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Reviewed, UniProtKB/Swiss-Prot Q9Y6X2 (PIAS3_HUMAN)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    E3 SUMO-protein ligase PIAS3
Alternative name(s):
    Protein inhibitor of activated STAT protein 3
Gene names
Name: PIAS3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length628 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context.

Pathway

Protein modification; protein sumoylation.

Subunit structure

Binds SUMO1 and UBE2I. Interacts with AR, GFI1, HMGA2, IRF1, MITF, NCOA2, as well as with STAT3, after treatment with IL6, CNTF or OSM and with STAT5, after PRL stimulation By similarity. Interacts with PLAG1.

Subcellular location

Nucleus speckle By similarity.

Tissue specificity

Widely expressed. Ref.4

Induction

By dihydrotestosterone in prostate cancer cells. Ref.5

Domain

The LXXLL motif is a transcriptional coregulator signature.

Post-translational modification

Sumoylated By similarity.

Sequence similarities

Belongs to the PIAS family.

Contains 1 SAP domain.

Contains 1 SP-RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMUbl conjugation
Gene Ontology (GO)
   Biological processmodification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 628628E3 SUMO-protein ligase PIAS3
PRO_0000218979

Regions

Domain11 – 4535SAP
Zinc finger303 – 38078SP-RING-type
Region450 – 46011SUMO1-binding By similarity
Motif19 – 235LXXLL motif
Compositional bias81 – 13353Pro-rich

Natural variations

Natural variant3901S → C: dbSNP rs17354559.
VAR_050535

Sequences

Sequence LengthMass (Da)Tools
Q9Y6X2-1 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: 7C06EF599D48F87D

FASTA62868,017
        10         20         30         40         50         60 
MAELGELKHM VMSFRVSELQ VLLGFAGRNK SGRKHELLAK ALHLLKSSCA PSVQMKIKEL 

        70         80         90        100        110        120 
YRRRFPRKTL GPSDLSLLSL PPGTSPVGSP GPLAPIPPTL LAPGTLLGPK REVDMHPPLP 

       130        140        150        160        170        180 
QPVHPDVTMK PLPFYEVYGE LIRPTTLAST SSQRFEEAHF TFALTPQQVQ QILTSREVLP 

       190        200        210        220        230        240 
GAKCDYTIQV QLRFCLCETS CPQEDYFPPN LFVKVNGKLC PLPGYLPPTK NGAEPKRPSR 

       250        260        270        280        290        300 
PINITPLARL SATVPNTIVV NWSSEFGRNY SLSVYLVRQL TAGTLLQKLR AKGIRNPDHS 

       310        320        330        340        350        360 
RALIKEKLTA DPDSEVATTS LRVSLMCPLG KMRLTVPCRA LTCAHLQSFD AALYLQMNEK 

       370        380        390        400        410        420 
KPTWTCPVCD KKAPYESLII DGLFMEILSS CSDCDEIQFM EDGSWCPMKP KKEASEVCPP 

       430        440        450        460        470        480 
PGYGLDGLQY SPVQGGDPSE NKKKVEVIDL TIESSSDEED LPPTKKHCSV TSAAIPALPG 

       490        500        510        520        530        540 
SKGVLTSGHQ PSSVLRSPAM GTLGGDFLSS LPLHEYPPAF PLGADIQGLD LFSFLQTESQ 

       550        560        570        580        590        600 
HYGPSVITSL DEQDALGHFF QYRGTPSHFL GPLAPTLGSS HCSATPAPPP GRVSSIVAPG 

       610        620 
GALREGHGGP LPSGPSLTGC RSDIISLD 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and chromosomal assignment of a human gene encoding protein inhibitor of activated STAT3 (PIAS3)."
Ueki N., Seki N., Yano K., Saito T., Masuho Y., Muramatsu M.-A.
J. Hum. Genet. 44:193-196(1999) [PubMed: 10319586] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-628.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood and Muscle.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 310-628.
Tissue: Mammary cancer.
[4]"Specific inhibition of Stat3 signal transduction by PIAS3."
Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K.
Science 278:1803-1805(1997) [PubMed: 9388184] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Protein inhibitor of activated STAT3 regulates androgen receptor signaling in prostate carcinoma cells."
Junicho A., Matsuda T., Yamamoto T., Kishi H., Korkmaz K., Saatcioglu F., Fuse H., Muraguchi A.
Biochem. Biophys. Res. Commun. 278:9-13(2000) [PubMed: 11071847] [Abstract]
Cited for: INTERACTION WITH AR, INDUCTION.
[6]"The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting with the STAT3 inhibitor PIAS3."
Roedel B., Tavassoli K., Karsunky H., Schmidt T., Bachmann M., Schaper F., Heinrich P., Shuai K., Elsaesser H.-P., Moeroey T.
EMBO J. 19:5845-5855(2000) [PubMed: 11060035] [Abstract]
Cited for: INTERACTION WITH GFI1.
[7]"Repression of the transactivating capacity of the oncoprotein PLAG1 by SUMOylation."
Van Dyck F., Delvaux E.L.D., Van de Ven W.J.M., Chavez M.V.
J. Biol. Chem. 279:36121-36131(2004) [PubMed: 15208321] [Abstract]
Cited for: INTERACTION WITH PLAG1.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB021868 mRNA. Translation: BAA78533.1. Different initiation.
BC001154 mRNA. Translation: AAH01154.1. Different initiation.
BC030556 mRNA. Translation: AAH30556.1. Different initiation.
IPIIPI00005789.
PIRT34525.
RefSeqNP_006090.2.
UniGeneHs.435761

3D structure databases

SMRQ9Y6X2. Positions 1-65.
ModBaseSearch...

Proteomic databases

PRIDEQ9Y6X2.

Genome annotation databases

EnsemblENSG00000131788. Homo sapiens. [Contig view]
GeneID10401.
KEGGhsa:10401.

Organism-specific databases

GeneCardsGC01P144287.
H-InvDBHIX0000976.
HGNCHGNC:16861. PIAS3.
MIM605987. gene.
PharmGKBPA134989011.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9Y6X2.
HOVERGENQ9Y6X2.
OMAQ9Y6X2. CSVTSAA.

Enzyme and pathway databases

Pathway_Interaction_DBar_pathway. Coregulation of Androgen receptor activity.
il6_7pathway. IL6-mediated signaling events.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Gene expression databases

BgeeQ9Y6X2.
CleanExHS_PIAS3.
GermOnlineENSG00000131788. Homo sapiens.

Family and domain databases

InterProIPR003034. SAP_DNA_bd.
IPR004181. Znf_MIZ.
[Graphical view]
PfamPF02037. SAP. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio39416.
SOURCESearch...

Entry information

Entry namePIAS3_HUMAN
AccessionPrimary (citable) accession number: Q9Y6X2
Secondary accession number(s): Q9UFI3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: December 7, 2004
Last modified: June 16, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents