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O88907 (PIAS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Pias1
Synonyms:Ddxbp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Pathway

Protein modification; protein sumoylation.

Subunit structure

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 By similarity. Interacts with PML (isoform PML-12) Ref.5 Ref.6 Ref.9 Ref.11

Subcellular location

Nucleus speckle By similarity. NucleusPML body. Note: Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton By similarity. Ref.6 Ref.11

Tissue specificity

Expressed in kidney, heart, spleen, brain and cerebellum; weak expression, if any, in liver and lung. Ref.4

Developmental stage

Expressed as early as 7.6 dpc. Expression remains high through 15.5 dpc. Ref.4

Domain

The LXXLL motif is a transcriptional coregulator signature.

The SP-RING-type domain is required for promoting EKLF sumoylation.

Post-translational modification

Sumoylated By similarity. Ref.6 Ref.7 Ref.8

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.

Sequence similarities

Belongs to the PIAS family.

Contains 1 PINIT domain.

Contains 1 SAP domain.

Contains 1 SP-RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from sequence alignment Ref.1. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 16127449. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein sumoylation

Inferred from direct assay Ref.11. Source: UniProtKB

protein-DNA complex assembly

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 16522640. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

SUMO ligase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

transcription corepressor activity

Inferred from sequence alignment Ref.1. Source: MGI

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 16816390. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SufuQ9Z0P73EBI-3508327,EBI-3508336

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 651650E3 SUMO-protein ligase PIAS1
PRO_0000218975

Regions

Domain11 – 4535SAP
Domain124 – 288165PINIT
Repeat520 – 52341
Repeat557 – 56042
Repeat598 – 60143; approximate
Repeat612 – 61544; approximate
Zinc finger320 – 39778SP-RING-type
Region462 – 47312SUMO1-binding By similarity
Region520 – 615964 X 4 AA repeats of N-T-S-L
Motif19 – 235LXXLL motif
Motif56 – 649Nuclear localization signal Potential
Motif368 – 38013Nuclear localization signal Potential
Compositional bias577 – 63458Ser-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3031Asymmetric dimethylarginine; by PRMT1 By similarity
Modified residue4851Phosphoserine Ref.10
Modified residue4871Phosphothreonine Ref.10
Modified residue5031Phosphoserine By similarity
Modified residue5101Phosphoserine By similarity
Modified residue5221Phosphoserine By similarity

Experimental info

Mutagenesis3461C → G: Loss of promotion of EKLF sumoylation; when associated with G-351 and A-356. Ref.8
Mutagenesis3511C → G: Loss of promotion of EKLF sumoylation; when associated with G-346 and A-356. Ref.8
Mutagenesis3561C → A: Loss of promotion of EKLF sumoylation; when associated with G-346 and G-351. Ref.8
Mutagenesis3631I → S: Loss of promotion of EKLF sumoylation. Ref.8
Mutagenesis3721W → A: Loss of promotion of NCOA2 sumoylation. Ref.6
Mutagenesis375 – 3762PV → AA: Loss of promotion of EKLF sumoylation.
Sequence conflict3201P → S in AAC36701. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O88907 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: 8844364E8FEE4F7F

FASTA65171,618
        10         20         30         40         50         60 
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL 

        70         80         90        100        110        120 
YRRRFPQKIM TPADLSIPNV HSSPMPPTLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL 

       130        140        150        160        170        180 
ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ 

       190        200        210        220        230        240 
ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG 

       250        260        270        280        290        300 
VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRTYSM AVYLVKQLSS TVLLQRLRAK 

       310        320        330        340        350        360 
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT 

       370        380        390        400        410        420 
LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GSWAPMRSKK 

       430        440        450        460        470        480 
EVQEVTASYN GVDGCLSSTL EHQVASHNQS SNKNKKVEVI DLTIDSSSDE EEEEPPAKRT 

       490        500        510        520        530        540 
CPSLSPTSPL SNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL 

       550        560        570        580        590        600 
QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 

       610        620        630        640        650 
LPATNGSSSG SNSSLVSSNS LRESHGHGVA SRSSADTASI FGIIPDIISL D 

« Hide

References

« Hide 'large scale' references
[1]"Inhibition of Stat1-mediated gene activation by PIAS1."
Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D., Shuai K.
Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: B-cell.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary tumor.
[4]"Cloning and analysis of a murine Pias family member, Pias-gamma, in developing skin and neurons."
Sturm S., Koch M., White F.A.
J. Mol. Neurosci. 14:107-121(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Tissue: Brain.
[5]"ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation."
Kotaja N., Aittomaeki S., Silvennoinen O., Palvimo J.J., Jaenne O.A.
Mol. Endocrinol. 14:1986-2000(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AR.
[6]"PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases."
Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.
Mol. Cell. Biol. 22:5222-5234(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUMO1; UBE2I AND NCOA2, SUBCELLULAR LOCATION, SUMOYLATION OF AR AND NCOA2, MUTAGENESIS OF TRP-372.
[7]"PIAS proteins promote SUMO-1 conjugation to STAT1."
Ungureanu D., Vanhatupa S., Kotaja N., Yang J., Aittomaeki S., Jaenne O.A., Palvimo J.J., Silvennoinen O.
Blood 102:3311-3313(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STAT1 SUMOYLATION.
[8]"Sumoylation of EKLF promotes transcriptional repression and is involved in inhibition of megakaryopoiesis."
Siatecka M., Xue L., Bieker J.J.
Mol. Cell. Biol. 27:8547-8560(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION OF KLF1, MUTAGENESIS OF CYS-346; CYS-351; CYS-356; ILE-363 AND 375-PRO-VAL-376.
[9]"SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C1.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485 AND THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF077950 mRNA. Translation: AAC36701.1.
AK075708 mRNA. Translation: BAC35902.1.
BC051417 mRNA. Translation: AAH51417.1.
CCDSCCDS40665.1.
RefSeqNP_062637.2. NM_019663.3.
UniGeneMm.431253.
Mm.491651.

3D structure databases

ProteinModelPortalO88907.
SMRO88907. Positions 1-65, 135-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208005. 28 interactions.
DIPDIP-29277N.
IntActO88907. 16 interactions.
MINTMINT-4107556.

PTM databases

PhosphoSiteO88907.

Proteomic databases

PaxDbO88907.
PRIDEO88907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098651; ENSMUSP00000096248; ENSMUSG00000032405.
GeneID56469.
KEGGmmu:56469.
UCSCuc009qas.1. mouse.

Organism-specific databases

CTD8554.
MGIMGI:1913125. Pias1.

Phylogenomic databases

eggNOGNOG125513.
HOGENOMHOG000230594.
HOVERGENHBG053598.
InParanoidO88907.
KOK04706.
OMAGRTYSMA.
OrthoDBEOG7HF1JB.
PhylomeDBO88907.
TreeFamTF323787.

Enzyme and pathway databases

UniPathwayUPA00886.

Gene expression databases

ArrayExpressO88907.
BgeeO88907.
CleanExMM_PIAS1.
GenevestigatorO88907.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
InterProIPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERPTHR10782:SF11. PTHR10782:SF11. 1 hit.
PfamPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIAS1. mouse.
NextBio312730.
PROO88907.
SOURCESearch...

Entry information

Entry namePIAS1_MOUSE
AccessionPrimary (citable) accession number: O88907
Secondary accession number(s): Q8C6H5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: December 7, 2004
Last modified: July 9, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot