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Q64337

- SQSTM_MOUSE

UniProt

Q64337 - SQSTM_MOUSE

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Protein

Sequestosome-1

Gene

Sqstm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 kinase C binding Source: UniProtKB
  4. SH2 domain binding Source: UniProtKB
  5. transcription cofactor activity Source: MGI
  6. ubiquitin binding Source: UniProtKB
  7. 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
Complete GO annotation...

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-KW
  6. endosome Source: UniProtKB-KW
  7. extracellular vesicular exosome Source: Ensembl
  8. lysosome Source: UniProtKB-KW
  9. nucleus Source: UniProtKB-KW
  10. pre-autophagosomal structure Source: MGI
Complete GO annotation...

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. 1 Publication
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 – 1781Phosphoserine1 Publication
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei249 – 2491PhosphoserineBy similarity
Modified residuei266 – 2661PhosphoserineBy similarity
Modified residuei269 – 2691Phosphothreonine1 Publication
Modified residuei272 – 2721Phosphothreonine1 Publication
Modified residuei330 – 3301PhosphoserineBy similarity
Modified residuei334 – 3341Phosphoserine1 Publication
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

BgeeiQ64337.
CleanExiMM_SQSTM1.
ExpressionAtlasiQ64337. baseline and differential.
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. 43 interactions.
DIPiDIP-38490N.
IntActiQ64337. 19 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

        10         20         30         40         50
MASFTVKAYL LGKEEATREI RRFSFCFSPE PEAEAQAAAG PGPCERLLSR
60 70 80 90 100
VAVLFPTLRP GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK
110 120 130 140 150
EKKECRREHR PPCAQEAPRN MVHPNVICDG CNGPVVGTRY KCSVCPDYDL
160 170 180 190 200
CSVCEGKGLH REHSKLIFPN PFGHLSDSFS HSRWLRKLKH GHFGWPGWEM
210 220 230 240 250
GPPGNWSPRP PRAGDGRPCP TAESASAPPE DPNVNFLKNV GESVAAALSP
260 270 280 290 300
LGIEVDIDVE HGGKRSRLTP TTPESSSTGT EDKSNTQPSS CSSEVSKPDG
310 320 330 340 350
AGEGPAQSLT EQMKKIALES VGQPEEQMES GNCSGGDDDW THLSSKEVDP
360 370 380 390 400
STGELQSLQM PESEGPSSLD PSQEGPTGLK EAALYPHLPP EADPRLIESL
410 420 430 440
SQMLSMGFSD EGGWLTRLLQ TKNYDIGAAL DTIQYSKHPP PL
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. 43 interactions.
DIPi DIP-38490N.
IntActi Q64337. 19 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

Bgeei Q64337.
CleanExi MM_SQSTM1.
ExpressionAtlasi Q64337. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 127 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