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Q64337

- SQSTM_MOUSE

UniProt

Q64337 - SQSTM_MOUSE

Protein

Sequestosome-1

Gene

Sqstm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. May be involved in cell differentiation, apoptosis, immune response and regulation of K+ channels. Adapter that mediates the interaction between TRAF6 and CYLD.2 Publications

    Regions

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

    GO - Molecular functioni

    1. identical protein binding Source: MGI
    2. K63-linked polyubiquitin binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein kinase C binding Source: UniProtKB
    5. SH2 domain binding Source: UniProtKB
    6. transcription cofactor activity Source: MGI
    7. ubiquitin binding Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. autophagy Source: UniProtKB
    3. cell differentiation Source: UniProtKB-KW
    4. immune system process Source: UniProtKB-KW
    5. macroautophagy Source: UniProtKB
    6. positive regulation of protein phosphorylation Source: Ensembl
    7. protein heterooligomerization Source: Ensembl
    8. regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    9. regulation of RNA biosynthetic process Source: GOC

    Keywords - Biological processi

    Apoptosis, Autophagy, Differentiation, Immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_202271. NRIF signals cell death from the nucleus.
    REACT_214670. p75NTR recruits signalling complexes.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_224208. Interleukin-1 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sequestosome-1
    Alternative name(s):
    STONE14
    Ubiquitin-binding protein p62
    Gene namesi
    Name:Sqstm1
    Synonyms:A170, STAP
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:107931. Sqstm1.

    Subcellular locationi

    Cytoplasm 1 Publication. Late endosome 1 Publication. Nucleus 1 Publication. Endoplasmic reticulum 1 Publication. Lysosome By similarity. Cytoplasmic vesicleautophagosome By similarity. CytoplasmP-body By similarity
    Note: Sarcomere. In cardiac muscles localizes to the sarcomeric band. May also localize to the hepatocellular carcinoma. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum By similarity. Commonly found in inclusion bodies containing polyubiquitinated protein aggregates By similarity. Co-localizes with TRIM5 in the cytoplasmic bodies By similarity.By similarity

    GO - Cellular componenti

    1. aggresome Source: MGI
    2. autophagic vacuole Source: UniProtKB
    3. cytoplasmic mRNA processing body Source: UniProtKB
    4. cytoplasmic vesicle Source: UniProtKB-KW
    5. endoplasmic reticulum Source: UniProtKB-SubCell
    6. late endosome Source: UniProtKB-SubCell
    7. lysosome Source: UniProtKB-SubCell
    8. nucleus Source: UniProtKB-SubCell
    9. pre-autophagosomal structure Source: MGI

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    Impaired induced osteoclastogenesis.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi337 – 3393DDD → AAA: Greatly decreases interaction with MAP1LC3B.
    Mutagenesisi340 – 3401W → A: Greatly decreases interaction with MAP1LC3B. 1 Publication
    Mutagenesisi343 – 3431L → A: Greatly decreases interaction with MAP1LC3B. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 442441Sequestosome-1PRO_0000072177Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei148 – 1481PhosphotyrosineBy similarity
    Modified residuei178 – 1781Phosphoserine2 Publications
    Modified residuei207 – 2071PhosphoserineBy similarity
    Modified residuei249 – 2491PhosphoserineBy similarity
    Modified residuei266 – 2661PhosphoserineBy similarity
    Modified residuei269 – 2691Phosphothreonine2 Publications
    Modified residuei272 – 2721Phosphothreonine2 Publications
    Modified residuei330 – 3301PhosphoserineBy similarity
    Modified residuei334 – 3341Phosphoserine2 Publications
    Modified residuei357 – 3571PhosphoserineBy similarity
    Modified residuei363 – 3631PhosphoserineBy similarity
    Modified residuei368 – 3681PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ64337.
    PaxDbiQ64337.
    PRIDEiQ64337.

    PTM databases

    PhosphoSiteiQ64337.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Inductioni

    By diethylmaleate, paraquat, menadione, sodium arsenite and cadmium chloride, arsenite and arsenate. By MG132, MG115, lactacystin and proteasome inhibitor I (PSI). By serum starvation, okadaic acid and glucose oxidase. Also up-regulated by RANK-L (at protein level). By etoposide and trichostatin. By the parkinsonian mimetic 6-hydroxydopamine (6-OHDA). By TGF-beta.7 Publications

    Gene expression databases

    ArrayExpressiQ64337.
    BgeeiQ64337.
    CleanExiMM_SQSTM1.
    GenevestigatoriQ64337.

    Interactioni

    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, 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 AJUBA, PRKCZ and TRAF6. 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. Identified in a heterotrimeric complex with ubiquitin and ZFAND5, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule By similarity. Interacts with TRAF6 and CYLD. Identified in a complex with TRAF6 and CYLD. 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.By similarityCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KEAP1Q141452EBI-645025,EBI-751001From a different organism.
    Keap1Q9Z2X86EBI-645025,EBI-647110
    MAP1LC3BQ9GZQ86EBI-645025,EBI-373144From a different organism.
    Map2k5Q9WVS73EBI-645025,EBI-446144

    Protein-protein interaction databases

    BioGridi201982. 40 interactions.
    DIPiDIP-38490N.
    IntActiQ64337. 16 interactions.
    MINTiMINT-1728610.
    STRINGi10090.ENSMUSP00000099835.

    Structurei

    Secondary structure

    1
    442
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni350 – 3523
    Helixi394 – 40512
    Helixi411 – 4133
    Helixi414 – 4218
    Turni422 – 4243
    Helixi426 – 4327

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RRUNMR-A391-438[»]
    2ZJDX-ray1.56B/D334-344[»]
    3ADEX-ray2.80B346-359[»]
    3B0FX-ray1.40A/B391-438[»]
    3WDZX-ray2.60B346-359[»]
    ProteinModelPortaliQ64337.
    SMRiQ64337. Positions 3-102, 389-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ64337.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10283OPRAdd
    BLAST
    Domaini391 – 43646UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 5049Interaction with LCKBy similarityAdd
    BLAST
    Regioni43 – 10765Interaction with PRKCZ and dimerizationBy similarityAdd
    BLAST
    Regioni50 – 8031Interaction with PAWRBy similarityAdd
    BLAST
    Regioni122 – 224103Interaction with GABRR3By similarityAdd
    BLAST
    Regioni170 – 22051LIM protein-bindingBy similarityAdd
    BLAST
    Regioni269 – 442174Interaction with NTRK1By similarityAdd
    BLAST
    Regioni323 – 34422MAP1LC3B-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi228 – 2336TRAF6-bindingBy similarity
    Motifi338 – 3436LIR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi272 – 29625Ser-richAdd
    BLAST

    Domaini

    The UBA domain binds specifically 'Lys-63'-linked polyubiquitin chains of polyubiquitinated substrates. Mediates the interaction with TRIM55 By similarity. Both the UBA and OPR domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies By similarity.By similarity
    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.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

    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.
    GeneTreeiENSGT00390000002781.
    HOGENOMiHOG000154407.
    HOVERGENiHBG052750.
    InParanoidiQ64337.
    KOiK14381.
    OMAiDAIQYSK.
    OrthoDBiEOG74R1RT.
    PhylomeDBiQ64337.
    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: Q64337-1) [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

    MASFTVKAYL LGKEEATREI RRFSFCFSPE PEAEAQAAAG PGPCERLLSR    50
    VAVLFPTLRP GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK 100
    EKKECRREHR PPCAQEAPRN MVHPNVICDG CNGPVVGTRY KCSVCPDYDL 150
    CSVCEGKGLH REHSKLIFPN PFGHLSDSFS HSRWLRKLKH GHFGWPGWEM 200
    GPPGNWSPRP PRAGDGRPCP TAESASAPPE DPNVNFLKNV GESVAAALSP 250
    LGIEVDIDVE HGGKRSRLTP TTPESSSTGT EDKSNTQPSS CSSEVSKPDG 300
    AGEGPAQSLT EQMKKIALES VGQPEEQMES GNCSGGDDDW THLSSKEVDP 350
    STGELQSLQM PESEGPSSLD PSQEGPTGLK EAALYPHLPP EADPRLIESL 400
    SQMLSMGFSD EGGWLTRLLQ TKNYDIGAAL DTIQYSKHPP PL 442
    Length:442
    Mass (Da):48,163
    Last modified:November 1, 1996 - v1
    Checksum:iED4CCCA7741D35CA
    GO
    Isoform 2 (identifier: Q64337-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         353-390: Missing.

    Show »
    Length:404
    Mass (Da):44,192
    Checksum:iCF977864ABEA77BA
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei353 – 39038Missing in isoform 2. 2 PublicationsVSP_015842Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40930 mRNA. Translation: AAB17127.1.
    U57413 mRNA. Translation: AAB02908.1.
    AK028898 mRNA. Translation: BAC26183.1.
    AL627187 Genomic DNA. Translation: CAI25117.1.
    AL627187 Genomic DNA. Translation: CAI25118.1.
    BC006019 mRNA. Translation: AAH06019.1.
    CCDSiCCDS24629.1. [Q64337-1]
    CCDS70176.1. [Q64337-2]
    PIRiJC4978.
    RefSeqiNP_001277698.1. NM_001290769.1. [Q64337-2]
    NP_035148.1. NM_011018.3. [Q64337-1]
    UniGeneiMm.40828.

    Genome annotation databases

    EnsembliENSMUST00000015981; ENSMUSP00000015981; ENSMUSG00000015837. [Q64337-2]
    ENSMUST00000102774; ENSMUSP00000099835; ENSMUSG00000015837. [Q64337-1]
    GeneIDi18412.
    KEGGimmu:18412.
    UCSCiuc007irw.1. mouse. [Q64337-1]
    uc007irx.1. mouse. [Q64337-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40930 mRNA. Translation: AAB17127.1 .
    U57413 mRNA. Translation: AAB02908.1 .
    AK028898 mRNA. Translation: BAC26183.1 .
    AL627187 Genomic DNA. Translation: CAI25117.1 .
    AL627187 Genomic DNA. Translation: CAI25118.1 .
    BC006019 mRNA. Translation: AAH06019.1 .
    CCDSi CCDS24629.1. [Q64337-1 ]
    CCDS70176.1. [Q64337-2 ]
    PIRi JC4978.
    RefSeqi NP_001277698.1. NM_001290769.1. [Q64337-2 ]
    NP_035148.1. NM_011018.3. [Q64337-1 ]
    UniGenei Mm.40828.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RRU NMR - A 391-438 [» ]
    2ZJD X-ray 1.56 B/D 334-344 [» ]
    3ADE X-ray 2.80 B 346-359 [» ]
    3B0F X-ray 1.40 A/B 391-438 [» ]
    3WDZ X-ray 2.60 B 346-359 [» ]
    ProteinModelPortali Q64337.
    SMRi Q64337. Positions 3-102, 389-438.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201982. 40 interactions.
    DIPi DIP-38490N.
    IntActi Q64337. 16 interactions.
    MINTi MINT-1728610.
    STRINGi 10090.ENSMUSP00000099835.

    PTM databases

    PhosphoSitei Q64337.

    Proteomic databases

    MaxQBi Q64337.
    PaxDbi Q64337.
    PRIDEi Q64337.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015981 ; ENSMUSP00000015981 ; ENSMUSG00000015837 . [Q64337-2 ]
    ENSMUST00000102774 ; ENSMUSP00000099835 ; ENSMUSG00000015837 . [Q64337-1 ]
    GeneIDi 18412.
    KEGGi mmu:18412.
    UCSCi uc007irw.1. mouse. [Q64337-1 ]
    uc007irx.1. mouse. [Q64337-2 ]

    Organism-specific databases

    CTDi 8878.
    MGIi MGI:107931. Sqstm1.

