{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q13501","secondaryAccessions":["A6NFN7","B2R661","B3KUW5","Q13446","Q9BUV7","Q9BVS6","Q9UEU1"],"uniProtkbId":"SQSTM_HUMAN","entryAudit":{"firstPublicDate":"2005-10-11","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":239,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"evidences":[{"evidenceCode":"ECO:0000312","source":"Proteomes","id":"UP000005640"}],"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Sequestosome-1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8551575"}],"value":"EBI3-associated protein of 60 kDa"},"shortNames":[{"value":"EBIAP"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8551575"}],"value":"p60"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8650207"}],"value":"Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8650207"}],"value":"Ubiquitin-binding protein p62"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"30266909"}],"value":"p62"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16286508"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:11280"}],"value":"SQSTM1"},"synonyms":[{"value":"ORCA"},{"value":"OSIL"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q64337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10356400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11244088"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12471037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15340068"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15802564"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15911346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15953362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16079148"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16286508"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17580304"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19931284"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20168092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20452972"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22017874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22622177"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24128730"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25101860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26344566"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27368102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28380357"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28404643"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29343546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29507397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33393215"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33472082"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33509017"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34471133"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34893540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831301"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37802024"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40542578"}],"value":"Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024, PubMed:40542578). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O08623"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q64337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10356400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10708586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11244088"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11755531"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12471037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12813044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12887891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15340068"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15802564"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15870274"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15953362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16286508"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17580304"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19931284"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20168092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20357094"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20452972"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20495340"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21149568"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21923101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22178386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22421968"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22792322"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23274085"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24089205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24668264"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25040165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25101860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25127057"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25422469"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26344566"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27498865"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28404643"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28871090"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29288164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30143514"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30266909"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31281713"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32185393"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33393215"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34164402"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34471133"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35831301"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38103557"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8551575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8618896"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8650207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8910285"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9566925"}],"value":"Homooligomer or heterooligomer; may form homotypic arrays (PubMed:12887891, PubMed:19931284). Dimerization interferes with ubiquitin binding (PubMed:19931284). Component of a ternary complex with PAWR and PRKCZ (PubMed:11755531). Forms a complex with JUB/Ajuba, PRKCZ and TRAF6 (PubMed:15870274). Identified in a complex with TRAF6 and CYLD (By similarity). Identified in a heterotrimeric complex with ubiquitin and ZFAND5, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (PubMed:21923101). Interacts (via LIR motif) with MAP1LC3A and MAP1LC3B, as well as with other ATG8 family members, including GABARAP, GABARAPL1 and GABARAPL2; these interactions are necessary for the recruitment MAP1 LC3 family members to inclusion bodies containing polyubiquitinated protein