Q64337 (SQSTM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sequestosome-1

Alternative name(s):
STONE14
Ubiquitin-binding protein p62

Gene names

Name:	Sqstm1
Synonyms:	A170, STAP

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	442 AA.
Sequence status	Complete.
Protein existence	Evidence 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 vesicle › autophagosome By similarity. Cytoplasm › P-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 process	Apoptosis Autophagy Differentiation Immunity
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Endosome Lysosome Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation 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: Compara protein heterooligomerization Inferred from electronic annotation. Source: Compara regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	aggresome 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_function	K63-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 zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KEAP1	Q14145	2	EBI-645025,EBI-751001	From a different organism.
Keap1	Q9Z2X8	6	EBI-645025,EBI-647110
MAP1LC3B	Q9GZQ8	6	EBI-645025,EBI-373144	From a different organism.
Map2k5	Q9WVS7	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 442

442

Sequestosome-1

PRO_0000072177

Regions

Domain

20 – 102

83

OPR

Domain

391 – 436

46

UBA

Zinc finger

122 – 167

46

ZZ-type

Region

1 – 50

50

Interaction with LCK By similarity

Region

43 – 107

65

Interaction with PRKCZ and dimerization By similarity

Region

50 – 80

31

Interaction with PAWR By similarity

Region

122 – 224

103

Interaction with GABRR3 By similarity

Region

170 – 220

51

LIM protein-binding By similarity

Region

269 – 442

174

Interaction with NTRK1 By similarity

Region

323 – 344

22

MAP1LC3B-binding By similarity

Motif

228 – 233

6

TRAF6-binding By similarity

Compositional bias

272 – 296

25

Ser-rich

Amino acid modifications

Modified residue

24

1

Phosphoserine Ref.15

Modified residue

148

1

Phosphotyrosine By similarity

Modified residue

178

1

Phosphoserine Ref.18

Modified residue

207

1

Phosphoserine By similarity

Modified residue

249

1

Phosphoserine By similarity

Modified residue

266

1

Phosphoserine By similarity

Modified residue

269

1

Phosphothreonine Ref.18

Modified residue

272

1

Phosphothreonine Ref.18

Modified residue

330

1

Phosphoserine By similarity

Modified residue

334

1

Phosphoserine Ref.17

Modified residue

357

1

Phosphoserine By similarity

Modified residue

363

1

Phosphoserine By similarity

Modified residue

367

1

Phosphoserine Ref.12

Modified residue

368

1

Phosphoserine By similarity

Natural variations

Alternative sequence

353 – 390

38

Missing in isoform 2.

VSP_015842

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

442

Helix Strand Turn

Details...

Turn

350 – 352

3

Helix

394 – 405

12

Helix

411 – 413

3

Helix

414 – 421

8

Turn

422 – 424

3

Helix

426 – 432

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: ED4CCCA7741D35CA	FASTA	442	48,163
	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
	Isoform 2 [UniParc]. Checksum: CF977864ABEA77BA	FASTA	404	44,192
	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 STEADPRLIE 370 380 390 400 SLSQMLSMGF SDEGGWLTRL LQTKNYDIGA ALDTIQYSKH PPPL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, MASS SPECTROMETRY. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Macrophage.
[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, MASS SPECTROMETRY. 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.

IPI

IPI00133374.
IPI00474373.

PIR

JC4978.

RefSeq

NP_035148.1. NM_011018.2.

UniGene

Mm.40828.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q64337.

SMR

Q64337. Positions 3-102, 389-438.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q64337. 10 interactions.

STRING

10090.ENSMUSP00000099835.

PTM databases

PhosphoSite

Q64337.

Proteomic databases

PaxDb

Q64337.

PRIDE

Q64337.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000015981; ENSMUSP00000015981; ENSMUSG00000015837.
ENSMUST00000102774; ENSMUSP00000099835; ENSMUSG00000015837.

GeneID

18412.

KEGG

mmu:18412.

UCSC

uc007irw.1. mouse.
uc007irx.1. mouse.

Organism-specific databases

CTD

8878.

MGI

MGI:107931. Sqstm1.

Phylogenomic databases

eggNOG

NOG278569.

GeneTree

ENSGT00390000002781.

HOGENOM

HOG000154407.

HOVERGEN

HBG052750.

InParanoid

Q64337.

KO

K14381.

OMA

KECRREH.

Gene expression databases

ArrayExpress

Q64337.

Bgee

Q64337.

CleanEx

MM_SQSTM1.

Genevestigator

Q64337.

GermOnline

ENSMUSG00000015837. Mus musculus.

Family and domain databases

InterPro

IPR000270. OPR_PB1.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000433. Znf_ZZ.
[Graphical view]

Pfam

PF00564. PB1. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]

SMART

SM00666. PB1. 1 hit.
SM00165. UBA. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS50030. UBA. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SQSTM1. mouse.

EvolutionaryTrace

Q64337.

NextBio

294036.

SOURCE

Search...

Entry information

Entry name

SQSTM_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program