P28700: Rxra; NbExp=3; IntAct=EBI-645025, EBI-346715;
CC Q64337; P48281: Vdr; NbExp=3; IntAct=EBI-645025, EBI-346797;
CC Q64337; Q14145: KEAP1; Xeno; NbExp=2; IntAct=EBI-645025, EBI-751001;
CC Q64337; Q9GZQ8: MAP1LC3B; Xeno; NbExp=6; IntAct=EBI-645025, EBI-373144;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16286508,
CC ECO:0000269|PubMed:22792322}. Late endosome
CC {ECO:0000269|PubMed:16286508}. Nucleus {ECO:0000269|PubMed:16286508}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:16286508}. Lysosome
CC {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}.
CC Nucleus, PML body {ECO:0000250|UniProtKB:Q13501}. Cytoplasm, myofibril,
CC sarcomere. Note=In cardiac muscles, localizes to the sarcomeric band
CC (By similarity). May also localize to the hepatocellular carcinoma (By
CC similarity). Colocalizes with TRIM13 in the perinuclear endoplasmic
CC reticulum (By similarity). Commonly found in inclusion bodies
CC containing polyubiquitinated protein aggregates (PubMed:20421418). Co-
CC localizes with TRIM5 in the cytoplasmic bodies (By similarity). When
CC nuclear export is blocked by treatment with leptomycin B, accumulates
CC in PML bodies (By similarity). {ECO:0000250|UniProtKB:Q13501,
CC ECO:0000269|PubMed:20421418}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64337-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64337-2; Sequence=VSP_015842;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10458914}.
CC -!- INDUCTION: By diethylmaleate, paraquat, menadione, sodium arsenite and
CC cadmium chloride, arsenite and arsenate. By MG132, MG115, lactacystin
CC and proteasome inhibitor I (PSI). By serum starvation, okadaic acid and
CC glucose oxidase. Also up-regulated by RANK-L (at protein level). By
CC etoposide and trichostatin. By the parkinsonian mimetic 6-
CC hydroxydopamine (6-OHDA). By TGF-beta. {ECO:0000269|PubMed:10458914,
CC ECO:0000269|PubMed:11162503, ECO:0000269|PubMed:12745069,
CC ECO:0000269|PubMed:14960283, ECO:0000269|PubMed:15890008,
CC ECO:0000269|PubMed:8806656, ECO:0000269|PubMed:9125146}.
CC -!- DOMAIN: The UBA domain binds specifically 'Lys-63'-linked polyubiquitin
CC chains of polyubiquitinated substrates. Mediates the interaction with
CC TRIM55. Both the UBA and PB1 domains are necessary and sufficient for
CC the localization into the ubiquitin-containing inclusion bodies.
CC {ECO:0000250|UniProtKB:Q13501}.
CC -!- DOMAIN: The PB1 domain mediates homooligomerization and interactions
CC with FHOD3, MAP2K5, NBR1, PRKCI, PRKCZ and WDR81. Both the PB1 and UBA
CC domains are necessary and sufficient for the localization into the
CC ubiquitin-containing inclusion bodies. {ECO:0000250|UniProtKB:Q13501}.
CC -!- DOMAIN: The ZZ-type zinc finger mediates the interaction with RIPK1.
CC {ECO:0000250|UniProtKB:Q13501}.
CC -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction
CC with ATG8 family proteins. {ECO:0000250|UniProtKB:Q13501}.
CC -!- PTM: Phosphorylated. May be phosphorylated by PRKCZ. Phosphorylated in
CC vitro by TTN (By similarity). Phosphorylation at Ser-405 by ULK1 is
CC stimulated by SESN2 (By similarity). Phosphorylated at Ser-405 by TBK1,
CC leading to promote relocalization of 'Lys-63'-linked ubiquitinated
CC STING1 to autophagosomes (By similarity). Phosphorylation at Ser-351 by
CC MTOR promotes interaction with KEAP1 and inactivation of the BCR(KEAP1)
CC complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of
CC phase II detoxifying enzymes (PubMed:24011591).
CC {ECO:0000250|UniProtKB:Q13501, ECO:0000269|PubMed:24011591}.
CC -!- PTM: Ubiquitinated by UBE2J1 and RNF26 at Lys-437: ubiquitinated SQSTM1
CC attracts specific vesicle-associated adapters, forming a molecular
CC bridge that restrains cognate vesicles in the perinuclear region and
CC organizes the endosomal pathway for efficient cargo transport.
CC Deubiquitination by USP15 releases target vesicles for fast transport
CC into the cell periphery. Ubiquitinated by the BCR(KEAP1) complex at
CC Lys-422, increasing SQSTM1 sequestering activity and promoting its
CC degradation. Ubiquitinated via 'Lys-29' and 'Lys-33'-linked
CC polyubiquitination leading to xenophagic targeting of bacteria and
CC inhibition of their replication. {ECO:0000250|UniProtKB:Q13501}.
CC -!- DISRUPTION PHENOTYPE: Impaired induced osteoclastogenesis.
CC {ECO:0000269|PubMed:14960283}.
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DR EMBL; U40930; AAB17127.1; -; mRNA.
DR EMBL; U57413; AAB02908.1; -; mRNA.
DR EMBL; AK028898; BAC26183.1; -; mRNA.
DR EMBL; AL627187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006019; AAH06019.1; -; mRNA.
DR CCDS; CCDS24629.1; -. [Q64337-1]
DR CCDS; CCDS70176.1; -. [Q64337-2]
DR PIR; JC4978; JC4978.
DR RefSeq; NP_001277698.1; NM_001290769.1. [Q64337-2]
DR RefSeq; NP_035148.1; NM_011018.3. [Q64337-1]
DR PDB; 2RRU; NMR; -; A=391-438.
DR PDB; 2ZJD; X-ray; 1.56 A; B/D=334-344.
DR PDB; 3ADE; X-ray; 2.80 A; B=346-359.
DR PDB; 3B0F; X-ray; 1.40 A; A/B=391-438.
DR PDB; 3WDZ; X-ray; 2.60 A; B=346-359.
DR PDBsum; 2RRU; -.
DR PDBsum; 2ZJD; -.
DR PDBsum; 3ADE; -.
DR PDBsum; 3B0F; -.
DR PDBsum; 3WDZ; -.
DR AlphaFoldDB; Q64337; -.
DR BMRB; Q64337; -.
DR SMR; Q64337; -.
DR BioGRID; 201982; 94.
DR CORUM; Q64337; -.
DR DIP; DIP-38490N; -.
DR ELM; Q64337; -.
DR IntAct; Q64337; 27.
DR MINT; Q64337; -.
DR STRING; 10090.ENSMUSP00000099835; -.
DR iPTMnet; Q64337; -.
DR PhosphoSitePlus; Q64337; -.
DR SwissPalm; Q64337; -.
DR EPD; Q64337; -.
DR jPOST; Q64337; -.
DR MaxQB; Q64337; -.
DR PaxDb; Q64337; -.
DR PeptideAtlas; Q64337; -.
DR PRIDE; Q64337; -.
DR ProteomicsDB; 261649; -. [Q64337-1]
DR ProteomicsDB; 261650; -. [Q64337-2]
DR Antibodypedia; 761; 1370 antibodies from 47 providers.
DR DNASU; 18412; -.
DR Ensembl; ENSMUST00000015981; ENSMUSP00000015981; ENSMUSG00000015837. [Q64337-2]
DR Ensembl; ENSMUST00000102774; ENSMUSP00000099835; ENSMUSG00000015837. [Q64337-1]
DR GeneID; 18412; -.
DR KEGG; mmu:18412; -.
DR UCSC; uc007irw.2; mouse. [Q64337-1]
DR UCSC; uc007irx.2; mouse. [Q64337-2]
DR CTD; 8878; -.
DR MGI; MGI:107931; Sqstm1.
DR VEuPathDB; HostDB:ENSMUSG00000015837; -.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00390000002781; -.
DR HOGENOM; CLU_038011_1_0_1; -.
DR InParanoid; Q64337; -.
DR OMA; IWHPLQW; -.
DR OrthoDB; 1275680at2759; -.
DR PhylomeDB; Q64337; -.
DR TreeFam; TF328470; -.
DR Reactome; R-MMU-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
DR Reactome; R-MMU-209560; NF-kB is activated and signals survival.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9664873; Pexophagy.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR BioGRID-ORCS; 18412; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Sqstm1; mouse.
DR EvolutionaryTrace; Q64337; -.
DR PRO; PR:Q64337; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q64337; protein.
DR Bgee; ENSMUSG00000015837; Expressed in dentate gyrus of hippocampal formation granule cell and 279 other tissues.
DR ExpressionAtlas; Q64337; baseline and differential.
DR Genevisible; Q64337; MM.
DR GO; GO:0016235; C:aggresome; IDA:MGI.
DR GO; GO:0044753; C:amphisome; ISO:MGI.
DR GO; GO:0044754; C:autolysosome; IDA:MGI.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0097413; C:Lewy body; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0097225; C:sperm midpiece; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:ARUK-UCL.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; TAS:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035973; P:aggrephagy; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0070342; P:brown fat cell proliferation; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; IMP:MGI.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:ARUK-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0061635; P:regulation of protein complex stability; ISO:MGI.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0098780; P:response to mitochondrial depolarisation; ISO:MGI.
DR GO; GO:0061912; P:selective autophagy; ISS:UniProtKB.
DR GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR CDD; cd06402; PB1_p62; 1.
DR CDD; cd14320; UBA_SQSTM; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR IDEAL; IID50150; -.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034866; PB1_p62.
DR InterPro; IPR033741; SQSTM_UBA.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF16577; UBA_5; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Autophagy;
KW Cytoplasm; Cytoplasmic vesicle; Differentiation; Endoplasmic reticulum;
KW Endosome; Immunity; Isopeptide bond; Lysosome; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT CHAIN 2..442
FT /note="Sequestosome-1"
FT /id="PRO_0000072177"
FT DOMAIN 3..102
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 391..436
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 123..173
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 2..50
FT /note="Interaction with LCK"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT REGION 43..107
FT /note="Interaction with PRKCZ and dimerization"
FT /evidence="ECO:0000250|UniProtKB:O08623"
FT REGION 50..80
FT /note="Interaction with PAWR"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT REGION 122..224
FT /note="Interaction with GABRR3"
FT /evidence="ECO:0000250|UniProtKB:O08623"
FT REGION 170..220
FT /note="LIM protein-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT REGION 204..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..442
FT /note="Interaction with NTRK1"
FT /evidence="ECO:0000250|UniProtKB:O08623"
FT REGION 321..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..344
FT /note="MAP1LC3B-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT REGION 349..354
FT /note="Interaction with KEAP1"
FT /evidence="ECO:0000269|PubMed:20173742,
FT ECO:0000269|PubMed:20421418"
FT MOTIF 228..233
FT /note="TRAF6-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOTIF 338..343
FT /note="LIR"
FT COMPBIAS 268..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 148
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 351
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:24011591"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT MOD_RES 405
FT /note="Phosphoserine; by ULK1 and TBK1"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT CROSSLNK 437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13501"
FT VAR_SEQ 353..390
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015842"
FT MUTAGEN 7
FT /note="K->A: Abolished oligomerization without affecting
FT interaction with KEAP1; when associated with A-69."
FT /evidence="ECO:0000269|PubMed:20173742"
FT MUTAGEN 69
FT /note="D->A: Abolished oligomerization without affecting
FT interaction with KEAP1; when associated with A-7."
FT /evidence="ECO:0000269|PubMed:20173742"
FT MUTAGEN 337..339
FT /note="DDD->AAA: Greatly decreases interaction with
FT MAP1LC3B."
FT /evidence="ECO:0000269|PubMed:18524774"
FT MUTAGEN 340
FT /note="W->A: Greatly decreases interaction with MAP1LC3B."
FT /evidence="ECO:0000269|PubMed:18524774"
FT MUTAGEN 343
FT /note="L->A: Greatly decreases interaction with MAP1LC3B."
FT /evidence="ECO:0000269|PubMed:18524774"
FT MUTAGEN 349..354
FT /note="DPSTGE->AAAAAA: Abolishes interaction with KEAP1."
FT /evidence="ECO:0000269|PubMed:20421418"
FT MUTAGEN 349
FT /note="D->A: Strongly decreased interaction with KEAP1."
FT /evidence="ECO:0000269|PubMed:20173742"
FT MUTAGEN 350
FT /note="P->A: Strongly decreased interaction with KEAP1."
FT /evidence="ECO:0000269|PubMed:20173742"
FT MUTAGEN 351
FT /note="S->A: Does not affect interaction with KEAP1.
FT Decreased phosphorylation by MTOR."
FT /evidence="ECO:0000269|PubMed:20173742,
FT ECO:0000269|PubMed:24011591"
FT MUTAGEN 351
FT /note="S->E: Phosphomimetic mutant; promotes interaction
FT with KEAP1 and nuclear accumulation of NFE2L2/NRF2."
FT /evidence="ECO:0000269|PubMed:24011591"
FT MUTAGEN 352
FT /note="T->A: Strongly decreased interaction with KEAP1."
FT /evidence="ECO:0000269|PubMed:20173742"
FT MUTAGEN 353
FT /note="G->A: Strongly decreased interaction with KEAP1."
FT /evidence="ECO:0000269|PubMed:20173742"
FT MUTAGEN 354
FT /note="E->A: Strongly decreased interaction with KEAP1."
FT /evidence="ECO:0000269|PubMed:20173742"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:3WDZ"
FT HELIX 394..405
FT /evidence="ECO:0007829|PDB:3B0F"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:3B0F"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:3B0F"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:3B0F"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:3B0F"
SQ SEQUENCE 442 AA; 48163 MW; ED4CCCA7741D35CA CRC64;
MASFTVKAYL LGKEEATREI RRFSFCFSPE PEAEAQAAAG PGPCERLLSR VAVLFPTLRP
GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK EKKECRREHR PPCAQEAPRN
MVHPNVICDG CNGPVVGTRY KCSVCPDYDL CSVCEGKGLH REHSKLIFPN PFGHLSDSFS
HSRWLRKLKH GHFGWPGWEM GPPGNWSPRP PRAGDGRPCP TAESASAPPE DPNVNFLKNV
GESVAAALSP LGIEVDIDVE HGGKRSRLTP TTPESSSTGT EDKSNTQPSS CSSEVSKPDG
AGEGPAQSLT EQMKKIALES VGQPEEQMES GNCSGGDDDW THLSSKEVDP STGELQSLQM
PESEGPSSLD PSQEGPTGLK EAALYPHLPP EADPRLIESL SQMLSMGFSD EGGWLTRLLQ
TKNYDIGAAL DTIQYSKHPP PL
