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UniProtKB - O08623 (SQSTM_RAT)

Entry version 165 (11 Dec 2019)
Sequence version 1 (01 Jul 1997)
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Protein

Sequestosome-1

Gene

Sqstm1

Organism
Rattus norvegicus (Rat)
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. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery (By similarity). Involved in midbody ring degradation (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:11244088, PubMed:11500922). May play a role in titin/TTN downstream signaling in muscle cells (By similarity). May regulate signaling cascades through ubiquitination (By similarity). 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 (By similarity). 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 (By similarity). Promotes relocalization of 'Lys-63'-linked ubiquitinated TMEM173/STING to autophagosomes (By similarity). 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 (By similarity).By similarity2 Publications
More potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2.1 Publication

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 fingeri119 – 164ZZ-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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

<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):
Protein kinase C-zeta-interacting protein
Short name:
PKC-zeta-interacting protein
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:Zip
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 10

Organism-specific databases

Rat genome database

More...RGDi		69287 Sqstm1

<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

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 interaction with PRKCI. 1 Publication1
Mutagenesisi21 – 22RR → AA: Reduces interaction with PRKCI. 1 Publication2
Mutagenesisi67D → A: No effect on interaction with PRKCI. Abolishes homooligomerization; when associated with A-67. 2 Publications1
Mutagenesisi69D → A: Abolishes homooligomerization; when associated with A-67. 1 Publication1
Mutagenesisi94R → A: Reduces interaction with PRKCI. 1 Publication1

<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 methionineiRemovedBy similarity
<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_00000721792 – 439Sequestosome-1Add BLAST438

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-acetylalanineBy similarity1
Modified residuei24PhosphoserineBy similarity1
Modified residuei145PhosphotyrosineBy similarity1
Modified residuei173PhosphoserineBy similarity1
Modified residuei175PhosphoserineBy similarity1
Modified residuei204PhosphoserineBy similarity1
Modified residuei246PhosphoserineBy similarity1
Modified residuei263PhosphoserineBy similarity1
Modified residuei266PhosphothreonineCombined sources1
Modified residuei269PhosphoserineBy similarity1
Modified residuei305PhosphoserineBy similarity1
Modified residuei327PhosphoserineBy similarity1
Modified residuei331PhosphoserineBy similarity1
Modified residuei348PhosphoserineBy similarity1
Modified residuei354PhosphoserineCombined sources1
Modified residuei360PhosphoserineBy similarity1
Modified residuei364PhosphoserineBy similarity1
Modified residuei365PhosphoserineBy similarity1
Modified residuei402Phosphoserine; by ULK1 and TBK1By similarity1
<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-linki419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<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 (PubMed:9177193). Phosphorylated in vitro by TTN (By similarity). May be phosphorylated by PRKCZ. Phosphorylation at Ser-402 by ULK1 is stimulated by SESN2 (By similarity). Phosphorylated at Ser-402 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated TMEM173/STING to autophagosomes (By similarity). Phosphorylation at Ser-348 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 similarity1 Publication
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. Deubiquitination by USP15 releases target vesicles for fast transport into the cell periphery. Ubiquitinated by the BCR(KEAP1) complex at Lys-419, increasing SQSTM1 sequestering activity and promoting its degradation. Ubiquitinated via 'Lys-29' and 'Lys-33'-linked polyubiquitination leading to xenophagic targeting of bacteria and inhibition of their replication.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O08623

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

More...PaxDbi		O08623

PRoteomics IDEntifications database

More...PRIDEi		O08623

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O08623

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

More...PhosphoSitePlusi		O08623

<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. In brain, mainly expressed by neurons, especially pyramidal neurons in the cerebral cortex and hippocampus. Also expressed by Purkinje cells and neurons in the dentate nucleus of the cerebellum and neurons of the basal ganglia (at protein level).4 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Maximal expression is detected at postnatal day 13 (P13) (at protein level).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 the proteasome inhibitors MG132 and lactacystin. By intoxication with 3,5-diethoxycarbonyl-1,4-dihydrocollidine (DCC). By okadaic acid and kainate (at protein level). Isoform 1 and isoform 2 relative amounts are changed upon up-regulation of the expression by NGF.5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000003147 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O08623 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O08623 RN

<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.

Interacts directly with PRKCI and PRKCZ (Probable).

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

Interacts with the proteasome subunits PSMD4 and PSMC2.

Interacts with K63-polyubiquitinated MAPT/TAU.

Interacts with IKBKB through PRKCZ and PRKCI.

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 AJUBA, PRKCZ and TRAF6.

Interacts with TRAF6 and CYLD.

Identified in a complex with TRAF6 and CYLD.

Identified in a heterotrimeric complex with ubiquitin and ZFAND5, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (By similarity). Forms ternary complexes with PRKCZ and KCNAB2 or PRKCZ and GABBR3.

Interacts with KCNAB1, GABRR1, GABRR2 and GABRR3.

Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6.

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

Interacts with NBR1 and TRIM55. 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 (By similarity).

Interacts with FHOD3 (By similarity).

Interacts with TRMI5 (By similarity).

Interacts with SESN1 (By similarity).

Interacts with SESN2 (By similarity).

Interacts with ULK1.

Interacts with UBD (By similarity).

Interacts with WDR81; the interaction is direct and regulates the interaction of SQSTM1 with ubiquitinated proteins (By similarity).

Interacts with WDFY3; this interaction is required to recruit WDFY3 to cytoplasmic bodies and to PML bodies (By similarity).

Interacts with TRIM23 (By similarity).

Interacts with LRRC25 (By similarity).

Interacts with TRIM50 (By similarity).

Interacts with TRIM16 (By similarity).

Interacts with TMEM173/STING; leading to relocalization of TMEM173/STING to autophagosomes (By similarity).

Interacts (when phosphorylated at Ser-348) with KEAP1; the interaction is direct and inactivates the BCR(KEAP1) complex by sequestering KEAP1 in inclusion bodies, promoting its degradation.

By similarityCurated

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		250206, 24 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O08623

Protein interaction database and analysis system

More...IntActi		O08623, 5 interactors

Molecular INTeraction database

More...MINTi		O08623

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000056021

<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

1439
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		O08623

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O08623

<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 – 100PB1PROSITE-ProRule annotationAdd BLAST98
Domaini388 – 433UBAPROSITE-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 – 48Interaction with LCKBy similarityAdd BLAST47
Regioni41 – 105Interaction with PRKCZ and dimerization2 PublicationsAdd BLAST65
Regioni48 – 78Interaction with PAWRBy similarityAdd BLAST31
Regioni119 – 221Interaction with GABRR31 PublicationAdd BLAST103
Regioni167 – 217LIM protein-bindingBy similarityAdd BLAST51
Regioni266 – 439Interaction with NTRK11 PublicationAdd BLAST174
Regioni320 – 341MAP1LC3B-bindingBy similarityAdd BLAST22
Regioni346 – 351Interaction with KEAP1By similarity6

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>Motifi225 – 230TRAF6-bindingBy similarity6
Motifi335 – 340LIR6

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 biasi269 – 293Ser-richAdd BLAST25

<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.By similarity
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.By similarity
The ZZ-type zinc finger mediates the interaction with RIPK1.By similarity
The LIR (LC3-interacting region) motif mediates the interaction with ATG8 family proteins.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri119 – 164ZZ-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 HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000154407

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O08623

KEGG Orthology (KO)

More...KOi		K14381

Identification of Orthologs from Complete Genome Data

More...OMAi		WHPLQWF

Database of Orthologous Groups

More...OrthoDBi		1275680at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O08623

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)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 3 <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 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: O08623-1) [UniParc]FASTAAdd to basket
Also known as: Zip1, B20

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 LGKEEAAREI RRFSFCFSPE PEAEAAAGPG PCERLLSRVA 
        60         70         80         90        100
VLFPALRPGG FQAHYRDEDG DLVAFSSDEE LTMAMSYVKD DIFRIYIKEK 
       110        120        130        140        150
KECRREHRPP CAQEARSMVH PNVICDGCNG PVVGTRYKCS VCPDYDLCSV 
       160        170        180        190        200
CEGKGLHREH SKLIFPNPFG HLSDSFSHSR WLRKLKHGHF GWPGWEMGPP 
       210        220        230        240        250
GNWSPRPPRA GDGRPCPTAE SASAPSEDPN VNFLKNVGES VAAALSPLGI 
       260        270        280        290        300
EVDIDVEHGG KRSRLTPTSA ESSSTGTEDK SGTQPSSCSS EVSKPDGAGE 
       310        320        330        340        350
GPAQSLTEQM KKIALESVGQ PEELMESDNC SGGDDDWTHL SSKEVDPSTG 
       360        370        380        390        400
ELQSLQMPES EGPSSLDPSQ EGPTGLKEAA LYPHLPPEAD PRLIESLSQM 
       410        420        430 
LSMGFSDEGG WLTRLLQTKN YDIGAALDTI QYSKHPPPL
Note: Major isoform except in central nervous system.
Length:439
Mass (Da):47,681
Last modified:July 1, 1997 - 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:iE611F296E2B11464
GO
Isoform 2 (identifier: O08623-2) [UniParc]FASTAAdd to basket
Also known as: Zip2, B24

The sequence of this isoform differs from the canonical sequence as follows:
     222-248: Missing.

