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Q13501 (SQSTM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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):
EBI3-associated protein of 60 kDa
Short name=EBIAP
Short name=p60
Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa
Ubiquitin-binding protein p62
Gene names
Name:SQSTM1
Synonyms:ORCA, OSIL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length440 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. Adapter that mediates the interaction between TRAF6 and CYLD By similarity. May be involved in cell differentiation, apoptosis, immune response and regulation of K+ channels. Ref.12 Ref.14 Ref.15 Ref.19 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31 Ref.53

Subunit structure

Homooligomer or heterooligomer; may form homotypic arrays. Dimerization interferes with ubiquitin binding. Interacts directly with PRKCI and PRKCZ Probable. Forms ternary complexes with PRKCZ and KCNAB2 or PRKCZ and GABBR3. Also interacts with KCNAB1, GABRR1, GABRR2 and GABRR3. Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 By similarity. Interacts with EBI3, LCK, RASA1, PRKCZ, PRKCI, NR2F2, NTRK1, NTRK2, NTRK3, NBR1, MAP2K5, TRIM13, TRIM55 and MAPKAPK5. Interacts with the proteasome subunits PSMD4 and PSMC2. Interacts with K63-polyubiquitinated MAPT/TAU. Interacts with IKBKB through PRKCZ and PRKCI. Interacts with NGFR through TRAF6 and bridges that complex to NTRK1. Forms a complex with MAP2K5 and PRKCZ or PRKCI. Component of a ternary complex with PAWR and PRKCZ. Upon TNF-alpha stimulation, interacts with RIPK1 problably bridging IKBKB to the TNF-R1 complex composed of TNF-R1/TNFRSF1A, TRADD and RIPK1. Forms a complex with JUB/Ajuba, PRKCZ and TRAF6. Interacts with TRAF6 and CYLD. Identified in a complex with TRAF6 and CYLD By similarity. Identified in a heterotrimeric complex with ubiquitin and ZFAND5, where ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule. Directly interacts with MAP1LC3A and MAP1LC3B, as well as with other MAP1 LC3 family members, including GABARAP, GABARAPL1 and GABARAPL2; these interactions are necessary for the recruitment MAP1 LC3 family members to inclusion bodies containing polyubiquitinated protein aggregates and for their degradation by autophagy. Interacts with FHOD3. Interacts with TRMI5. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27 Ref.28 Ref.31 Ref.34 Ref.40 Ref.41 Ref.44 Ref.46 Ref.47 Ref.49 Ref.51 Ref.53

Subcellular location

Cytoplasm. Late endosome. Lysosome. Cytoplasmic vesicleautophagosome. Nucleus. Endoplasmic reticulum. CytoplasmP-body. Note: Sarcomere By similarity. In cardiac muscles localizes to the sarcomeric band By similarity. Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co-localizes with TRIM5 in the cytoplasmic bodies. Ref.7 Ref.11 Ref.13 Ref.16 Ref.18 Ref.19 Ref.23 Ref.26 Ref.27 Ref.41 Ref.44 Ref.46

Tissue specificity

Ubiquitously expressed. Ref.2

Induction

By proteasomal inhibitor PSI and prostaglandin J2 (PGJ2) (at protein level). By phorbol 12-myristate 13-acetate (PMA). Ref.6 Ref.22 Ref.29

Domain

The UBA domain binds specifically 'Lys-63'-linked polyubiquitin chains of polyubiquitinated substrates. Mediates the interaction with TRIM55. Both the UBA and OPR domains are necessary and sufficient for the localization into the ubiquitin-containing inclusion bodies. Ref.14 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27 Ref.31 Ref.50

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. Ref.14 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27 Ref.31 Ref.50

The ZZ-type zinc finger mediates the interaction with RIPK1. Ref.14 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27 Ref.31 Ref.50

Post-translational modification

Phosphorylated. May be phosphorylated by PRKCZ By similarity. Phosphorylated in vitro by TTN. Ref.31

Involvement in disease

Paget disease of bone (PDB) [MIM:602080]: Metabolic bone disease affecting the axial skeleton and characterized by focal areas of increased and disorganized bone turn-over due to activated osteoclasts. Manifestations of the disease include bone pain, deformity, pathological fractures, deafness, neurological complications and increased risk of osteosarcoma. PDB is a chronic disease affecting 2 to 3% of the population above the age of 40 years.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60

In a cell model for Huntington disease (HD), appears to form a shell surrounding aggregates of mutant HTT that may protect cells from apoptosis, possibly by recruiting autophagosomal components to the polyubiquitinated protein aggregates. Ref.26

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
Polymorphism
   DiseaseDisease mutation
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement. Source: Reactome

autophagy

Inferred from mutant phenotype Ref.34. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

endosomal transport

Traceable author statement Ref.50. Source: UniProtKB

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Traceable author statement Ref.2. Source: UniProtKB

macroautophagy

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.50. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein localization

Traceable author statement Ref.2. Source: UniProtKB

protein phosphorylation

Non-traceable author statement Ref.8. Source: GOC

regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.50. Source: UniProtKB

regulation of Ras protein signal transduction

Non-traceable author statement Ref.8. Source: UniProtKB

response to stress

Traceable author statement Ref.50. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.9. Source: ProtInc

   Cellular_componentaggresome

Inferred from electronic annotation. Source: Ensembl

autophagic vacuole

Inferred from direct assay Ref.34. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from direct assay Ref.41. Source: UniProtKB

cytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Traceable author statement Ref.2. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

late endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

pre-autophagosomal structure

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSH2 domain binding

Inferred from direct assay Ref.2. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16169070PubMed 20562859PubMed 21900206. Source: IntAct

protein kinase C binding

Inferred from physical interaction PubMed 14676191. Source: UniProtKB

protein kinase binding

Inferred from direct assay Ref.2. Source: UniProtKB

protein serine/threonine kinase activity

Non-traceable author statement Ref.8. Source: UniProtKB

receptor tyrosine kinase binding

Traceable author statement Ref.2. Source: ProtInc

ubiquitin binding

Inferred from direct assay Ref.50. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13501-1)

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: Q13501-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.48
Chain2 – 440439Sequestosome-1
PRO_0000072176

Regions

Domain20 – 10283OPR
Domain389 – 43446UBA
Zinc finger122 – 16746ZZ-type
Region2 – 5049Interaction with LCK
Region43 – 10765Interaction with PRKCZ and dimerization By similarity
Region50 – 8031Interaction with PAWR
Region122 – 224103Interaction with GABRR3 By similarity
Region170 – 22051LIM protein-binding (LB)
Region269 – 440172Interaction with NTRK1 By similarity
Region321 – 34222MAP1LC3B-binding
Motif228 – 2336TRAF6-binding
Compositional bias272 – 29423Ser-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.48
Modified residue1481Phosphotyrosine Ref.30
Modified residue1701Phosphoserine Ref.36 Ref.42
Modified residue2071Phosphoserine Ref.42
Modified residue2491Phosphoserine Ref.42
Modified residue2661Phosphoserine Ref.42
Modified residue2691Phosphothreonine Ref.33 Ref.35 Ref.36
Modified residue2721Phosphoserine Ref.33 Ref.35 Ref.36 Ref.42 Ref.45
Modified residue3281Phosphoserine Ref.36
Modified residue3321Phosphoserine Ref.32 Ref.36 Ref.42
Modified residue3551Phosphoserine Ref.39
Modified residue3611Phosphoserine Ref.39
Modified residue3661Phosphoserine Ref.36

Natural variations

Alternative sequence1 – 8484Missing in isoform 2.
VSP_015841
Natural variant1171A → V. Ref.54
Corresponds to variant rs147810437 [ dbSNP | Ensembl ].
VAR_023590
Natural variant2381K → E Polymorphism confirmed at protein level. Ref.61
Corresponds to variant rs11548633 [ dbSNP | Ensembl ].
VAR_068915
Natural variant2741E → D.
Corresponds to variant rs55793208 [ dbSNP | Ensembl ].
VAR_061707
Natural variant2741E → Q. Ref.54
VAR_023591
Natural variant3871P → L in PDB. Ref.56
VAR_023592
Natural variant3921P → L in PDB; no effect on polyubiquitin-binding. Ref.50 Ref.54 Ref.55 Ref.57 Ref.58 Ref.59
Corresponds to variant rs104893941 [ dbSNP | Ensembl ].
VAR_023593
Natural variant3991S → P in PDB. Ref.57
VAR_023594
Natural variant4041M → T in PDB. Ref.57
VAR_023595
Natural variant4041M → V in PDB; loss of polyubiquitin-binding. Ref.59 Ref.60
VAR_023596
Natural variant4111G → S in PDB; no effect on polyubiquitin-binding. Ref.60
VAR_023597
Natural variant4251G → R in PDB; loss of polyubiquitin-binding and increased activation of NF-kappa-B. Ref.53 Ref.57 Ref.59 Ref.60
VAR_023598

Experimental info

Mutagenesis71K → A: Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69. Ref.20 Ref.21
Mutagenesis91Y → F: No effect on interaction with LCK. Ref.2
Mutagenesis131K → A: No effect on interaction with PRKCI. Ref.20
Mutagenesis21 – 222RR → AA: Loss of interaction with PRKCI. Alters dimerization.
Mutagenesis671Y → A: No effect on interaction with PRKCZ. Ref.20
Mutagenesis691D → A: No effect on interactions with PRKCZ, PRKCI and NBR1. Loss of localization in cytoplasmic inclusion bodies. Loss of dimerization; when associated with A-7. Ref.20 Ref.21 Ref.26
Mutagenesis711D → A: No effect on interaction with PRKCI. Ref.20
Mutagenesis731D → A: No effect on interactions with PRKCZ and PRKCI. Ref.20 Ref.21
Mutagenesis801D → A: No effect on interaction with PRKCI. Ref.20
Mutagenesis821E → A: No effect on interaction with PRKCI. Ref.20
Mutagenesis323 – 3242EE → AA: No effect on MAP1LC3B-binding.
Mutagenesis3321S → A: No effect on MAP1LC3B-binding. Ref.34
Mutagenesis335 – 3373DDD → ADA: 75% decrease in MAP1LC3B-binding. Ref.34
Mutagenesis3381W → A: Strong decrease in MAP1LC3B-binding. Ref.34
Mutagenesis3421S → A: No effect on MAP1LC3B-binding. Ref.34
Mutagenesis3981L → V: No effect on polyubiquitin-binding. Ref.24
Mutagenesis4061F → V: Loss of polyubiquitin-binding. Ref.24
Mutagenesis4091E → K: Decreased activation of NF-kappa-B. Ref.53
Mutagenesis4101G → K: Decreased activation of NF-kappa-B. Ref.53
Mutagenesis4131L → V: No effect on polyubiquitin-binding. Ref.24
Mutagenesis4171L → V: Loss of polyubiquitin-binding. Ref.24
Mutagenesis4311I → V: Partial loss of polyubiquitin-binding. Loss of localization to cytoplasmic inclusion bodies. Ref.24 Ref.26
Sequence conflict3211R → A in AAA93299. Ref.1

Secondary structure

............. 440
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 462D94C171F337CD

FASTA44047,687
        10         20         30         40         50         60 
MASLTVKAYL LGKEDAAREI RRFSFCCSPE PEAEAEAAAG PGPCERLLSR VAALFPALRP 

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

       130        140        150        160        170        180 
MVHPNVICDG CNGPVVGTRY KCSVCPDYDL CSVCEGKGLH RGHTKLAFPS PFGHLSEGFS 

       190        200        210        220        230        240 
HSRWLRKVKH GHFGWPGWEM GPPGNWSPRP PRAGEARPGP TAESASGPSE DPSVNFLKNV 

       250        260        270        280        290        300 
GESVAAALSP LGIEVDIDVE HGGKRSRLTP VSPESSSTEE KSSSQPSSCC SDPSKPGGNV 

       310        320        330        340        350        360 
EGATQSLAEQ MRKIALESEG RPEEQMESDN CSGGDDDWTH LSSKEVDPST GELQSLQMPE 

       370        380        390        400        410        420 
SEGPSSLDPS QEGPTGLKEA ALYPHLPPEA DPRLIESLSQ MLSMGFSDEG GWLTRLLQTK 

       430        440 
NYDIGAALDT IQYSKHPPPL 

« Hide

Isoform 2 [UniParc].

Checksum: 56E985FFBF86EC1B
Show »

FASTA35638,629

References

« Hide 'large scale' references
[1]"A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes."
Devergne O., Hummel M., Koeppen H., Le Beau M.M., Nathanson E.C., Kieff E., Birkenbach M.
J. Virol. 70:1143-1153(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 345-361 AND 394-411, INTERACTION WITH EBI3.
Tissue: B-cell.
[2]"Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain."
Joung I., Strominger J.L., Shin J.
Proc. Natl. Acad. Sci. U.S.A. 93:5991-5995(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 51-96; 184-187; 213-217; 239-264 AND 268-281, TISSUE SPECIFICITY, INTERACTION WITH LCK, MUTAGENESIS OF TYR-9.
Tissue: Cervix carcinoma.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Caudate nucleus and Trachea.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Pancreas, Placenta, Skin and Uterus.
[6]"Genomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding protein."
Vadlamudi R.K., Shin J.
FEBS Lett. 435:138-142(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72, INDUCTION.
[7]"Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent."
Stumptner C., Heid H., Fuchsbichler A., Hauser H., Mischinger H.-J., Zatloukal K., Denk H.
Am. J. Pathol. 154:1701-1710(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-60; 166-174 AND 379-388, SUBCELLULAR LOCATION.
[8]"Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region."
Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.
Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LCK AND RASA1.
[9]"p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins."
Vadlamudi R.K., Joung I., Strominger J.L., Shin J.
J. Biol. Chem. 271:20235-20237(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBIQUITIN.
[10]"A p56(lck) ligand serves as a coactivator of an orphan nuclear hormone receptor."
Marcus S.L., Winrow C.J., Capone J.P., Rachubinski R.A.
J. Biol. Chem. 271:27197-27200(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2F2.
[11]"Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62."
Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.
Mol. Cell. Biol. 18:3069-3080(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCI AND PRKCZ, SUBCELLULAR LOCATION.
[12]"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIPK1; PRKCZ; PRKCI; IKBKB; TRADD AND TNFRSF1A, FUNCTION.
[13]"p62 functions as a p38 MAP kinase regulator."
Sudo T., Maruyama M., Osada H.
Biochem. Biophys. Res. Commun. 269:521-525(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPKAPK5, SUBCELLULAR LOCATION.
[14]"The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway."
Sanz L., Diaz-Meco M.T., Nakano H., Moscat J.
EMBO J. 19:1576-1586(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF6 AND RIPK1, DOMAIN, FUNCTION.
[15]"The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor."
Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A., Moscat J.
J. Biol. Chem. 276:7709-7712(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NTRK1; TRAF6; NGFR AND PRKCZ, FUNCTION.
[16]"p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases."
Zatloukal K., Stumptner C., Fuchsbichler A., Heid H., Schnoelzer M., Kenner L., Kleinert R., Prinz M., Aguzzi A., Denk H.
Am. J. Pathol. 160:255-263(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition."
Chang S., Kim J.H., Shin J.
FEBS Lett. 510:57-61(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAWR AND PRKCZ.
[18]"Mallory body -- a disease-associated type of sequestosome."
Stumptner C., Fuchsbichler A., Heid H., Zatloukal K., Denk H.
Hepatology 35:1053-1062(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[19]"Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling."
Geetha T., Wooten M.W.
J. Biol. Chem. 278:4730-4739(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NTRK1; NTRK2 AND NTRK3, SUBCELLULAR LOCATION, FUNCTION.
[20]"Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins."
Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A., Michaelsen E., Bjoerkoey G., Johansen T.
J. Biol. Chem. 278:34568-34581(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCI; PRKCZ; MAP2K5 AND NBR1, DOMAIN, MUTAGENESIS OF LYS-7; LYS-13; 21-ARG-ARG-22; TYR-67; ASP-69; ASP-71; ASP-73; ASP-80 AND GLU-82, DIMERIZATION.
[21]"PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62."
Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.
Mol. Cell 12:39-50(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCZ, DOMAIN, OLIGOMERIZATION, MUTAGENESIS OF LYS-7; ASP-69 AND ASP-73.
[22]"p62 overexpression in breast tumors and regulation by prostate-derived Ets factor in breast cancer cells."
Thompson H.G.R., Harris J.W., Wold B.J., Lin F., Brody J.P.
Oncogene 22:2322-2333(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[23]"Transcriptional activation of p62/A170/ZIP during the formation of the aggregates: possible mechanisms and the role in Lewy body formation in Parkinson's disease."
Nakaso K., Yoshimoto Y., Nakano T., Takeshima T., Fukuhara Y., Yasui K., Araga S., Yanagawa T., Ishii T., Nakashima K.
Brain Res. 1012:42-51(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[24]"Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation."
Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W.
Mol. Cell. Biol. 24:8055-8068(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF6; PSMC2 AND PSMD4, DOMAIN, MUTAGENESIS OF LEU-398; PHE-406; LEU-413; LEU-417 AND ILE-431, FUNCTION.
[25]"The p62 scaffold regulates nerve growth factor-induced NF-kappaB activation by influencing TRAF6 polyubiquitination."
Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T., Moscat J.
J. Biol. Chem. 280:35625-35629(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[26]"p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death."
Bjorkoy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., Stenmark H., Johansen T.
J. Cell Biol. 171:603-614(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION, INTERACTION WITH MAP1LC3B, DOMAIN, POSSIBLE PROTECTIVE ROLE IN HD, MUTAGENESIS OF ASP-69 AND ILE-431.
[27]"Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation."
Babu J.R., Geetha T., Wooten M.W.
J. Neurochem. 94:192-203(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPT, DOMAIN, SUBCELLULAR LOCATION, FUNCTION.
[28]"The LIM protein Ajuba influences interleukin-1-induced NF-kappaB activation by affecting the assembly and activity of the protein kinase Czeta/p62/TRAF6 signaling complex."
Feng Y., Longmore G.D.
Mol. Cell. Biol. 25:4010-4022(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AJUBA AND LIMD1.
[29]"Inhibition of sequestosome 1/p62 up-regulation prevents aggregation of ubiquitinated proteins induced by prostaglandin J2 without reducing its neurotoxicity."
Wang Z., Figueiredo-Pereira M.E.
Mol. Cell. Neurosci. 29:222-231(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, FUNCTION.
[30]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"The kinase domain of titin controls muscle gene expression and protein turnover."
Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E., Kristensen J., Brandmeier B., Franzen G., Hedberg B., Gunnarsson L.G., Hughes S.M., Marchand S., Sejersen T., Richard I., Edstroem L., Ehler E., Udd B., Gautel M.
Science 308:1599-1603(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NBR1 AND TRIM55, PHOSPHORYLATION, DOMAINS, FUNCTION.
[32]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
J. Biol. Chem. 282:24131-24145(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GABARAP; GABARAPL1; GABARAPL2; MAP1LC3A AND MAP1LC3B, MUTAGENESIS OF 323-GLU-GLU-324; SER-332; 335-ASP--ASP-337; TRP-338 AND SER-342.
[35]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; THR-269; SER-272; SER-328; SER-332 AND SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[40]"Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance."
Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., Ehler E.
J. Cell Biol. 191:1159-1172(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FHOD3.
[41]"p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha."
O'Connor C., Pertel T., Gray S., Robia S.L., Bakowska J.C., Luban J., Campbell E.M.
J. Virol. 84:5997-6006(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM5, SUBCELLULAR LOCATION.
[42]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-207; SER-249; SER-266; SER-272 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[43]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"Independent interactions of ubiquitin-binding domains in a ubiquitin-mediated ternary complex."
Garner T.P., Strachan J., Shedden E.C., Long J.E., Cavey J.R., Shaw B., Layfield R., Searle M.S.
Biochemistry 50:9076-9087(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ZFAND5 AND UBIQUITIN, SUBCELLULAR LOCATION.
[45]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]"TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells."
Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R.
Biochim. Biophys. Acta 1823:316-326(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM13, SUBCELLULAR LOCATION.
[47]"TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death."
Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.
Cell Death Differ. 19:1525-1535(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1LC3A.
[48]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[49]"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1LC3B.
[50]"Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone."
Ciani B., Layfield R., Cavey J.R., Sheppard P.W., Searle M.S.
J. Biol. Chem. 278:37409-37412(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 387-436, CHARACTERIZATION OF VARIANT LEU-392, DOMAIN.
