Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13501

- SQSTM_HUMAN

UniProt

Q13501 - SQSTM_HUMAN

Protein

Sequestosome-1

Gene

SQSTM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Autophagy receptor that 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. Involved in midbody ring degradation. 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.By similarity13 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri122 – 16746ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB
    4. protein kinase C binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. receptor tyrosine kinase binding Source: ProtInc
    7. SH2 domain binding Source: UniProtKB
    8. ubiquitin binding Source: UniProtKB
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. autophagy Source: UniProtKB
    3. cell differentiation Source: UniProtKB-KW
    4. endosomal transport Source: UniProtKB
    5. immune system process Source: UniProtKB-KW
    6. intracellular signal transduction Source: UniProtKB
    7. macroautophagy Source: UniProtKB
    8. negative regulation of apoptotic process Source: Reactome
    9. neurotrophin TRK receptor signaling pathway Source: Reactome
    10. positive regulation of apoptotic process Source: Reactome
    11. positive regulation of macroautophagy Source: UniProtKB
    12. positive regulation of protein phosphorylation Source: Ensembl
    13. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    14. protein heterooligomerization Source: Ensembl
    15. protein localization Source: UniProtKB
    16. protein phosphorylation Source: GOC
    17. regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    18. regulation of Ras protein signal transduction Source: UniProtKB
    19. response to stress Source: UniProtKB
    20. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Biological processi

    Apoptosis, Autophagy, Differentiation, Immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_13415. p75NTR recruits signalling complexes.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_22442. Interleukin-1 signaling.
    SignaLinkiQ13501.

    Names & Taxonomyi

    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
    Gene namesi
    Name:SQSTM1
    Synonyms:ORCA, OSIL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:11280. SQSTM1.

    Subcellular locationi

    Cytoplasm. Late endosome. Lysosome. Cytoplasmic vesicleautophagosome. Nucleus. Endoplasmic reticulum. CytoplasmP-body
    Note: Sarcomere By similarity. In cardiac muscles localizes to the sarcomeric band By similarity. Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co-localizes with TRIM5 in the cytoplasmic bodies.By similarity