    Phylogenomic databases

    eggNOGi NOG278569.
    GeneTreei ENSGT00390000002781.
    HOGENOMi HOG000154407.
    HOVERGENi HBG052750.
    InParanoidi Q64337.
    KOi K14381.
    OMAi DAIQYSK.
    OrthoDBi EOG74R1RT.
    PhylomeDBi Q64337.
    TreeFami TF328470.

    Enzyme and pathway databases

    Reactomei REACT_202271. NRIF signals cell death from the nucleus.
    REACT_214670. p75NTR recruits signalling complexes.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_224208. Interleukin-1 signaling.

    Miscellaneous databases

    ChiTaRSi SQSTM1. mouse.
    EvolutionaryTracei Q64337.
    NextBioi 294036.
    PROi Q64337.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64337.
    Bgeei Q64337.
    CleanExi MM_SQSTM1.
    Genevestigatori Q64337.

    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. "Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p56lck-associated protein in reponse to oxidative stress."
      Ishii T., Yanagawa T., Kawane T., Yuki K., Seita J., Yoshida H., Bannai S.
      Biochem. Biophys. Res. Commun. 226:456-460(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
      Strain: ddY.
      Tissue: Macrophage.
    2. "Murine cDNA similar to EBI3-associated protein p60 mRNA."
      Morris J.C., Long A., Finnerty H., Fitz L., Towler P., Turner K., Wood C.R.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Skin.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Mammary gland.
    6. "Low micromolar levels of hydrogen peroxide and proteasome inhibitors induce the 60-kDa A170 stress protein in murine peritoneal macrophages."
      Ishii T., Yanagawa T., Yuki K., Kawane T., Yoshida H., Bannai S.
      Biochem. Biophys. Res. Commun. 232:33-37(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "Phosphorylation of A170 stress protein by casein kinase II-like activity in macrophages."
      Yanagawa T., Yuki K., Yoshida H., Bannai S., Ishii T.
      Biochem. Biophys. Res. Commun. 241:157-163(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    8. "Cloning, expression profile, and genomic organization of the mouse STAP/A170 gene."
      Okazaki M., Ito S., Kawakita K., Takeshita S., Kawai S., Makishima F., Oda H., Kakinuma A.
      Genomics 60:87-95(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    9. "Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells."
      Kuusisto E., Suuronen T., Salminen A.
      Biochem. Biophys. Res. Commun. 280:223-228(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Activation of Nrf2 and accumulation of ubiquitinated A170 by arsenic in osteoblasts."
      Aono J., Yanagawa T., Itoh K., Li B., Yoshida H., Kumagai Y., Yamamoto M., Ishii T.
      Biochem. Biophys. Res. Commun. 305:271-277(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis."
      Duran A., Serrano M., Leitges M., Flores J.M., Picard S., Brown J.P., Moscat J., Diaz-Meco M.T.
      Dev. Cell 6:303-309(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, INTERACTION WITH TRAF6, DISRUPTION PHENOTYPE.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    13. "Microarray expression profiling identifies early signaling transcripts associated with 6-OHDA-induced dopaminergic cell death."
      Holtz W.A., Turetzky J.M., O'Malley K.L.
      Antioxid. Redox Signal. 7:639-648(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    14. "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: SUBCELLULAR LOCATION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Deubiquitinating enzyme CYLD negatively regulates RANK signaling and osteoclastogenesis in mice."
      Jin W., Chang M., Paul E.M., Babu G., Lee A.J., Reiley W., Wright A., Zhang M., You J., Sun S.C.
      J. Clin. Invest. 118:1858-1866(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CYLD AND TRAF6, IDENTIFICATION IN A COMPLEX WITH CYLD AND TRAF6.
    17. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; THR-269 AND THR-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 335-344 IN COMPLEX WITH MAP1LC3B, MUTAGENESIS OF 337-ASP--ASP-339; TRP-340 AND LEU-343, INTERACTION WITH GABARAP AND GABARAPL2.

    Entry informationi

    Entry nameiSQSTM_MOUSE
    AccessioniPrimary (citable) accession number: Q64337
    Secondary accession number(s): Q99JM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3