| UniProt ID | PIAS3_MOUSE | |
|---|---|---|
| UniProt AC | O54714 | |
| Protein Name | E3 SUMO-protein ligase PIAS3 | |
| Gene Name | Pias3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 628 | |
| Subcellular Localization | Cytoplasm . Nucleus . Nucleus speckle . Colocalizes with MITF in the nucleus (PubMed:11709556). Colocalizes with GFI1 in nuclear dots (PubMed:11060035). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349). | |
| Protein Description | Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. Repressor of STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Repressor of MITF transcriptional activity. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1 (By similarity). Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity).. | |
| Protein Sequence | MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPGPLAPIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILNSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSAVQEGIQPESKKRVEVIDLTIESSSDEEDLPPTKKHCPVTSAAIPALPGSKGALTSGHQPSSVLRSPAMGTLGSDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYGPSVITSLDEQDTLGHFFQYRGTPSHFLGPLAPTLGSSHRSSTPAPPPGRVSSIVAPGSSLREGHGGPLPSGPSLTGCRSDVISLD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAELGELKH ------CCCHHHHHH | 22.26 | - | |
| 295 | Asymmetric dimethylarginine | KLRAKGIRNPDHSRA HHHHCCCCCCHHHHH | 58.24 | - | |
| 404 | Phosphorylation | IQFMEDGSWCPMKPK EEECCCCCCCCCCCC | 37.51 | - | |
| 423 | Phosphorylation | EVCPPPGYGLDGLQY CCCCCCCCCCCCHHH | 21.93 | 29514104 | |
| 430 | Phosphorylation | YGLDGLQYSAVQEGI CCCCCHHHHHHHCCC | 12.02 | 29514104 | |
| 454 | Phosphorylation | VIDLTIESSSDEEDL EEEEEECCCCCCCCC | 31.15 | 22817900 | |
| 455 | Phosphorylation | IDLTIESSSDEEDLP EEEEECCCCCCCCCC | 29.08 | - | |
| 456 | Phosphorylation | DLTIESSSDEEDLPP EEEECCCCCCCCCCC | 59.32 | - | |
| 472 | Phosphorylation | KKHCPVTSAAIPALP CCCCCCCCCCCCCCC | 18.88 | - | |
| 492 | Phosphorylation | LTSGHQPSSVLRSPA CCCCCCCCHHHCCCC | 26.89 | - | |
| 583 | Phosphorylation | TLGSSHRSSTPAPPP CCCCCCCCCCCCCCC | 32.89 | 23527152 | |
| 585 | Phosphorylation | GSSHRSSTPAPPPGR CCCCCCCCCCCCCCC | 25.39 | 24759943 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PIAS3_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PIAS3_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PIAS3_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PIAS3_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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