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UniProtKB - O88907 (PIAS1_MOUSE)

UniProt

O88907 - PIAS1_MOUSE

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Protein

E3 SUMO-protein ligase PIAS1

Gene

Pias1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri320 – 39778SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • fat cell differentiation Source: UniProtKB
  • JAK-STAT cascade Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • positive regulation of protein sumoylation Source: UniProtKB
  • protein sumoylation Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-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-4551638. SUMOylation of chromatin organization proteins.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-877312. Regulation of IFNG signaling.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS1 (EC:6.3.2.-)
Alternative name(s):
DEAD/H box-binding protein 1
Protein inhibitor of activated STAT protein 1
Gene namesi
Name:Pias1
Synonyms:Ddxbp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1913125. Pias1.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: MGI
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi346 – 3461C → G: Loss of promotion of EKLF sumoylation; when associated with G-351 and A-356. 1 Publication
Mutagenesisi351 – 3511C → G: Loss of promotion of EKLF sumoylation; when associated with G-346 and A-356. 1 Publication
Mutagenesisi356 – 3561C → A: Loss of promotion of EKLF sumoylation; when associated with G-346 and G-351. 1 Publication
Mutagenesisi363 – 3631I → S: Loss of promotion of EKLF sumoylation. 1 Publication
Mutagenesisi372 – 3721W → A: Loss of promotion of NCOA2 sumoylation. 1 Publication
Mutagenesisi375 – 3762PV → AA: Loss of promotion of EKLF sumoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 651650E3 SUMO-protein ligase PIAS1PRO_0000218975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki46 – 46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki238 – 238Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei303 – 3031Asymmetric dimethylarginine; by PRMT1By similarity
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei468 – 4681PhosphoserineBy similarity
Modified residuei483 – 4831PhosphoserineCombined sources
Modified residuei485 – 4851PhosphoserineCombined sources
Modified residuei487 – 4871PhosphothreonineCombined sources
Modified residuei488 – 4881PhosphoserineCombined sources
Modified residuei491 – 4911PhosphoserineCombined sources
Modified residuei503 – 5031PhosphoserineBy similarity
Modified residuei510 – 5101PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity

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.
PhosphoSiteiO88907.

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.
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

WithEntry#Exp.IntActNotes
SufuQ9Z0P73EBI-3508327,EBI-3508336

GO - Molecular functioni

  • enzyme binding Source: MGI
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi208005. 35 interactions.
DIPiDIP-29277N.
IntActiO88907. 16 interactions.
MINTiMINT-4107556.
STRINGi10090.ENSMUSP00000096248.

Structurei

3D structure databases

ProteinModelPortaliO88907.
SMRiO88907. Positions 1-65, 135-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
BLAST
Domaini124 – 288165PINITPROSITE-ProRule annotationAdd
BLAST
Repeati520 – 52341
Repeati557 – 56042
Repeati598 – 60143; approximate
Repeati612 – 61544; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni462 – 47312SUMO1-bindingBy similarityAdd
BLAST
Regioni520 – 615964 X 4 AA repeats of N-T-S-LAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 235LXXLL motif
Motifi56 – 649Nuclear localization signalSequence analysis
Motifi368 – 38013Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi577 – 63458Ser-richAdd
BLAST

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
Contains 1 PINIT domain.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation
Contains 1 SP-RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri320 – 39778SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiO88907.
KOiK04706.
OMAiGRTYSMA.
OrthoDBiEOG091G08G5.
PhylomeDBiO88907.
TreeFamiTF323787.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF11. PTHR10782:SF11. 1 hit.
PfamiPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201P → S in AAC36701 (PubMed:9724754).Curated

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.

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. Positions 1-65, 135-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208005. 35 interactions.
DIPiDIP-29277N.
IntActiO88907. 16 interactions.
MINTiMINT-4107556.
STRINGi10090.ENSMUSP00000096248.

PTM databases

iPTMnetiO88907.
PhosphoSiteiO88907.

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.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiO88907.
KOiK04706.
OMAiGRTYSMA.
OrthoDBiEOG091G08G5.
PhylomeDBiO88907.
TreeFamiTF323787.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-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.

Miscellaneous databases

ChiTaRSiPias1. mouse.
PROiO88907.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032405.
CleanExiMM_PIAS1.
ExpressionAtlasiO88907. baseline and differential.
GenevisibleiO88907. MM.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF11. PTHR10782:SF11. 1 hit.
PfamiPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIAS1_MOUSE
AccessioniPrimary (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: September 7, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.