aggregates and for their degradation by autophagy (PubMed:16286508, PubMed:17580304, PubMed:22421968, PubMed:24089205, PubMed:24668264). Interacts directly with PRKCI and PRKCZ (PubMed:10356400, PubMed:12813044, PubMed:12887891, PubMed:9566925). Interacts with EBI3, LCK, RASA1, NR2F2, NTRK1, NTRK2, NTRK3, NBR1, MAP2K5 and MAPKAPK5 (PubMed:10708586, PubMed:11244088, PubMed:12471037, PubMed:8551575, PubMed:8618896, PubMed:8650207, PubMed:8910285). Upon TNF stimulation, interacts with RIPK1 probably bridging IKBKB to the TNF-R1 complex composed of TNF-R1/TNFRSF1A, TRADD and RIPK1 (PubMed:10747026). Interacts with the proteasome subunits PSMD4 and PSMC2 (PubMed:15340068). Interacts with TRAF6 (PubMed:10747026). Interacts with 'Lys-63'-linked polyubiquitinated MAPT/TAU (PubMed:15953362). Interacts with FHOD3 (PubMed:21149568). Interacts with CYLD (PubMed:32185393). Interacts with SESN1 (PubMed:23274085). Interacts with SESN2 (PubMed:23274085, PubMed:25040165). Interacts with ULK1 (PubMed:25040165). Interacts with UBD (PubMed:25422469). Interacts with WDR81; the interaction is direct and regulates the interaction of SQSTM1 with ubiquitinated proteins (PubMed:28404643). Interacts with WDFY3; this interaction is required to recruit WDFY3 to cytoplasmic bodies and to PML bodies (PubMed:20168092). Interacts with LRRC25 (PubMed:29288164). Interacts with STING1; leading to relocalization of STING1 to autophagosomes (PubMed:29496741). Interacts (when phosphorylated at Ser-349) with KEAP1; the interaction is direct and inactivates the BCR(KEAP1) complex by sequestering KEAP1 in inclusion bodies, promoting its degradation (PubMed:20452972, PubMed:20495340, PubMed:37306101). Interacts with MOAP1; promoting dissociation of SQSTM1 inclusion bodies that sequester KEAP1 (PubMed:33393215). Interacts with GBP1 (By similarity). Interacts with TAX1BP1 (PubMed:34471133). Interacts with (ubiquitinated) PEX5; specifically binds PEX5 ubiquitinated at 'Lys-209' in response to reactive oxygen species (ROS) (PubMed:26344566). Interacts (via PB1 domain) with TNS2; the interaction leads to sequestration of TNS2 in cytoplasmic aggregates with SQSTM1 and promotes TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). Interacts with IRS1; the interaction is disrupted by the presence of tensin TNS2 (PubMed:25101860). Interacts with TRIM5 (PubMed:20357094, PubMed:25127057). Interacts with TRIM11 (when ubiquitinated); promoting AIM2 recruitment to autophagosomes and autophagy-dependent degradation of AIM2 (PubMed:27498865). Interacts with TRIM13 (PubMed:22178386). Interacts with TRIM16 (PubMed:30143514). Interacts with TRIM23 (PubMed:28871090). Interacts with TRIM50 (PubMed:22792322). Interacts with TRIM55 (PubMed:15802564). Interacts with ECSIT; this interaction inhibits TLR4 signaling via functional regulation of the TRAF6-ECSIT complex (PubMed:31281713). Interacts with GABRR1, GABRR2 and GABRR3 (By similarity). Interacts with WDR83 (PubMed:38103557). Interacts with GRB2 (PubMed:35831301). Interacts with USP12; the interaction is independent of USP12 deubiquitinase activity and may be involved in regulation of autophagic flux (PubMed:30266909). Interacts with ASB6 (PubMed:34164402)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","intActId":"EBI-77613"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"P54253","geneName":"ATXN1","intActId":"EBI-930964"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"O95817","geneName":"BAG3","intActId":"EBI-747185"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q16543","geneName":"CDC37","intActId":"EBI-295634"},"numberOfExperiments":8,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"P57739","geneName":"CLDN2","intActId":"EBI-751440"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"P34972","geneName":"CNR2","intActId":"EBI-2835940"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q15038","geneName":"DAZAP2","intActId":"EBI-724310"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"O14576-2","geneName":"DYNC1I1","intActId":"EBI-25840445"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"O14682","geneName":"ENC1","intActId":"EBI-6425462"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q2V2M9","geneName":"FHOD3","intActId":"EBI-6395541"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q2V2M9-4","geneName":"FHOD3","intActId":"EBI-6395505"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"O95166","geneName":"GABARAP","intActId":"EBI-712001"},"numberOfExperiments":17,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q9H0R8","geneName":"GABARAPL1","intActId":"EBI-746969"},"numberOfExperiments":18,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"P60520","geneName":"GABARAPL2","intActId":"EBI-720116"},"numberOfExperiments":24,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"P0DMV8","geneName":"HSPA1A","intActId":"EBI-11052499"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q9Y6K9","geneName":"IKBKG","intActId":"EBI-81279"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q14145","geneName":"KEAP1","intActId":"EBI-751001"},"numberOfExperiments":21,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q5S007","geneName":"LRRK2","intActId":"EBI-5323863"},"numberOfExperiments":19,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q9UDY8","geneName":"MALT1","intActId":"EBI-1047372"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q9H492","geneName":"MAP1LC3A","intActId":"EBI-720768"},"numberOfExperiments":16,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q9GZQ8","geneName":"MAP1LC3B","intActId":"EBI-373144"},"numberOfExperiments":31,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q13501","intActId":"EBI-307104"},"interactantTwo":{"uniProtKBAccession":"Q9BXW4","geneName":"MAP1LC3C","intActId":"EBI-2603996"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LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O08623"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11786419"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11981755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15158159"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15953362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17580304"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20168092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20357094"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22017874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22178386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29343546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29507397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37802024"}],"value":"In cardiac muscle, localizes to the sarcomeric band (By similarity). Localizes to cytoplasmic membraneless inclusion bodies, known as p62 bodies, containing polyubiquitinated protein aggregates (PubMed:11786419, PubMed:20357094, PubMed:22017874, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37306101, PubMed:37802024). In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease (PubMed:15158159). In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates (PubMed:11981755). Enriched in Rosenthal fibers of pilocytic astrocytoma (PubMed:11786419). In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes (PubMed:15953362, PubMed:17580304). Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum (PubMed:22178386). Co-localizes with TRIM5 in cytoplasmic bodies (PubMed:20357094). When nuclear export is blocked by treatment with leptomycin B, accumulates in PML bodies (PubMed:20168092)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15953362"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16286508"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17580304"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20168092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37802024"}],"value":"Cytoplasmic vesicle, autophagosome","id":"SL-0023"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34471133"}],"value":"Preautophagosomal structure","id":"SL-0220"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11786419"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11981755"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20168092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20357094"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21923101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22017874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22792322"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29343546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29507397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37802024"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20168092"}],"value":"Nucleus, PML body","id":"SL-0465"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12471037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9566925"}],"value":"Late endosome","id":"SL-0152"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9566925"}],"value":"Lysosome","id":"SL-0158"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10708586"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22178386"}],"value":"Endoplasmic reticulum","id":"SL-0095"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O08623"}],"value":"Cytoplasm, myofibril, sarcomere","id":"SL-0313"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q13501-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q13501-2"],"sequenceIds":["VSP_015841"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8650207"}],"value":"Ubiquitously expressed"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25101860"}],"value":"During myogenesis, there is a marked increase in levels in fully differentiated myotubes compared to undifferentiated myoblasts"}],"commentType":"DEVELOPMENTAL STAGE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12700667"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15911346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20452972"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9762895"}],"value":"By proteasomal inhibitor PSI and prostaglandin J2 (PGJ2) (at protein level). By phorbol 12-myristate 13-acetate (PMA). Expression is directly activated by NFE2L2/NRF2; creating a positive feedback loop (PubMed:20452972)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12857745"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15340068"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15802564"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28322253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"}],"value":"The UBA domain binds specifically 'Lys-63'-linked polyubiquitin chains of polyubiquitinated substrates (PubMed:12857745, PubMed:15340068, PubMed:28322253, PubMed:31857589). Mediates the interaction with TRIM55 (PubMed:15802564). Both the UBA and PB1 domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies (PubMed:15802564)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12813044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12887891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15802564"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28404643"}],"value":"The PB1 domain mediates homooligomerization and interactions with FHOD3, MAP2K5, NBR1, PRKCI, PRKCZ and WDR81 (PubMed:12813044, PubMed:12887891, PubMed:15802564, PubMed:28404643). Both the PB1 and UBA domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies (PubMed:15802564)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10747026"}],"value":"The ZZ-type zinc finger mediates the interaction with RIPK1"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23908376"}],"value":"The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q64337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15802564"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22017874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25040165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37306101"}],"value":"Phosphorylation at Ser-407 by ULK1 destabilizes the UBA dimer interface and increases binding affinity to ubiquitinated proteins (By similarity). Phosphorylation at Ser-407 also primes for subsequent phosphorylation at Ser-403 (By similarity). Phosphorylation at Ser-403 by CK2 or ULK1 promotes binding to ubiquitinated proteins by increasing the affinity between the UBA domain and polyubiquitin chains (PubMed:22017874, PubMed:25040165). Phosphorylation at Ser-403 by ULK1 is stimulated by SESN2 (PubMed:25040165). Phosphorylated at Ser-403 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Phosphorylation at Ser-349 by ULK1 promotes interaction with KEAP1 and inactivation of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes (PubMed:37306101). Phosphorylated in vitro by TTN (PubMed:15802564)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27368102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27880896"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28322253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28380357"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33472082"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40542578"}],"value":"Ubiquitinated by UBE2J1 and RNF26 at Lys-435: ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Ubiquitination by UBE2D2 and UBE2D3 increases its ability to bind polyubiquitin chains by destabilizing the UBA dimer interface (PubMed:28322253). Deubiquitination by USP15 releases target vesicles for fast transport into the cell periphery (PubMed:27368102). Ubiquitinated by the BCR(KEAP1) complex at Lys-420, increasing SQSTM1 sequestering activity and promoting its degradation (PubMed:28380357). Ubiquitinated via 'Lys-29' and 'Lys-33'-linked polyubiquitination leading to xenophagic targeting of bacteria and inhibition of their replication (PubMed:27880896). Ubiquitinated by TRIM25, targeting SQSTM1 for lysosomal degradation, thereby inhibiting autophagy activation (PubMed:40542578)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31857589"}],"value":"Acetylated at Lys-420 and Lys-435 by KAT5/TIP60, promotes activity by destabilizing the UBA dimer interface and increases binding affinity to ubiquitinated proteins (PubMed:31857589). 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