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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)DescriptionActionsGraphical viewLength
Zinc fingeri331 – 408SP-RING-typePROSITE-ProRule annotationAdd BLAST78

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

Keywordsi

Molecular functionDNA-binding, Ligase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71056. Pias2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23L → A: Loss of enhancement of AR and NR3C1-dependent transactivation; no effect on interaction with AR and NR3C1; when associated with A-305. 1 Publication1
Mutagenesisi304L → A: Loss of enhancement of AR and NR3C1-dependent transactivation; no effect on interaction with AR and NR3C1; when associated with A-23. 1 Publication1
Mutagenesisi324K → R: No effect on auto-sumoylation; when associated with R-326. 1 Publication1
Mutagenesisi326K → R: No effect on auto-sumoylation; when associated with R-324. 1 Publication1
Mutagenesisi379K → R: No effect on auto-sumoylation; when associated with R-380. 1 Publication1
Mutagenesisi380K → R: No effect on auto-sumoylation; when associated with R-379. 1 Publication1
Mutagenesisi383W → A: Loss of promotion of JUN sumoylation; no loss of interaction with SUMO1 and UBE2I. 1 Publication1
Mutagenesisi385C → S: Loss of NCOA2-binding; when associated with S-388. 1 Publication1
Mutagenesisi388C → S: Loss of NCOA2-binding; when associated with S-385. 1 Publication1
Mutagenesisi390K → R: No effect on auto-sumoylation; when associated with R-391. 1 Publication1
Mutagenesisi391K → R: No effect on auto-sumoylation; when associated with R-390. 1 Publication1
Mutagenesisi430K → R: No effect on auto-sumoylation; when associated with R-431. 1 Publication1
Mutagenesisi431K → R: No effect on auto-sumoylation; when associated with R-430. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002189781 – 572E3 SUMO-protein ligase PIAS2Add BLAST572

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei476PhosphoserineBy similarity1
Modified residuei477PhosphoserineBy similarity1
Modified residuei478PhosphoserineBy similarity1
Cross-linki489Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei499PhosphoserineBy similarity1
Cross-linki502Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6AZ28.

PTM databases

iPTMnetiQ6AZ28.
PhosphoSitePlusiQ6AZ28.

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 interactors.
STRINGi10116.ENSRNOP00000023886.

Structurei

3D structure databases

ProteinModelPortaliQ6AZ28.
SMRiQ6AZ28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 45SAPPROSITE-ProRule annotationAdd BLAST35
Domaini134 – 299PINITPROSITE-ProRule annotationAdd BLAST166

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni467 – 473SUMO1-bindingBy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi19 – 23LXXLL motif5
Motifi484 – 492Nuclear localization signalBy similarity9

Domaini

The LXXLL motif is a transcriptional coregulator signature.

Sequence similaritiesi

Belongs to the PIAS family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri331 – 408SP-RING-typePROSITE-ProRule annotationAdd BLAST78

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.
InterProiView protein in InterPro
IPR027228. PIAS2.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR036361. SAP_dom_sf.
IPR004181. Znf_MIZ.
PANTHERiPTHR10782:SF12. PTHR10782:SF12. 1 hit.
PfamiView protein in Pfam
PF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
SMARTiView protein in SMART
SM00513. SAP. 1 hit.
SUPFAMiSSF68906. SSF68906. 1 hit.
PROSITEiView protein in PROSITE
PS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti50T → S in AAD13349 (PubMed:9920921).Curated1
Sequence conflicti320R → K in AAD13349 (PubMed:9920921).Curated1

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.

Similar proteinsi

Entry informationi

Entry nameiPIAS2_RAT
AccessioniPrimary (citable) accession number: Q6AZ28
Secondary accession number(s): Q9Z177
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 13, 2004
Last modified: October 25, 2017
This is version 115 of the entry and version 1 of the sequence. See 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