PIAS1 (protein inhibitor of activated STAT 1) is a nuclear SP-RING-type SUMO E3 ligase of the PIAS family (orthologous to yeast Siz1/Siz2) and a transcriptional coregulator. It comprises an N-terminal SAP domain that binds A/T-rich DNA and chromatin and contains an LXXLL coregulator motif, a PINIT domain, a zinc-coordinating SP-RING that binds the SUMO E2 UBE2I/UBC9, a SUMO-interacting motif, and a Ser/Thr-rich C-terminus. By bridging UBE2I and substrates, PIAS1 catalyses SUMO1 and SUMO2/3 conjugation to many nuclear proteins, including p53, c-Jun, Mdm2, Sp3, HIC1, Nkx2.5, MTA1, Blimp-1/PRDM1, FLASH, nuclear receptors, BRCA1 and MRE11. Independently of or in addition to its ligase activity, PIAS1 directly binds activated transcription factors and blocks their DNA binding: it was discovered as a specific inhibitor of interferon-activated, tyrosine-phosphorylated STAT1 dimers and also inhibits NF-kB p65, so Pias1-deficient cells overexpress subsets of interferon- and NF-kB-inducible genes and show enhanced innate immune responses. Depending on partner and context PIAS1 can also coactivate transcription (e.g. FLASH/c-Myb, androgen receptor). PIAS1 is recruited to DNA double-strand breaks via its SAP domain, where with PIAS4 it promotes SUMO accrual, BRCA1/53BP1/RNF168 retention and repair, and it SUMOylates MRE11 on chromatin to stabilise it for DNA end resection. PIAS1 localises to the nucleoplasm, nuclear speckles and PML nuclear bodies.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000082 G1/S transition of mitotic cell cycle | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara projection from rat Pias1 asserting involvement in the G1/S transition. No human data in the cached literature show PIAS1 executing a cell-cycle transition step; any cell-cycle effect (e.g. via KLF8 sumoylation, per UniProt) is an indirect consequence of transcription factor modification. Reason: PIAS1 is a SUMO E3 ligase and transcriptional coregulator; effects on cell-cycle progression are downstream outcomes of substrate sumoylation rather than a direct role in the G1/S machinery. Retaining it as a process annotation overstates PIAS1's role. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt interaction results in SUMO ligation and repression of KLF8 |
| GO:0000122 negative regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: IBA: PIAS family members negatively regulate RNA polymerase II transcription. Human PIAS1 inhibits STAT1- and NF-kB p65-dependent gene activation by blocking their DNA binding, and sumoylates many repressors/activators. Reason: Consistent with direct experimental evidence for human PIAS1 inhibiting STAT1 and p65 target-gene activation; the PAINT node placement across PIAS orthologs is sound. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:15657437 PIAS1 blocks the DNA binding activity of p65 both in vitro and in vivo |
| GO:0000122 negative regulation of transcription by RNA polymerase II | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara projection of negative regulation of Pol II transcription from mouse Pias1. Well supported for human PIAS1 by STAT1 and NF-kB inhibition data. Reason: Same biology as the IBA; human PIAS1 blocks STAT1 and p65 DNA binding and represses their target genes. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:15657437 PIAS1 blocks the DNA binding activity of p65 both in vitro and in vivo |
| GO:0000122 negative regulation of transcription by RNA polymerase II | ISS GO_REF:0000024 | ACCEPT | Summary: ISS from mouse Msx1 (P13297) data, reflecting PIAS1 cooperation with Msx1 in repressing myogenic target genes. Although the donor is a partner rather than an ortholog, negative regulation of Pol II transcription is independently well established for PIAS1. Reason: The term is correct for PIAS1 on the basis of human STAT1/NF-kB evidence regardless of the unusual ISS source. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon file:human/PIAS1/PIAS1-uniprot.txt to the nuclear periphery, whereby MSX1 is brought into the proximity of |
| GO:0000785 chromatin | IBA GO_REF:0000033 | ACCEPT | Summary: IBA placing PIAS proteins on chromatin. Human PIAS1 sumoylates MRE11 predominantly in chromatin fractions, is recruited to damaged chromatin via its SAP domain, and interacts with FLASH in a chromatin context. Reason: Chromatin association via the SAP domain is a conserved PIAS/Siz feature and is experimentally supported for human PIAS1. Supporting Evidence: PMID:36050397 the major enhancement of MRE11 SUMOylation by PIAS1 was detected in chromatin fractions PMID:36050397 PIAS1 is recruited to damaged chromatin, which facilitates MRE11 SUMOylation to enhance MRE11 stability by antagonizing ubiquitylation. |
| GO:0000976 transcription cis-regulatory region binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from mouse Pias1, which binds the TAAT core enhancer of MyoD together with Msx1. Human PIAS1's SAP domain binds A/T-rich DNA in vitro without demonstrated sequence specificity. Reason: DNA binding by the SAP domain is real but low-specificity and accessory to PIAS1's coregulator/E3 roles; the mouse data indicate it can occupy cis-regulatory regions, mainly in complex with Msx1. Retain as non-core. Supporting Evidence: PMID:15133049 it has a strong affinity toward A/T-rich DNA file:human/PIAS1/PIAS1-uniprot.txt In vitro, binds |
| GO:0000976 transcription cis-regulatory region binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS from mouse Pias1 (O88907) for binding to cis-regulatory regions (MyoD core enhancer). Human SAP domain binds A/T-rich DNA in vitro. Reason: As for the IEA: plausible but accessory DNA-binding activity, not a core function. Supporting Evidence: PMID:15133049 it has a strong affinity toward A/T-rich DNA file:human/PIAS1/PIAS1-uniprot.txt In vitro, binds |
| GO:0003714 transcription corepressor activity | TAS PMID:10805787 Distinct roles of the NH2- and COOH-terminal domains of the ... | MODIFY | Summary: TAS from the PIAS1-STAT1 domain-mapping paper. PIAS1 inhibits STAT1 by directly binding the STAT1 dimer and blocking its DNA-binding activity, rather than by bridging STAT1 to repressive machinery as a classical corepressor does. Reason: GO:0140416 transcription regulator inhibitor activity (a regulator that inhibits a transcription regulator via direct binding and/or post-translational modification) precisely matches the mechanism and is already supported by IBA and IDA for PIAS1; 'transcription corepressor activity' implies a recruited cofactor that is not how PIAS1 inhibits STAT1. STAT1 inhibition by PIAS1 does not require STAT1 sumoylation, and PIAS1 is not the E3 for STAT1 (PMID:12764129), reinforcing that this is direct inhibition of a transcription regulator rather than corepressor recruitment. Proposed replacements: transcription regulator inhibitor activity Supporting Evidence: PMID:10805787 A mutant PIAS1 lacking the Stat1-interacting domain failed to inhibit Stat1-mediated gene activation. PMID:10805787 IFN treatment induces the association of PIAS1 and Stat1, which results in the inhibition of Stat1-mediated gene activation. PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:12764129 inhibition of STAT1 by PIAS proteins does not require SUMO modification of STAT1 file:human/PIAS1/PIAS1-deep-research-openscientist.md functions as a **selective transcriptional repressor that does not require SUMOylation of its target** |
| GO:0005515 protein binding | IPI PMID:14752048 Modification of de novo DNA methyltransferase 3a (Dnmt3a) by... | REMOVE | Summary: IPI with mouse Dnmt3a. The paper shows Dnmt3a interacts with Ubc9, PIAS1 and PIASxalpha and is SUMO-1 modified, but the abstract does not attribute Dnmt3a sumoylation specifically to PIAS1. Reason: Generic protein binding is uninformative. The interaction is not disputed, but the paper (abstract-only in cache) does not support a more specific MF for PIAS1 than the SUMO ligase activity already annotated elsewhere. Supporting Evidence: PMID:14752048 Dnmt3a interacts with multiple components of the sumoylation machinery, namely the E2 sumo conjugating enzyme Ubc9 and the E3 sumo ligases PIAS1 and PIASxalpha |
| GO:0005515 protein binding | IPI PMID:15133049 NMR structure of the N-terminal domain of SUMO ligase PIAS1 ... | MODIFY | Summary: IPI with p53 (TP53): GST pull-down shows that the N-terminal four-helix SAP domain of PIAS1 binds p53, a PIAS1 sumoylation substrate. Reason: The paper supports a specific binding function - binding to the p53 transcription factor via the SAP domain - so GO:0002039 p53 binding is more informative than generic protein binding. Proposed replacements: p53 binding Supporting Evidence: PMID:15133049 this domain possesses a binding ability to tumor suppressor p53, a target protein for sumoylation by PIAS1 PMID:11583632 PIAS1 catalyzed the sumoylation of p53 both in U2OS cells and in vitro in a domain-dependent manner |
| GO:0005515 protein binding | IPI PMID:16154161 SUMO-1 modification of centrosomal protein hNinein promotes ... | REMOVE | Summary: IPI with hNinein (Q8N4C6) from a yeast two-hybrid screen confirmed by GST pull-down; hNinein is SUMO-1 modified. Reason: Generic protein binding is uninformative; the paper does not show PIAS1 to be the E3 for hNinein, so no more specific MF is supported. Removal does not imply the interaction is false. Supporting Evidence: PMID:16154161 SUMOylation enhancing enzymes, including PIAS1 and PIASxalpha, as binding |
| GO:0005515 protein binding | IPI PMID:18579533 Regulation of cardiac specific nkx2.5 gene activity by small... | MODIFY | Summary: IPI with Nkx2.5 (P52952), a homeodomain transcription factor. PIAS1 co-associates with Nkx2.5 and, via its RING domain, stimulates SUMO-1 conjugation to Nkx2.5 at K51. Reason: Nkx2.5 is a DNA-binding transcription factor that PIAS1 binds and sumoylates; GO:0140297 DNA-binding transcription factor binding captures the informative content of this interaction. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:18579533 PIAS1 Stimulated SUMO-1 Conjugation to Nkx2.5 PMID:18579533 E3 ligase PIAS proteins PIAS1, PIASx, and PIASy, but not PIAS3, enhanced |
| GO:0005515 protein binding | IPI PMID:21338522 PIAS1 interacts with FLASH and enhances its co-activation of... | MODIFY | Summary: IPI with FLASH/CASP8AP2 (Q9UKL3), a c-Myb coactivator. PIAS1 interacts with FLASH (Y2H, pull-down, co-IP, colocalization), enhances FLASH sumoylation at K1813, and co-activates FLASH in a RING-dependent manner. Reason: FLASH is a transcription coactivator; GO:0001223 transcription coactivator binding is the informative MF supported by this paper, alongside SUMO ligase activity toward FLASH. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:21338522 Taken together PIAS1 seems to function as a SUMO E3 ligase enhancing the sumoylation of FLASH. PMID:21338522 Taken together, these data imply that PIAS1 acts as a co-activator of FLASH in a RING finger-dependent manner |
| GO:0005515 protein binding | IPI PMID:21911577 A physical interaction network of dengue virus and human pro... | REMOVE | Summary: IPI with a dengue virus polyprotein chain from a high-throughput yeast two-hybrid screen of DENV proteins against a human liver library. Reason: Generic protein binding from a high-throughput viral-host Y2H screen; uninformative about PIAS1 function and not followed up for PIAS1. Removal does not imply the interaction is false. Supporting Evidence: PMID:21911577 we used high-throughput yeast two-hybrid assays to screen the 10 DENV proteins against a human liver activation domain library |
| GO:0005515 protein binding | IPI PMID:21965678 SUMOylation and SUMO-interacting motif (SIM) of metastasis t... | MODIFY | Summary: IPI with MTA1 (Q13330), a NuRD corepressor subunit. PIAS proteins enhance SUMO2/3 modification of MTA1, which regulates its corepressor function. Reason: MTA1 is a transcription corepressor; GO:0001222 transcription corepressor binding is more informative than generic protein binding. The ligase activity on MTA1 is captured by the SUMO transferase rows from the same paper. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:21965678 Protein inhibitor of activated STAT (PIAS) proteins enhance SUMOylation of MTA1 |
| GO:0005515 protein binding | IPI PMID:22555612 SUMOylation of Blimp-1 is critical for plasma cell different... | MODIFY | Summary: IPI with Blimp-1/PRDM1 (O75626), a transcriptional repressor and master regulator of plasma cell differentiation; PIAS1 mediates SUMO1 modification of Blimp-1 at K816. Reason: Blimp-1 is a DNA-binding transcription factor; GO:0140297 DNA-binding transcription factor binding is the informative MF. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:22555612 a modification mediated by SUMO E3 ligase PIAS1 |
| GO:0005515 protein binding | IPI PMID:23275563 Development and application of a DNA microarray-based yeast ... | REMOVE | Summary: IPI with huntingtin (HTT) from a DNA-microarray-based yeast two-hybrid screen. The authors report that the HTT-PIAS1 association was not confirmed in their LUMIER validation assay. Reason: Generic protein binding from a Y2H screen that failed orthogonal validation; uninformative and weakly supported. Supporting Evidence: PMID:23275563 The associations of ERCC6L, EVL and HMG20A with HTT were confirmed in LUMIER assays, whereas those with PIAS1 and ZNF451 were not. |
| GO:0005515 protein binding | IPI PMID:23275563 Development and application of a DNA microarray-based yeast ... | REMOVE | Summary: IPI with ataxin-1 (ATXN1) from the same DNA-microarray yeast two-hybrid system paper. Reason: Generic protein binding from a high-throughput Y2H screen; uninformative about PIAS1 function. Removal does not imply the interaction is false. Supporting Evidence: PMID:23275563 PIAS1 (Protein inhibitor of STAT) is a Sumo ligase |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: IPI with p53 from a systematic in situ proximity ligation assay of endogenous protein pairs in HeLa cells. Reason: The endogenous PIAS1-p53 proximity corroborates the well-characterised direct p53 binding by the PIAS1 SAP domain (PMID:15133049) and p53 sumoylation by PIAS1 (PMID:11583632); p53 binding is more informative than generic protein binding. Proposed replacements: p53 binding Supporting Evidence: PMID:25241761 employed a highly sensitive and specific technique, an in situ proximity ligation assay, to investigate 1204 endogenous PPIs in HeLa cells PMID:15133049 this domain possesses a binding ability to tumor suppressor p53, a target protein for sumoylation by PIAS1 |
| GO:0005515 protein binding | IPI PMID:27211601 SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodi... | MODIFY | Summary: IPI with SUMO5 (SUMO1P1, G2XKQ0). Co-IP showed SUMO5 interacts with the SUMO E3s Pc2 and PIAS1 but not PIASx-alpha. Reason: PIAS1 contains a SUMO-interacting motif (UniProt region 462-473 'SUMO1-binding'), and non-covalent SUMO binding is an established feature of PIAS E3s. GO:0032183 SUMO binding is the informative MF here. Biochemical/structural work shows the PIAS C-terminal SIM2 binds SUMO1 and is needed for UBC9-PIAS1-SUMO1 complex formation (PMID:32348746). Proposed replacements: SUMO binding Supporting Evidence: PMID:27211601 SUMO5 specifically interacted with SUMO E3 enzymes Pc2 and PIAS1, but not with PIASx-Ξ± file:human/PIAS1/PIAS1-uniprot.txt SUMO1-binding PMID:32348746 we demonstrate PIAS-SIM2 binds to SUMO1 |
