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Entry version 205 (16 Oct 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Sequestosome-1

Gene

SQSTM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Autophagy receptor required for selective macroautophagy (aggrephagy). Functions as a bridge between polyubiquitinated cargo and autophagosomes. Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:28404643, PubMed:22622177). Along with WDFY3, involved in the formation and autophagic degradation of cytoplasmic ubiquitin-containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with WDFY3, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:24128730, PubMed:20168092). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K+ channels. 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). Promotes relocalization of 'Lys-63'-linked ubiquitinated TMEM173/STING to autophagosomes (PubMed:29496741). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357).By similarity19 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri122 – 167ZZ-typePROSITE-ProRule annotationAdd BLAST46

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processApoptosis, Autophagy, Differentiation, Immunity
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-205043 NRIF signals cell death from the nucleus
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-5205685 Pink/Parkin Mediated Mitophagy
R-HSA-9020702 Interleukin-1 signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q13501

SIGNOR Signaling Network Open Resource

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SIGNORi
Q13501

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
Q13501 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sequestosome-1
Alternative name(s):
EBI3-associated protein of 60 kDa
Short name:
EBIAP
Short name:
p60
Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa
Ubiquitin-binding protein p62
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SQSTM1
Synonyms:ORCA, OSIL
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:11280 SQSTM1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601530 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q13501

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Lysosome, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Paget disease of bone 3 (PDB3)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of bone remodeling characterized by increased bone turnover affecting one or more sites throughout the skeleton, primarily the axial skeleton. Osteoclastic overactivity followed by compensatory osteoblastic activity leads to a structurally disorganized mosaic of bone (woven bone), which is mechanically weaker, larger, less compact, more vascular, and more susceptible to fracture than normal adult lamellar bone.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_023592387P → L in PDB3 and FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs776749939EnsemblClinVar.1
Natural variantiVAR_023593392P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 PublicationsCorresponds to variant dbSNP:rs104893941EnsemblClinVar.1
Natural variantiVAR_023594399S → P in PDB3. 1 Publication1
Natural variantiVAR_023595404M → T in PDB3. 1 PublicationCorresponds to variant dbSNP:rs1247551175Ensembl.1
Natural variantiVAR_023596404M → V in PDB3; loss of polyubiquitin-binding. 2 PublicationsCorresponds to variant dbSNP:rs771966860Ensembl.1
Natural variantiVAR_023597411G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 PublicationsCorresponds to variant dbSNP:rs143511494Ensembl.1
Natural variantiVAR_023598425G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 PublicationsCorresponds to variant dbSNP:rs757212984Ensembl.1
In a cell model for Huntington disease (HD), appears to form a shell surrounding aggregates of mutant HTT that may protect cells from apoptosis, possibly by recruiting autophagosomal components to the polyubiquitinated protein aggregates.1 Publication
Frontotemporal dementia and/or amyotrophic lateral sclerosis 3 (FTDALS3)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. Some FTDALS3 patients may also develop Paget disease of bone.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07389916A → V in FTDALS3. 1 Publication1
Natural variantiVAR_07390133A → V in FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs200396166EnsemblClinVar.1
Natural variantiVAR_07390280D → E in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs148366738Ensembl.1
Natural variantiVAR_07390390V → M in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs181263868EnsemblClinVar.1
Natural variantiVAR_073906107R → W in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs771903158Ensembl.1
Natural variantiVAR_073912129D → N in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs753212399Ensembl.1
Natural variantiVAR_073914153V → I in FTDALS3. 2 PublicationsCorresponds to variant dbSNP:rs145056421Ensembl.1
Natural variantiVAR_073916212R → C in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs201263163Ensembl.1
Natural variantiVAR_073918219G → V in FTDALS3. 1 Publication1
Natural variantiVAR_073919226S → P in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs765200636Ensembl.1
Natural variantiVAR_073920228P → L in FTDALS3. 2 PublicationsCorresponds to variant dbSNP:rs151191977EnsemblClinVar.1
Natural variantiVAR_073921232P → T in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs1225746517Ensembl.1
Natural variantiVAR_073922238Missing in FTDALS3. 3 Publications1
Natural variantiVAR_073923258D → N in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs774986849Ensembl.1
Natural variantiVAR_073927318S → P in FTDALS3. 1 Publication1
Natural variantiVAR_073929321R → C in FTDALS3. 2 PublicationsCorresponds to variant dbSNP:rs140226523EnsemblClinVar.1
Natural variantiVAR_073930329D → G in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs148294622Ensembl.1
Natural variantiVAR_073932348P → L in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs772889843EnsemblClinVar.1
Natural variantiVAR_073934370S → P in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs143956614EnsemblClinVar.1
Natural variantiVAR_073935381A → V in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs772122047Ensembl.1
Natural variantiVAR_023592387P → L in PDB3 and FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs776749939EnsemblClinVar.1
Natural variantiVAR_023593392P → L in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 9 PublicationsCorresponds to variant dbSNP:rs104893941EnsemblClinVar.1
Natural variantiVAR_023597411G → S in PDB3 and FTDALS3; no effect on polyubiquitin-binding. 2 PublicationsCorresponds to variant dbSNP:rs143511494Ensembl.1
Natural variantiVAR_023598425G → R in PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 5 PublicationsCorresponds to variant dbSNP:rs757212984Ensembl.1
Natural variantiVAR_073936430T → P in FTDALS3. 1 PublicationCorresponds to variant dbSNP:rs770118706Ensembl.1
Neurodegeneration with ataxia, dystonia, and gaze palsy, childhood-onset (NADGP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder characterized by gait abnormalities, ataxia, dysarthria, dystonia, vertical gaze palsy, and cognitive decline. Disease onset is in childhood or adolescence. NADGP transmission pattern is consistent with autosomal recessive inheritance.
Related information in OMIM
Myopathy, distal, with rimmed vacuoles (DMRV)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant myopathy with adult onset, characterized by muscle weakness of the distal upper and lower limbs, walking difficulties, and proximal weakness of the shoulder girdle muscles. Muscle biopsy shows rimmed vacuoles.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi7K → A: Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69. 2 Publications1
Mutagenesisi9Y → F: No effect on interaction with LCK. 1 Publication1
Mutagenesisi13K → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi21 – 22RR → AA: Loss of interaction with PRKCI. Alters dimerization. 1 Publication2
Mutagenesisi67Y → A: No effect on interaction with PRKCZ. 1 Publication1
Mutagenesisi69D → A: No effect on interactions with PRKCZ, PRKCI and NBR1. Loss of localization in cytoplasmic inclusion bodies. Loss of dimerization; when associated with A-7. 3 Publications1
Mutagenesisi71D → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi73D → A: No effect on interactions with PRKCZ and PRKCI. 2 Publications1
Mutagenesisi80D → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi82E → A: No effect on interaction with PRKCI. 1 Publication1
Mutagenesisi323 – 324EE → AA: No effect on MAP1LC3B-binding. 1 Publication2
Mutagenesisi332S → A: No effect on MAP1LC3B-binding. 1 Publication1
Mutagenesisi335 – 337DDD → ADA: 75% decrease in MAP1LC3B-binding. 1 Publication3
Mutagenesisi338W → A: Strong decrease in MAP1LC3B-binding, disrupts interaction with GABARAP. 2 Publications1
Mutagenesisi342S → A: No effect on MAP1LC3B-binding. 1 Publication1
Mutagenesisi347D → A: Strongly decreased interaction with KEAP1. 1 Publication1
Mutagenesisi350T → A: Strongly decreased interaction with KEAP1. 1 Publication1
Mutagenesisi351G → A: Strongly decreased interaction with KEAP1. 1 Publication1
Mutagenesisi352E → A: Strongly decreased interaction with KEAP1. 1 Publication1
Mutagenesisi398L → V: No effect on polyubiquitin-binding. 1 Publication1
Mutagenesisi403S → A: Abolished ability to promote relocalization of 'Lys-63'-linked ubiquitinated TMEM173/STING to autophagosomes. 1 Publication1
Mutagenesisi406F → V: Loss of polyubiquitin-binding. 1 Publication1
Mutagenesisi409E → K: Decreased activation of NF-kappa-B. 1 Publication1
Mutagenesisi410G → K: Decreased activation of NF-kappa-B. 1 Publication1
Mutagenesisi413L → V: No effect on polyubiquitin-binding. 1 Publication1
Mutagenesisi417L → V: Loss of polyubiquitin-binding. 1 Publication1
Mutagenesisi420K → R: Decreased ubiquitination by the BCR(KEAP1) complex, leading to decreased sequestering activity. 1 Publication1
Mutagenesisi431I → V: Partial loss of polyubiquitin-binding. Loss of localization to cytoplasmic inclusion bodies. 2 Publications1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNET

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DisGeNETi
8878

MalaCards human disease database

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MalaCardsi
SQSTM1
MIMi167250 phenotype
616437 phenotype
617145 phenotype
617158 phenotype

Open Targets

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OpenTargetsi
ENSG00000161011

