UniProtKB - O88907 (PIAS1_MOUSE)
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Protein
E3 SUMO-protein ligase PIAS1
Gene
Pias1
Organism
Mus musculus (Mouse)
Status
Functioni
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, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA (By similarity). The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (PubMed:24061474).By similarity2 Publications
Catalytic activityi
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
: protein sumoylation Pathwayi
This protein is involved in the pathway protein sumoylation, which is part of Protein modification.View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 320 – 397 | SP-RING-typePROSITE-ProRule annotationAdd BLAST | 78 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- enzyme binding Source: MGI
- protein C-terminus binding Source: Ensembl
- protein domain specific binding Source: Ensembl
- SUMO ligase activity Source: MGI
- SUMO transferase activity Source: MGI
- transcription corepressor activity Source: MGI
- transcription factor binding Source: UniProtKB
- ubiquitin protein ligase binding Source: BHF-UCL
- zinc ion binding Source: InterPro
GO - Biological processi
- fat cell differentiation Source: UniProtKB
- G1/S transition of mitotic cell cycle Source: Ensembl
- JAK-STAT cascade Source: MGI
- negative regulation of apoptotic process Source: Ensembl
- negative regulation of transcription by RNA polymerase II Source: BHF-UCL
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
- positive regulation of protein sumoylation Source: UniProtKB
- positive regulation of smooth muscle cell differentiation Source: Ensembl
- positive regulation of transcription, DNA-templated Source: Ensembl
- protein-DNA complex assembly Source: Ensembl
- protein sumoylation Source: UniProtKB
- regulation of cell proliferation Source: UniProtKB
- spermatogenesis Source: Ensembl
- transcription, DNA-templated Source: UniProtKB-KW
- visual learning Source: Ensembl
Keywordsi
Molecular function | DNA-binding, Transferase |
Biological process | Transcription, Transcription regulation, Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-3108214. SUMOylation of DNA damage response and repair proteins. R-MMU-3232118. SUMOylation of transcription factors. R-MMU-4551638. SUMOylation of chromatin organization proteins. R-MMU-5696395. Formation of Incision Complex in GG-NER. R-MMU-877312. Regulation of IFNG signaling. |
UniPathwayi | UPA00886. |
Names & Taxonomyi
Protein namesi | Recommended name: E3 SUMO-protein ligase PIAS1 (EC:2.3.2.27)Alternative name(s): DEAD/H box-binding protein 1 Protein inhibitor of activated STAT protein 1 RING-type E3 ubiquitin transferase PIAS1Curated |
Gene namesi | Name:Pias1 Synonyms:Ddxbp1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1913125. Pias1. |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 346 | C → G: Loss of promotion of EKLF sumoylation; when associated with G-351 and A-356. 1 Publication | 1 | |
Mutagenesisi | 351 | C → G: Loss of promotion of EKLF sumoylation; when associated with G-346 and A-356. 1 Publication | 1 | |
Mutagenesisi | 356 | C → A: Loss of promotion of EKLF sumoylation; when associated with G-346 and G-351. 1 Publication | 1 | |
Mutagenesisi | 363 | I → S: Loss of promotion of EKLF sumoylation. 1 Publication | 1 | |
Mutagenesisi | 372 | W → A: Loss of promotion of NCOA2 sumoylation. 1 Publication | 1 | |
Mutagenesisi | 375 – 376 | PV → AA: Loss of promotion of EKLF sumoylation. 1 Publication | 2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000218975 | 2 – 651 | E3 SUMO-protein ligase PIAS1Add BLAST | 650 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Cross-linki | 40 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 46 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 137 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 238 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 303 | Asymmetric dimethylarginine; by PRMT1By similarity | 1 | |
Cross-linki | 453 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 467 | PhosphoserineBy similarity | 1 | |
Modified residuei | 468 | PhosphoserineBy similarity | 1 | |
Modified residuei | 483 | PhosphoserineCombined sources | 1 | |
Modified residuei | 485 | PhosphoserineCombined sources | 1 | |
Modified residuei | 487 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 488 | PhosphoserineCombined sources | 1 | |
Modified residuei | 491 | PhosphoserineCombined sources | 1 | |
Cross-linki | 493 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 503 | PhosphoserineBy similarity | 1 | |
Modified residuei | 510 | PhosphoserineBy similarity | 1 | |
Modified residuei | 522 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Sumoylated.By similarity
Dimethylated by PRMT1 at Arg-303 in the late phase of interferon gamma (IFN-gamma) signaling, leading to preferential interaction with STAT1 and thus resulting in release of STAT1 from its target gene.By similarity
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | O88907. |
PaxDbi | O88907. |
PeptideAtlasi | O88907. |
PRIDEi | O88907. |
PTM databases
iPTMneti | O88907. |
PhosphoSitePlusi | O88907. |
Expressioni
Tissue specificityi
Expressed in kidney, heart, spleen, brain and cerebellum; weak expression, if any, in liver and lung.1 Publication
Developmental stagei
Expressed as early as 7.6 dpc. Expression remains high through 15.5 dpc (PubMed:10854042). In 3T3-L1 cells, expression is transiently induced during late adipocyte differentiation (PubMed:24061474).2 Publications
Gene expression databases
Bgeei | ENSMUSG00000032405. |
CleanExi | MM_PIAS1. |
ExpressionAtlasi | O88907. baseline and differential. |
Genevisiblei | O88907. MM. |
Interactioni
Subunit structurei
Interacts with STAT1 (By similarity). Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with DDX21, CSRP2, AXIN1, JUN, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3 (preferentially when SUMO-modified). Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase (By similarity). Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its sumoylation (By similarity). Interacts with SUMO1, UBE2I, NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with DDX5. Interacts with MTA1 (By similarity). Interacts with PML (isoform PML-12).By similarity4 Publications
Binary interactionsi
GO - Molecular functioni
- enzyme binding Source: MGI
- protein C-terminus binding Source: Ensembl
- protein domain specific binding Source: Ensembl
- transcription factor binding Source: UniProtKB
- ubiquitin protein ligase binding Source: BHF-UCL
Protein-protein interaction databases
BioGridi | 208005. 35 interactors. |
CORUMi | O88907. |
DIPi | DIP-29277N. |
IntActi | O88907. 18 interactors. |
MINTi | O88907. |
STRINGi | 10090.ENSMUSP00000096248. |
Structurei
3D structure databases
ProteinModelPortali | O88907. |
SMRi | O88907. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 11 – 45 | SAPPROSITE-ProRule annotationAdd BLAST | 35 | |
Domaini | 124 – 288 | PINITPROSITE-ProRule annotationAdd BLAST | 165 | |
Repeati | 520 – 523 | 1 | 4 | |
Repeati | 557 – 560 | 2 | 4 | |
Repeati | 598 – 601 | 3; approximate | 4 | |
Repeati | 612 – 615 | 4; approximate | 4 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 462 – 473 | SUMO1-bindingBy similarityAdd BLAST | 12 | |
Regioni | 520 – 615 | 4 X 4 AA repeats of N-T-S-LAdd BLAST | 96 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 19 – 23 | LXXLL motif | 5 | |
Motifi | 56 – 64 | Nuclear localization signalSequence analysis | 9 | |
Motifi | 368 – 380 | Nuclear localization signalSequence analysisAdd BLAST | 13 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 577 – 634 | Ser-richAdd BLAST | 58 |
Domaini
The LXXLL motif is a transcriptional coregulator signature.
The SP-RING-type domain is required for promoting EKLF sumoylation.
Sequence similaritiesi
Belongs to the PIAS family.Curated
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 320 – 397 | SP-RING-typePROSITE-ProRule annotationAdd BLAST | 78 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG2169. Eukaryota. ENOG410XQ2E. LUCA. |
GeneTreei | ENSGT00550000074410. |
HOGENOMi | HOG000230594. |
HOVERGENi | HBG053598. |
InParanoidi | O88907. |
KOi | K04706. |
OMAi | GRTYSMA. |
OrthoDBi | EOG091G08G5. |
PhylomeDBi | O88907. |
TreeFami | TF323787. |
Family and domain databases
Gene3Di | 1.10.720.30. 1 hit. 3.30.40.10. 1 hit. |
InterProi | View protein in InterPro IPR023321. PINIT. IPR003034. SAP_dom. IPR036361. SAP_dom_sf. IPR004181. Znf_MIZ. IPR013083. Znf_RING/FYVE/PHD. |
Pfami | View protein in Pfam PF14324. PINIT. 1 hit. PF02891. zf-MIZ. 1 hit. |
SMARTi | View protein in SMART SM00513. SAP. 1 hit. |
SUPFAMi | SSF68906. SSF68906. 1 hit. |
PROSITEi | View protein in PROSITE PS51466. PINIT. 1 hit. PS50800. SAP. 1 hit. PS51044. ZF_SP_RING. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O88907-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS
60 70 80 90 100
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPPTLS PSTIPQLTYD
110 120 130 140 150
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL
160 170 180 190 200
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL
210 220 230 240 250
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI
260 270 280 290 300
NITSLVRLST TVPNTIVVSW TAEIGRTYSM AVYLVKQLSS TVLLQRLRAK
310 320 330 340 350
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT
360 370 380 390 400
CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT
410 420 430 440 450
DCDEIQFKED GSWAPMRSKK EVQEVTASYN GVDGCLSSTL EHQVASHNQS
460 470 480 490 500
SNKNKKVEVI DLTIDSSSDE EEEEPPAKRT CPSLSPTSPL SNKGILSLPH
510 520 530 540 550
QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS
560 570 580 590 600
GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS
610 620 630 640 650
LPATNGSSSG SNSSLVSSNS LRESHGHGVA SRSSADTASI FGIIPDIISL
D
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 320 | P → S in AAC36701 (PubMed:9724754).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF077950 mRNA. Translation: AAC36701.1. AK075708 mRNA. Translation: BAC35902.1. BC051417 mRNA. Translation: AAH51417.1. |
CCDSi | CCDS40665.1. |
RefSeqi | NP_062637.2. NM_019663.3. |
UniGenei | Mm.431253. Mm.491651. |
Genome annotation databases
Ensembli | ENSMUST00000098651; ENSMUSP00000096248; ENSMUSG00000032405. |
GeneIDi | 56469. |
KEGGi | mmu:56469. |
UCSCi | uc009qas.1. mouse. |
Similar proteinsi
Entry informationi
Entry namei | PIAS1_MOUSE | |
Accessioni | O88907Primary (citable) accession number: O88907 Secondary accession number(s): Q8C6H5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 5, 2002 |
Last sequence update: | December 7, 2004 | |
Last modified: | March 28, 2018 | |
This is version 162 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |