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PIAS3 (protein inhibitor of activated STAT, 3)

Written2010-04Gilles Spoden, Werner Zwerschke
Institute for Medical Microbiology, Hygiene, University Medical Center of the Johannes Gutenberg University Mainz, Hochhaus am Augustus-platz, 55131 Mainz, Germany (GS); Cell Metabolism, Differentiation Research Group, Institute for Biomedical Aging Research, Rennweg 10, 6020 Innsbruck, Austria (ZW); Tumorvirology Research Group, Tyrolean Cancer Research Institute at Medical University Innsbruck, Innrain 66, 6020 Innsbruck, Austria (ZW)

(Note : for Links provided by Atlas : click)


Alias (NCBI)FLJ14651
HGNC Alias symbFLJ14651
HGNC Alias namezinc finger, MIZ-type containing 5
LocusID (NCBI) 10401
Atlas_Id 41709
Location 1q21.1  [Link to chromosome band 1q21]
Location_base_pair Starts at 145848522 and ends at 145859081 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping PIAS3.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
PIAS3 (1q21.1)::C12orf45 (12q23.3)PIAS3 (1q21.1)::PODN (1p32.3)PIAS3 (1q21.1)::REN (1q32.1)
RPAP3 (12q13.11)::PIAS3 (1q21.1)RPS21 (20q13.33)::PIAS3 (1q21.1)


Note The gene codes for a protein of the PIAS family (protein inhibitor of activated STAT (signal transducer and activator of transcription)). PIAS3 regulates the activity of several transcription factors by direct protein-protein interaction. Further, PIAS3 is a SUMO (small ubiquitin-like modifier)-E3 ligase, catalyzing the covalent, post-translational modification of specific target proteins with SUMO. Different splice variants of PIAS3 have been identified but the full-length sequence of some of these variants has not been described.
  Figure 1. PIAS3 gene 10559 bp. Exons 1 to 14 (UTR in white, coding sequence in red) Exon 1: 1-115 (5'UTR: 1-91); Exon 2: 2075-2492; Exon 3: 2650-2734; Exon 4: 2963-3013; Exon 5: 3255-3345; Exon 6: 4201-4335; Exon 7: 4518-4623; Exon 8: 5195-5268; Exon 9: 5417-5577; Exon 10: 7928-8061; Exon 11: 8142-8310; Exon 12: 8495-8628; Exon 13: 8812-8849; Exon 14: 9369-10559 (3'UTR: 9636-10559).
Description The human PIAS3 gene is 10559 bp long and consists of 14 exons and 13 introns.
Transcription Transcript length 2902 bp (CDS 1887 bp ; residues 628 aa).
Pseudogene No pseudogene reported.


