| + |
PRKN | down-regulates quantity by destabilization 
ubiquitination
|
SQSTM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278524 |
Lys13 |
VKAYLLGkEDAAREI |
Homo sapiens |
|
| pmid |
sentence |
| 26746706 |
Once activated, parkin interacts with and subsequently ubiquitinates p62 at the K13 residue, resulting in the degradation of p62 via the proteasomal dependent pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIM21 | down-regulates activity
ubiquitination
|
SQSTM1 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278602 |
Lys7 |
kAYLLGKE |
Homo sapiens |
|
| pmid |
sentence |
| 26942676 |
TRIM21 directly ubiquitylates p62 at residue K7 to inhibit its oligomerization and sequestration function.|TRIM21 negatively regulates p62 mediated sequestration of Keap1 and antioxidant response. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates 
phosphorylation
|
SQSTM1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169012 |
Ser272 |
RSRLTPVsPESSSTE |
Homo sapiens |
|
| pmid |
sentence |
| 20974803 |
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 |
| 20974803 |
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/CDK1 | up-regulates
phosphorylation
|
SQSTM1 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216932 |
Ser272 |
RSRLTPVsPESSSTE |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 20974803 |
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 |
| 20974803 |
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 |
| + |
CSNK1A1 | up-regulates activity
phosphorylation
|
SQSTM1 |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273769 |
Ser349 |
SSKEVDPsTGELQSL |
Mus musculus |
|
| pmid |
sentence |
| 37723657 |
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 |
| + |
TBK1 | up-regulates
phosphorylation
|
SQSTM1 |
0.705 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191944 |
Ser403 |
ESLSQMLsMGFSDEG |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 22921120 |
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 |
| + |
ULK1 | down-regulates quantity by destabilization
phosphorylation
|
SQSTM1 |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278349 |
Ser403 |
ESLSQMLsMGFSDEG |
Homo sapiens |
|
| pmid |
sentence |
| 25040165 |
ULK1 phosphorylates p62 at the Ser403 site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGFR | down-regulates activity
phosphorylation
|
SQSTM1 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277500 |
Tyr433 |
AALDTIQySKHPPPL |
Homo sapiens |
|
| pmid |
sentence |
| 31931029 |
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 |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
SQSTM1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272446 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25721664 |
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 |
| + |
PEX5 | up-regulates activity
binding
|
SQSTM1 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262793 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26344566 |
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 |
| + |
MAP1LC3B | up-regulates
binding
|
SQSTM1 |
0.834 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156356 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17580304 |
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 |
| 19250911 |
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 |
| + |
RNF26 | up-regulates activity
ubiquitination
|
SQSTM1 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269830 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 27368102 |
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 |
| + |
USP15 | down-regulates activity
deubiquitination
|
SQSTM1 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269829 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 27368102 |
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 |
| + |
BNIP1 | up-regulates activity
binding
|
SQSTM1 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271932 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21931693 |
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 |
| + |
GABARAPL1 | up-regulates activity
binding
|
SQSTM1 |
0.788 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156304 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17580304 |
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 |
| + |
MAP1LC3A | up-regulates
binding
|
SQSTM1 |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156353 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17580304 |
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 |
| 19250911 |
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 |
| + |
FBXO3 | down-regulates quantity by destabilization
binding
|
SQSTM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272444 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25721664 |
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 |
| + |
SQSTM1 | down-regulates quantity by destabilization
binding
|
SOD1 |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262801 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 19765191 |
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 |
| + |
SQSTM1 | up-regulates quantity
binding
|
WDFY3 |
0.574 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266792 |
|
|
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 20168092 |
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 |
| + |
NBR1 | up-regulates
binding
|
SQSTM1 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184273 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19250911 |
Nbr1 and p62 interact and form oligomers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GABARAPL2 | up-regulates activity
binding
|
SQSTM1 |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156307 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17580304 |
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 |
| + |
NEDD4 | down-regulates quantity by destabilization
ubiquitination
|
SQSTM1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278637 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28085563 |
Depletion of NEDD4 dramatically reduced the LC3 protein level and elevated the SQSTM1 protein level.|Furthermore, SQSTM1 is ubiquitinated by NEDD4 while LC3 functions as an activator of NEDD4 ligase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SQSTM1
- 
- 