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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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri312 – 38978SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • 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

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-3232118. SUMOylation of transcription factors.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5696395. Formation of Incision Complex in GG-NER.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi708413. Pias3.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus 1 Publication
  • Nucleus speckle By similarity

  • Note: Colocalizes with MITF in the nucleus. Colocalizes with GFI1 in nuclear dots. Colocalizes with SUMO1 in nuclear granules.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • dendrite Source: RGD
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: RGD
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 628627E3 SUMO-protein ligase PIAS3PRO_0000218981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Cross-linki46 – 46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei295 – 2951Asymmetric dimethylarginineBy similarity
Cross-linki307 – 307Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei455 – 4551PhosphoserineBy similarity
Modified residuei456 – 4561PhosphoserineBy similarity
Modified residuei472 – 4721PhosphoserineBy similarity
Modified residuei492 – 4921PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO70260.

PTM databases

PhosphoSiteiO70260.

Expressioni

Tissue specificityi

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

Gene expression databases

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

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi249779. 1 interaction.
DIPiDIP-47656N.
IntActiO70260. 1 interaction.
STRINGi10116.ENSRNOP00000028814.

Structurei

3D structure databases

ProteinModelPortaliO70260.
SMRiO70260. Positions 1-65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
BLAST
Domaini115 – 280166PINITPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 200199Interaction with CCAR2By similarityAdd
BLAST
Regioni450 – 46011SUMO1-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi19 – 235LXXLL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 13353Pro-richAdd
BLAST

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 fingeri312 – 38978SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
GeneTreeiENSGT00550000074410.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiO70260.
KOiK16064.
OMAiGELKHMV.
OrthoDBiEOG7HF1JB.
PhylomeDBiO70260.
TreeFamiTF323787.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027226. PIAS3.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF10. PTHR10782:SF10. 2 hits.
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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliO70260.
SMRiO70260. Positions 1-65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249779. 1 interaction.
DIPiDIP-47656N.
IntActiO70260. 1 interaction.
STRINGi10116.ENSRNOP00000028814.

Protein family/group databases

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

PTM databases

PhosphoSiteiO70260.

Proteomic databases

PaxDbiO70260.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10401.
RGDi708413. Pias3.

Phylogenomic databases

eggNOGiKOG2169. Eukaryota.
ENOG410XQ2E. LUCA.
GeneTreeiENSGT00550000074410.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiO70260.
KOiK16064.
OMAiGELKHMV.
OrthoDBiEOG7HF1JB.
PhylomeDBiO70260.
TreeFamiTF323787.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-RNO-3232118. SUMOylation of transcription factors.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5696395. Formation of Incision Complex in GG-NER.

Miscellaneous databases

NextBioi616161.
PROiO70260.

Gene expression databases

ExpressionAtlasiO70260. baseline and differential.
GenevisibleiO70260. RN.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027226. PIAS3.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF10. PTHR10782:SF10. 2 hits.
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

  1. "Cloning and expression of a novel K+ channel regulatory protein, KChAP."
    Wible B.A., Yang Q., Kuryshev Y.A., Accili E.A., Brown A.M.
    J. Biol. Chem. 273:11745-11751(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "A new role for the STAT3 inhibitor, PIAS3: a repressor of microphthalmia transcription factor."
    Levy C., Nechushtan H., Razin E.
    J. Biol. Chem. 277:1962-1966(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MITF.
  3. "The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer."
    Rycyzyn M.A., Clevenger C.V.
    Proc. Natl. Acad. Sci. U.S.A. 99:6790-6795(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAT5.

Entry informationi

Entry nameiPIAS3_RAT
AccessioniPrimary (citable) accession number: O70260
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: March 1, 2002
Last modified: March 16, 2016
This is version 111 of the entry and version 2 of the sequence. [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

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.