  Figure 2. The schematic domain structure of human PIAS3 protein is shown. SAP domain: nuclear localization and binding to DNA, transcription factors, coregulators. PINIT: nuclear retention, transcriptional repression. SP-RING: protein-protein interactions, interacts with the SUMO conjugase Ubc9, sumoylation. SIM: binding to SUMO. S/T: variable region, binding to coactivators.
Description The human PIAS3 protein is a E3 SUMO-protein ligase consisting of 628 amino acids. It contains 5 conserved regions, the SAP, PINIT, SP-RING, SIM and S/T domains (figure 2).
Expression PIAS3 is ubiquitously expressed.
Localisation Nuclear as well as cytoplasmic localization.
Function PIAS3 belongs to the mammalian protein inhibitor of activated STAT (PIAS) protein family, originally identified as cytokine-induced inhibitors of the STAT family of transcription factors. This protein class, referred to as SUMO-E3 ligases, increases the efficiency of SUMO conjugation. SUMO, a small ubiquitin-like modifier protein, is conjugated to a large number of cellular target proteins. Similar to enzymatic ubiquitination, the conjugation of specific SUMO proteins (SUMO-1-SUMO-3) to target proteins requires an E1-activating enzyme (Aos1/Uba2) as well as an E2-type SUMO-1-conjugating enzyme (Ubc9). Similar to many ubiquitin E3 ligases, these proteins contain a putative RING finger-like structure (SP-RING, figure 2), which is essential for their SUMO-E3 ligase activities toward various target proteins. Sumoylation is a dynamic process with highly diverse outcomes, ranging from changes in subcellular localization, signal transduction, transcriptional regulation to altered activity and stability of the modified protein. PIAS3 do, however, not only operate as SUMO-E3, since its coregulator effects are often independent of its RING-finger like domain but dependent on its capability to interact with sumoylated proteins via its conserved SIM (SUMO-interacting motif) or SAP (scaffold attachment factor-A/B/acinus/PIAS) domain (figure 2). Beside the N-terminal SAP, the SIM and the RING-type zinc-binding domain, a PINIT motif, and a serine/ threonine-rich C-terminal region (S/T) is conserved in PIAS3 (figure 2).
PIAS3 is involved in cytoplasmic regulation, such as functional interaction of PIAS3 with metabotropic glutamate receptor-8, voltage-gated potassium channel Kv1.5 and pyruvate kinase subtype M2, but the majority of so far reported interactions of the PIAS3 protein occurred with transcription factors or other proteins linked to nuclear regulation. PIAS3 can act in both transcriptional repression and activation. PIAS3 has been shown to repress STAT3 and Stat5 dependent transcriptional activation by blocking the DNA-binding of the factor without influencing its sumoylation. It interacts with and promotes sumoylation of the photoreceptor-specific transcription factor Nr2e3 when bound to specific promoters, which converts the factor to a transcriptional repressor. Moreover, PIAS3 was described as a repressor of microphthalmia transcription factor (MITF) and it was shown that PIAS3 blocks NF-kB mediated transcriptional activation by interacting with the p65/RelA subunit. Repression of IRF1-mediated transcription by PIAS3 has also been shown. PIAS3 has been shown to activate transcription mediated by Smad proteins through forming a complex with Smads and coactivator p300/CBP; moreover, PIAS proteins enhance steroid receptor-dependent transcription through an SP-RING-mediated interaction and sumoylation of the coactivator protein GRIP1/SCR2. Finally, PIAS3 was shown to modulate the ability of TIF2 to mediate ligand-enhanced transcription activation positively or negatively, for different steroid receptors.
Homology The mammalian PIAS family consists of seven structurally related proteins (PIAS1, PIAS3, PIAS3b, PIASxa, PIASxb, PIASy, and PIASyE6) encoded by four genes. PIAS orthologs are found in nonvertebrate animal species, plants and yeasts.

Implicated in

Entity Prostate Cancer
Oncogenesis PIAS3 is expressed in normal prostate and in prostate cancer cells and has been shown to modulate the transcriptional activity of androgen receptor in prostate cancer cells. Moreover, PIAS3 (KChAP) induces increased K+ efflux and apoptosis in prostate cancer lines.
Entity Glioblastoma multiforme (GBM)
Oncogenesis The activation of STATs and loss of their natural inhibitors SOCS and PIAS is common in various human cancers. STAT3, a cytoplasmic transcription factor that becomes activated in response to a variety of cytokines and growth factors is aberrantly activated in GBM tumors. STAT3 activation correlates with strongly reduced PIAS3 protein expression in GBM tissues. Inhibition of PIAS3 resulted in enhanced glioblastoma cellular proliferation, and, conversely, PIAS3 overexpression inhibits STAT3 transcriptional activity, expression of STAT3-regulated genes, and cell proliferation. This suggests that the loss of PIAS3 in GBM contributes to enhanced STAT3 transcriptional activity and subsequent cell proliferation.
Entity Melanoma
Oncogenesis PIAS3 functions as a key molecule in suppressing the transcriptional activity of both MITF and STAT3, two transcription factors that play a major role in the development, proliferation and survival of mast cells and melanocytes. In addition to its role in normal cell signaling, constitutively activated STAT3 signaling directly contributes to oncogenesis in many human cancers. STAT3 cooperates with MITF in the induction of cellular transformation. Evidence was provided suggesting that PIAS3 halt proliferation and induce apoptotic cell death in mast cells and in melanoma cells by inhibiting the transcriptional activity of the two oncogenic factors MITF and STAT3. Therefore PIAS3 may play a role in tumor suppression by inhibiting oncogenic processes induced by STAT3 and MITF.
Entity Non-small cell lung cancer (NSCLC)
Disease The Epidermal Growth Factor Receptor (EGFR)-STAT3 axis plays an important role in oncogenic signaling of non-small cell lung cancer (NSCLC). The negative regulator of STAT3-mediated transcriptional activation, PIAS3, was shown to modulate oncogenic EGFR-STAT3 signaling in lung cancer. Overexpression of PIAS3 decreases STAT3 transcriptional activity and proliferation of NSCLC cells and when used in conjunction with EGFR inhibitors, further increased the anti-proliferative effects. This suggests that PIAS3 acts as an inhibitor of EGFR-STAT3 induced oncogenic action.

To be noted

TAR syndrome (Thrombocytopenia-absent radius) is a rare genetic disorder characterized by low platelet counts and bilateral radial aplasia. TAR is also frequently associated with cardiac abnormalities and cow's milk intolerance. In 2007 a research article described a common microdeletion of 200 kb on chromosome 1q21.1 in patients with TAR syndrome. PIAS3 is one of 11 genes encompassed by this microdeletion.


STATs in oncogenesis.
Bowman T, Garcia R, Turkson J, Jove R.
Oncogene. 2000 May 15;19(21):2474-88. (REVIEW)
PMID 10851046
Loss of protein inhibitors of activated STAT-3 expression in glioblastoma multiforme tumors: implications for STAT-3 activation and gene expression.
Brantley EC, Nabors LB, Gillespie GY, Choi YH, Palmer CA, Harrison K, Roarty K, Benveniste EN.
Clin Cancer Res. 2008 Aug 1;14(15):4694-704.
PMID 18676737
The role of STATs in transcriptional control and their impact on cellular function.
Bromberg J, Darnell JE Jr.
Oncogene. 2000 May 15;19(21):2468-73. (REVIEW)
PMID 10851045
Specific inhibition of Stat3 signal transduction by PIAS3.
Chung CD, Liao J, Liu B, Rao X, Jay P, Berta P, Shuai K.
Science. 1997 Dec 5;278(5344):1803-5.
PMID 9388184
The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L.
Duval D, Duval G, Kedinger C, Poch O, Boeuf H.
FEBS Lett. 2003 Nov 6;554(1-2):111-8.
PMID 14596924
Concepts in sumoylation: a decade on.
Geiss-Friedlander R, Melchior F.
Nat Rev Mol Cell Biol. 2007 Dec;8(12):947-56. (REVIEW)
PMID 18000527
Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells.
Gross M, Liu B, Tan J, French FS, Carey M, Shuai K.
Oncogene. 2001 Jun 28;20(29):3880-7.
PMID 11439351
The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family.
Hari KL, Cook KR, Karpen GH.
Genes Dev. 2001 Jun 1;15(11):1334-48.
PMID 11390354
SP-RING for SUMO: new functions bloom for a ubiquitin-like protein.
Hochstrasser M.
Cell. 2001 Oct 5;107(1):5-8.
PMID 11595179
PIAS3 suppresses NF-kappaB-mediated transcription by interacting with the p65/RelA subunit.
Jang HD, Yoon K, Shin YJ, Kim J, Lee SY.
J Biol Chem. 2004 Jun 4;279(23):24873-80. Epub 2004 Mar 26.
PMID 15140884
PIAS3 (protein inhibitor of activated STAT-3) modulates the transcriptional activation mediated by the nuclear receptor coactivator TIF2.
Jimenez-Lara AM, Heine MJ, Gronemeyer H.
FEBS Lett. 2002 Aug 28;526(1-3):142-6.
PMID 12208521
Protein modification by SUMO.
Johnson ES.
Annu Rev Biochem. 2004;73:355-82. (REVIEW)
PMID 15189146
STAT3 and MITF cooperatively induce cellular transformation through upregulation of c-fos expression.
Joo A, Aburatani H, Morii E, Iba H, Yoshimura A.
Oncogene. 2004 Jan 22;23(3):726-34.
PMID 14737107
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. 2000 Nov 11;278(1):9-13.
PMID 11071847
Complex inheritance pattern resembling autosomal recessive inheritance involving a microdeletion in thrombocytopenia-absent radius syndrome.
Klopocki E, Schulze H, Strauss G, Ott CE, Hall J, Trotier F, Fleischhauer S, Greenhalgh L, Newbury-Ecob RA, Neumann LM, Habenicht R, Konig R, Seemanova E, Megarbane A, Ropers HH, Ullmann R, Horn D, Mundlos S.
Am J Hum Genet. 2007 Feb;80(2):232-40. Epub 2006 Dec 21.
PMID 17236129
Cooperative interaction between protein inhibitor of activated signal transducer and activator of transcription-3 with epidermal growth factor receptor blockade in lung cancer.
Kluge A, Dabir S, Kern J, Nethery D, Halmos B, Ma P, Dowlati A.
Int J Cancer. 2009 Oct 1;125(7):1728-34.
PMID 19569236
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 JJ, Janne OA.
J Biol Chem. 2002 May 17;277(20):17781-8. Epub 2002 Mar 13.
PMID 11893729
Identifying a common molecular mechanism for inhibition of MITF and STAT3 by PIAS3.
Levy C, Lee YN, Nechushtan H, Schueler-Furman O, Sonnenblick A, Hacohen S, Razin E.
Blood. 2006 Apr 1;107(7):2839-45. Epub 2005 Dec 20.
PMID 16368885
A new role for the STAT3 inhibitor, PIAS3: a repressor of microphthalmia transcription factor.
Levy C, Nechushtan H, Razin E.
J Biol Chem. 2002 Jan 18;277(3):1962-6. Epub 2001 Nov 14.
PMID 11709556
Role played by microphthalmia transcription factor phosphorylation and its Zip domain in its transcriptional inhibition by PIAS3.
Levy C, Sonnenblick A, Razin E.
Mol Cell Biol. 2003 Dec;23(24):9073-80.
PMID 14645519
Activation of Smad transcriptional activity by protein inhibitor of activated STAT3 (PIAS3).
Long J, Wang G, Matsuura I, He D, Liu F.
Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):99-104. Epub 2003 Dec 22.
PMID 14691252
SUMOylation regulates kainate-receptor-mediated synaptic transmission.
Martin S, Nishimune A, Mellor JR, Henley JM.
Nature. 2007 May 17;447(7142):321-5. Epub 2007 May 7.
PMID 17486098
Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif.
Minty A, Dumont X, Kaghad M, Caput D.
J Biol Chem. 2000 Nov 17;275(46):36316-23.
PMID 10961991
The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses.
Miura K, Rus A, Sharkhuu A, Yokoi S, Karthikeyan AS, Raghothama KG, Baek D, Koo YD, Jin JB, Bressan RA, Yun DJ, Hasegawa PM.
Proc Natl Acad Sci U S A. 2005 May 24;102(21):7760-5. Epub 2005 May 13.
PMID 15894620
PIAS3 induces SUMO-1 modification and transcriptional repression of IRF-1.
Nakagawa K, Yokosawa H.
FEBS Lett. 2002 Oct 23;530(1-3):204-8.
PMID 12387893
PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription.
Nishida T, Yasuda H.
J Biol Chem. 2002 Nov 1;277(44):41311-7. Epub 2002 Aug 9.
PMID 12177000
Overexpression of PIAS3 suppresses cell growth and restores the drug sensitivity of human lung cancer cells in association with PI3-K/Akt inactivation.
Ogata Y, Osaki T, Naka T, Iwahori K, Furukawa M, Nagatomo I, Kijima T, Kumagai T, Yoshida M, Tachibana I, Kawase I.
Neoplasia. 2006 Oct;8(10):817-25.
PMID 17032498
Pias3-dependent SUMOylation directs rod photoreceptor development.
Onishi A, Peng GH, Hsu C, Alexis U, Chen S, Blackshaw S.
Neuron. 2009 Jan 29;61(2):234-46.
PMID 19186166
PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription.
Palvimo JJ.
Biochem Soc Trans. 2007 Dec;35(Pt 6):1405-8. (REVIEW)
PMID 18031232
The intranuclear prolactin/cyclophilin B complex as a transcriptional inducer.
Rycyzyn MA, Clevenger CV.
Proc Natl Acad Sci U S A. 2002 May 14;99(10):6790-5. Epub 2002 May 7.
PMID 11997457
PIAS proteins: pleiotropic interactors associated with SUMO.
Rytinki MM, Kaikkonen S, Pehkonen P, Jaaskelainen T, Palvimo JJ.
Cell Mol Life Sci. 2009 Sep;66(18):3029-41. Epub 2009 Jun 13.
PMID 19526197
PIAS/SUMO: new partners in transcriptional regulation.
Schmidt D, Muller S.
Cell Mol Life Sci. 2003 Dec;60(12):2561-74. (REVIEW)
PMID 14685683
Sumoylation of the estrogen receptor alpha hinge region regulates its transcriptional activity.
Sentis S, Le Romancer M, Bianchin C, Rostan MC, Corbo L.
Mol Endocrinol. 2005 Nov;19(11):2671-84. Epub 2005 Jun 16.
PMID 15961505
Regulation of gene-activation pathways by PIAS proteins in the immune system.
Shuai K, Liu B.
Nat Rev Immunol. 2005 Aug;5(8):593-605. (REVIEW)
PMID 16056253
Interplay between MITF, PIAS3, and STAT3 in mast cells and melanocytes.
Sonnenblick A, Levy C, Razin E.
Mol Cell Biol. 2004 Dec;24(24):10584-92.
PMID 15572665
The SUMO-E3 ligase PIAS3 targets pyruvate kinase M2.
Spoden GA, Morandell D, Ehehalt D, Fiedler M, Jansen-Durr P, Hermann M, Zwerschke W.
J Cell Biochem. 2009 May 15;107(2):293-302.
PMID 19308990
Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators.
Tan JA, Hall SH, Hamil KG, Grossman G, Petrusz P, French FS.
J Biol Chem. 2002 May 10;277(19):16993-7001. Epub 2002 Mar 4.
PMID 11877418
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.
J Hum Genet. 1999;44(3):193-6.
PMID 10319586
Ubiquitin-dependent proteolytic control of SUMO conjugates.
Uzunova K, Gottsche K, Miteva M, Weisshaar SR, Glanemann C, Schnellhardt M, Niessen M, Scheel H, Hofmann K, Johnson ES, Praefcke GJ, Dohmen RJ.
J Biol Chem. 2007 Nov 23;282(47):34167-75. Epub 2007 Aug 29.
PMID 17728242
Increased K+ efflux and apoptosis induced by the potassium channel modulatory protein KChAP/PIAS3beta in prostate cancer cells.
Wible BA, Wang L, Kuryshev YA, Basu A, Haldar S, Brown AM.
J Biol Chem. 2002 May 17;277(20):17852-62. Epub 2002 Mar 4.
PMID 11877452
Cloning and expression of a novel K+ channel regulatory protein, KChAP.
Wible BA, Yang Q, Kuryshev YA, Accili EA, Brown AM.
J Biol Chem. 1998 May 8;273(19):11745-51.
PMID 9565597
A specific epitope of protein inhibitor of activated STAT3 is responsible for the induction of apoptosis in rat transformed mast cells.
Yagil Z, Kay G, Nechushtan H, Razin E.
J Immunol. 2009 Feb 15;182(4):2168-75.
PMID 19201870


This paper should be referenced as such :
Spoden, G ; Zwerschke, W
PIAS3 (protein inhibitor of activated STAT, 3)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(1):39-42.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)PIAS3   16861
Atlas Explorer : (Salamanque)PIAS3
Entrez_Gene (NCBI)PIAS3    protein inhibitor of activated STAT 3
GeneCards (Weizmann)PIAS3
Ensembl hg19 (Hinxton)ENSG00000131788 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000131788 [Gene_View]  ENSG00000131788 [Sequence]  chr1:145848522-145859081 [Contig_View]  PIAS3 [Vega]
ICGC DataPortalENSG00000131788
TCGA cBioPortalPIAS3
Genatlas (Paris)PIAS3
SOURCE (Princeton)PIAS3
Genetics Home Reference (NIH)PIAS3
Genomic and cartography
GoldenPath hg38 (UCSC)PIAS3  -     chr1:145848522-145859081 -  1q21.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PIAS3  -     1q21.1   [Description]    (hg19-Feb_2009)
GoldenPathPIAS3 - 1q21.1 [CytoView hg19]  PIAS3 - 1q21.1 [CytoView hg38]
Genome Data Viewer NCBIPIAS3 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB021868 AK027557 AK125158 AK294231 AK304039
RefSeq transcript (Entrez)NM_006099
Consensus coding sequences : CCDS (NCBI)PIAS3
Gene ExpressionPIAS3 [ NCBI-GEO ]   PIAS3 [ EBI - ARRAY_EXPRESS ]   PIAS3 [ SEEK ]   PIAS3 [ MEM ]
Gene Expression Viewer (FireBrowse)PIAS3 [ Firebrowse - Broad ]
GenevisibleExpression of PIAS3 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10401
GTEX Portal (Tissue expression)PIAS3
Human Protein AtlasENSG00000131788-PIAS3 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9Y6X2   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9Y6X2  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9Y6X2
Catalytic activity : Enzyme2.3.2.- [ Enzyme-Expasy ]   2.3.2.-2.3.2.- [ IntEnz-EBI ]   2.3.2.- [ BRENDA ]   2.3.2.- [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)PINIT (PS51466)    SAP (PS50800)    ZF_SP_RING (PS51044)   
Domains : Interpro (EBI)PIAS1/PIAS3    PINIT    PINIT_sf    SAP_dom    SAP_dom_sf    Znf_MIZ    Znf_RING/FYVE/PHD   
Domain families : Pfam (Sanger)PINIT (PF14324)    zf-MIZ (PF02891)   
Domain families : Pfam (NCBI)pfam14324    pfam02891   
Domain families : Smart (EMBL)SAP (SM00513)  
Conserved Domain (NCBI)PIAS3
PDB Europe4MVT   
Structural Biology KnowledgeBase4MVT   
SCOP (Structural Classification of Proteins)4MVT   
CATH (Classification of proteins structures)4MVT   
AlphaFold pdb e-kbQ9Y6X2   
Human Protein Atlas [tissue]ENSG00000131788-PIAS3 [tissue]
Protein Interaction databases
IntAct (EBI)Q9Y6X2
Ontologies - Pathways
Ontology : AmiGOnegative regulation of transcription by RNA polymerase II  transcription coregulator activity  protein binding  nucleoplasm  cytoplasm  regulation of transcription by RNA polymerase II  protein C-terminus binding  zinc ion binding  response to hormone  positive regulation of gene expression  negative regulation of gene expression  potassium channel regulator activity  nuclear speck  protein sumoylation  protein sumoylation  protein sumoylation  protein sumoylation  SUMO transferase activity  SUMO transferase activity  enzyme binding  dendrite  negative regulation of protein sumoylation  positive regulation of protein sumoylation  synapse  negative regulation of osteoclast differentiation  positive regulation of membrane potential  protein N-terminus binding  SUMO ligase activity  TNFSF11-mediated signaling pathway  
Ontology : EGO-EBInegative regulation of transcription by RNA polymerase II  transcription coregulator activity  protein binding  nucleoplasm  cytoplasm  regulation of transcription by RNA polymerase II  protein C-terminus binding  zinc ion binding  response to hormone  positive regulation of gene expression  negative regulation of gene expression  potassium channel regulator activity  nuclear speck  protein sumoylation  protein sumoylation  protein sumoylation  protein sumoylation  SUMO transferase activity  SUMO transferase activity  enzyme binding  dendrite  negative regulation of protein sumoylation  positive regulation of protein sumoylation  synapse  negative regulation of osteoclast differentiation  positive regulation of membrane potential  protein N-terminus binding  SUMO ligase activity  TNFSF11-mediated signaling pathway  
REACTOMEQ9Y6X2 [protein]
REACTOME PathwaysR-HSA-5696395 [pathway]   
NDEx NetworkPIAS3
Atlas of Cancer Signalling NetworkPIAS3
Wikipedia pathwaysPIAS3
Orthology - Evolution
GeneTree (enSembl)ENSG00000131788
Phylogenetic Trees/Animal Genes : TreeFamPIAS3
Homologs : HomoloGenePIAS3
Homology/Alignments : Family Browser (UCSC)PIAS3
Gene fusions - Rearrangements
Fusion : MitelmanPIAS3::REN [1q21.1/1q32.1]  
Fusion : FusionHubACP6--PIAS3    ANKRD35--PIAS3    PIAS3--ANKRD35    PIAS3--BZRAP1    PIAS3--C12ORF45    PIAS3--GBA    PIAS3--PODN    PIAS3--POLR3C    PIAS3--REN    PIAS3--UBB   
RNF115--PIAS3    RPAP3--PIAS3    RPS21--PIAS3    XIST--PIAS3   
Fusion : QuiverPIAS3
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPIAS3 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PIAS3
Exome Variant ServerPIAS3
GNOMAD BrowserENSG00000131788
Varsome BrowserPIAS3
ACMGPIAS3 variants
Genomic Variants (DGV)PIAS3 [DGVbeta]
DECIPHERPIAS3 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPIAS3 
ICGC Data PortalPIAS3 
TCGA Data PortalPIAS3 
Broad Tumor PortalPIAS3
OASIS PortalPIAS3 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPIAS3  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DPIAS3
Mutations and Diseases : HGMDPIAS3
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)PIAS3
DoCM (Curated mutations)PIAS3
CIViC (Clinical Interpretations of Variants in Cancer)PIAS3
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry PIAS3
NextProtQ9Y6X2 [Medical]
Target ValidationPIAS3
Huge Navigator PIAS3 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDPIAS3
Pharm GKB GenePA134989011
Clinical trialPIAS3
DataMed IndexPIAS3
PubMed127 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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