| + |
PIAS1 | down-regulates 
sumoylation
|
FHL1 |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154801 |
Lys144 |
GTGSFFPkGEDFYCV |
Homo sapiens |
|
| pmid |
sentence |
| 17509614 |
Pias1 (the protein inhibitor of activated stat1) interacts with kyot2 directly and attenuates kyot2-mediated transcriptional repression. We demonstrate that kyot2 is modified by sumoylation at two lysine residues, k144 and k171. Sumoylation of the transfected kyot2 is enhanced by pias1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154805 |
Lys300 |
PRGPGLVkAPVWWPM |
Homo sapiens |
|
| pmid |
sentence |
| 17509614 |
Pias1 (the protein inhibitor of activated stat1) interacts with kyot2 directly and attenuates kyot2-mediated transcriptional repression. We demonstrate that kyot2 is modified by sumoylation at two lysine residues, k144 and k171. Sumoylation of the transfected kyot2 is enhanced by pias1 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PIAS1 | down-regulates activity
sumoylation
|
SATB2 |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268932 |
Lys233 |
YKKYKKIkVERVERE |
Homo sapiens |
|
| pmid |
sentence |
| 14701874 |
We found that SATB2 differs from the closely related thymocyte-specific protein SATB1 by modifications of two lysines with the small ubiquitive related modifier (SUMO), which are augmented specifically by the SUMO E3 ligase PIAS1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269112 |
Lys350 |
PPIPRAVkPEPTNSS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14701874 |
We found that SATB2 differs from the closely related thymocyte-specific protein SATB1 by modifications of two lysines with the small ubiquitive related modifier (SUMO), which are augmented specifically by the SUMO E3 ligase PIAS1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PIAS1 | up-regulates activity 
sumoylation
|
AKT |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252737 |
Lys276 |
NVVYRDLkLENLMLD |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 23884910 |
Although multiple sites on Akt could be SUMOylated, K276 was identified as a major SUMO acceptor site. K276R or E278A mutation reduced SUMOylation of Akt but had little effect on its ubiquitination. Strikingly, these mutations also completely abolished Akt kinase activity. In support of these results, we found that expression of PIAS1 and SUMO1 increased Akt activity, whereas expression of SENP1 reduced Akt1 activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PIAS1 | up-regulates activity
sumoylation
|
AKT1 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252735 |
Lys276 |
NVVYRDLkLENLMLD |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 23884910 |
Although multiple sites on Akt could be SUMOylated, K276 was identified as a major SUMO acceptor site. K276R or E278A mutation reduced SUMOylation of Akt but had little effect on its ubiquitination. Strikingly, these mutations also completely abolished Akt kinase activity. In support of these results, we found that expression of PIAS1 and SUMO1 increased Akt activity, whereas expression of SENP1 reduced Akt1 activity. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PIAS1 | up-regulates
sumoylation
|
DDX5 |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153719 |
Lys53 |
WNLDELPkFEKNFYQ |
Homo sapiens |
|
| pmid |
sentence |
| 17369852 |
We demonstrate that the sumo e3 ligase pias1 interacts with p68 and enhances its sumo modification in vivo / sumo modification enhances p68 transcriptional repression activity and inhibits the ability of p68 to function as a coactivator of p53. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIAS1 | up-regulates
sumoylation
|
PRDM1 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197265 |
Lys816 |
PLVPVKVkQETVEPM |
Homo sapiens |
|
| pmid |
sentence |
| 22555612 |
Blimp_1 is subjected to pias1_mediated sumoylation at lysine 816 / it appears that sumo_modified blimp_1 is a more potent transcriptional repressor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates quantity by destabilization
phosphorylation
|
PIAS1 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276924 |
Ser13 |
ELKQMVMsLRVSELQ |
Mus musculus |
MLE-12 Cell |
| pmid |
sentence |
| 26157031 |
We discovered a ubiquitin E3 ligase, HECTD2, which ubiquitinated and mediated the degradation of PIAS1, thus increasing inflammation in an experimental pneumonia model. We found that GSK3β phosphorylation of PIAS1 provided a phosphodegron for HECTD2 targeting. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276923 |
Ser17 |
MVMSLRVsELQVLLG |
Mus musculus |
MLE-12 Cell |
| pmid |
sentence |
| 26157031 |
We discovered a ubiquitin E3 ligase, HECTD2, which ubiquitinated and mediated the degradation of PIAS1, thus increasing inflammation in an experimental pneumonia model. We found that GSK3β phosphorylation of PIAS1 provided a phosphodegron for HECTD2 targeting. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
CSNK2A1 | up-regulates
phosphorylation
|
PIAS1 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184039 |
Ser466 |
VIDLTIDsSSDEEEE |
Homo sapiens |
|
| pmid |
sentence |
| 19217413 |
Ck2 phosphorylates serine residues adjacent to the sim of pias1 these findings show that the phosphosim module mediates binding to free sumo and sumo conjugates in a phosphorylation-dependent mode, with ck2 being the critical kinase involvedin this process. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184043 |
Ser467 |
IDLTIDSsSDEEEEE |
Homo sapiens |
|
| pmid |
sentence |
| 19217413 |
Ck2 phosphorylates serine residues adjacent to the sim of pias1 these findings show that the phosphosim module mediates binding to free sumo and sumo conjugates in a phosphorylation-dependent mode, with ck2 being the critical kinase involvedin this process. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184047 |
Ser468 |
DLTIDSSsDEEEEEP |
Homo sapiens |
|
| pmid |
sentence |
| 19217413 |
Ck2 phosphorylates serine residues adjacent to the sim of pias1 these findings show that the phosphosim module mediates binding to free sumo and sumo conjugates in a phosphorylation-dependent mode, with ck2 being the critical kinase involvedin this process. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | up-regulates activity
phosphorylation
|
PIAS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259866 |
Ser510 |
SPVSRTPsLPAVDTS |
Homo sapiens |
|
| pmid |
sentence |
| 27256105 |
Mechanically, we found that AMPKα1 directly phosphorylated protein inhibitor of activated STAT-1 (PIAS1), the SUMO E3-ligase of Runx2, at serine 510, to promote its SUMO E3-ligase activity. Finally, mutation of protein inhibitor of activated STAT-1 at serine 510 suppressed m |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK2 | up-regulates
phosphorylation
|
PIAS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199944 |
Ser522 |
DTSYINTsLIQDYRH |
Homo sapiens |
|
| pmid |
sentence |
| 23202365 |
T he mitogen-activated protein kinase (mapk)-activated protein kinase-2 is a proinflammatory kinase and phosphorylates pias1 at the ser522 residue. Activation of mapk-activated protein kinase-2 enhances p53-sumoylation, but a pias1 phosphorylation mutant, pias1-s522a, abolished this p53-sumoylation, suggesting a critical role for pias1-s522 phosphorylation in its sumo ligase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skin |
| + |
PIAS1 | up-regulates
sumoylation
|
SMAD4 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123462 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15028714 |
These data demonstrate that pias1 protein positively modulates tgf-beta responses as a sumo e3 ligase for smad4 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIAS1 | down-regulates
binding
|
STAT1 |
0.786 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202039 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23663276 |
Socs1 and socs3 target jak1 and gp130, respectively, near the plasma membrane to prevent cytoplasmic stats from being activated, whereas pias1 principally targets activated stat1 in the cell nucleus and prevents it from binding to dna. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120548 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14699505 |
Pias1 inhibits binding of stat1 dimers to the response elements in the promoters of target genes |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
PIAS1 | up-regulates
sumoylation
|
RPA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162153 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20016603 |
Pias1 and pias4 promote brca1 accumulation and sumoylation, rpa phosphorylation, and dsb repair |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HECTD2 | down-regulates quantity by destabilization
polyubiquitination
|
PIAS1 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272421 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26157031 |
We discovered a ubiquitin E3 ligase, HECTD2, which ubiquitinated and mediated the degradation of PIAS1, thus increasing inflammation in an experimental pneumonia model. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIAS1 | up-regulates
sumoylation
|
TP53BP1 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162156 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20016603 |
Pias1 and pias4 are recruited to dna-damage sites and mediate 53bp1 recruitment and sumoylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NDN | down-regulates quantity by destabilization
binding
|
PIAS1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253387 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24911587 |
Necdin bound to PIAS1 central domains that are highly conserved among PIAS family proteins and suppressed PIAS1-dependent sumoylation of the substrates STAT1 and PML (promyelocytic leukemia protein). Remarkably, necdin promoted degradation of PIAS1 via the ubiquitin-proteasome pathway. In transfected HEK293A cells, amino- and carboxyl-terminally truncated mutants of PIAS1 bound to necdin but failed to undergo necdin-dependent ubiquitination. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PIAS1
- 
- 