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Q64337 (SQSTM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sequestosome-1
Alternative name(s):
STONE14
Ubiquitin-binding protein p62
Gene names
Name:Sqstm1
Synonyms:A170, STAP
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures). Links ALIS to the autophagic machinery via direct interaction with MAP1 LC3 family members. 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. Ref.11 Ref.16

Subunit structure

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. Ref.11 Ref.16

Subcellular location

Cytoplasm. Late endosome. Nucleus. Endoplasmic reticulum. 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. Ref.14

Tissue specificity

Widely expressed. Ref.8

Induction

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. Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Domain

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.

The OPR domain mediates homooligomerization and interactions with FHOD3, MAP2K5, NBR1, PRKCI and PRKCZ By similarity. 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.

Post-translational modification

Phosphorylated. May be phosphorylated by PRKCZ. Phosphorylated in vitro by TTN By similarity. Ref.7

Disruption phenotype

Impaired induced osteoclastogenesis. Ref.11

Sequence similarities

Contains 1 OPR domain.

Contains 1 UBA domain.

Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
   Biological processApoptosis
Autophagy
Differentiation
Immunity
   Cellular componentCytoplasm
Cytoplasmic vesicle
Endoplasmic reticulum
Endosome
Lysosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

macroautophagy

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of RNA biosynthetic process

Traceable author statement Ref.8. Source: GOC

   Cellular_componentaggresome

Inferred from direct assay PubMed 22792322. Source: MGI

autophagic vacuole

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

late endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

pre-autophagosomal structure

Inferred from direct assay PubMed 21220506. Source: MGI

   Molecular_functionK63-linked polyubiquitin binding

Inferred from direct assay PubMed 16252010. Source: UniProtKB

SH2 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

identical protein binding

Inferred from direct assay PubMed 21220506. Source: MGI

protein kinase C binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription cofactor activity

Traceable author statement Ref.8. Source: MGI

ubiquitin binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q64337-1)

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.
Isoform 2 (identifier: Q64337-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 442441Sequestosome-1
PRO_0000072177

Regions

Domain20 – 10283OPR
Domain391 – 43646UBA
Zinc finger122 – 16746ZZ-type
Region2 – 5049Interaction with LCK By similarity
Region43 – 10765Interaction with PRKCZ and dimerization By similarity
Region50 – 8031Interaction with PAWR By similarity
Region122 – 224103Interaction with GABRR3 By similarity
Region170 – 22051LIM protein-binding By similarity
Region269 – 442174Interaction with NTRK1 By similarity
Region323 – 34422MAP1LC3B-binding By similarity
Motif228 – 2336TRAF6-binding By similarity
Compositional bias272 – 29625Ser-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1481Phosphotyrosine By similarity
Modified residue1781Phosphoserine Ref.18
Modified residue2071Phosphoserine By similarity
Modified residue2491Phosphoserine By similarity
Modified residue2661Phosphoserine By similarity
Modified residue2691Phosphothreonine Ref.18
Modified residue2721Phosphothreonine Ref.18
Modified residue3301Phosphoserine By similarity
Modified residue3341Phosphoserine Ref.17
Modified residue3571Phosphoserine By similarity
Modified residue3631Phosphoserine By similarity
Modified residue3681Phosphoserine By similarity

Natural variations

Alternative sequence353 – 39038Missing in isoform 2.
VSP_015842

Secondary structure

........... 442
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: ED4CCCA7741D35CA

FASTA44248,163
        10         20         30         40         50         60 
MASFTVKAYL LGKEEATREI RRFSFCFSPE PEAEAQAAAG PGPCERLLSR VAVLFPTLRP 

        70         80         90        100        110        120 
GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK EKKECRREHR PPCAQEAPRN 

       130        140        150        160        170        180 
MVHPNVICDG CNGPVVGTRY KCSVCPDYDL CSVCEGKGLH REHSKLIFPN PFGHLSDSFS 

       190        200        210        220        230        240 
HSRWLRKLKH GHFGWPGWEM GPPGNWSPRP PRAGDGRPCP TAESASAPPE DPNVNFLKNV 

       250        260        270        280        290        300 
GESVAAALSP LGIEVDIDVE HGGKRSRLTP TTPESSSTGT EDKSNTQPSS CSSEVSKPDG 

       310        320        330        340        350        360 
AGEGPAQSLT EQMKKIALES VGQPEEQMES GNCSGGDDDW THLSSKEVDP STGELQSLQM 

       370        380        390        400        410        420 
PESEGPSSLD PSQEGPTGLK EAALYPHLPP EADPRLIESL SQMLSMGFSD EGGWLTRLLQ 

       430        440 
TKNYDIGAAL DTIQYSKHPP PL 

« Hide

Isoform 2 [UniParc].

Checksum: CF977864ABEA77BA
Show »

FASTA40444,192

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC4978.
RefSeqNP_035148.1. NM_011018.2.
XP_006532513.1. XM_006532450.1.
UniGeneMm.40828.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRUNMR-A391-438[»]
2ZJDX-ray1.56B/D334-344[»]
3ADEX-ray2.80B346-359[»]
3B0FX-ray1.40A/B391-438[»]
3WDZX-ray2.60B346-359[»]
ProteinModelPortalQ64337.
SMRQ64337. Positions 3-102, 126-171, 389-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201982. 38 interactions.
IntActQ64337. 16 interactions.
MINTMINT-1728610.
STRING10090.ENSMUSP00000099835.

PTM databases

PhosphoSiteQ64337.

Proteomic databases

PaxDbQ64337.
PRIDEQ64337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015981; ENSMUSP00000015981; ENSMUSG00000015837. [Q64337-2]
ENSMUST00000102774; ENSMUSP00000099835; ENSMUSG00000015837. [Q64337-1]
GeneID18412.
KEGGmmu:18412.
UCSCuc007irw.1. mouse. [Q64337-1]
uc007irx.1. mouse. [Q64337-2]

Organism-specific databases

CTD8878.
MGIMGI:107931. Sqstm1.

Phylogenomic databases

eggNOGNOG278569.
GeneTreeENSGT00390000002781.
HOGENOMHOG000154407.
HOVERGENHBG052750.
InParanoidQ64337.
KOK14381.
OMASVCPNYD.
OrthoDBEOG74R1RT.
PhylomeDBQ64337.
TreeFamTF328470.

Gene expression databases

ArrayExpressQ64337.
BgeeQ64337.
CleanExMM_SQSTM1.
GenevestigatorQ64337.

Family and domain databases

InterProIPR000270. OPR_PB1.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000433. Znf_ZZ.
[Graphical view]
PfamPF00564. PB1. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
SMARTSM00666. PB1. 1 hit.
SM00165. UBA. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSQSTM1. mouse.
EvolutionaryTraceQ64337.
NextBio294036.
PROQ64337.
SOURCESearch...

Entry information

Entry nameSQSTM_MOUSE
AccessionPrimary (citable) accession number: Q64337
Secondary accession number(s): Q99JM8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot