Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 200 (13 Feb 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
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).By similarity16 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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

More...
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

More...
SignaLinki
Q13501

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q13501

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
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

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000161011.19

Human Gene Nomenclature Database

More...
HGNCi
HGNC:11280 SQSTM1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
601530 gene

neXtProt; the human protein knowledge platform

More...
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.
See also OMIM:167250
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.
See also OMIM:616437
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07389916A → V in FTDALS3. 1 Publication1
Natural variantiVAR_07390133A → V in FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs200396166Ensembl.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.
See also OMIM:617145
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.
See also OMIM:617158

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
Mutagenesisi398L → V: No effect on polyubiquitin-binding. 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
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

More...
DisGeNETi
8878

MalaCards human disease database

More...
MalaCardsi
SQSTM1
MIMi167250 phenotype
616437 phenotype
617145 phenotype
617158 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000161011

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

More...
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

More...
PharmGKBi
PA36109

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SQSTM1

Domain mapping of disease mutations (DMDM)

More...
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
Modified residuei148PhosphotyrosineCombined sources1
Modified residuei170PhosphoserineCombined sources1
Modified residuei176PhosphoserineCombined sources1
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 residuei355PhosphoserineCombined sources1
Modified residuei361PhosphoserineCombined sources1
Modified residuei365PhosphoserineBy similarity1
Modified residuei366PhosphoserineCombined sources1
Modified residuei403Phosphoserine; by ULK11 Publication1
<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-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. Phosphorylation at Ser-403 by ULK1 is stimulated by SESN2 (PubMed:25040165).By similarity2 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).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q13501

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q13501

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q13501

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

More...
PaxDbi
Q13501

PeptideAtlas

More...
PeptideAtlasi
Q13501

PRoteomics IDEntifications database

More...
PRIDEi
Q13501

ProteomicsDB human proteome resource

More...
ProteomicsDBi
59496
59497 [Q13501-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q13501

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

More...
PhosphoSitePlusi
Q13501

SwissPalm database of S-palmitoylation events

More...
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).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q13501 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q13501 HS

Organism-specific databases

Human Protein Atlas

More...
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).By similarityCurated39 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)

More...
BioGridi
114397, 316 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q13501

Database of interacting proteins

More...
DIPi
DIP-34443N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q13501

Protein interaction database and analysis system

More...
IntActi
Q13501, 152 interactors

Molecular INTeraction database

More...
MINTi
Q13501

STRING: functional protein association networks

More...
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
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q02NMR-A387-436[»]
2JY7NMR-A387-436[»]
2JY8NMR-A387-436[»]
2K0BNMR-X387-436[»]
2KNVNMR-A/B387-436[»]
4MJSX-ray2.50B/D/F/H/J/L/N/P/R/T/V/X3-102[»]
4UF8electron microscopy10.90A/B/C/I3-102[»]
4UF9electron microscopy10.30A/B/D1-122[»]
5YP7X-ray1.42A/D126-180[»]
5YP8X-ray1.45A/B126-180[»]
5YPAX-ray2.50A/B126-180[»]
5YPBX-ray2.90A/B/C/D126-180[»]
5YPCX-ray1.96A/B/C/D126-180[»]
5YPEX-ray2.85A/B/C/D126-180[»]
5YPFX-ray2.95A/B/C/D126-180[»]
5YPGX-ray2.20A/B126-180[»]
5YPHX-ray1.63A/B126-180[»]
6MJ7X-ray1.41A120-171[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q13501

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q13501

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q13501

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 102PB1PROSITE-ProRule annotationAdd BLAST100
Domaini389 – 434UBAPROSITE-ProRule annotationAdd BLAST46

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 50Interaction with LCKAdd BLAST49
Regioni43 – 107Interaction with PRKCZ and dimerizationBy similarityAdd BLAST65
Regioni50 – 80Interaction with PAWR1 PublicationAdd BLAST31
Regioni122 – 224Interaction with GABRR3By similarityAdd BLAST103
Regioni170 – 220LIM protein-binding (LB)Add BLAST51
Regioni269 – 440Interaction with NTRK1By similarityAdd BLAST172
Regioni321 – 342MAP1LC3B-bindingAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi228 – 233TRAF6-binding6
Motifi336 – 341LIR6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi272 – 294Ser-richAdd BLAST23

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The UBA domain binds specifically 'Lys-63'-linked polyubiquitin chains of polyubiquitinated substrates. Mediates the interaction with TRIM55. Both the UBA and PB1 domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies.2 Publications
The PB1 domain mediates homooligomerization and interactions with FHOD3, MAP2K5, NBR1, PRKCI, PRKCZ and WDR81. Both the PB1 and UBA domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies.4 Publications
The ZZ-type zinc finger mediates the interaction with RIPK1.1 Publication
The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri122 – 167ZZ-typePROSITE-ProRule annotationAdd BLAST46

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4582 Eukaryota
ENOG410XYAV LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000002781

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG052750

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q13501

KEGG Orthology (KO)

More...
KOi
K14381

Identification of Orthologs from Complete Genome Data

More...
OMAi
KNCDIGA

Database of Orthologous Groups

More...
OrthoDBi
1275680at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q13501

TreeFam database of animal gene trees

More...
TreeFami
TF328470

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06402 PB1_p62, 1 hit
cd14320 UBA_SQSTM, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000270 PB1_dom
IPR034866 PB1_p62
IPR033741 SQSTM_UBA
IPR015940 UBA
IPR009060 UBA-like_sf
IPR000433 Znf_ZZ

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00564 PB1, 1 hit
PF16577 UBA_5, 1 hit
PF00569 ZZ, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00666 PB1, 1 hit
SM00165 UBA, 1 hit
SM00291 ZnF_ZZ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46934 SSF46934, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51745 PB1, 1 hit
PS50030 UBA, 1 hit
PS01357 ZF_ZZ_1, 1 hit
PS50135 ZF_ZZ_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13501-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MASLTVKAYL LGKEDAAREI RRFSFCCSPE PEAEAEAAAG PGPCERLLSR
60 70 80 90 100
VAALFPALRP GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK
110 120 130 140 150
EKKECRRDHR PPCAQEAPRN MVHPNVICDG CNGPVVGTRY KCSVCPDYDL
160 170 180 190 200
CSVCEGKGLH RGHTKLAFPS PFGHLSEGFS HSRWLRKVKH GHFGWPGWEM
210 220 230 240 250
GPPGNWSPRP PRAGEARPGP TAESASGPSE DPSVNFLKNV GESVAAALSP
260 270 280 290 300
LGIEVDIDVE HGGKRSRLTP VSPESSSTEE KSSSQPSSCC SDPSKPGGNV
310 320 330 340 350
EGATQSLAEQ MRKIALESEG RPEEQMESDN CSGGDDDWTH LSSKEVDPST
360 370 380 390 400
GELQSLQMPE SEGPSSLDPS QEGPTGLKEA ALYPHLPPEA DPRLIESLSQ
410 420 430 440
MLSMGFSDEG GWLTRLLQTK NYDIGAALDT IQYSKHPPPL
Length:440
Mass (Da):47,687
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i462D94C171F337CD
GO
Isoform 2 (identifier: Q13501-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Show »
Length:356
Mass (Da):38,629
Checksum:i56E985FFBF86EC1B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EMC7E7EMC7_HUMAN
Sequestosome-1
SQSTM1
378Annotation score:

Annotation score:1 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>
C9JRJ8C9JRJ8_HUMAN
Sequestosome-1
SQSTM1
140Annotation score:

Annotation score:1 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>
E9PFW8E9PFW8_HUMAN
Sequestosome-1
SQSTM1
167Annotation score:

Annotation score:1 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>
E3W990E3W990_HUMAN
Sequestosome-1
SQSTM1
190Annotation score:

Annotation score:1 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>
D6RBF1D6RBF1_HUMAN
Sequestosome-1
SQSTM1
69Annotation score:

Annotation score:1 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>
C9J6J8C9J6J8_HUMAN
Sequestosome-1
SQSTM1
73Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti321R → A in AAA93299 (PubMed:8551575).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07389916A → V in FTDALS3. 1 Publication1
Natural variantiVAR_07390017A → V1 PublicationCorresponds to variant dbSNP:rs141502868Ensembl.1
Natural variantiVAR_07390133A → V in FTDALS3. 3 PublicationsCorresponds to variant dbSNP:rs200396166Ensembl.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_073904103K → R1 PublicationCorresponds to variant dbSNP:rs748170760Ensembl.1
Natural variantiVAR_073905107R → Q1 Publication