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Protein

E3 SUMO-protein ligase PIAS2

Gene

Pias2

Organism
Rattus norvegicus (Rat)
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. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity (By similarity). Sumoylates PML at'Lys-65' and 'Lys-160' (By similarity).By similarity

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 fingeri331 – 40878SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • androgen receptor binding Source: RGD
  • DNA binding Source: UniProtKB-KW
  • estrogen receptor binding Source: RGD
  • glucocorticoid receptor binding Source: RGD
  • ligase activity Source: UniProtKB-KW
  • protein domain specific binding Source: RGD
  • SUMO transferase activity Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • androgen receptor signaling pathway Source: RGD
  • positive regulation of dendrite morphogenesis Source: RGD
  • positive regulation of transcription, DNA-templated Source: RGD
  • protein sumoylation Source: UniProtKB
  • regulation of androgen receptor signaling pathway Source: MGI
  • regulation of transcription, DNA-templated Source: RGD
  • response to organic substance Source: RGD
  • response to testosterone Source: RGD
  • spermatogenesis Source: RGD
  • 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

UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS2 (EC:6.3.2.-)
Alternative name(s):
Androgen receptor-interacting protein 3
Short name:
ARIP3
DAB2-interacting protein
Short name:
DIP
Msx-interacting-zinc finger protein
Protein inhibitor of activated STAT x
Protein inhibitor of activated STAT2
Gene namesi
Name:Pias2
Synonyms:Miz1, Piasx
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71056. Pias2.

Subcellular locationi

  • Nucleus speckle 2 Publications
  • NucleusPML body By similarity
  • Nucleus 1 Publication

  • Note: Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs) (By similarity). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349).By similarity1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231L → A: Loss of enhancement of AR and NR3C1-dependent transactivation; no effect on interaction with AR and NR3C1; when associated with A-305. 1 Publication
Mutagenesisi304 – 3041L → A: Loss of enhancement of AR and NR3C1-dependent transactivation; no effect on interaction with AR and NR3C1; when associated with A-23. 1 Publication
Mutagenesisi324 – 3241K → R: No effect on auto-sumoylation; when associated with R-326. 1 Publication
Mutagenesisi326 – 3261K → R: No effect on auto-sumoylation; when associated with R-324. 1 Publication
Mutagenesisi379 – 3791K → R: No effect on auto-sumoylation; when associated with R-380. 1 Publication
Mutagenesisi380 – 3801K → R: No effect on auto-sumoylation; when associated with R-379. 1 Publication
Mutagenesisi383 – 3831W → A: Loss of promotion of JUN sumoylation; no loss of interaction with SUMO1 and UBE2I. 1 Publication
Mutagenesisi385 – 3851C → S: Loss of NCOA2-binding; when associated with S-388. 1 Publication
Mutagenesisi388 – 3881C → S: Loss of NCOA2-binding; when associated with S-385. 1 Publication
Mutagenesisi390 – 3901K → R: No effect on auto-sumoylation; when associated with R-391. 1 Publication
Mutagenesisi391 – 3911K → R: No effect on auto-sumoylation; when associated with R-390. 1 Publication
Mutagenesisi430 – 4301K → R: No effect on auto-sumoylation; when associated with R-431. 1 Publication
Mutagenesisi431 – 4311K → R: No effect on auto-sumoylation; when associated with R-430. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572E3 SUMO-protein ligase PIAS2PRO_0000218978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki249 – 249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki430 – 430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki443 – 443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei476 – 4761PhosphoserineBy similarity
Modified residuei477 – 4771PhosphoserineBy similarity
Modified residuei478 – 4781PhosphoserineBy similarity
Cross-linki489 – 489Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei499 – 4991PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6AZ28.

PTM databases

PhosphoSiteiQ6AZ28.

Expressioni

Tissue specificityi

Mainly expressed in testis.1 Publication

Developmental stagei

Expressed in spermatogonia and in primary spermatocytes up to late pachytene stage (at protein level).

Interactioni

Subunit structurei

Binds SUMO1 and UBE2I. Interacts with AXIN1, JUN, MDM2, PARK7, TP53 and TP73 isoform alpha, but not TP73 isoform beta. Interacts with STAT4 following IL12 and IFN-alpha stimulation of T-cells. Interacts also with GTF2I, GTF2IRD1, IKFZ1, DAB2 and MSX2, as well as with several steroid receptors, including ESR1, ESR2, NR3C1, PGR, AR, and with NCOA2. Sumoylation of a target protein seems to enhance the interaction. Binds to sumoylated ELK1. Binds DNA, such as CDKN1A promoter, in a sequence-specific manner. Interacts with PLAG1. 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 IFIH1/MDA5 (By similarity). Interacts with PML (By similarity).By similarity

GO - Molecular functioni

  • androgen receptor binding Source: RGD
  • estrogen receptor binding Source: RGD
  • glucocorticoid receptor binding Source: RGD
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

BioGridi249702. 3 interactions.
STRINGi10116.ENSRNOP00000023886.

Structurei

3D structure databases

ProteinModelPortaliQ6AZ28.
SMRiQ6AZ28. Positions 1-65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
BLAST
Domaini134 – 299166PINITPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni467 – 4737SUMO1-bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 235LXXLL motif
Motifi484 – 4929Nuclear localization signalBy similarity

Domaini

The LXXLL motif is a transcriptional coregulator signature.

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 fingeri331 – 40878SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiQ6AZ28.
KOiK16063.
PhylomeDBiQ6AZ28.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027228. PIAS2.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF12. PTHR10782:SF12. 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.

Q6AZ28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCT
60 70 80 90 100
PAVQIKIREL YRRRYPRTLE GLSDLSTIKS SVFSLDGSSS PVEPDLAVAG
110 120 130 140 150
IHSLPSTSIA PHSPSSPVAS VLLQDTKPTF EMQQPSPPIP PVHPDVQLKT
160 170 180 190 200
LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI FALTPQQVRE ICISRDFLPG
210 220 230 240 250
GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP LPGYAPPPKN
260 270 280 290 300
GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT
310 320 330 340 350
SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK
360 370 380 390 400
MRLTIPCRAV TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD
410 420 430 440 450
GLFMEILNDC SDVDEIKFQE DGSWCPMRPK KEAMKVTSQP CTKVESSSVF
460 470 480 490 500
SKPCSVTVAS DASKKKIDVI DLTIESSSDE EEDPPAKRKC IFMSETQSSP
510 520 530 540 550
TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP VSSMSSDLPG
560 570
EQRRNDINNE VQLGTSSDTV QQ
Length:572
Mass (Da):63,431
Last modified:September 13, 2004 - v1
Checksum:iE107F8B26403D2FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501T → S in AAD13349 (PubMed:9920921).Curated
Sequence conflicti320 – 3201R → K in AAD13349 (PubMed:9920921).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044058 mRNA. Translation: AAD13349.1.
BC078775 mRNA. Translation: AAH78775.1.
RefSeqiNP_445789.1. NM_053337.1.
UniGeneiRn.227054.

Genome annotation databases

GeneIDi83422.
KEGGirno:83422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044058 mRNA. Translation: AAD13349.1.
BC078775 mRNA. Translation: AAH78775.1.
RefSeqiNP_445789.1. NM_053337.1.
UniGeneiRn.227054.

3D structure databases

ProteinModelPortaliQ6AZ28.
SMRiQ6AZ28. Positions 1-65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249702. 3 interactions.
STRINGi10116.ENSRNOP00000023886.

PTM databases

PhosphoSiteiQ6AZ28.

Proteomic databases

PaxDbiQ6AZ28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83422.
KEGGirno:83422.

Organism-specific databases

CTDi9063.
RGDi71056. Pias2.

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiQ6AZ28.
KOiK16063.
PhylomeDBiQ6AZ28.

Enzyme and pathway databases

UniPathwayiUPA00886.

Miscellaneous databases

NextBioi615835.
PROiQ6AZ28.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027228. PIAS2.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF12. PTHR10782:SF12. 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...

Publicationsi

« Hide 'large scale' publications
  1. "A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins."
    Moilanen A.-M., Karvonen U., Poukka H., Yan W., Toppari J., Jaenne O.A., Palvimo J.J.
    J. Biol. Chem. 274:3700-3704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "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; ESR1; ESR2; NR3C1 AND PGR.
  4. "Androgen receptor-interacting protein 3 and other PIAS proteins cooperate with glucocorticoid receptor-interacting protein 1 in steroid receptor-dependent signaling."
    Kotaja N., Vihinen M., Palvimo J.J., Jaenne O.A.
    J. Biol. Chem. 277:17781-17788(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA2, MUTAGENESIS OF LEU-23; LEU-304; CYS-385 AND CYS-388.
  5. "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 AR, SUMOYLATION OF AR; JUN AND NCOA2, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-324; LYS-326; LYS-379; LYS-380; TRP-383; LYS-390; LYS-391; LYS-430 AND LYS-431.
  6. Cited for: STAT1 SUMOYLATION.

Entry informationi

Entry nameiPIAS2_RAT
AccessioniPrimary (citable) accession number: Q6AZ28
Secondary accession number(s): Q9Z177
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 13, 2004
Last modified: February 17, 2016
This is version 105 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.