[51]"Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch."
Long J., Gallagher T.R., Cavey J.R., Sheppard P.W., Ralston S.H., Layfield R., Searle M.S.
J. Biol. Chem. 283:5427-5440(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 387-436, INTERACTION WITH UBIQUITIN.
[52]"Conformation and dynamics of the three-helix bundle UBA domain of p62 from experiment and simulation."
Evans C.L., Long J.E., Gallagher T.R., Hirst J.D., Searle M.S.
Proteins 71:227-240(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 387-436.
[53]"Dimerisation of the UBA domain of p62 inhibits ubiquitin binding and regulates NF-kappaB signalling."
Long J., Garner T.P., Pandya M.J., Craven C.J., Chen P., Shaw B., Williamson M.P., Layfield R., Searle M.S.
J. Mol. Biol. 396:178-194(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 387-436, SUBUNIT, FUNCTION, MUTAGENESIS OF GLU-409 AND GLY-410, CHARACTERIZATION OF VARIANT PDB ARG-425.
[54]"Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone."
Laurin N., Brown J.P., Morissette J., Raymond V.
Am. J. Hum. Genet. 70:1582-1588(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDB LEU-392, VARIANTS VAL-117 AND GLN-274.
[55]"Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease."
Hocking L.J., Lucas G.J.A., Daroszewska A., Mangion J., Olavesen M., Cundy T., Nicholson G.C., Ward L., Bennett S.T., Wuyts W., Van Hul W., Ralston S.H.
Hum. Mol. Genet. 11:2735-2739(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDB LEU-392.
[56]"Three novel mutations in SQSTM1 identified in familial Paget's disease of bone."
Johnson-Pais T.L., Wisdom J.H., Weldon K.S., Cody J.D., Hansen M.F., Singer F.R., Leach R.J.
J. Bone Miner. Res. 18:1748-1753(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDB LEU-387.
[57]"Familial Paget's disease in The Netherlands: occurrence, identification of new mutations in the sequestosome 1 gene, and their clinical associations."
Eekhoff E.W.M., Karperien M., Houtsma D., Zwinderman A.H., Dragoiescu C., Kneppers A.L.J., Papapoulos S.E.
Arthritis Rheum. 50:1650-1654(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDB LEU-392; PRO-399; THR-404 AND ARG-425.
[58]"Identification of SQSTM1 mutations in familial Paget's disease in Australian pedigrees."
Good D.A., Busfield F., Fletcher B.H., Lovelock P.K., Duffy D.L., Kesting J.B., Andersen J., Shaw J.T.E.
Bone 35:277-282(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDB LEU-392.
[59]"Two novel mutations at exon 8 of the Sequestosome 1 (SQSTM1) gene in an Italian series of patients affected by Paget's disease of bone (PDB)."
Falchetti A., Di Stefano M., Marini F., Del Monte F., Mavilia C., Strigoli D., De Feo M.L., Isaia G., Masi L., Amedei A., Cioppi F., Ghinoi V., Maddali Bongi S., Di Fede G., Sferrazza C., Rini G.B., Melchiorre D., Matucci-Cerinic M., Brandi M.L.
J. Bone Miner. Res. 19:1013-1017(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDB LEU-392; VAL-404 AND ARG-425.
[60]"Novel UBA domain mutations of SQSTM1 in Paget's disease of bone: genotype phenotype correlation, functional analysis, and structural consequences."
Hocking L.J., Lucas G.J.A., Daroszewska A., Cundy T., Nicholson G.C., Donath J., Walsh J.P., Finlayson C., Cavey J.R., Ciani B., Sheppard P.W., Searle M.S., Layfield R., Ralston S.H.
J. Bone Miner. Res. 19:1122-1127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDB VAL-404; SER-411 AND ARG-425, CHARACTERIZATION OF VARIANTS VAL-404; SER-411 AND ARG-425.
[61]"Detection and validation of non-synonymous coding SNPs from orthogonal analysis of shotgun proteomics data."
Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A., Hendrickson R.C., Stephenson J.L. Jr.
J. Proteome Res. 6:2331-2340(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLU-238, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41806 mRNA. Translation: AAA93299.1.
U46751 mRNA. Translation: AAC52070.1.
AK098077 mRNA. Translation: BAG53577.1.
AK312451 mRNA. Translation: BAG35358.1.
AC008393 Genomic DNA. No translation available.
BC000951 mRNA. Translation: AAH00951.1.
BC001874 mRNA. Translation: AAH01874.1.
BC003139 mRNA. Translation: AAH03139.1.
BC017222 mRNA. Translation: AAH17222.1.
BC019111 mRNA. Translation: AAH19111.1.
AF060494 Genomic DNA. Translation: AAC64516.1.
RefSeqNP_001135770.1. NM_001142298.1.
NP_001135771.1. NM_001142299.1.
NP_003891.1. NM_003900.4.
UniGeneHs.724025.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q02NMR-A387-436[»]
2JY7NMR-A387-436[»]
2JY8NMR-A387-436[»]
2K0BNMR-X387-436[»]
2KNVNMR-A/B387-436[»]
ProteinModelPortalQ13501.
SMRQ13501. Positions 3-102, 125-172, 387-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114397. 369 interactions.
DIPDIP-34443N.
IntActQ13501. 112 interactions.
MINTMINT-269914.
STRING9606.ENSP00000374455.