Show »
Length:412
Mass (Da):45,001
Checksum:i0AF172634A51767A
GO
Isoform 3 (identifier: O08623-3) [UniParc]FASTAAdd to basket
Also known as: Zip3

The sequence of this isoform differs from the canonical sequence as follows:
     222-234: ASAPSEDPNVNFL → GKAGVCTGFKCHK
     235-439: Missing.

Show »
Length:234
Mass (Da):26,067
Checksum:iB0D9DCF8BD017FBA
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0H2UHB5A0A0H2UHB5_RAT
Sequestosome-1
Sqstm1
234Annotation 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>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_015843222 – 248Missing in isoform 2. CuratedAdd BLAST27
Alternative sequenceiVSP_015844222 – 234ASAPS…NVNFL → GKAGVCTGFKCHK in isoform 3. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_015845235 – 439Missing in isoform 3. 1 PublicationAdd BLAST205

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Y08355 mRNA Translation: CAA69642.1
AF439403 mRNA Translation: AAO15463.1
BC061575 mRNA Translation: AAH61575.1

NCBI Reference Sequences

More...RefSeqi		NP_787037.2, NM_175843.4 [O08623-1]
NP_853528.1, NM_181550.1 [O08623-3]
XP_006246275.1, XM_006246213.2 [O08623-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000059255; ENSRNOP00000056021; ENSRNOG00000003147 [O08623-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		113894

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:113894

UCSC genome browser

More...UCSCi		RGD:69287 rat [O08623-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08355 mRNA Translation: CAA69642.1
AF439403 mRNA Translation: AAO15463.1
BC061575 mRNA Translation: AAH61575.1
RefSeqiNP_787037.2, NM_175843.4 [O08623-1]
NP_853528.1, NM_181550.1 [O08623-3]
XP_006246275.1, XM_006246213.2 [O08623-2]

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
2K6QNMR-B331-346[»]
2KKCNMR-A3-100[»]
2KTRNMR-A/B3-100[»]
SMRiO08623
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi250206, 24 interactors
CORUMiO08623
IntActiO08623, 5 interactors
MINTiO08623
STRINGi10116.ENSRNOP00000056021

PTM databases

iPTMnetiO08623
PhosphoSitePlusiO08623

Proteomic databases

jPOSTiO08623
PaxDbiO08623
PRIDEiO08623

Genome annotation databases

EnsembliENSRNOT00000059255; ENSRNOP00000056021; ENSRNOG00000003147 [O08623-1]
GeneIDi113894
KEGGirno:113894
UCSCiRGD:69287 rat [O08623-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8878
RGDi69287 Sqstm1

Phylogenomic databases

eggNOGiKOG4582 Eukaryota
ENOG410XYAV LUCA
GeneTreeiENSGT00390000002781
HOGENOMiHOG000154407
InParanoidiO08623
KOiK14381
OMAiWHPLQWF
OrthoDBi1275680at2759
PhylomeDBiO08623

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO08623

Protein Ontology

More...PROi		PR:O08623

Gene expression databases

BgeeiENSRNOG00000003147 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
ExpressionAtlasiO08623 baseline and differential
GenevisibleiO08623 RN

Family and domain databases

CDDicd06402 PB1_p62, 1 hit
cd14320 UBA_SQSTM, 1 hit
InterProiView protein in InterPro
IPR000270 PB1_dom
IPR034866 PB1_p62
IPR033741 SQSTM_UBA
IPR015940 UBA
IPR009060 UBA-like_sf
IPR000433 Znf_ZZ
PfamiView protein in Pfam
PF00564 PB1, 1 hit
PF16577 UBA_5, 1 hit
PF00569 ZZ, 1 hit
SMARTiView protein in SMART
SM00666 PB1, 1 hit
SM00165 UBA, 1 hit
SM00291 ZnF_ZZ, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
PROSITEiView protein in PROSITE
PS51745 PB1, 1 hit
PS50030 UBA, 1 hit
PS01357 ZF_ZZ_1, 1 hit
PS50135 ZF_ZZ_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSQSTM_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O08623
Secondary accession number(s): Q8CH59
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: July 1, 1997
Last modified: December 11, 2019
This is version 165 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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