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Index > Protein center > PIAS2(Gene name) > Human
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  • PIAS2 (Gene name),
  • E3 SUMO-protein ligase PIAS2 (Protein name ),  PIAS2_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Gene name:
    PIAS2(PIASX);
    Protein name:
    E3 SUMO-protein ligase PIAS2;
    Alternative:
    DAB2-interacting protein(DIP);Androgen receptor-interacting protein 3(ARIP3);PIAS-NY protein;Msx-interacting zinc finger protein(Miz1);Protein inhibitor of activated STAT2;Protein inhibitor of activated STAT x;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    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 (By similarity). 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 G(1) phase.
    Function:
    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 coregulator 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 the 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. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2-alpha.
    Subcellular Location:
    Nucleus speckle Nucleus PML body Colocalizes at least partially with promyelocytic leukemia nuclear bodies.
    Protein Attributes:
    Sequence length:
    621
    Sequence:
    50:
    MADFEELRNM | VSSFRVSELQ | VLLGFAGRNK | SGRKHDLLMR | ALHLLKSGCS | 
    100:
    PAVQIKIREL | YRRRYPRTLE | GLSDLSTIKS | SVFSLDGGSS | PVEPDLAVAG | 
    150:
    IHSLPSTSVT | PHSPSSPVGS | VLLQDTKPTF | EMQQPSPPIP | PVHPDVQLKN | 
    200:
    LPFYDVLDVL | IKPTSLVQSS | IQRFQEKFFI | FALTPQQVRE | ICISRDFLPG | 
    250:
    GRRDYTVQVQ | LRLCLAETSC | PQEDNYPNSL | CIKVNGKLFP | LPGYAPPPKN | 
    300:
    GIEQKRPGRP | LNITSLVRLS | SAVPNQISIS | WASEIGKNYS | MSVYLVRQLT | 
    350:
    SAMLLQRLKM | KGIRNPDHSR | ALIKEKLTAD | PDSEIATTSL | RVSLMCPLGK | 
    400:
    MRLTIPCRAV | TCTHLQCFDA | ALYLQMNEKK | PTWICPVCDK | KAAYESLILD | 
    450:
    GLFMEILNDC | SDVDEIKFQE | DGSWCPMRPK | KEAMKVSSQP | CTKIESSSVL | 
    500:
    SKPCSVTVAS | EASKKKVDVI | DLTIESSSDE | EEDPPAKRKC | IFMSETQSSP | 
    550:
    TKGVLMYQPS | SVRVPSVTSV | DPAAIPPSLT | DYSVPFHHTP | ISSMSSDLPG | 
    600:
    LDFLSLIPVD | PQYCPPMFLD | SLTSPLTASS | TSVTTTSSHE | SSTHVSSSSS | 
    621:
    RSETGVITSS | GSNIPDIISL | D
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    UniGene:
    SMR:
    MIM:
    UniGene:
    KEGG:
    Pfam:
    Pfam:
    String:
    Uniprot:
     
    FOR
    ELISA Kit for Human E3 SUMO-protein ligase PIAS2
    ELISA Kit for Human E3 SUMO-protein ligase PIAS2
    ELISA Kit for Human E3 SUMO-protein ligase PIAS2
    CLIA Kit for Human E3 SUMO-protein ligase PIAS2
    CLIA Kit for Human E3 SUMO-protein ligase PIAS2
    CLIA Kit for Human E3 SUMO-protein ligase PIAS2
    Polyclonal Antibody for Human E3 SUMO-protein ligase PIAS2
    Polyclonal Antibody for Human E3 SUMO-protein ligase PIAS2
    Polyclonal Antibody for Human E3 SUMO-protein ligase PIAS2
    Monoclonal Antibody for Human E3 SUMO-protein ligase PIAS2
    Monoclonal Antibody for Human E3 SUMO-protein ligase PIAS2
    Monoclonal Antibody for Human E3 SUMO-protein ligase PIAS2
    Protein for Human E3 SUMO-protein ligase PIAS2
    Protein for Human E3 SUMO-protein ligase PIAS2
    Protein for Human E3 SUMO-protein ligase PIAS2

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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PIAS2-ALPHA AND PIAS2-BETA)
      tissue: B-cell.
    2. 2.
      "Molecular cloning and characterization of a novel splicing variant of PIASx."
      Zheng Y. , Zhou Z.-M. , Yin L.-L. , Li J.-M. , Sha J.-H.