PTM databases

PhosphoSiteQ13501.

Polymorphism databases

DMDM74735628.

Proteomic databases

PaxDbQ13501.
PRIDEQ13501.

Protocols and materials databases

DNASU8878.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360718; ENSP00000353944; ENSG00000161011. [Q13501-2]
ENST00000376929; ENSP00000366128; ENSG00000161011. [Q13501-2]
ENST00000389805; ENSP00000374455; ENSG00000161011. [Q13501-1]
ENST00000402874; ENSP00000385553; ENSG00000161011. [Q13501-2]
GeneID8878.
KEGGhsa:8878.
UCSCuc003mkw.4. human. [Q13501-1]

Organism-specific databases

CTD8878.
GeneCardsGC05P179234.
HGNCHGNC:11280. SQSTM1.
HPACAB004587.
MIM601530. gene.
602080. phenotype.
neXtProtNX_Q13501.
Orphanet803. Amyotrophic lateral sclerosis.
280110. Paget disease of bone.
PharmGKBPA36109.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278569.
HOVERGENHBG052750.
InParanoidQ13501.
KOK14381.
OMASVCPNYD.
PhylomeDBQ13501.
TreeFamTF328470.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.
SignaLinkQ13501.

Gene expression databases

ArrayExpressQ13501.
BgeeQ13501.
CleanExHS_SQSTM1.
GenevestigatorQ13501.

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. human.
EvolutionaryTraceQ13501.
GeneWikiSequestosome_1.
GenomeRNAi8878.
NextBio33335.
PROQ13501.
SOURCESearch...

Entry information

Entry nameSQSTM_HUMAN
AccessionPrimary (citable) accession number: Q13501
Secondary accession number(s): A6NFN7 expand/collapse secondary AC list , B2R661, B3KUW5, Q13446, Q9BUV7, Q9BVS6, Q9UEU1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM