Relation Results

Summary

Name SQSTM1
Full Name Sequestosome-1
Synonyms EBI3-associated protein of 60 kDa, EBIAP, p60, Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, Ubiquitin-binding protein p62 | ORCA, OSIL
Primary ID Q13501
Links - -
Type protein
Relations 22
Pathways Autophagy
Function Autophagy receptor required for selective macroautophagy (aggrephagy). Functions as a bridge between polyubiquitinated cargo and autophagosomes. Inter ...
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Type: Score: Layout: SPV 
0.350.3550.40.7010.3360.8610.7860.8310.380.4840.3650.2620.20.3410.7830.5270.5780.302CDK1SQSTM1CyclinB/CDK1CSNK1A1TBK1EGFRGABARAPL2GABARAPL1MAP1LC3BPEX5NBR1RNF26USP15FBXO3BNIP1MAP1LC3ASOD1WDFY3Cullin 1-RBX1-Skp1

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ CDK1up-regulates img/direct-activation.png phosphorylation SQSTM1 0.35
Identifier Residue Sequence Organism Cell Line
SIGNOR-169012 Ser272 RSRLTPVsPESSSTE Homo sapiens
pmid sentence
Here we show that cdk1 phosphorylates p62 in vitro and in vivo at t269 and s272, which is necessary for the maintenance of appropriate cyclin b1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis.
Identifier Residue Sequence Organism Cell Line
SIGNOR-169016 Thr269 GGKRSRLtPVSPESS Homo sapiens
pmid sentence
Here we show that cdk1 phosphorylates p62 in vitro and in vivo at t269 and s272, which is necessary for the maintenance of appropriate cyclin b1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis.
Publications: 2 Organism: Homo Sapiens
+ CyclinB/CDK1up-regulates img/direct-activation.png phosphorylation SQSTM1 0.355
Identifier Residue Sequence Organism Cell Line
SIGNOR-216932 Ser272 RSRLTPVsPESSSTE Homo sapiens Lung Cancer Cell
pmid sentence
Here we show that cdk1 phosphorylates p62 in vitro and in vivo at t269 and s272, which is necessary for the maintenance of appropriate cyclin b1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis.
Identifier Residue Sequence Organism Cell Line
SIGNOR-216936 Thr269 GGKRSRLtPVSPESS Homo sapiens Lung Cancer Cell
pmid sentence
Here we show that cdk1 phosphorylates p62 in vitro and in vivo at t269 and s272, which is necessary for the maintenance of appropriate cyclin b1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis.
Publications: 2 Organism: Homo Sapiens
+ CSNK1A1up-regulates activity img/direct-activation.png phosphorylation SQSTM1 0.4
Identifier Residue Sequence Organism Cell Line
SIGNOR-273769 Ser349 SSKEVDPsTGELQSL Mus musculus
pmid sentence
Mechanistically, CSNK1A1 interacted with STING1 upon the CGAS-STING1 pathway activation and promoted STING1 autophagic degradation by enhancing the phosphorylation of SQSTM1/p62 at serine 351 (serine 349 in human), which was critical for SQSTM1-mediated STING1 autophagic degradation.
Publications: 1 Organism: Mus Musculus
+ TBK1up-regulates img/direct-activation.png phosphorylation SQSTM1 0.701
Identifier Residue Sequence Organism Cell Line
SIGNOR-191944 Ser403 ESLSQMLsMGFSDEG Homo sapiens Macrophage
pmid sentence
Tbk-1 coordinated assembly and function of the autophagic machinery and phosphorylated the autophagic adaptor p62 (sequestosome 1) on ser-403, a residue essential for its role in autophagic clearance.
Publications: 1 Organism: Homo Sapiens
+ EGFRdown-regulates activity img/direct_inhibition.png phosphorylation SQSTM1 0.336
Identifier Residue Sequence Organism Cell Line
SIGNOR-277500 Tyr433 AALDTIQySKHPPPL Homo sapiens
pmid sentence
Here we found that EGFR-stimulated phosphorylation of SQSTM1 at tyrosine 433 induces dimerization of its UBA domain, which disturbs the sequestration function of SQSTM1 and causes autophagic flux blocking.
Publications: 1 Organism: Homo Sapiens
+ GABARAPL2up-regulates activity img/direct-activation.png binding SQSTM1 0.861
Identifier Residue Sequence Organism Cell Line
SIGNOR-156307 Homo sapiens HeLa Cell
pmid sentence
P62 binds both to lc3a and -b and the related gabarap family proteins/this interaction is necessary for autophagic degradation of p62-positive cytoplasmic inclusion bodies containing ubiquitinated proteins. We also demonstrate that alis are indistinguisha
Publications: 1 Organism: Homo Sapiens
Pathways:Autophagy
+ GABARAPL1up-regulates activity img/direct-activation.png binding SQSTM1 0.786
Identifier Residue Sequence Organism Cell Line
SIGNOR-156304 Homo sapiens HeLa Cell
pmid sentence
P62 binds both to lc3a and -b and the related gabarap family proteins/this interaction is necessary for autophagic degradation of p62-positive cytoplasmic inclusion bodies containing ubiquitinated proteins. We also demonstrate that alis are indistinguisha
Publications: 1 Organism: Homo Sapiens
Pathways:Autophagy
+ MAP1LC3Bup-regulates img/direct-activation.png binding SQSTM1 0.831
Identifier Residue Sequence Organism Cell Line
SIGNOR-156356 Homo sapiens
pmid sentence
Sqstm1/p62 (named a170 in the mouse;hereafter p62) is the first proposed example of such proteins (bj_?_?Rk_?_?Y et al.,2005). It binds polyubiquitinated protein aggregates via its uba domain and interacts with lc3 on the autophagosome/ this interaction is necessary for autophagic degradation of p62-positive cytoplasmic inclusion bodies containing ubiquitinated proteins. We also demonstrate that alis are indistinguishable from p62 inclusion bodies and that p62 is required for their formation.
Identifier Residue Sequence Organism Cell Line
SIGNOR-184255 Homo sapiens
pmid sentence
Sqstm1/p62 (named a170 in the mouse;hereafter p62) is the first proposed example of such proteins (bj_?_?Rk_?_?Y et al.,2005). It binds polyubiquitinated protein aggregates via its uba domain and interacts with lc3 on the autophagosome/ this interaction is necessary for autophagic degradation of p62-positive cytoplasmic inclusion bodies containing ubiquitinated proteins. We also demonstrate that alis are indistinguishable from p62 inclusion bodies and that p62 is required for their formation.
Publications: 2 Organism: Homo Sapiens
+ PEX5up-regulates activity img/direct-activation.png binding SQSTM1 0.38
Identifier Residue Sequence Organism Cell Line
SIGNOR-262793 Homo sapiens HEK-293 Cell
pmid sentence
Specificity for autophagy of peroxisomes (pexophagy) is provided by ATM phosphorylation of PEX5 at Ser 141, which promotes PEX5 monoubiquitylation at Lys 209, and recognition of ubiquitylated PEX5 by the autophagy adaptor protein p62, directing the autophagosome to peroxisomes to induce pexophagy. 
Publications: 1 Organism: Homo Sapiens
+ NBR1up-regulates img/direct-activation.png binding SQSTM1 0.484
Identifier Residue Sequence Organism Cell Line
SIGNOR-184273 Homo sapiens
pmid sentence
Nbr1 and p62 interact and form oligomers.
Publications: 1 Organism: Homo Sapiens
+ RNF26up-regulates activity img/direct-activation.png ubiquitination SQSTM1 0.365
Identifier Residue Sequence Organism Cell Line
SIGNOR-269830 Homo sapiens HeLa Cell
pmid sentence
SQSTM1 Is a Substrate for RNF26 and the DUB USP15. Catalytically competent RNF26 (light red) recruits SQSTM1 (blue) and mediates ubiquitin ligation (red), which serves to attract UBDs of specific vesicle-associated adaptors.
Publications: 1 Organism: Homo Sapiens
+ USP15down-regulates activity img/direct_inhibition.png deubiquitination SQSTM1 0.262
Identifier Residue Sequence Organism Cell Line
SIGNOR-269829 Homo sapiens HeLa Cell
pmid sentence
SQSTM1 Is a Substrate for RNF26 and the DUB USP15. Catalytically competent RNF26 (light red) recruits SQSTM1 (blue) and mediates ubiquitin ligation (red), which serves to attract UBDs of specific vesicle-associated adaptors. Dissociation of the RNF26/SQSTM1 complex, promoted by the DUB USP15 (yellow), releases target vesicles for (4) fast transport into the cell periphery.
Publications: 1 Organism: Homo Sapiens
+ FBXO3down-regulates quantity by destabilization img/direct_inhibition.png binding SQSTM1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272444 Homo sapiens HEK-293 Cell
pmid sentence
F-box protein Fbxo3 targets Smurf1 ubiquitin ligase for ubiquitination and degradation. Here we show that another F-box protein Fbxo3, belonging to the FBXO type protein family, also interacts with and targets Smurf1 for poly-ubiquitination and proteasomal degradation. The SCF complex is composed of F-box protein, Skp1, Cullin1 (Cul1) and ROC1. Fbxo3, whose substrates are few, forms SCF Fbxo3 ubiquitin ligase and regulates the degradations of Fbxl2, p62, HIPK2 and p300 through the ubiquitin-proteasome pathway.
Publications: 1 Organism: Homo Sapiens
+ BNIP1up-regulates activity img/direct-activation.png binding SQSTM1 0.341
Identifier Residue Sequence Organism Cell Line
SIGNOR-271932 Homo sapiens HEK-293 Cell
pmid sentence
RNF185 functions as a ubiquitin E3 ligase, enabling BNIP1-p62 interaction. BNIP1 is polyubiquitinated by RNF185 and associates with autophagy receptor p62. In addition, we checked the endogenous localization of BNIP1 and p62 in HeLa cells (Fig. 7F). Alexa Fluor 488 conjugated endogenous BNIP1 and TRITIC conjugated endogenous p62 overlapped well in the cytoplasm, further providing the locational evidence for the recruitment of p62 by BNIP1.
Publications: 1 Organism: Homo Sapiens
+ MAP1LC3Aup-regulates img/direct-activation.png binding SQSTM1 0.783
Identifier Residue Sequence Organism Cell Line
SIGNOR-156353 Homo sapiens
pmid sentence
Sqstm1/p62 (named a170 in the mouse;hereafter p62) is the first proposed example of such proteins (bj_?_?Rk_?_?Y et al.,2005). It binds polyubiquitinated protein aggregates via its uba domain and interacts with lc3 on the autophagosome/ this interaction is necessary for autophagic degradation of p62-positive cytoplasmic inclusion bodies containing ubiquitinated proteins. We also demonstrate that alis are indistinguishable from p62 inclusion bodies and that p62 is required for their formation.
Identifier Residue Sequence Organism Cell Line
SIGNOR-184198 Homo sapiens
pmid sentence
Sqstm1/p62 (named a170 in the mouse;hereafter p62) is the first proposed example of such proteins (bj_?_?Rk_?_?Y et al.,2005). It binds polyubiquitinated protein aggregates via its uba domain and interacts with lc3 on the autophagosome/ this interaction is necessary for autophagic degradation of p62-positive cytoplasmic inclusion bodies containing ubiquitinated proteins. We also demonstrate that alis are indistinguishable from p62 inclusion bodies and that p62 is required for their formation.
Publications: 2 Organism: Homo Sapiens
+ SQSTM1down-regulates quantity by destabilization img/direct_inhibition.png binding SOD1 0.527
Identifier Residue Sequence Organism Cell Line
SIGNOR-262801 Mus musculus MEF Cell
pmid sentence
 This study provides a novel molecular mechanism by which mutant SOD1 can be recognized by p62 in an ubiquitin-independent fashion and targeted for the autophagy-lysosome degradation pathway.
Publications: 1 Organism: Mus Musculus
Pathways:Autophagy
+ SQSTM1up-regulates quantity img/direct-activation.png binding WDFY3 0.578
Identifier Residue Sequence Organism Cell Line
SIGNOR-266792 Homo sapiens Fibroblast
pmid sentence
 We show here that p62 is required to recruit the large phosphoinositide-binding protein ALFY to cytoplasmic p62 bodies generated upon amino acid starvation or puromycin-treatment. ALFY, as well as p62, is required for formation and autophagic degradation of cytoplasmic ubiquitin-positive inclusions. 
Publications: 1 Organism: Homo Sapiens
+ Cullin 1-RBX1-Skp1down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination SQSTM1 0.302
Identifier Residue Sequence Organism Cell Line
SIGNOR-272446 Homo sapiens HEK-293 Cell
pmid sentence
F-box protein Fbxo3 targets Smurf1 ubiquitin ligase for ubiquitination and degradation. Here we show that another F-box protein Fbxo3, belonging to the FBXO type protein family, also interacts with and targets Smurf1 for poly-ubiquitination and proteasomal degradation. The SCF complex is composed of F-box protein, Skp1, Cullin1 (Cul1) and ROC1. Fbxo3, whose substrates are few, forms SCF Fbxo3 ubiquitin ligase and regulates the degradations of Fbxl2, p62, HIPK2 and p300 through the ubiquitin-proteasome pathway.
Publications: 1 Organism: Homo Sapiens
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