Relation Results

Summary

Name PIAS1
Full Name E3 SUMO-protein ligase PIAS1
Synonyms DEAD/H box-binding protein 1, Gu-binding protein, GBP, Protein inhibitor of activated STAT protein 1, RNA helicase II-binding protein | DDXBP1
Primary ID O75925
Links - -
Type protein
Relations 22
Function Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tether ...
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Type: Score: Layout: SPV 
0.2580.5710.3830.3830.5340.3270.3360.3350.20.20.30.790.5020.3990.3940.2PIAS1FHL1SATB2AKT1AKTDDX5PRDM1GSK3BCSNK2A1PRKAA1MAPKAPK2NDNSTAT1TP53BP1SMAD4HECTD2RPA2

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ down-regulates img/direct_inhibition.png sumoylation FHL1 0.258
Identifier Residue Sequence Organism Cell Line
SIGNOR-154801 Lys144 GTGSFFPkGEDFYCV Homo sapiens
pmid sentence
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
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
+ down-regulates activity img/direct_inhibition.png sumoylation SATB2 0.571
Identifier Residue Sequence Organism Cell Line
SIGNOR-268932 Lys233 YKKYKKIkVERVERE Homo sapiens
pmid sentence
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
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
+ up-regulates activity img/direct-activation.png sumoylation AKT1 0.383
Identifier Residue Sequence Organism Cell Line
SIGNOR-252735 Lys276 NVVYRDLkLENLMLD Mus musculus MEF Cell
pmid sentence
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
+ up-regulates activity img/direct-activation.png sumoylation AKT 0.383
Identifier Residue Sequence Organism Cell Line
SIGNOR-252737 Lys276 NVVYRDLkLENLMLD Mus musculus MEF Cell
pmid sentence
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
+ up-regulates img/direct-activation.png sumoylation DDX5 0.534
Identifier Residue Sequence Organism Cell Line
SIGNOR-153719 Lys53 WNLDELPkFEKNFYQ Homo sapiens
pmid sentence
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
+ up-regulates img/direct-activation.png sumoylation PRDM1 0.327
Identifier Residue Sequence Organism Cell Line
SIGNOR-197265 Lys816 PLVPVKVkQETVEPM Homo sapiens
pmid sentence
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
+ down-regulates quantity by destabilization img/direct_inhibition.png phosphorylation PIAS1 0.336
Identifier Residue Sequence Organism Cell Line
SIGNOR-276924 Ser13 ELKQMVMsLRVSELQ Mus musculus MLE-12 Cell
pmid sentence
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
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
+ up-regulates img/direct-activation.png phosphorylation PIAS1 0.335
Identifier Residue Sequence Organism Cell Line
SIGNOR-184039 Ser466 VIDLTIDsSSDEEEE Homo sapiens
pmid sentence
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
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
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
+ up-regulates activity img/direct-activation.png phosphorylation PIAS1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-259866 Ser510 SPVSRTPsLPAVDTS Homo sapiens
pmid sentence
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
+ up-regulates img/direct-activation.png phosphorylation PIAS1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-199944 Ser522 DTSYINTsLIQDYRH Homo sapiens
pmid sentence
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
+ down-regulates quantity by destabilization img/direct_inhibition.png binding PIAS1 0.3
Identifier Residue Sequence Organism Cell Line
SIGNOR-253387 Homo sapiens
pmid sentence
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
+ down-regulates img/direct_inhibition.png binding STAT1 0.79
Identifier Residue Sequence Organism Cell Line
SIGNOR-120548 Homo sapiens
pmid sentence
Pias1 inhibits binding of stat1 dimers to the response elements in the promoters of target genes
Identifier Residue Sequence Organism Cell Line
SIGNOR-202039 Homo sapiens
pmid sentence
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.
Publications: 2 Organism: Homo Sapiens
Tissue: Muscle, Skeletal Muscle
+ up-regulates img/direct-activation.png sumoylation TP53BP1 0.502
Identifier Residue Sequence Organism Cell Line
SIGNOR-162156 Homo sapiens
pmid sentence
Pias1 and pias4 are recruited to dna-damage sites and mediate 53bp1 recruitment and sumoylation.
Publications: 1 Organism: Homo Sapiens
+ up-regulates img/direct-activation.png sumoylation SMAD4 0.399
Identifier Residue Sequence Organism Cell Line
SIGNOR-123462 Homo sapiens
pmid sentence
These data demonstrate that pias1 protein positively modulates tgf-beta responses as a sumo e3 ligase for smad4
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination PIAS1 0.394
Identifier Residue Sequence Organism Cell Line
SIGNOR-272421 Homo sapiens HEK-293 Cell
pmid sentence
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
+ up-regulates img/direct-activation.png sumoylation RPA2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-162153 Homo sapiens
pmid sentence
Pias1 and pias4 promote brca1 accumulation and sumoylation, rpa phosphorylation, and dsb repair
Publications: 1 Organism: Homo Sapiens
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