| GO:0005515 protein binding | IPI PMID:28842558 HSP70-Hrd1 axis precludes the oncorepressor potential of N-t... | MODIFY | Summary: IPI with Blimp-1/PRDM1 (O75626) by co-IP and colocalization in lymphoma cells; the paper cites PIAS1 as the E3 catalysing Sumo-1 modification of Blimp-1. Reason: Blimp-1 is a DNA-binding transcription factor; GO:0140297 DNA-binding transcription factor binding is the informative MF. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:28842558 PIAS1 clearly colocalized with Blimp-1 proteins prior to MG132 treatment PMID:28842558 PIAS1 catalyzes the Sumo-1-mediated modification of WT Blimp-1 |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:A0A0S2Z5Q7 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:G5E9A7 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:O00628 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:O14832 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:O43464 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:O43933 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:O60333-2 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:O76024 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P01023 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P02545 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P02545-2 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P04792 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P05129 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P07686 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P19404 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P26378-2 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P28358 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P28799 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P29474 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P35240 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P35240-4 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P37840 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P41219 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P42858 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P45381 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P48643 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P50897 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P51608 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P54252 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P54253 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:P54577 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q13216-2 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q16143 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q16595 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q16637 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q53GS7 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q6NUL7 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q7Z699 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q92870-2 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q9NUW8 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q9P1N4 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: IPI with UniProtKB:Q9UBB4 from a systematic yeast two-hybrid interactome screen of neurodegenerative disease proteins (~30,000 candidate interactions). Not followed up for PIAS1 in this study. Reason: Generic protein binding from a high-throughput Y2H screen is uninformative about PIAS1 molecular function and the paper provides no evidence for a more specific activity (e.g. sumoylation of this partner). Removal reflects lack of functional information, not a claim that the interaction is false. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of βΌ500 ND-related proteins and integration of literature interactions |
| GO:0005634 nucleus | IDA PMID:14752048 Modification of de novo DNA methyltransferase 3a (Dnmt3a) by... | ACCEPT | Summary: IDA (Dnmt3a/SUMO paper) placing PIAS1 in the nucleus. PIAS1 is a predominantly nuclear protein with two predicted NLSs. Reason: Nuclear localization is well established and fundamental to PIAS1 function as a nuclear SUMO E3 and transcriptional coregulator. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus PMID:12393906 Mdm2 is also sumoylated in an in vitro system containing PIASxbeta, PIAS1, and RanBP2 |
| GO:0005634 nucleus | IDA PMID:27068747 Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2Ξ±... | ACCEPT | Summary: IDA (hDREF paper): Myc-PIAS1 forms nuclear foci overlapping hDREF foci, consistent with PML nuclear bodies. Reason: Direct imaging supports nuclear localization. Supporting Evidence: PMID:27068747 Most of hDREF foci overlapped with PIAS1 foci, suggesting that hDREF might exist in the PML nuclear bodies. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Combined automated IEA for nucleus. Reason: Correct; consistent with experimental data. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | ISS GO_REF:0000024 | ACCEPT | Summary: ISS from mouse Pias1 for nucleus. Reason: Correct; consistent with experimental data. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | TAS PMID:9724754 Inhibition of Stat1-mediated gene activation by PIAS1. | ACCEPT | Summary: TAS from the original PIAS1/STAT1 paper; PIAS1 associates with activated STAT1, which acts in the nucleus. Reason: Nuclear localization is well established. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005654 nucleoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for nucleoplasm across PIAS/Siz orthologs. Reason: Correct; PIAS1 is a nucleoplasmic protein enriched in nuclear bodies. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005654 nucleoplasm | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara projection of nucleoplasm from mouse. Reason: Correct. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2997616 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-2997616) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-2997616 PIAS1,4 SUMOylate BRCA1 with SUMO2,3 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2997709 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-2997709) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-2997709 PIAS1,4 SUMOylate BRCA1 with SUMO1 at lysine-109 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3000434 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3000434) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-3000434 PML TRIM27, PIAS1, and PIAS2-1 can each SUMOylate MDM2 with SUMO1 at lysine-182 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3247493 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3247493) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-3247493 PIAS1 SUMOylates SP3 with SUMO1 at lysine-551 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3465545 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3465545) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-3465545 PIAS1,3,4 SUMOylate MTA1 with SUMO2,3 at lysine-509 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3900194 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3900194) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-3900194 PIAS1 SUMOylates DDX5 at lysine-53 with SUMO2 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3968414 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3968414) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-3968414 UBC9 and PIAS1 SUMOylate FOXL2 with SUMO1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4085347 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4085347) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4085347 PIAS1 SUMOylates SAFB at lysine-231 and lysine-294 with SUMO1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4085372 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4085372) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4085372 PIAS1 SUMOylates SAFB at lysine 231 and lysine 294 with SUMO2,3 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4086036 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4086036) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4086036 PIAS1,3 SUMOylate NRIP1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4090281 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4090281) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4090281 PIAS1,2-1 SUMOylate deacetylated HIC1 at lysine-333 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4090288 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4090288) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4090288 PIAS1,3 SUMOylates MBD1 at lysine-499 and lysine-538 of the reference sequence |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4090390 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4090390) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4090390 PIAS1,2-1 SUMOylate AR at lysine-386 and lysine-520 with SUMO1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4090408 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4090408) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4090408 PIAS1,3 SUMOylate ESR1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4341016 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4341016) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4341016 PIAS1 SUMOylates NR3C2 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4546385 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4546385) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4546385 PIAS1,3 SUMOylate NR5A1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4546386 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4546386) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4546386 PIAS1,3 SUMOylate NR5A1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4568848 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4568848) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4568848 PIAS1,2-1 SUMOylate XRCC4 at lysine-210 with SUMO1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4615839 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4615839) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4615839 PIAS1 SUMOylates SATB1 at lysine-744 with SUMO2,3 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4615900 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4615900) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4615900 PIAS1 SUMOylates SATB2 at lysine-233 and lysine-350 with SUMO3 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4615905 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4615905) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4615905 PIAS1 SUMOylates SATB1 at lysine-744 with SUMO1 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4719424 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4719424) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4719424 PIAS1 SUMOylates THRB with SUMO1 at lysine-50, lysine-146, and lysine-443 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4719448 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4719448) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4719448 PIAS1 SUMOylates THRB with SUMO3 at lysine-50, lysine-146, and lysine-443 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4755494 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4755494) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-4755494 PIAS1,2-1 SUMOylate NR5A2 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5228521 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-5228521) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-5228521 PIAS1, PIAS4 SUMOylate CASP8AP2 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6804468 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-6804468) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-6804468 PIAS1 SUMOylates SP3 with SUMO2 at lysine-551 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6804485 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-6804485) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-6804485 PIAS1 and possibly other SUMO E3 ligases SUMOylates L3MBTL2 with SUMO2 at lysine-675 and lysine-700 near the C-terminus |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-877281 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-877281) placing PIAS1 in the nucleoplasm, where it SUMOylates nuclear substrates or binds activated STAT1. Reason: Nucleoplasm is the correct compartment for the PIAS1 reactions curated by Reactome. Supporting Evidence: Reactome:R-HSA-877281 PIAS1 protein interacts directly with phoshorylated STAT1 dimers and inhibit the transcriptional activity of STAT1 by blocking the DNA-binding domain of STAT1 |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | MARK AS OVER ANNOTATED | Summary: IEA from UniProt subcellular location 'Cytoplasm, cytoskeleton', which rests on a partial redistribution of PIAS1 along the cytoskeleton upon interaction with overexpressed CSRP2. Reason: PIAS1 is predominantly nuclear; the cytoskeletal signal is a conditional overexpression-dependent redistribution, not an established physiological residence. Not wrong, but over-represents the evidence. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Interaction with CSRP2 |
| GO:0006974 DNA damage response | IDA PMID:36050397 Crosstalk between SUMOylation and ubiquitylation controls DN... | ACCEPT | Summary: IDA: PIAS1 is the major SUMO E3 for MRE11; it is recruited to damaged chromatin and SUMOylates MRE11 to stabilise it and permit DNA end resection. Consistent with earlier work showing PIAS1/PIAS4 are recruited to DSBs and promote DSB repair. Reason: Direct participation via SUMOylation of DDR proteins (MRE11, BRCA1) is well supported in human cells. Supporting Evidence: PMID:36050397 PIAS1 is recruited to damaged chromatin, which facilitates MRE11 SUMOylation to enhance MRE11 stability by antagonizing ubiquitylation. PMID:20016603 we show that PIAS1 and PIAS4 promote DSB repair and confer IR resistance |
| GO:0007259 cell surface receptor signaling pathway via JAK-STAT | TAS PMID:10805787 Distinct roles of the NH2- and COOH-terminal domains of the ... | MODIFY | Summary: TAS from PMID:10805787 placing PIAS1 in JAK-STAT signaling. PIAS1 does not transduce the signal; it terminates it by binding the activated STAT1 dimer and blocking DNA binding. Reason: The appropriate process is the negative regulation term GO:0046426, already supported for PIAS1 by IDA and IBA. Proposed replacements: negative regulation of receptor signaling pathway via JAK-STAT Supporting Evidence: PMID:10805787 IFN treatment induces the association of PIAS1 and Stat1, which results in the inhibition of Stat1-mediated gene activation. PMID:10805787 A mutant PIAS1 lacking the Stat1-interacting domain failed to inhibit Stat1-mediated gene activation. PMID:17540171 inhibits immune responses by selectively blocking the |
| GO:0007283 spermatogenesis | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara projection from rat. PIAS1 is most highly expressed in testis, but no data show PIAS1 executes a step of spermatogenesis; Pias1-null mice are viable. Reason: Expression in testis and sumoylation of germ-cell transcription factors do not amount to a direct role in spermatogenesis; this developmental process is at best an indirect, non-core consequence. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Expressed in numerous tissues with highest level in |
| GO:0008270 zinc ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO IEA based on the SP-RING-type zinc finger (aa 320-405). The SP-RING coordinates zinc and is required for UBE2I binding and E3 activity (C351 mutation abolishes UBE2I binding). Reason: Zinc coordination by the SP-RING is a structural requirement of the catalytic E3 module. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SP-RING-type file:human/PIAS1/PIAS1-uniprot.txt C->A,S: Loss of UBE2I-binding; almost complete loss |
| GO:0008542 visual learning | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara projection from rat Pias1. Rat hippocampal studies link PIAS1-mediated STAT1 sumoylation to learning behaviour, which is a downstream organismal outcome of transcription factor modification. Reason: Behavioural phenotypes are indirect consequences of PIAS1's molecular activity; 'visual learning' does not describe a process PIAS1 itself executes and is not core for human PIAS1. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Functions as an E3-type small ubiquitin-like modifier (SUMO) |
| GO:0016605 PML body | IEA GO_REF:0000120 | ACCEPT | Summary: IEA for PML body. PIAS1 localises to PML nuclear bodies, where it SUMOylates PML. Reason: Supported by UniProt (by similarity to mouse) and by the overlap of PIAS1 foci with PML-body-associated hDREF foci. PIAS1 is a constituent PML-NB protein recruited in a SIM-dependent manner (PMID:27099310). Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Nucleus, PML body PMID:27068747 Most of hDREF foci overlapped with PIAS1 foci, suggesting that hDREF might exist in the PML nuclear bodies. PMID:27099310 PIAS1 is a constituent PML-NB protein. file:human/PIAS1/PIAS1-deep-research-openscientist.md Within the nucleus, PIAS1 is a constituent of **promyelocytic leukemia nuclear bodies (PML-NBs)**. |
| GO:0016605 PML body | ISS GO_REF:0000024 | ACCEPT | Summary: ISS from mouse Pias1: colocalizes with PML bodies. Reason: Consistent with human imaging data and with PIAS1 SUMOylating PML. PIAS1 is a constituent PML-NB protein recruited in a SIM-dependent manner (PMID:27099310). Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Nucleus, PML body PMID:27068747 Most of hDREF foci overlapped with PIAS1 foci, suggesting that hDREF might exist in the PML nuclear bodies. PMID:27099310 PIAS1 is a constituent PML-NB protein. file:human/PIAS1/PIAS1-deep-research-openscientist.md Within the nucleus, PIAS1 is a constituent of **promyelocytic leukemia nuclear bodies (PML-NBs)**. |
| GO:0016607 nuclear speck | IEA GO_REF:0000044 | ACCEPT | Summary: IEA from UniProt subcellular location 'Nucleus speckle', which is based on experimental data (PMID:12393906, PMID:9177271). Reason: Nuclear speckle localization is experimentally documented. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt speckle {ECO:0000269|PubMed:12393906, ECO:0000269|PubMed:9177271} |
| GO:0016925 protein sumoylation | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for protein sumoylation across the PIAS/Siz E3 family. Reason: Core process; PIAS1 is an SP-RING E3 that directly catalyses SUMO conjugation to many substrates. Supporting Evidence: PMID:11583632 PIAS1 catalyzed the sumoylation of p53 both in U2OS cells and in vitro in a domain-dependent manner PMID:20972456 the E3 activity of the five mammalian PIAS proteins and their yeast homologues, Siz1 and Siz2, is associated with a different RING-like domain, SP-RING |
| GO:0016925 protein sumoylation | IDA PMID:18579533 Regulation of cardiac specific nkx2.5 gene activity by small... | ACCEPT | Summary: IDA: PIAS1 stimulates SUMO-1 conjugation to Nkx2.5 in a RING-domain-dependent manner. Reason: Direct experimental support for PIAS1 performing substrate sumoylation. Supporting Evidence: PMID:18579533 PIAS1 Stimulated SUMO-1 Conjugation to Nkx2.5 |
| GO:0016925 protein sumoylation | IEA GO_REF:0000120 | ACCEPT | Summary: Combined automated IEA for protein sumoylation. Reason: Core process; correct. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Functions as an E3-type small ubiquitin-like modifier (SUMO) |
| GO:0016925 protein sumoylation | ISS GO_REF:0000024 | ACCEPT | Summary: ISS from mouse Pias1 for protein sumoylation. Reason: Core process; correct. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Functions as an E3-type small ubiquitin-like modifier (SUMO) |
| GO:0016925 protein sumoylation | TAS Reactome:R-HSA-3108232 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3108232) for PIAS1-catalysed protein sumoylation. Reason: Core process; Reactome curates PIAS1 as the E3 for this SUMOylation event. Supporting Evidence: Reactome:R-HSA-3108232 SUMO proteins are conjugated to lysine residues of target proteins via an isopeptide bond with the C-terminal glycine of SUMO |
| GO:0016925 protein sumoylation | TAS Reactome:R-HSA-3247493 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3247493) for PIAS1-catalysed protein sumoylation. Reason: Core process; Reactome curates PIAS1 as the E3 for this SUMOylation event. Supporting Evidence: Reactome:R-HSA-3247493 PIAS1 SUMOylates SP3 with SUMO1 at lysine-551 |
| GO:0016925 protein sumoylation | TAS Reactome:R-HSA-3465545 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-3465545) for PIAS1-catalysed protein sumoylation. Reason: Core process; Reactome curates PIAS1 as the E3 for this SUMOylation event. Supporting Evidence: Reactome:R-HSA-3465545 PIAS1,3,4 SUMOylate MTA1 with SUMO2,3 at lysine-509 |
| GO:0016925 protein sumoylation | TAS Reactome:R-HSA-6804468 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-6804468) for PIAS1-catalysed protein sumoylation. Reason: Core process; Reactome curates PIAS1 as the E3 for this SUMOylation event. Supporting Evidence: Reactome:R-HSA-6804468 PIAS1 SUMOylates SP3 with SUMO2 at lysine-551 |
| GO:0016925 protein sumoylation | TAS Reactome:R-HSA-6804485 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-6804485) for PIAS1-catalysed protein sumoylation. Reason: Core process; Reactome curates PIAS1 as the E3 for this SUMOylation event. Supporting Evidence: Reactome:R-HSA-6804485 PIAS1 and possibly other SUMO E3 ligases SUMOylates L3MBTL2 with SUMO2 at lysine-675 and lysine-700 near the C-terminus |
| GO:0019789 SUMO transferase activity | EXP PMID:12356736 Transcription factor Sp3 is silenced through SUMO modificati... | ACCEPT | Summary: EXP: recombinant GST-PIAS1 interacts with Ubc9 and drives efficient SUMO-1/SUMO-2 conjugation to Sp3 in vitro, defining PIAS1 as an E3 for Sp3. Reason: Direct biochemical evidence for SUMO transfer activity. Supporting Evidence: PMID:12356736 PIAS1 strongly stimulated SUMO conjugation to Sp3, thus acting as an E3 ligase for SUMO conjugation to Sp3 PMID:12356736 This result identifies PIAS1 as an acting E3 ligase for SUMO conjugation to Sp3 |
| GO:0019789 SUMO transferase activity | EXP PMID:12393906 Sumoylation of Mdm2 by protein inhibitor of activated STAT (... | ACCEPT | Summary: EXP: PIAS1 sumoylates Mdm2 in cells and in a reconstituted in vitro system. Reason: Direct evidence for SUMO transfer to Mdm2 (abstract-only in cache, but explicit). Supporting Evidence: PMID:12393906 Mdm2 is also sumoylated in an in vitro system containing PIASxbeta, PIAS1, and RanBP2 |
| GO:0019789 SUMO transferase activity | EXP PMID:17283066 An acetylation/deacetylation-SUMOylation switch through a ph... | ACCEPT | Summary: EXP: PIAS1 acts as a bona fide SUMO E3 for the HIC1 tumour suppressor at its psiKXEP motif. Reason: Direct evidence for SUMO transfer to HIC1. Supporting Evidence: PMID:17283066 a bona fide E3 ligase for HIC1, PIAS1 |
| GO:0019789 SUMO transferase activity | EXP PMID:20972456 SUMO E3 ligase activity of TRIM proteins. | ACCEPT | Summary: EXP annotation to the TRIM SUMO E3 paper. The cached text discusses PIAS proteins as established SP-RING SUMO E3s but its experiments focus on TRIM proteins and PIASy; PIAS1 is not explicitly assayed in the cached text. Reason: The activity is unquestionably correct for PIAS1 and the curator (likely Reactome) may have drawn on supplementary data; per policy we defer rather than remove an experimental annotation whose full basis we cannot see. Supporting Evidence: PMID:20972456 the E3 activity of the five mammalian PIAS proteins and their yeast homologues, Siz1 and Siz2, is associated with a different RING-like domain, SP-RING PMID:11583632 PIAS1 catalyzed the sumoylation of p53 both in U2OS cells and in vitro in a domain-dependent manner |
| GO:0019789 SUMO transferase activity | EXP PMID:21965678 SUMOylation and SUMO-interacting motif (SIM) of metastasis t... | ACCEPT | Summary: EXP: PIAS proteins, including PIAS1, enhance SUMO2/3 modification of MTA1. Reason: Supports SUMO transfer to MTA1 (abstract-only in cache). Supporting Evidence: PMID:21965678 Protein inhibitor of activated STAT (PIAS) proteins enhance SUMOylation of MTA1 |
| GO:0019789 SUMO transferase activity | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA machine-learning IEA for SUMO transferase activity. Reason: Correct; matches experimental data. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Functions as an E3-type small ubiquitin-like modifier (SUMO) |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-2997616 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-2997616) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-2997616 PIAS1,4 SUMOylate BRCA1 with SUMO2,3 |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-2997709 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-2997709) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-2997709 PIAS1,4 SUMOylate BRCA1 with SUMO1 at lysine-109 |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-4086036 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4086036) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-4086036 PIAS1,3 SUMOylate NRIP1 |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-4090288 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4090288) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-4090288 PIAS1,3 SUMOylates MBD1 at lysine-499 and lysine-538 of the reference sequence |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-4090408 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4090408) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-4090408 PIAS1,3 SUMOylate ESR1 |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-4546385 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4546385) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-4546385 PIAS1,3 SUMOylate NR5A1 |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-4546386 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-4546386) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-4546386 PIAS1,3 SUMOylate NR5A1 |
| GO:0019789 SUMO transferase activity | TAS Reactome:R-HSA-5228521 | ACCEPT | Summary: Reactome TAS (Reactome:R-HSA-5228521) curating PIAS1 as the E3 enzyme in a SUMOylation reaction. Reason: Correct; PIAS1 SUMO transferase activity is well established. Supporting Evidence: Reactome:R-HSA-5228521 PIAS1, PIAS4 SUMOylate CASP8AP2 |
| GO:0019899 enzyme binding | IPI PMID:17087506 Human cystathionine beta-synthase is a target for sumoylatio... | TOO GENERAL | Summary: IPI with cystathionine beta-synthase (CBS), identified in a yeast two-hybrid screen along with other sumoylation pathway components; CBS is SUMO-1 modified. Reason: 'Enzyme binding' is a generic binding term that conveys no functional information here; the CBS interaction reflects CBS being a sumoylation substrate, which is better represented by PIAS1's SUMO ligase activity. Removal does not dispute the interaction. TOO_GENERAL rather than REMOVE: ubiquitin protein ligase binding, kept in this review, entails this term, so the claim is true but less informative. Supporting Evidence: PMID:17087506 have identified several components of the sumoylation pathway including Ubc9, PIAS1, PIAS3, Pc2, and RanBPM |
| GO:0019904 protein domain specific binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from rat for protein domain specific binding. Reason: The row is transferred from the rat ortholog, where it rests on direct-assay and physical-interaction annotations, and PIAS1 does make domain-mapped contacts of this kind: its N-terminus binds the C-terminus of MSX1 and recruits MSX1 to target promoters, as this review records. The term names neither the partner nor the consequence, but it is true as stated, and a true annotation is not removed for being uninformative. Such contacts serve the SUMO ligase and coregulator functions that are core to PIAS1, so this row is kept as non-core. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt terminus) with MSX1 (via C-terminus); the interaction is required for |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from mouse for ubiquitin protein ligase binding. Human PIAS1 binds and SUMOylates the ubiquitin ligase Mdm2, and has been linked to ubiquitin ligase-dependent turnover of substrates. Reason: Plausible (e.g. Mdm2 is a PIAS1 substrate) but peripheral to the core E3/coregulator functions. Supporting Evidence: PMID:12393906 Mdm2 is also sumoylated in an in vitro system containing PIASxbeta, PIAS1, and RanBP2 |
| GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from mouse: PIAS1-mediated sumoylation primes substrates such as PML and C/EBPbeta for ubiquitin-mediated degradation. Reason: SUMO-primed degradation is a real downstream consequence of PIAS1 E3 activity on specific substrates, but not a core function. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt their ubiquitin-mediated degradation (By similarity) file:human/PIAS1/PIAS1-uniprot.txt adipogenesis by promoting the SUMOylation and degradation of CEBPB |
| GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS from mouse Pias1 for SUMO-primed proteasomal degradation (PML, C/EBPbeta). Reason: As above; substrate-specific downstream consequence. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt their ubiquitin-mediated degradation (By similarity) file:human/PIAS1/PIAS1-uniprot.txt adipogenesis by promoting the SUMOylation and degradation of CEBPB |
| GO:0033235 positive regulation of protein sumoylation | IDA PMID:17696781 Sumoylation of the zinc finger protein ZXDC enhances the fun... | MODIFY | Summary: IDA from the ZXDC sumoylation paper, where multiple SUMO E3 ligases facilitate ZXDC sumoylation. As the E3 itself, PIAS1 directly carries out protein sumoylation rather than regulating it. Reason: For a SUMO E3 ligase the participation term GO:0016925 protein sumoylation is appropriate; 'positive regulation of protein sumoylation' should be reserved for factors that modulate the E1/E2/E3 machinery. Proposed replacements: protein sumoylation Supporting Evidence: PMID:17696781 Multiple SUMO E3 ligase enzymes and HDAC4 can facilitate ZXDC sumoylation |
| GO:0033235 positive regulation of protein sumoylation | IDA PMID:21965678 SUMOylation and SUMO-interacting motif (SIM) of metastasis t... | MODIFY | Summary: IDA: PIAS proteins enhance SUMOylation of MTA1. PIAS1 acts as the E3 and so directly performs the sumoylation. Reason: Use the participation term GO:0016925 protein sumoylation for the E3 rather than a regulation term. Proposed replacements: protein sumoylation Supporting Evidence: PMID:21965678 Protein inhibitor of activated STAT (PIAS) proteins enhance SUMOylation of MTA1 |
| GO:0033235 positive regulation of protein sumoylation | IEA GO_REF:0000107 | MODIFY | Summary: Ensembl Compara projection from rat for positive regulation of protein sumoylation. Reason: PIAS1 is a SUMO E3 that directly catalyses sumoylation; GO:0016925 protein sumoylation is the appropriate term. Proposed replacements: protein sumoylation Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Functions as an E3-type small ubiquitin-like modifier (SUMO) |
| GO:0034399 nuclear periphery | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from mouse: Pias1 localises with Msx1 to the nuclear periphery in myoblasts. Reason: Context-specific localization dependent on Msx1; not a general residence of PIAS1. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt to the nuclear periphery, whereby MSX1 is brought into the proximity of |
| GO:0034399 nuclear periphery | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ISS from mouse Pias1: nuclear periphery localization with Msx1. Reason: Context-specific localization dependent on Msx1. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt to the nuclear periphery, whereby MSX1 is brought into the proximity of |
| GO:0042127 regulation of cell population proliferation | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara projection from mouse for regulation of cell population proliferation. Reason: Proliferation effects are indirect outcomes of PIAS1 regulating transcription factors (STAT1, NF-kB, p53, KLF8); the term is too broad and indirect to describe PIAS1 function. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt role as a transcriptional coregulation in various cellular pathways |
| GO:0042127 regulation of cell population proliferation | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: ISS from mouse Pias1 for regulation of cell population proliferation. Reason: Indirect downstream outcome of transcriptional coregulation. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt role as a transcriptional coregulation in various cellular pathways |
| GO:0043066 negative regulation of apoptotic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara projection from rat for negative regulation of apoptotic process. Reason: Any anti-apoptotic effect is an indirect consequence of PIAS1 modulating transcription factors such as p53 and NF-kB; not a direct role in apoptosis. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt role as a transcriptional coregulation in various cellular pathways |
| GO:0045444 fat cell differentiation | IEA GO_REF:0000107 | MODIFY | Summary: Ensembl Compara projection from mouse: Pias1 SUMOylates C/EBPbeta, promoting its degradation, and thereby restrains adipogenesis. Reason: The mouse source data (PMID:24061474) show PIAS1 overexpression inhibits and knockdown promotes adipogenesis, dependent on its E3 activity, i.e. negative regulation of fat cell differentiation rather than participation in differentiation itself. Aligned with the mouse Pias1 review, which modifies the source IDA row the same way. A substrate-specific, non-core context of PIAS1 E3 activity. Proposed replacements: negative regulation of fat cell differentiation Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt adipogenesis by promoting the SUMOylation and degradation of CEBPB PMID:24061474 adipogenesis was inhibited by overexpression of wild-type PIAS1 and promoted by knockdown of PIAS1 |
| GO:0045893 positive regulation of DNA-templated transcription | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from rat. PIAS1 can enhance transcription in some contexts, e.g. co-activating FLASH/c-Myb and androgen receptor. Reason: Context-dependent coactivation is documented but secondary to the predominant inhibitory role of PIAS1. Supporting Evidence: PMID:21338522 Taken together, these data imply that PIAS1 acts as a co-activator of FLASH in a RING finger-dependent manner |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:15280358 ZNF76, a novel transcriptional repressor targeting TATA-bind... | KEEP AS NON CORE | Summary: IDA (acts upstream of): overexpression of PIAS1 with SUMO-1 SUMOylates the TBP-targeting repressor ZNF76, disrupting the ZNF76-TBP interaction and partially relieving repression of p53-mediated transactivation. Reason: The effect is real but indirect (relief of a repressor via substrate sumoylation) and observed under overexpression; non-core. Supporting Evidence: PMID:15280358 Overexpression of PIAS1 and SUMO-1 abolishes the interaction between ZNF76 and TBP and partially relieves the repressive effect of ZNF76 |
| GO:0046426 negative regulation of receptor signaling pathway via JAK-STAT | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for negative regulation of receptor signaling via JAK-STAT, with human PIAS1 among the experimental sources (expected and appropriate). Reason: Core process: PIAS1 is the founding inhibitor of STAT1 signaling, confirmed in Pias1-null mice. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:15311277 PIAS1 selectively regulates a subset of IFN-gamma- or IFN-beta-inducible genes by interfering with the recruitment of STAT1 to the gene promoter PMID:17540171 inhibits immune responses by selectively blocking the |
| GO:0046426 negative regulation of receptor signaling pathway via JAK-STAT | IDA PMID:9724754 Inhibition of Stat1-mediated gene activation by PIAS1. | ACCEPT | Summary: IDA: PIAS1 blocks STAT1 DNA binding and inhibits IFN-induced STAT1-mediated gene activation; association requires STAT1 Tyr701 phosphorylation. Reason: Founding observation for PIAS1, later supported genetically in knockout mice. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:15311277 PIAS1 selectively regulates a subset of IFN-gamma- or IFN-beta-inducible genes by interfering with the recruitment of STAT1 to the gene promoter PMID:17540171 inhibits immune responses by selectively blocking the |
| GO:0051152 positive regulation of smooth muscle cell differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from rat for positive regulation of smooth muscle cell differentiation (PIAS1 interacts with CSRP2 and has been linked to SRF-dependent smooth-muscle gene programs). Reason: Tissue-specific downstream context of PIAS1 coregulator activity; non-core. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Interaction with CSRP2 |
| GO:0060261 positive regulation of transcription initiation by RNA polymerase II | IDA PMID:15280358 ZNF76, a novel transcriptional repressor targeting TATA-bind... | KEEP AS NON CORE | Summary: IDA: PIAS1-mediated sumoylation of ZNF76 at K411 abolishes ZNF76-TBP interaction, partially relieving ZNF76 repression of TBP-dependent transcription. Reason: Indirect effect via a single substrate in overexpression assays; retained as non-core. Supporting Evidence: PMID:15280358 ZNF76 is sumoylated by PIAS1 at lysine 411 PMID:15280358 Overexpression of PIAS1 and SUMO-1 abolishes the interaction between ZNF76 and TBP and partially relieves the repressive effect of ZNF76 |
| GO:0061665 SUMO ligase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for SUMO ligase activity across the PIAS/Siz SP-RING family. Reason: Core MF; the SP-RING E3 activity is deeply conserved from yeast Siz1/Siz2 to human PIAS1. Supporting Evidence: PMID:20972456 the E3 activity of the five mammalian PIAS proteins and their yeast homologues, Siz1 and Siz2, is associated with a different RING-like domain, SP-RING PMID:11583632 PIAS1 catalyzed the sumoylation of p53 both in U2OS cells and in vitro in a domain-dependent manner |
| GO:0061665 SUMO ligase activity | IDA PMID:15280358 ZNF76, a novel transcriptional repressor targeting TATA-bind... | ACCEPT | Summary: IDA: PIAS1 SUMOylates ZNF76 at lysine 411. Reason: Direct support for E3 activity. Supporting Evidence: PMID:15280358 ZNF76 is sumoylated by PIAS1 at lysine 411 |
| GO:0061665 SUMO ligase activity | IDA PMID:16337145 Acetylation and alternative splicing regulate ZNF76-mediated... | ACCEPT | Summary: IDA from the ZNF76 acetylation/splicing follow-up, which builds on PIAS1-mediated ZNF76 sumoylation; the abstract does not itself restate the ligase assay. Reason: PIAS1 SUMO ligase activity toward ZNF76 is established in PMID:15280358; defer to the curator for this abstract-only follow-up paper. Supporting Evidence: PMID:16337145 We previously showed that ZNF76 is a general transcription repressor targeting PMID:15280358 ZNF76 is sumoylated by PIAS1 at lysine 411 |
| GO:0061665 SUMO ligase activity | IDA PMID:18579533 Regulation of cardiac specific nkx2.5 gene activity by small... | ACCEPT | Summary: IDA: PIAS1 stimulates SUMO-1 conjugation to Nkx2.5; a RING mutant is defective. Reason: Direct support for E3 activity. Supporting Evidence: PMID:18579533 PIAS1 Stimulated SUMO-1 Conjugation to Nkx2.5 |
| GO:0061665 SUMO ligase activity | IDA PMID:27068747 Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2Ξ±... | ACCEPT | Summary: IDA: GST-PIAS1 used as a known positive-control SUMO E3 for Mi2alpha in in vitro SUMOylation reactions. Reason: In vitro E3 activity of recombinant PIAS1 shown. Supporting Evidence: PMID:27068747 known E3 ligases (GST-PIAS1 or GST-Pc2) |
| GO:0061665 SUMO ligase activity | IDA PMID:36050397 Crosstalk between SUMOylation and ubiquitylation controls DN... | ACCEPT | Summary: IDA: PIAS1 is the major SUMO E3 for MRE11; purified PIAS1 enhances SUMO2 modification of MRE11 in vitro, and knockdown reduces MRE11 SUMOylation in cells. Reason: Strong direct biochemical and cellular evidence. Supporting Evidence: PMID:36050397 PIAS1 is the major SUMO E3 ligase for MRE11 PMID:36050397 An in vitro SUMOylation assay also revealed that SUMO2 modification of MRE11 was greatly enhanced by PIAS1 |
| GO:0061665 SUMO ligase activity | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara projection from mouse for SUMO ligase activity. Reason: Core MF; correct. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt Functions as an E3-type small ubiquitin-like modifier (SUMO) |
| GO:0065004 protein-DNA complex assembly | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Ensembl Compara projection from rat for protein-DNA complex assembly. Reason: PIAS1 predominantly inhibits transcription factor-DNA complex formation (STAT1, p65); promotion of complex assembly may occur for specific partners (e.g. SUMO-stabilised Nkx2.5 complexes, Msx1) but is not a general PIAS1 activity. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:15657437 PIAS1 blocks the DNA binding activity of p65 both in vitro and in vivo |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from mouse (SynGO-type annotation) placing Pias1 at glutamatergic synapses. Reason: PIAS1 is primarily nuclear; a synaptic pool is reported in mouse but is peripheral to its core nuclear functions. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0099523 presynaptic cytosol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from mouse placing Pias1 in presynaptic cytosol. Reason: Peripheral to the predominantly nuclear localization of PIAS1. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0099524 postsynaptic cytosol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from mouse placing Pias1 in postsynaptic cytosol. Reason: Peripheral to the predominantly nuclear localization of PIAS1. Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0140297 DNA-binding transcription factor binding | IEA GO_REF:0000107 | ACCEPT | Summary: Ensembl Compara projection from mouse for DNA-binding transcription factor binding. Human PIAS1 directly binds STAT1 dimers, NF-kB p65, p53, Sp3, Nkx2.5, Blimp-1 and many nuclear receptors. Reason: Binding transcription factors is central to PIAS1's coregulator and E3 functions. Supporting Evidence: PMID:10805787 A mutant PIAS1 lacking the Stat1-interacting domain failed to inhibit Stat1-mediated gene activation. PMID:15133049 this domain possesses a binding ability to tumor suppressor p53, a target protein for sumoylation by PIAS1 file:human/PIAS1/PIAS1-uniprot.txt TP53 and STAT1 |
| GO:0140416 transcription regulator inhibitor activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for transcription regulator inhibitor activity, with human PIAS1 among the experimental sources. Reason: Core MF: PIAS1 inhibits activated STAT1 and NF-kB p65 by directly binding them and blocking DNA binding. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:15657437 PIAS1 blocks the DNA binding activity of p65 both in vitro and in vivo PMID:17540171 inhibits immune responses by selectively blocking the PMID:18031232 PIAS proteins do not operate merely as SUMO E3s, since their co-regulator effects are often independent of their RING finger but dependent on their SIM (SUMO-interacting motif) or SAP (scaffold attachment factor-A/B/acinus/PIAS) domain capable of interacting with DNA. |
| GO:0140416 transcription regulator inhibitor activity | IDA PMID:9724754 Inhibition of Stat1-mediated gene activation by PIAS1. | ACCEPT | Summary: IDA: PIAS1 blocks the DNA-binding activity of STAT1 and inhibits STAT1-mediated gene activation. Reason: Core MF, directly demonstrated. Supporting Evidence: PMID:9724754 PIAS1, but not other PIAS proteins, blocked the DNA binding activity of Stat1 and inhibited Stat1-mediated gene activation in response to interferon PMID:17540171 inhibits immune responses by selectively blocking the |
| GO:1904377 positive regulation of protein localization to cell periphery | IEA GO_REF:0000107 | MODIFY | Summary: Ensembl Compara projection from mouse for positive regulation of protein localization to cell periphery. The likely biological basis (Pias1 recruiting Msx1 to the nuclear periphery) concerns the nuclear periphery, not the cell periphery. Reason: The projected term mis-states the compartment. The mouse source (PMID:16600910) shows Pias1 tethering Msx1 at the nuclear periphery, captured by GO:1990139 protein localization to nuclear periphery; aligned with the mouse Pias1 review, which modifies the source IDA row the same way. A peripheral, context-specific (non-core) role. Proposed replacements: protein localization to nuclear periphery Supporting Evidence: file:human/PIAS1/PIAS1-uniprot.txt to the nuclear periphery, whereby MSX1 is brought into the proximity of |
| GO:0043124 negative regulation of canonical NF-kappaB signal transduction | IDA PMID:15657437 Negative regulation of NF-kappaB signaling by PIAS1. | NEW | Summary: PIAS1 binds the p65 subunit of NF-kB after its cytokine-induced nuclear translocation and blocks p65 DNA binding in vitro and in vivo; Pias1-null cells show increased p65 promoter occupancy and elevated expression of a subset of NF-kB target genes, and null mice show elevated proinflammatory cytokines. Reason: Participation: PIAS1 itself performs the inhibitory step (direct binding of p65 and occlusion of its DNA-binding activity), the same mechanism by which it inhibits STAT1. Comparator check (QuickGO, 2026-10): other direct NF-kB inhibitors NFKBIA and TNFAIP3, and the paralog PIAS4, carry GO:0043124, so the term is used for gene products standing in this role. No current PIAS1 annotation covers NF-kB inhibition. Supporting Evidence: PMID:15657437 PIAS1 blocks the DNA binding activity of p65 both in vitro and in vivo PMID:15657437 The binding of PIAS1 to p65 inhibits cytokine-induced NF-kappaB-dependent gene activation PMID:17540171 inhibits immune responses by selectively blocking the binding of NF-kappaB and STAT1 to gene promoters PMID:17540171 Upon TNF treatment, wild-type PIAS1, but not the Ser90A mutant, becomes rapidly associated with the promoters of NF-kappaB target genes file:human/PIAS1/PIAS1-deep-research-openscientist.md Upon cytokine stimulation, the p65 (RelA) subunit translocates to the nucleus and interacts with PIAS1. |
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Download this section (compressed HTML)Q: Does PIAS1 inhibition of STAT1 and NF-kB p65 DNA binding require its SP-RING E3 activity, or is it a purely binding-based (ligase-independent) mechanism in physiological settings?
Q: To what extent are PIAS1 and PIAS4 redundant in the DNA double-strand break response, and which substrates (MRE11, BRCA1, 53BP1) are PIAS1-specific in vivo?
Q: What determines PIAS1 SUMO paralog selectivity (SUMO1 versus SUMO2/3) on substrates such as MTA1 and MRE11?
Q: Does the SAP domain confer any sequence preference in DNA binding that targets PIAS1 to specific cis-regulatory regions in human cells, as suggested for mouse Pias1 with Msx1?
Q: Does PIAS1 restrict incoming HSV-1 genomes at PML nuclear bodies through SUMO1 deposition on specific viral or host substrates, and how redundant is this with PIAS4?
Experiment: Reconstitute PIAS1-knockout human cells with wild-type PIAS1, an SP-RING catalytic mutant (C351S) and a STAT1-binding-deficient C-terminal deletion; measure IFN-gamma- and TNF-induced target gene expression, STAT1/p65 ChIP occupancy and STAT1/p65 sumoylation.
Hypothesis: PIAS1 inhibits STAT1 and p65 target genes independently of its E3 activity.
Type: genetic complementation
Experiment: Quantitative SUMO2/3 proteomics (His-SUMO or K0-SUMO enrichment) after ionizing radiation in PIAS1, PIAS4 and double knockout cells to define PIAS1-specific DSB substrates, coupled with end-resection (RPA/BrdU ssDNA) assays.
Hypothesis: PIAS1 is a non-redundant E3 for a defined subset of DSB-associated substrates.
Type: proteomics
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