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
803 Amyotrophic lateral sclerosis
275864 Behavioral variant of frontotemporal dementia
275872 Frontotemporal dementia with motor neuron disease
280110 NON RARE IN EUROPE: Paget disease of bone

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36109

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q13501

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SQSTM1

Domain mapping of disease mutations (DMDM)

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DMDMi
74735628

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000721762 – 440Sequestosome-1Add BLAST439
Isoform 2 (identifier: Q13501-2)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei24PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei148PhosphotyrosineCombined sources1
Modified residuei170PhosphoserineCombined sources1
Modified residuei176PhosphoserineCombined sources1
Cross-linki189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei207PhosphoserineCombined sources1
Modified residuei233PhosphoserineCombined sources1
Modified residuei249PhosphoserineCombined sources1
Modified residuei266PhosphoserineCombined sources1
Modified residuei269PhosphothreonineCombined sources1
Modified residuei272PhosphoserineCombined sources1
Modified residuei306PhosphoserineCombined sources1
Modified residuei328PhosphoserineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Modified residuei349PhosphoserineBy similarity1
Modified residuei355PhosphoserineCombined sources1
Modified residuei361PhosphoserineCombined sources1
Modified residuei365PhosphoserineBy similarity1
Modified residuei366PhosphoserineCombined sources1
Modified residuei403Phosphoserine; by ULK1 and TBK12 Publications1
Cross-linki420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Isoform 2 (identifier: Q13501-2)
Modified residuei2N-acetylalanineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. May be phosphorylated by PRKCZ (By similarity). Phosphorylated in vitro by TTN (PubMed:15802564). 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 TMEM173/STING to autophagosomes (PubMed:29496741). Phosphorylation at Ser-349 by MTOR promotes interaction with KEAP1 and inactivation of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes (By similarity).By similarity3 Publications
Ubiquitinated by RNF26: 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). 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).3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q13501

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13501

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q13501

MaxQB - The MaxQuant DataBase

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MaxQBi
Q13501

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q13501

PeptideAtlas

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PeptideAtlasi
Q13501

PRoteomics IDEntifications database

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PRIDEi
Q13501

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
59496 [Q13501-1]
59497 [Q13501-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13501

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q13501

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q13501

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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 feeback loop (PubMed:20452972).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000161011 Expressed in 238 organ(s), highest expression level in left adrenal gland cortex

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q13501 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13501 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004587
HPA064165
HPA068843

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooligomer or heterooligomer; may form homotypic arrays. Dimerization interferes with ubiquitin binding.

Interacts directly with PRKCI and PRKCZ (Probable). Forms ternary complexes with PRKCZ and KCNAB2 or PRKCZ and GABBR3.

Also interacts with KCNAB1, GABRR1, GABRR2 and GABRR3.

Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (By similarity).

Interacts with EBI3, LCK, RASA1, PRKCZ, PRKCI, NR2F2, NTRK1, NTRK2, NTRK3, NBR1, MAP2K5, TRIM13, TRIM55 and MAPKAPK5.

Interacts with the proteasome subunits PSMD4 and PSMC2.

Interacts with K63-polyubiquitinated MAPT/TAU.

Interacts with IKBKB through PRKCZ and PRKCI.

Interacts with NGFR through TRAF6 and bridges that complex to NTRK1.

Forms a complex with MAP2K5 and PRKCZ or PRKCI.

Component of a ternary complex with PAWR and PRKCZ. Upon TNF-alpha stimulation, interacts with RIPK1 probably bridging IKBKB to the TNF-R1 complex composed of TNF-R1/TNFRSF1A, TRADD and RIPK1.

Forms a complex with JUB/Ajuba, PRKCZ and TRAF6.

Interacts with TRAF6 and CYLD.

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. Directly interacts with MAP1LC3A and MAP1LC3B, as well as with other MAP1 LC3 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.

Interacts with FHOD3.

Interacts with TRMI5.

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 TRIM23 (PubMed:28871090).

Interacts with LRRC25 (PubMed:29288164).

Interacts with TRIM50 (PubMed:22792322).

Interacts with TRIM16 (PubMed:30143514).

Interacts with TMEM173/STING; leading to relocalization of TMEM173/STING to autophagosomes.

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:20495340, PubMed:20452972).

By similarityCurated42 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114397, 341 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q13501

Database of interacting proteins

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DIPi
DIP-34443N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q13501

Protein interaction database and analysis system

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IntActi
Q13501, 169 interactors

Molecular INTeraction database

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MINTi
Q13501

STRING: functional protein association networks

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STRINGi
9606.ENSP00000374455

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
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