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Protein

E3 SUMO-protein ligase PIAS1

Gene

Pias1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Pathwayi: protein sumoylation

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 keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri320 – 397SP-RING-typePROSITE-ProRule annotationAdd BLAST78

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3232118 SUMOylation of transcription factors
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-4090294 SUMOylation of intracellular receptors
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1913125 Pias1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi346C → G: Loss of promotion of EKLF sumoylation; when associated with G-351 and A-356. 1 Publication1
Mutagenesisi351C → G: Loss of promotion of EKLF sumoylation; when associated with G-346 and A-356. 1 Publication1
Mutagenesisi356C → A: Loss of promotion of EKLF sumoylation; when associated with G-346 and G-351. 1 Publication1
Mutagenesisi363I → S: Loss of promotion of EKLF sumoylation. 1 Publication1
Mutagenesisi372W → A: Loss of promotion of NCOA2 sumoylation. 1 Publication1
Mutagenesisi375 – 376PV → AA: Loss of promotion of EKLF sumoylation. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002189752 – 651E3 SUMO-protein ligase PIAS1Add BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Cross-linki40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki238Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei303Asymmetric dimethylarginine; by PRMT1By similarity1
Cross-linki453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei467PhosphoserineBy similarity1
Modified residuei468PhosphoserineBy similarity1
Modified residuei483PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei487PhosphothreonineCombined sources1
Modified residuei488PhosphoserineCombined sources1
Modified residuei491PhosphoserineCombined sources1
Cross-linki493Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei503PhosphoserineBy similarity1
Modified residuei510PhosphoserineBy similarity1
Modified residuei522PhosphoserineBy similarity1

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 conjugation

Proteomic databases

EPDiO88907
PaxDbiO88907
PeptideAtlasiO88907
PRIDEiO88907

PTM databases

iPTMnetiO88907
PhosphoSitePlusiO88907

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

BgeeiENSMUSG00000032405 Expressed in 308 organ(s), highest expression level in secondary oocyte
CleanExiMM_PIAS1
ExpressionAtlasiO88907 baseline and differential
GenevisibleiO88907 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

Protein-protein interaction databases

BioGridi208005, 36 interactors
CORUMiO88907
DIPiDIP-29277N
IntActiO88907, 18 interactors
MINTiO88907
STRINGi10090.ENSMUSP00000096248

Structurei

3D structure databases

ProteinModelPortaliO88907
SMRiO88907
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 45SAPPROSITE-ProRule annotationAdd BLAST35
Domaini124 – 288PINITPROSITE-ProRule annotationAdd BLAST165
Repeati520 – 52314
Repeati557 – 56024
Repeati598 – 6013; approximate4
Repeati612 – 6154; approximate4

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni462 – 473SUMO1-bindingBy similarityAdd BLAST12
Regioni520 – 6154 X 4 AA repeats of N-T-S-LAdd BLAST96

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi19 – 23LXXLL motif5
Motifi56 – 64Nuclear localization signalSequence analysis9
Motifi368 – 380Nuclear localization signalSequence analysisAdd BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi577 – 634Ser-richAdd BLAST58

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 keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri320 – 397SP-RING-typePROSITE-ProRule annotationAdd BLAST78

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2169 Eukaryota
ENOG410XQ2E LUCA
GeneTreeiENSGT00550000074410
HOGENOMiHOG000230594
HOVERGENiHBG053598
InParanoidiO88907
KOiK04706
OrthoDBiEOG091G08G5
PhylomeDBiO88907
TreeFamiTF323787

Family and domain databases

Gene3Di1.10.720.30, 1 hit
2.60.120.780, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR023321 PINIT
IPR038654 PINIT_sf
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR004181 Znf_MIZ
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF14324 PINIT, 1 hit
PF02891 zf-MIZ, 1 hit
SMARTiView protein in SMART
SM00513 SAP, 1 hit
SUPFAMiSSF68906 SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS51466 PINIT, 1 hit
PS50800 SAP, 1 hit
PS51044 ZF_SP_RING, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

O88907-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:651
Mass (Da):71,618
Last modified:December 7, 2004 - v2
Checksum:i8844364E8FEE4F7F
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3U556Q3U556_MOUSE
E3 SUMO-protein ligase PIAS1
Pias1
577Annotation score:
A0A1L1SRS2A0A1L1SRS2_MOUSE
E3 SUMO-protein ligase PIAS1
Pias1
222Annotation score:
A0A1L1SQX9A0A1L1SQX9_MOUSE
E3 SUMO-protein ligase PIAS1
Pias1
85Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti320P → S in AAC36701 (PubMed:9724754).Curated1

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
CCDSiCCDS40665.1
RefSeqiNP_062637.2, NM_019663.3
UniGeneiMm.431253
Mm.491651

Genome annotation databases

EnsembliENSMUST00000098651; ENSMUSP00000096248; ENSMUSG00000032405
GeneIDi56469
KEGGimmu:56469
UCSCiuc009qas.1 mouse

Similar proteinsi

Cross-referencesi

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
CCDSiCCDS40665.1
RefSeqiNP_062637.2, NM_019663.3
UniGeneiMm.431253
Mm.491651

3D structure databases

ProteinModelPortaliO88907
SMRiO88907
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208005, 36 interactors
CORUMiO88907
DIPiDIP-29277N
IntActiO88907, 18 interactors
MINTiO88907
STRINGi10090.ENSMUSP00000096248

PTM databases

iPTMnetiO88907
PhosphoSitePlusiO88907

Proteomic databases

EPDiO88907
PaxDbiO88907
PeptideAtlasiO88907
PRIDEiO88907

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098651; ENSMUSP00000096248; ENSMUSG00000032405
GeneIDi56469
KEGGimmu:56469
UCSCiuc009qas.1 mouse

Organism-specific databases

CTDi8554
MGIiMGI:1913125 Pias1

Phylogenomic databases

eggNOGiKOG2169 Eukaryota
ENOG410XQ2E LUCA
GeneTreeiENSGT00550000074410
HOGENOMiHOG000230594
HOVERGENiHBG053598
InParanoidiO88907
KOiK04706
OrthoDBiEOG091G08G5
PhylomeDBiO88907
TreeFamiTF323787

Enzyme and pathway databases

UniPathwayi
UPA00886

ReactomeiR-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-3232118 SUMOylation of transcription factors
R-MMU-3232142 SUMOylation of ubiquitinylation proteins
R-MMU-3899300 SUMOylation of transcription cofactors
R-MMU-4090294 SUMOylation of intracellular receptors
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

Miscellaneous databases

ChiTaRSiPias1 mouse
PROiPR:O88907
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032405 Expressed in 308 organ(s), highest expression level in secondary oocyte
CleanExiMM_PIAS1
ExpressionAtlasiO88907 baseline and differential
GenevisibleiO88907 MM

Family and domain databases

Gene3Di1.10.720.30, 1 hit
2.60.120.780, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR023321 PINIT
IPR038654 PINIT_sf
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR004181 Znf_MIZ
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF14324 PINIT, 1 hit
PF02891 zf-MIZ, 1 hit
SMARTiView protein in SMART
SM00513 SAP, 1 hit
SUPFAMiSSF68906 SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS51466 PINIT, 1 hit
PS50800 SAP, 1 hit
PS51044 ZF_SP_RING, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPIAS1_MOUSE
AccessioniPrimary (citable) accession number: O88907
Secondary accession number(s): Q8C6H5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: December 7, 2004
Last modified: November 7, 2018
This is version 167 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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