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O88907

- PIAS1_MOUSE

UniProt

O88907 - PIAS1_MOUSE

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Protein
E3 SUMO-protein ligase PIAS1
Gene
Pias1, Ddxbp1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri320 – 39778SP-RING-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. SUMO ligase activity Source: Ensembl
  3. protein binding Source: UniProtKB
  4. transcription corepressor activity Source: MGI
  5. ubiquitin protein ligase binding Source: BHF-UCL
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. JAK-STAT cascade Source: MGI
  2. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  3. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. positive regulation of protein sumoylation Source: UniProtKB
  5. positive regulation of smooth muscle cell differentiation Source: Ensembl
  6. positive regulation of transcription, DNA-templated Source: Ensembl
  7. protein sumoylation Source: UniProtKB
  8. protein-DNA complex assembly Source: Ensembl
  9. regulation of cell proliferation Source: UniProtKB
  10. spermatogenesis Source: Ensembl
  11. 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

ReactomeiREACT_198645. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1913125. Pias1.

Subcellular locationi

Nucleus speckle By similarity. NucleusPML body
Note: Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton By similarity.2 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB-SubCell
  2. nuclear speck Source: UniProtKB-SubCell
  3. nucleus Source: MGI
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 651650E3 SUMO-protein ligase PIAS1
PRO_0000218975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei303 – 3031Asymmetric dimethylarginine; by PRMT1 By similarity
Modified residuei485 – 4851Phosphoserine1 Publication
Modified residuei487 – 4871Phosphothreonine1 Publication
Modified residuei503 – 5031Phosphoserine By similarity
Modified residuei510 – 5101Phosphoserine By similarity
Modified residuei522 – 5221Phosphoserine By similarity

Post-translational modificationi

Sumoylated By similarity.3 Publications
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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO88907.
PRIDEiO88907.

PTM databases

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.1 Publication

Gene expression databases

ArrayExpressiO88907.
BgeeiO88907.
CleanExiMM_PIAS1.
GenevestigatoriO88907.

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 By similarity. Interacts with PML (isoform PML-12).4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi208005. 28 interactions.
DIPiDIP-29277N.
IntActiO88907. 16 interactions.
MINTiMINT-4107556.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAP
Add
BLAST
Domaini124 – 288165PINIT
Add
BLAST
Repeati520 – 52341
Repeati557 – 56042
Repeati598 – 60143; approximate
Repeati612 – 61544; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni462 – 47312SUMO1-binding By similarity
Add
BLAST
Regioni520 – 615964 X 4 AA repeats of N-T-S-L
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 235LXXLL motif
Motifi56 – 649Nuclear localization signal Reviewed prediction
Motifi368 – 38013Nuclear localization signal Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi577 – 63458Ser-rich
Add
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.
Contains 1 PINIT domain.
Contains 1 SAP domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG125513.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiO88907.
KOiK04706.
OMAiGRTYSMA.
OrthoDBiEOG7HF1JB.
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

MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS    50
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPPTLS PSTIPQLTYD 100
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 150
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 200
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 250
NITSLVRLST TVPNTIVVSW TAEIGRTYSM AVYLVKQLSS TVLLQRLRAK 300
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT 350
CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT 400
DCDEIQFKED GSWAPMRSKK EVQEVTASYN GVDGCLSSTL EHQVASHNQS 450
SNKNKKVEVI DLTIDSSSDE EEEEPPAKRT CPSLSPTSPL SNKGILSLPH 500
QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS 550
GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 600
LPATNGSSSG SNSSLVSSNS LRESHGHGVA SRSSADTASI FGIIPDIISL 650
D 651
Length:651
Mass (Da):71,618
Last modified:December 7, 2004 - v2
Checksum:i8844364E8FEE4F7F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201P → S in AAC36701. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.

3D structure databases

ProteinModelPortali O88907.
SMRi O88907. Positions 1-65, 135-416.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208005. 28 interactions.
DIPi DIP-29277N.
IntActi O88907. 16 interactions.
MINTi MINT-4107556.

PTM databases

PhosphoSitei O88907.

Proteomic databases

PaxDbi O88907.
PRIDEi O88907.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000098651 ; ENSMUSP00000096248 ; ENSMUSG00000032405 .
GeneIDi 56469.
KEGGi mmu:56469.
UCSCi uc009qas.1. mouse.

Organism-specific databases

CTDi 8554.
MGIi MGI:1913125. Pias1.

Phylogenomic databases

eggNOGi NOG125513.
HOGENOMi HOG000230594.
HOVERGENi HBG053598.
InParanoidi O88907.
KOi K04706.
OMAi GRTYSMA.
OrthoDBi EOG7HF1JB.
PhylomeDBi O88907.
TreeFami TF323787.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_198645. Regulation of IFNG signaling.

Miscellaneous databases

ChiTaRSi PIAS1. mouse.
NextBioi 312730.
PROi O88907.
SOURCEi Search...

Gene expression databases

ArrayExpressi O88907.
Bgeei O88907.
CleanExi MM_PIAS1.
Genevestigatori O88907.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
InterProi IPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view ]
PANTHERi PTHR10782:SF11. PTHR10782:SF11. 1 hit.
Pfami PF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view ]
SMARTi SM00513. SAP. 1 hit.
[Graphical view ]
PROSITEi PS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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.

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 3, 2014
This is version 128 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

External Data

Dasty 3

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