    GO - Cellular componenti

    1. aggresome Source: Ensembl
    2. autophagic vacuole Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. cytoplasmic mRNA processing body Source: UniProtKB
    5. cytoplasmic vesicle Source: UniProtKB-KW
    6. cytosol Source: UniProtKB
    7. endoplasmic reticulum Source: UniProtKB-SubCell
    8. extracellular vesicular exosome Source: UniProt
    9. inclusion body Source: UniProtKB
    10. late endosome Source: UniProtKB-SubCell
    11. lysosome Source: UniProtKB-SubCell
    12. nucleoplasm Source: Reactome
    13. PML body Source: UniProtKB
    14. pre-autophagosomal structure Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Paget disease of bone (PDB) [MIM:602080]: Metabolic bone disease affecting the axial skeleton and characterized by focal areas of increased and disorganized bone turn-over due to activated osteoclasts. Manifestations of the disease include bone pain, deformity, pathological fractures, deafness, neurological complications and increased risk of osteosarcoma. PDB is a chronic disease affecting 2 to 3% of the population above the age of 40 years.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti387 – 3871P → L in PDB. 1 Publication
    VAR_023592
    Natural varianti392 – 3921P → L in PDB; no effect on polyubiquitin-binding. 5 Publications
    Corresponds to variant rs104893941 [ dbSNP | Ensembl ].
    VAR_023593
    Natural varianti399 – 3991S → P in PDB. 1 Publication
    VAR_023594
    Natural varianti404 – 4041M → T in PDB. 1 Publication
    VAR_023595
    Natural varianti404 – 4041M → V in PDB; loss of polyubiquitin-binding. 2 Publications
    VAR_023596
    Natural varianti411 – 4111G → S in PDB; no effect on polyubiquitin-binding. 1 Publication
    VAR_023597
    Natural varianti425 – 4251G → R in PDB; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 3 Publications
    VAR_023598
    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71K → A: Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69. 2 Publications
    Mutagenesisi9 – 91Y → F: No effect on interaction with LCK. 1 Publication
    Mutagenesisi13 – 131K → A: No effect on interaction with PRKCI. 1 Publication
    Mutagenesisi21 – 222RR → AA: Loss of interaction with PRKCI. Alters dimerization.
    Mutagenesisi67 – 671Y → A: No effect on interaction with PRKCZ. 1 Publication
    Mutagenesisi69 – 691D → 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 Publications
    Mutagenesisi71 – 711D → A: No effect on interaction with PRKCI. 1 Publication
    Mutagenesisi73 – 731D → A: No effect on interactions with PRKCZ and PRKCI. 2 Publications
    Mutagenesisi80 – 801D → A: No effect on interaction with PRKCI. 1 Publication
    Mutagenesisi82 – 821E → A: No effect on interaction with PRKCI. 1 Publication
    Mutagenesisi323 – 3242EE → AA: No effect on MAP1LC3B-binding.
    Mutagenesisi332 – 3321S → A: No effect on MAP1LC3B-binding. 1 Publication
    Mutagenesisi335 – 3373DDD → ADA: 75% decrease in MAP1LC3B-binding.
    Mutagenesisi338 – 3381W → A: Strong decrease in MAP1LC3B-binding, disupts interaction with GABARAP. 2 Publications
    Mutagenesisi342 – 3421S → A: No effect on MAP1LC3B-binding. 1 Publication
    Mutagenesisi398 – 3981L → V: No effect on polyubiquitin-binding. 1 Publication
    Mutagenesisi406 – 4061F → V: Loss of polyubiquitin-binding. 1 Publication
    Mutagenesisi409 – 4091E → K: Decreased activation of NF-kappa-B. 1 Publication
    Mutagenesisi410 – 4101G → K: Decreased activation of NF-kappa-B. 1 Publication
    Mutagenesisi413 – 4131L → V: No effect on polyubiquitin-binding. 1 Publication
    Mutagenesisi417 – 4171L → V: Loss of polyubiquitin-binding. 1 Publication
    Mutagenesisi431 – 4311I → V: Partial loss of polyubiquitin-binding. Loss of localization to cytoplasmic inclusion bodies. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi602080. phenotype.
    Orphaneti803. Amyotrophic lateral sclerosis.
    280110. Paget disease of bone.
    PharmGKBiPA36109.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 440439Sequestosome-1PRO_0000072176Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei148 – 1481Phosphotyrosine2 Publications
    Modified residuei170 – 1701Phosphoserine3 Publications
    Modified residuei207 – 2071Phosphoserine2 Publications
    Modified residuei249 – 2491Phosphoserine2 Publications
    Modified residuei266 – 2661Phosphoserine2 Publications
    Modified residuei269 – 2691Phosphothreonine4 Publications
    Modified residuei272 – 2721Phosphoserine6 Publications
    Modified residuei328 – 3281Phosphoserine2 Publications
    Modified residuei332 – 3321Phosphoserine4 Publications
    Modified residuei355 – 3551Phosphoserine2 Publications
    Modified residuei361 – 3611Phosphoserine2 Publications
    Modified residuei366 – 3661Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated. May be phosphorylated by PRKCZ By similarity. Phosphorylated in vitro by TTN.By similarity9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13501.
    PaxDbiQ13501.
    PRIDEiQ13501.

    PTM databases

    PhosphoSiteiQ13501.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Inductioni

    By proteasomal inhibitor PSI and prostaglandin J2 (PGJ2) (at protein level). By phorbol 12-myristate 13-acetate (PMA).3 Publications

    Gene expression databases

    ArrayExpressiQ13501.
    BgeeiQ13501.
    CleanExiHS_SQSTM1.
    GenevestigatoriQ13501.

    Organism-specific databases

    HPAiCAB004587.

    Interactioni

    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 problably 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.By similarity30 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-307104,EBI-307104
    ATG8P381823EBI-307104,EBI-2684From a different organism.
    BAG3O958173EBI-307104,EBI-747185
    CDC37Q165433EBI-307104,EBI-295634
    FHOD3Q2V2M96EBI-307104,EBI-6395541
    FHOD3Q2V2M9-44EBI-307104,EBI-6395505
    GABARAPO9516610EBI-307104,EBI-712001
    GABARAPL1Q9H0R87EBI-307104,EBI-746969
    GABARAPL2P6052012EBI-307104,EBI-720116
    IKBKGQ9Y6K92EBI-307104,EBI-81279
    KEAP1Q141458EBI-307104,EBI-751001
    Keap1Q9Z2X82EBI-307104,EBI-647110From a different organism.
    MALT1Q9UDY82EBI-307104,EBI-1047372
    MAP1LC3AQ9H4927EBI-307104,EBI-720768
    MAP1LC3BQ9GZQ815EBI-307104,EBI-373144
    MAP1LC3CQ9BXW42EBI-307104,EBI-2603996
    NBR1Q145966EBI-307104,EBI-742698
    PRKCIP417435EBI-307104,EBI-286199
    RAD23AP547252EBI-307104,EBI-746453
    SH3KBP1Q96B974EBI-307104,EBI-346595
    SMAD3P840223EBI-307104,EBI-347161
    TRAF6Q9Y4K32EBI-307104,EBI-359276
    UBCP0CG483EBI-307104,EBI-3390054
    vifP125042EBI-307104,EBI-779991From a different organism.

    Protein-protein interaction databases

    BioGridi114397. 375 interactions.
    DIPiDIP-34443N.
    IntActiQ13501. 112 interactions.
    MINTiMINT-269914.
    STRINGi9606.ENSP00000374455.

    Structurei

    Secondary structure

    1
    440
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi388 – 3903
    Helixi392 – 40211
    Turni403 – 4053
    Beta strandi409 – 4113
    Helixi412 – 4198
    Turni420 – 4223
    Helixi424 – 4318
    Beta strandi432 – 4343

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q02NMR-A387-436[»]
    2JY7NMR-A387-436[»]
    2JY8NMR-A387-436[»]
    2K0BNMR-X387-436[»]
    2KNVNMR-A/B387-436[»]
    ProteinModelPortaliQ13501.
    SMRiQ13501. Positions 3-102, 387-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13501.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10283OPRAdd
    BLAST
    Domaini389 – 43446UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 5049Interaction with LCKAdd
    BLAST
    Regioni43 – 10765Interaction with PRKCZ and dimerizationBy similarityAdd
    BLAST
    Regioni50 – 8031Interaction with PAWRAdd
    BLAST
    Regioni122 – 224103Interaction with GABRR3By similarityAdd
    BLAST
    Regioni170 – 22051LIM protein-binding (LB)Add
    BLAST
    Regioni269 – 440172Interaction with NTRK1By similarityAdd
    BLAST
    Regioni321 – 34222MAP1LC3B-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi228 – 2336TRAF6-binding
    Motifi336 – 3416LIR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi272 – 29423Ser-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 OPR domain.Curated
    Contains 1 UBA domain.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri122 – 16746ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG278569.
    HOVERGENiHBG052750.
    InParanoidiQ13501.
    KOiK14381.
    OMAiDAIQYSK.
    PhylomeDBiQ13501.
    TreeFamiTF328470.

    Family and domain databases

    InterProiIPR000270. OPR_PB1.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000433. Znf_ZZ.
    [Graphical view]
    PfamiPF00564. PB1. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view]
    SMARTiSM00666. PB1. 1 hit.
    SM00165. UBA. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS50030. UBA. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MASLTVKAYL LGKEDAAREI RRFSFCCSPE PEAEAEAAAG PGPCERLLSR    50
    VAALFPALRP GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK 100
    EKKECRRDHR PPCAQEAPRN MVHPNVICDG CNGPVVGTRY KCSVCPDYDL 150
    CSVCEGKGLH RGHTKLAFPS PFGHLSEGFS HSRWLRKVKH GHFGWPGWEM 200
    GPPGNWSPRP PRAGEARPGP TAESASGPSE DPSVNFLKNV GESVAAALSP 250
    LGIEVDIDVE HGGKRSRLTP VSPESSSTEE KSSSQPSSCC SDPSKPGGNV 300
    EGATQSLAEQ MRKIALESEG RPEEQMESDN CSGGDDDWTH LSSKEVDPST 350
    GELQSLQMPE SEGPSSLDPS QEGPTGLKEA ALYPHLPPEA DPRLIESLSQ 400
    MLSMGFSDEG GWLTRLLQTK NYDIGAALDT IQYSKHPPPL 440
    Length:440
    Mass (Da):47,687
    Last modified:November 1, 1996 - v1
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti321 – 3211R → A in AAA93299. (PubMed:8551575)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti117 – 1171A → V.1 Publication
    Corresponds to variant rs147810437 [ dbSNP | Ensembl ].
    VAR_023590
    Natural varianti238 – 2381K → E Polymorphism confirmed at protein level. 1 Publication
    Corresponds to variant rs11548633 [ dbSNP | Ensembl ].
    VAR_068915
    Natural varianti274 – 2741E → D.
    Corresponds to variant rs55793208 [ dbSNP | Ensembl ].
    VAR_061707
    Natural varianti274 – 2741E → Q.1 Publication
    VAR_023591
    Natural varianti387 – 3871P → L in PDB. 1 Publication
    VAR_023592
    Natural varianti392 – 3921P → L in PDB; no effect on polyubiquitin-binding. 5 Publications
    Corresponds to variant rs104893941 [ dbSNP | Ensembl ].
    VAR_023593
    Natural varianti399 – 3991S → P in PDB. 1 Publication
    VAR_023594
    Natural varianti404 – 4041M → T in PDB. 1 Publication
    VAR_023595
    Natural varianti404 – 4041M → V in PDB; loss of polyubiquitin-binding. 2 Publications
    VAR_023596
    Natural varianti411 – 4111G → S in PDB; no effect on polyubiquitin-binding. 1 Publication
    VAR_023597
    Natural varianti425 – 4251G → R in PDB; loss of polyubiquitin-binding and increased activation of NF-kappa-B. 3 Publications
    VAR_023598

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8484Missing in isoform 2. 2 PublicationsVSP_015841Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41806 mRNA. Translation: AAA93299.1.
    U46751 mRNA. Translation: AAC52070.1.
    AK098077 mRNA. Translation: BAG53577.1.
    AK312451 mRNA. Translation: BAG35358.1.
    AC008393 Genomic DNA. No translation available.
    BC000951 mRNA. Translation: AAH00951.1.
    BC001874 mRNA. Translation: AAH01874.1.
    BC003139 mRNA. Translation: AAH03139.1.
    BC017222 mRNA. Translation: AAH17222.1.
    BC019111 mRNA. Translation: AAH19111.1.
    AF060494 Genomic DNA. Translation: AAC64516.1.
    CCDSiCCDS34317.1. [Q13501-1]
    CCDS47355.1. [Q13501-2]
    RefSeqiNP_001135770.1. NM_001142298.1. [Q13501-2]
    NP_001135771.1. NM_001142299.1. [Q13501-2]
    NP_003891.1. NM_003900.4. [Q13501-1]
    UniGeneiHs.724025.

    Genome annotation databases

    EnsembliENST00000360718; ENSP00000353944; ENSG00000161011. [Q13501-2]
    ENST00000389805; ENSP00000374455; ENSG00000161011. [Q13501-1]
    GeneIDi8878.
    KEGGihsa:8878.
    UCSCiuc003mkw.4. human. [Q13501-1]

    Polymorphism databases

    DMDMi74735628.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U41806 mRNA. Translation: AAA93299.1 .
    U46751 mRNA. Translation: AAC52070.1 .
    AK098077 mRNA. Translation: BAG53577.1 .
    AK312451 mRNA. Translation: BAG35358.1 .
    AC008393 Genomic DNA. No translation available.
    BC000951 mRNA. Translation: AAH00951.1 .
    BC001874 mRNA. Translation: AAH01874.1 .
    BC003139 mRNA. Translation: AAH03139.1 .
    BC017222 mRNA. Translation: AAH17222.1 .
    BC019111 mRNA. Translation: AAH19111.1 .
    AF060494 Genomic DNA. Translation: AAC64516.1 .
    CCDSi CCDS34317.1. [Q13501-1 ]
    CCDS47355.1. [Q13501-2 ]
    RefSeqi NP_001135770.1. NM_001142298.1. [Q13501-2 ]
    NP_001135771.1. NM_001142299.1. [Q13501-2 ]
    NP_003891.1. NM_003900.4. [Q13501-1 ]
    UniGenei Hs.724025.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q02 NMR - A 387-436 [» ]
    2JY7 NMR - A 387-436 [» ]
    2JY8 NMR - A 387-436 [» ]
    2K0B NMR - X 387-436 [» ]
    2KNV NMR - A/B 387-436 [» ]
    ProteinModelPortali Q13501.
    SMRi Q13501. Positions 3-102, 387-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114397. 375 interactions.
    DIPi DIP-34443N.
    IntActi Q13501. 112 interactions.
    MINTi MINT-269914.
    STRINGi 9606.ENSP00000374455.

    PTM databases

    PhosphoSitei Q13501.

    Polymorphism databases

    DMDMi 74735628.

    Proteomic databases

    MaxQBi Q13501.
    PaxDbi Q13501.
    PRIDEi Q13501.

    Protocols and materials databases

    DNASUi 8878.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360718 ; ENSP00000353944 ; ENSG00000161011 . [Q13501-2 ]
    ENST00000389805 ; ENSP00000374455 ; ENSG00000161011 . [Q13501-1 ]
    GeneIDi 8878.
    KEGGi hsa:8878.
    UCSCi uc003mkw.4. human. [Q13501-1 ]

    Organism-specific databases

    CTDi 8878.
    GeneCardsi GC05P179234.
    HGNCi HGNC:11280. SQSTM1.
    HPAi CAB004587.
    MIMi 601530. gene.
    602080. phenotype.
    neXtProti NX_Q13501.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    280110. Paget disease of bone.
    PharmGKBi PA36109.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278569.
    HOVERGENi HBG052750.
    InParanoidi Q13501.
    KOi K14381.
    OMAi DAIQYSK.
    PhylomeDBi Q13501.
    TreeFami TF328470.

    Enzyme and pathway databases

    Reactomei REACT_13415. p75NTR recruits signalling complexes.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_22442. Interleukin-1 signaling.
    SignaLinki Q13501.

    Miscellaneous databases

    ChiTaRSi SQSTM1. human.
    EvolutionaryTracei Q13501.
    GeneWikii Sequestosome_1.
    GenomeRNAii 8878.
    NextBioi 33335.
    PROi Q13501.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13501.
    Bgeei Q13501.
    CleanExi HS_SQSTM1.
    Genevestigatori Q13501.

    Family and domain databases

    InterProi IPR000270. OPR_PB1.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000433. Znf_ZZ.
    [Graphical view ]
    Pfami PF00564. PB1. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view ]
    SMARTi SM00666. PB1. 1 hit.
    SM00165. UBA. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS50030. UBA. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes."
      Devergne O., Hummel M., Koeppen H., Le Beau M.M., Nathanson E.C., Kieff E., Birkenbach M.
      J. Virol. 70:1143-1153(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 345-361 AND 394-411, INTERACTION WITH EBI3.
      Tissue: B-cell.
    2. "Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain."
      Joung I., Strominger J.L., Shin J.
      Proc. Natl. Acad. Sci. U.S.A. 93:5991-5995(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 51-96; 184-187; 213-217; 239-264 AND 268-281, TISSUE SPECIFICITY, INTERACTION WITH LCK, MUTAGENESIS OF TYR-9.
      Tissue: Cervix carcinoma.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Caudate nucleus and Trachea.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Pancreas, Placenta, Skin and Uterus.
    6. "Genomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding protein."
      Vadlamudi R.K., Shin J.
      FEBS Lett. 435:138-142(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72, INDUCTION.
    7. "Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent."
      Stumptner C., Heid H., Fuchsbichler A., Hauser H., Mischinger H.-J., Zatloukal K., Denk H.
      Am. J. Pathol. 154:1701-1710(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-60; 166-174 AND 379-388, SUBCELLULAR LOCATION.
    8. "Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region."
      Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.
      Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LCK AND RASA1.
    9. "p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins."
      Vadlamudi R.K., Joung I., Strominger J.L., Shin J.
      J. Biol. Chem. 271:20235-20237(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBIQUITIN.
    10. "A p56(lck) ligand serves as a coactivator of an orphan nuclear hormone receptor."
      Marcus S.L., Winrow C.J., Capone J.P., Rachubinski R.A.
      J. Biol. Chem. 271:27197-27200(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2F2.
    11. "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62."
      Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.
      Mol. Cell. Biol. 18:3069-3080(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCI AND PRKCZ, SUBCELLULAR LOCATION.
    12. "The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
      Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
      EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIPK1; PRKCZ; PRKCI; IKBKB; TRADD AND TNFRSF1A, FUNCTION.
    13. Cited for: INTERACTION WITH MAPKAPK5, SUBCELLULAR LOCATION.
    14. "The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway."
      Sanz L., Diaz-Meco M.T., Nakano H., Moscat J.
      EMBO J. 19:1576-1586(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF6 AND RIPK1, DOMAIN, FUNCTION.
    15. "The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor."
      Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A., Moscat J.
      J. Biol. Chem. 276:7709-7712(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NTRK1; TRAF6; NGFR AND PRKCZ, FUNCTION.
    16. "p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases."
      Zatloukal K., Stumptner C., Fuchsbichler A., Heid H., Schnoelzer M., Kenner L., Kleinert R., Prinz M., Aguzzi A., Denk H.
      Am. J. Pathol. 160:255-263(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition."
      Chang S., Kim J.H., Shin J.
      FEBS Lett. 510:57-61(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAWR AND PRKCZ.
    18. "Mallory body -- a disease-associated type of sequestosome."
      Stumptner C., Fuchsbichler A., Heid H., Zatloukal K., Denk H.
      Hepatology 35:1053-1062(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    19. "Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling."
      Geetha T., Wooten M.W.
      J. Biol. Chem. 278:4730-4739(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NTRK1; NTRK2 AND NTRK3, SUBCELLULAR LOCATION, FUNCTION.
    20. "Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins."
      Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A., Michaelsen E., Bjoerkoey G., Johansen T.
      J. Biol. Chem. 278:34568-34581(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCI; PRKCZ; MAP2K5 AND NBR1, DOMAIN, MUTAGENESIS OF LYS-7; LYS-13; 21-ARG-ARG-22; TYR-67; ASP-69; ASP-71; ASP-73; ASP-80 AND GLU-82, DIMERIZATION.
    21. "PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62."
      Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.
      Mol. Cell 12:39-50(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCZ, DOMAIN, OLIGOMERIZATION, MUTAGENESIS OF LYS-7; ASP-69 AND ASP-73.
    22. "p62 overexpression in breast tumors and regulation by prostate-derived Ets factor in breast cancer cells."
      Thompson H.G.R., Harris J.W., Wold B.J., Lin F., Brody J.P.
      Oncogene 22:2322-2333(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    23. "Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson's disease."
      Nakaso K., Yoshimoto Y., Nakano T., Takeshima T., Fukuhara Y., Yasui K., Araga S., Yanagawa T., Ishii T., Nakashima K.
      Brain Res. 1012:42-51(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    24. "Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation."
      Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W.
      Mol. Cell. Biol. 24:8055-8068(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF6; PSMC2 AND PSMD4, DOMAIN, MUTAGENESIS OF LEU-398; PHE-406; LEU-413; LEU-417 AND ILE-431, FUNCTION.
    25. "The p62 scaffold regulates nerve growth factor-induced NF-kappaB activation by influencing TRAF6 polyubiquitination."
      Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T., Moscat J.
      J. Biol. Chem. 280:35625-35629(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death."
      Bjorkoy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., Stenmark H., Johansen T.
      J. Cell Biol. 171:603-614(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION, INTERACTION WITH MAP1LC3B, DOMAIN, POSSIBLE PROTECTIVE ROLE IN HD, MUTAGENESIS OF ASP-69 AND ILE-431.
    27. "Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation."
      Babu J.R., Geetha T., Wooten M.W.
      J. Neurochem. 94:192-203(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPT, DOMAIN, SUBCELLULAR LOCATION, FUNCTION.
    28. "The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex."
      Feng Y., Longmore G.D.
      Mol. Cell. Biol. 25:4010-4022(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AJUBA AND LIMD1.
    29. "Inhibition of sequestosome 1/p62 up-regulation prevents aggregation of ubiquitinated proteins induced by prostaglandin J2 without reducing its neurotoxicity."
      Wang Z., Figueiredo-Pereira M.E.
      Mol. Cell. Neurosci. 29:222-231(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION.
    30. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. Cited for: INTERACTION WITH NBR1 AND TRIM55, PHOSPHORYLATION, DOMAINS, FUNCTION.
    32. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
      Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
      J. Biol. Chem. 282:24131-24145(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GABARAP; GABARAPL1; GABARAPL2; MAP1LC3A AND MAP1LC3B, MUTAGENESIS OF 323-GLU-GLU-324; SER-332; 335-ASP--ASP-337; TRP-338 AND SER-342.
    35. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; THR-269; SER-272; SER-328; SER-332 AND SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    37. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    40. "p62/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies/ALIS and their degradation by autophagy."
      Clausen T.H., Lamark T., Isakson P., Finley K., Larsen K.B., Brech A., Overvatn A., Stenmark H., Bjorkoy G., Simonsen A., Johansen T.
      Autophagy 6:330-344(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH WDFY3, SUBCELLULAR LOCATION.
    41. "Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance."
      Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., Ehler E.
      J. Cell Biol. 191:1159-1172(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FHOD3.
    42. "p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha."
      O'Connor C., Pertel T., Gray S., Robia S.L., Bakowska J.C., Luban J., Campbell E.M.
      J. Virol. 84:5997-6006(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM5, SUBCELLULAR LOCATION.
    43. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-207; SER-249; SER-266; SER-272 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    44. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. "Independent interactions of ubiquitin-binding domains in a ubiquitin-mediated ternary complex."
      Garner T.P., Strachan J., Shedden E.C., Long J.E., Cavey J.R., Shaw B., Layfield R., Searle M.S.
      Biochemistry 50:9076-9087(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ZFAND5 AND UBIQUITIN, SUBCELLULAR LOCATION.
    46. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    47. "TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells."
      Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R.
      Biochim. Biophys. Acta 1823:316-326(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM13, SUBCELLULAR LOCATION.
    48. "TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death."
      Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.
      Cell Death Differ. 19:1525-1535(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1LC3A.
    49. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    50. "TRAF6 mediates ubiquitination of KIF23/MKLP1 and is required for midbody ring degradation by selective autophagy."
      Isakson P., Lystad A.H., Breen K., Koster G., Stenmark H., Simonsen A.
      Autophagy 9:1955-1964(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    51. "The LIR motif - crucial for selective autophagy."
      Birgisdottir A.B., Lamark T., Johansen T.
      J. Cell Sci. 126:3237-3247(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIR MOTIF.
    52. "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
      Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
      Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1LC3B.
    53. "Structural determinants in GABARAP required for the selective binding and recruitment of ALFY to LC3B-positive structures."
      Lystad A.H., Ichimura Y., Takagi K., Yang Y., Pankiv S., Kanegae Y., Kageyama S., Suzuki M., Saito I., Mizushima T., Komatsu M., Simonsen A.
      EMBO Rep. 15:557-565(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GABARAP, MUTAGENESIS OF TRP-338.
    54. "Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone."
      Ciani B., Layfield R., Cavey J.R., Sheppard P.W., Searle M.S.
      J. Biol. Chem. 278:37409-37412(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 387-436, CHARACTERIZATION OF VARIANT LEU-392, DOMAIN.
    55. "Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch."
      Long J., Gallagher T.R., Cavey J.R., Sheppard P.W., Ralston S.H., Layfield R., Searle M.S.
      J. Biol. Chem. 283:5427-5440(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 387-436, INTERACTION WITH UBIQUITIN.
    56. "Conformation and dynamics of the three-helix bundle UBA domain of p62 from experiment and simulation."
      Evans C.L., Long J.E., Gallagher T.R., Hirst J.D., Searle M.S.
      Proteins 71:227-240(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 387-436.
    57. "Dimerisation of the UBA domain of p62 inhibits ubiquitin binding and regulates NF-kappaB signalling."
      Long J., Garner T.P., Pandya M.J., Craven C.J., Chen P., Shaw B., Williamson M.P., Layfield R., Searle M.S.
      J. Mol. Biol. 396:178-194(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 387-436, SUBUNIT, FUNCTION, MUTAGENESIS OF GLU-409 AND GLY-410, CHARACTERIZATION OF VARIANT PDB ARG-425.
    58. "Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone."
      Laurin N., Brown J.P., Morissette J., Raymond V.
      Am. J. Hum. Genet. 70:1582-1588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PDB LEU-392, VARIANTS VAL-117 AND GLN-274.
    59. "Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease."
      Hocking L.J., Lucas G.J.A., Daroszewska A., Mangion J., Olavesen M., Cundy T., Nicholson G.C., Ward L., Bennett S.T., Wuyts W., Van Hul W., Ralston S.H.
      Hum. Mol. Genet. 11:2735-2739(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PDB LEU-392.
    60. "Three novel mutations in SQSTM1 identified in familial Paget's disease of bone."
      Johnson-Pais T.L., Wisdom J.H., Weldon K.S., Cody J.D., Hansen M.F., Singer F.R., Leach R.J.
      J. Bone Miner. Res. 18:1748-1753(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PDB LEU-387.
    61. "Familial Paget's disease in The Netherlands: occurrence, identification of new mutations in the sequestosome 1 gene, and their clinical associations."
      Eekhoff E.W.M., Karperien M., Houtsma D., Zwinderman A.H., Dragoiescu C., Kneppers A.L.J., Papapoulos S.E.
      Arthritis Rheum. 50:1650-1654(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PDB LEU-392; PRO-399; THR-404 AND ARG-425.
    62. "Identification of SQSTM1 mutations in familial Paget's disease in Australian pedigrees."
      Good D.A., Busfield F., Fletcher B.H., Lovelock P.K., Duffy D.L., Kesting J.B., Andersen J., Shaw J.T.E.
      Bone 35:277-282(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PDB LEU-392.
    63. "Two novel mutations at exon 8 of the Sequestosome 1 (SQSTM1) gene in an Italian series of patients affected by Paget's disease of bone (PDB)."
      Falchetti A., Di Stefano M., Marini F., Del Monte F., Mavilia C., Strigoli D., De Feo M.L., Isaia G., Masi L., Amedei A., Cioppi F., Ghinoi V., Maddali Bongi S., Di Fede G., Sferrazza C., Rini G.B., Melchiorre D., Matucci-Cerinic M., Brandi M.L.
      J. Bone Miner. Res. 19:1013-1017(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PDB LEU-392; VAL-404 AND ARG-425.
    64. "Novel UBA domain mutations of SQSTM1 in Paget's disease of bone: genotype phenotype correlation, functional analysis, and structural consequences."
      Hocking L.J., Lucas G.J.A., Daroszewska A., Cundy T., Nicholson G.C., Donath J., Walsh J.P., Finlayson C., Cavey J.R., Ciani B., Sheppard P.W., Searle M.S., Layfield R., Ralston S.H.
      J. Bone Miner. Res. 19:1122-1127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PDB VAL-404; SER-411 AND ARG-425, CHARACTERIZATION OF VARIANTS VAL-404; SER-411 AND ARG-425.
    65. "Detection and validation of non-synonymous coding SNPs from orthogonal analysis of shotgun proteomics data."
      Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A., Hendrickson R.C., Stephenson J.L. Jr.
      J. Proteome Res. 6:2331-2340(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLU-238, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSQSTM_HUMAN
    AccessioniPrimary (citable) accession number: Q13501
    Secondary accession number(s): A6NFN7
    , B2R661, B3KUW5, Q13446, Q9BUV7, Q9BVS6, Q9UEU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3