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Protein

E3 SUMO-protein ligase PIAS3

Gene

Pias3

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 and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1. Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (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 fingeri312 – 389SP-RING-typePROSITE-ProRule annotationAdd BLAST78

GO - Molecular functioni

  • enzyme binding Source: Ensembl
  • ligase activity Source: UniProtKB-KW
  • potassium channel regulator activity Source: RGD
  • protein C-terminus binding Source: RGD
  • protein N-terminus binding Source: RGD
  • SUMO transferase activity Source: Ensembl
  • zinc ion binding Source: InterPro

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-3232118. SUMOylation of transcription factors.
R-RNO-4615885. SUMOylation of DNA replication proteins.
UniPathwayiUPA00886.

Protein family/group databases

TCDBi8.A.15.1.1. the k(+) channel accessory protein (kchap) family.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS3 (EC:6.3.2.-)
Alternative name(s):
KChAP
Potassium channel-associated protein
Protein inhibitor of activated STAT protein 3
Gene namesi
Name:Pias3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi708413. Pias3.

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

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002189812 – 628E3 SUMO-protein ligase PIAS3Add BLAST627

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Cross-linki40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei295Asymmetric dimethylarginineBy similarity1
Cross-linki307Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei455PhosphoserineBy similarity1
Modified residuei456PhosphoserineBy similarity1
Cross-linki466Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei472PhosphoserineBy similarity1
Cross-linki482Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei492PhosphoserineBy similarity1

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO70260.

PTM databases

iPTMnetiO70260.
PhosphoSitePlusiO70260.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in lung, kidney and spleen.1 Publication

Gene expression databases

BgeeiENSRNOG00000021218.
ExpressionAtlasiO70260. baseline and differential.
GenevisibleiO70260. RN.

Interactioni

Subunit structurei

Binds SUMO1 and UBE2I. Interacts with AR, BCL11A, GFI1, HMGA2, IRF1, MITF, NCOA2, as well as with STAT3, after treatment with IL6, CNTF or OSM and with STAT5, after PRL stimulation. Interacts with PLAG1 (By similarity). Interacts with ZFHX3. Interacts with MTA1. Interacts with CCAR2 (via N-terminus) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Grik2P422603EBI-7974636,EBI-7809795

GO - Molecular functioni

  • enzyme binding Source: Ensembl
  • protein C-terminus binding Source: RGD
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi249779. 1 interactor.
DIPiDIP-47656N.
IntActiO70260. 4 interactors.
STRINGi10116.ENSRNOP00000028814.

Structurei

3D structure databases

ProteinModelPortaliO70260.
SMRiO70260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 45SAPPROSITE-ProRule annotationAdd BLAST35
Domaini115 – 280PINITPROSITE-ProRule annotationAdd BLAST166

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 200Interaction with CCAR2By similarityAdd BLAST199
Regioni450 – 460SUMO1-bindingBy similarityAdd BLAST11

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi19 – 23LXXLL motif5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi81 – 133Pro-richAdd BLAST53

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 fingeri312 – 389SP-RING-typePROSITE-ProRule annotationAdd BLAST78

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
GeneTreeiENSGT00550000074410.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiO70260.
KOiK16064.
OMAiTIVVNWS.
OrthoDBiEOG091G08G5.
PhylomeDBiO70260.
TreeFamiTF323787.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiView protein in InterPro
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR036361. SAP_dom_sf.
IPR004181. Znf_MIZ.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O70260-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELGELKHM VMSFRVSELQ VLLGFAGRNK SGRKHELLAK ALHLLKSSCA
60 70 80 90 100
PSVQMKIKEL YRRRFPRKTL GPSDLSLLSL PPGTSPVGSP SPLASIPPTL
110 120 130 140 150
LTPGTLLGPK REVDMHPPLP QPVHPDVTMK PLPFYEVYGE LIRPTTLAST
160 170 180 190 200
SSQRFEEAHF TFALTPQQLQ QILTSREVLP GAKCDYTIQV QLRFCLCETS
210 220 230 240 250
CPQEDYFPPN LFVKVNGKLC PLPGYLPPTK NGAEPKRPSR PINITPLARL
260 270 280 290 300
SATVPNTIVV NWSSEFGRNY SLSVYLVRQL TAGTLLQKLR AKGIRNPDHS
310 320 330 340 350
RALIKEKLTA DPDSEVATTS LRVSLMCPLG KMRLTVPCRA LTCAHLQSFD
360 370 380 390 400
AALYLQMNEK KPTWTCPVCD KKAPYESLII DGLFMEILNS CSDCDEIQFM
410 420 430 440 450
EDGSWCPMKP KKEASEVCPP PGYGLDGLQY SPVQEGNQSE NKKRVEVIDL
460 470 480 490 500
TIESSSDEED LPPTKKHCPV TSAAIPALPG SKGALTSGHQ PSSVLRSPAM
510 520 530 540 550
GTLGSDFLSS LPLHEYPPAF PLGADIQGLD LFSFLQTESQ HYSPSVITSL
560 570 580 590 600
DEQDTLGHFF QFRGTPPHFL GPLAPTLGSS HRSATPAPAP GRVSSIVAPG
610 620
SSLREGHGGP LPSGPSLTGC RSDVISLD
Length:628
Mass (Da):68,364
Last modified:March 1, 2002 - v2
Checksum:i6710FD5F0AEB13FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032872 mRNA. Translation: AAC40114.4.
RefSeqiNP_113972.2. NM_031784.2.
UniGeneiRn.14548.

Genome annotation databases

EnsembliENSRNOT00000028814; ENSRNOP00000028814; ENSRNOG00000021218.
GeneIDi83614.
KEGGirno:83614.
UCSCiRGD:708413. rat.

Similar proteinsi

Entry informationi

Entry nameiPIAS3_RAT
AccessioniPrimary (citable) accession number: O70260
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: March 1, 2002
Last modified: October 25, 2017
This is version 124 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Has been shown to interact with voltage-gated potassium channels, including the KCNB1 subunit, and to be critical for current enhancement. However, in view of its mostly nuclear subcellular location and its established function as a transcriptional coregulator, promoting the sumoylation of several transcription factors, the effect on potassium channels awaits further experimental confirmation.Curated

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