      Acta Pharmacol. Sin.25:1058-1064(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3);TISSUE SPECIFICITY;DEVELOPMENTAL STAGE
      tissue: Testis.
    3. 4.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PIAS2-ALPHA)
      tissue: Brain.
    4. 5.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: TISSUE SPECIFICITY
    5. 6.
      "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.275:36316-36323(2000) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH SUMO1; TP73 AND TP53
    6. 7.
      "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor."
      Takahashi K. , Taira T. , Niki T. , Seino C. , Iguchi-Ariga S.M.M. , Ariga H.
      J. Biol. Chem.276:37556-37563(2001) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH PARK7;SUBCELLULAR LOCATION
    7. 8.
      "Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells."
      Gross M. , Liu B. , Tan J.-A. , French F.S. , Carey M. , Shuai K.
      Oncogene20:3880-3887(2001) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: TISSUE SPECIFICITY
    8. 9.
      "SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling."
      Rui H.L. , Fan E. , Zhou H.M. , Xu Z. , Zhang Y. , Lin S.C.
      J. Biol. Chem.277:42981-42986(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH AXIN1
    9. 10.
      "Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes."
      Miyauchi Y. , Yogosawa S. , Honda R. , Nishida T. , Yasuda H.
      J. Biol. Chem.277:50131-50136(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SUMOYLATION OF MDM2;SUBCELLULAR LOCATION;MUTAGENESIS OF CYS-362
    10. 11.
      "Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity."
      Schmidt D. , Mueller S.
      Proc. Natl. Acad. Sci. U.S.A.99:2872-2877(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH JUN; TP53 AND UBE2I;SUMOYLATION;MUTAGENESIS OF CYS-362
    11. 12.
      "PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4."
      Arora T. , Liu B. , He H. , Kim J. , Murphy T.L. , Murphy K.M. , Modlin R.L. , Shuai K.
      J. Biol. Chem.278:21327-21330(2003) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH STAT4;SUBCELLULAR LOCATION
    12. 13.
      "Repression of the transactivating capacity of the oncoprotein PLAG1 by SUMOylation."
      Van Dyck F. , Delvaux E.L.D. , Van de Ven W.J.M. , Chavez M.V.
      J. Biol. Chem.279:36121-36131(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH PLAG1
    13. 14.
      "PIASx acts as an Elk-1 coactivator by facilitating derepression."
      Yang S.-H. , Sharrocks A.D.
      EMBO J.24:2161-2171(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH ELK1
    14. 15.
      "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
      Shinbo Y. , Niki T. , Taira T. , Ooe H. , Takahashi-Niki K. , Maita C. , Seino C. , Iguchi-Ariga S.M.M. , Ariga H.
      Cell Death Differ.13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PARK7 SUMOYLATION
    15. 16.
      "Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation."
      Wei H. , Wang X. , Gan B. , Urvalek A.M. , Melkoumian Z.K. , Guan J.-L. , Zhao J.
      J. Biol. Chem.281:16664-16671(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH KLF8
    16. 17.
      "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V. , Vermeulen M. , Santamaria A. , Kumar C. , Miller M.L. , Jensen L.J. , Gnad F. , Cox J. , Jensen T.S. , Nigg E.A. , Brunak S. , Mann M.
      Sci. Signal.3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Cervix carcinoma.
    17. 18.
      "MDA5 is SUMOylated by PIAS2? in the upregulation of type I interferon signaling."
      Fu J. , Xiong Y. , Xu Y. , Cheng G. , Tang H.
      Mol. Immunol.48:415-422(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH IFIH1/MDA5
    18. 19.
      "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T. , Prokhorova T.A. , Akimov V. , Henningsen J. , Johansen P.T. , Kratchmarova I. , Kassem M. , Mann M. , Olsen J.V. , Blagoev B.
      Sci. Signal.4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-477 AND SER-478;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    19. 20.
      "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
      Rabellino A. , Carter B. , Konstantinidou G. , Wu S.Y. , Rimessi A. , Byers L.A. , Heymach J.V. , Girard L. , Chiang C.M. , Teruya-Feldstein J. , Scaglioni P.P.
      Cancer Res.72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;SUBCELLULAR LOCATION;INTERACTION WITH PML
    20. 21.
      "Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation."
      Song J. , Zhang Z. , Hu W. , Chen Y.
      J. Biol. Chem.280:40122-40129(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF 466-488 IN COMPLEX WITH SUMO1;MUTAGENESIS OF VAL-467; VAL-469; ILE-470; LEU-472 AND THR-473
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