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O75928

- PIAS2_HUMAN

UniProt

O75928 - PIAS2_HUMAN

Protein

E3 SUMO-protein ligase PIAS2

Gene

PIAS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (05 May 2009)
      Previous versions | rss
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    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 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. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys-160'.3 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri331 – 40878SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. DNA binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. SUMO ligase activity Source: BHF-UCL
    5. transcription coactivator activity Source: UniProtKB
    6. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. negative regulation of androgen receptor signaling pathway Source: UniProtKB
    3. positive regulation of transcription, DNA-templated Source: UniProtKB
    4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. protein sumoylation Source: UniProtKB
    6. regulation of osteoblast differentiation Source: Ensembl
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiO75928.
    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
    Short name:
    Miz1
    PIAS-NY protein
    Protein inhibitor of activated STAT x
    Protein inhibitor of activated STAT2
    Gene namesi
    Name:PIAS2
    Synonyms:PIASX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:17311. PIAS2.

    Subcellular locationi

    Nucleus speckle. NucleusPML body
    Note: Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs).

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB
    3. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi362 – 3621C → S or A: Loss of MDM2 and TP53 sumoylation and of autosumoylation; no loss of JUN- and TP53-binding. 2 Publications
    Mutagenesisi467 – 4671V → A: Reduces affinity for SUMO1. 1 Publication
    Mutagenesisi469 – 4691V → A: Abolishes binding to SUMO1. 1 Publication
    Mutagenesisi470 – 4701I → A: Abolishes binding to SUMO1. 1 Publication
    Mutagenesisi472 – 4721L → A: Abolishes binding to SUMO1. 1 Publication
    Mutagenesisi473 – 4731T → A: Reduces affinity for SUMO1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134933292.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 621621E3 SUMO-protein ligase PIAS2PRO_0000218976Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei476 – 4761Phosphoserine1 Publication
    Modified residuei477 – 4771Phosphoserine1 Publication
    Modified residuei478 – 4781Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO75928.
    PaxDbiO75928.
    PRIDEiO75928.

    PTM databases

    PhosphoSiteiO75928.

    Expressioni

    Tissue specificityi

    Mainly expressed in testis. Isoform 3 is expressed predominantly in adult testis, weakly in pancreas, embryonic testis and sperm, and at very low levels in other organs.3 Publications

    Developmental stagei

    Isoform 3 expression in adult testis is 14.2-fold stronger than in embryonic testis.1 Publication

    Inductioni

    Up-regulated transiently during myeloid differentiation in various cells lines, such as HL-60, U-937, K-562, induced by either phorbol ester (TPA) or retinoic acid.

    Gene expression databases

    ArrayExpressiO75928.
    BgeeiO75928.
    CleanExiHS_PIAS2.
    GenevestigatoriO75928.

    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 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 G1 phase. PIAS2-beta interacts with IFIH1/MDA5. Isoform PIAS2-alpha interacts with PML (isoform PML-12).By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GNB2L1P632442EBI-348555,EBI-296739
    MYCP011064EBI-348555,EBI-447544
    RUFY1Q96T513EBI-348555,EBI-3941207
    TP53P046372EBI-348555,EBI-366083
    UBE2IP632795EBI-348555,EBI-80168

    Protein-protein interaction databases

    BioGridi114523. 59 interactions.
    IntActiO75928. 26 interactions.
    MINTiMINT-1455373.
    STRINGi9606.ENSP00000381648.

    Structurei

    Secondary structure

    1
    621
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi154 – 16512
    Beta strandi173 – 1819
    Helixi185 – 1928
    Beta strandi195 – 1973
    Beta strandi203 – 21513
    Beta strandi231 – 2344
    Beta strandi237 – 2393
    Helixi264 – 2663
    Beta strandi271 – 2733
    Beta strandi275 – 2828
    Beta strandi289 – 29810
    Helixi301 – 3099
    Helixi316 – 32712
    Beta strandi340 – 3456
    Turni347 – 3493
    Beta strandi354 – 3596
    Helixi370 – 37910
    Turni386 – 3883
    Helixi394 – 3963
    Beta strandi397 – 4004
    Helixi401 – 4077
    Beta strandi415 – 4184
    Beta strandi469 – 4713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ASQNMR-B466-488[»]
    4FO9X-ray2.39A147-488[»]
    ProteinModelPortaliO75928.
    SMRiO75928. Positions 1-65, 147-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75928.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini134 – 299166PINITPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni467 – 4737SUMO1-binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 235LXXLL motif
    Motifi484 – 4929Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi571 – 61242Ser-richAdd
    BLAST
    Compositional biasi596 – 6027Poly-Ser

    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 fingeri331 – 40878SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG125513.
    HOGENOMiHOG000230594.
    HOVERGENiHBG053598.
    InParanoidiO75928.
    KOiK16063.
    OMAiPHESSTH.
    OrthoDBiEOG7HF1JB.
    PhylomeDBiO75928.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    InterProiIPR027228. PIAS2.
    IPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view]
    PANTHERiPTHR10782:SF12. PTHR10782:SF12. 1 hit.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform PIAS2-beta (identifier: O75928-1) [UniParc]FASTAAdd to Basket

    Also known as: PIASx-beta, Miz1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS    50
    PAVQIKIREL YRRRYPRTLE GLSDLSTIKS SVFSLDGGSS PVEPDLAVAG 100
    IHSLPSTSVT PHSPSSPVGS VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN 150
    LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI FALTPQQVRE ICISRDFLPG 200
    GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP LPGYAPPPKN 250
    GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 300
    SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK 350
    MRLTIPCRAV TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD 400
    GLFMEILNDC SDVDEIKFQE DGSWCPMRPK KEAMKVSSQP CTKIESSSVL 450
    SKPCSVTVAS EASKKKVDVI DLTIESSSDE EEDPPAKRKC IFMSETQSSP 500
    TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP ISSMSSDLPG 550
    LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSSHE SSTHVSSSSS 600
    RSETGVITSS GSNIPDIISL D 621
    Length:621
    Mass (Da):68,240
    Last modified:May 5, 2009 - v3
    Checksum:i6422B383345AD883
    GO
    Isoform PIAS2-alpha (identifier: O75928-2) [UniParc]FASTAAdd to Basket

    Also known as: PIASx-alpha, ARIP3

    The sequence of this isoform differs from the canonical sequence as follows:
         551-572: LDFLSLIPVDPQYCPPMFLDSL → EQRRNDINNELKLGTSSDTVQQ
         573-621: Missing.

    Show »
    Length:572
    Mass (Da):63,396
    Checksum:i63106D68C585F0ED
    GO
    Isoform 3 (identifier: O75928-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: MADFEELR → MNAGKQLQRTLH
         402-621: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:405
    Mass (Da):45,057
    Checksum:i6C16003BCDB6384E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441P → L in AAK48938. (PubMed:15301740)Curated
    Sequence conflicti616 – 6161D → E in AAC36705. (PubMed:9724754)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti207 – 2071V → A.
    Corresponds to variant rs16940108 [ dbSNP | Ensembl ].
    VAR_056693

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 88MADFEELR → MNAGKQLQRTLH in isoform 3. 1 PublicationVSP_012196
    Alternative sequencei402 – 621220Missing in isoform 3. 1 PublicationVSP_012197Add
    BLAST
    Alternative sequencei551 – 57222LDFLS…FLDSL → EQRRNDINNELKLGTSSDTV QQ in isoform PIAS2-alpha. 2 PublicationsVSP_050008Add
    BLAST
    Alternative sequencei573 – 62149Missing in isoform PIAS2-alpha. 2 PublicationsVSP_050009Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077953 mRNA. Translation: AAC36704.1.
    AF077954 mRNA. Translation: AAC36705.1.
    AF361054 mRNA. Translation: AAK48938.1.
    AC090241 Genomic DNA. No translation available.
    AC090373 Genomic DNA. No translation available.
    BC015190 mRNA. Translation: AAH15190.1.
    CCDSiCCDS32824.1. [O75928-1]
    CCDS32825.1. [O75928-2]
    RefSeqiNP_004662.2. NM_004671.3. [O75928-1]
    NP_775298.1. NM_173206.3. [O75928-2]
    UniGeneiHs.657844.

    Genome annotation databases

    EnsembliENST00000324794; ENSP00000317163; ENSG00000078043. [O75928-2]
    ENST00000585916; ENSP00000465676; ENSG00000078043. [O75928-1]
    GeneIDi9063.
    KEGGihsa:9063.
    UCSCiuc002lck.3. human. [O75928-1]
    uc002lcl.3. human. [O75928-2]
    uc002lcn.1. human. [O75928-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077953 mRNA. Translation: AAC36704.1 .
    AF077954 mRNA. Translation: AAC36705.1 .
    AF361054 mRNA. Translation: AAK48938.1 .
    AC090241 Genomic DNA. No translation available.
    AC090373 Genomic DNA. No translation available.
    BC015190 mRNA. Translation: AAH15190.1 .
    CCDSi CCDS32824.1. [O75928-1 ]
    CCDS32825.1. [O75928-2 ]
    RefSeqi NP_004662.2. NM_004671.3. [O75928-1 ]
    NP_775298.1. NM_173206.3. [O75928-2 ]
    UniGenei Hs.657844.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ASQ NMR - B 466-488 [» ]
    4FO9 X-ray 2.39 A 147-488 [» ]
    ProteinModelPortali O75928.
    SMRi O75928. Positions 1-65, 147-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114523. 59 interactions.
    IntActi O75928. 26 interactions.
    MINTi MINT-1455373.
    STRINGi 9606.ENSP00000381648.

    PTM databases

    PhosphoSitei O75928.

    Proteomic databases

    MaxQBi O75928.
    PaxDbi O75928.
    PRIDEi O75928.

    Protocols and materials databases

    DNASUi 9063.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324794 ; ENSP00000317163 ; ENSG00000078043 . [O75928-2 ]
    ENST00000585916 ; ENSP00000465676 ; ENSG00000078043 . [O75928-1 ]
    GeneIDi 9063.
    KEGGi hsa:9063.
    UCSCi uc002lck.3. human. [O75928-1 ]
    uc002lcl.3. human. [O75928-2 ]
    uc002lcn.1. human. [O75928-3 ]

    Organism-specific databases

    CTDi 9063.
    GeneCardsi GC18M044392.
    HGNCi HGNC:17311. PIAS2.
    MIMi 603567. gene.
    neXtProti NX_O75928.
    PharmGKBi PA134933292.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG125513.
    HOGENOMi HOG000230594.
    HOVERGENi HBG053598.
    InParanoidi O75928.
    KOi K16063.
    OMAi PHESSTH.
    OrthoDBi EOG7HF1JB.
    PhylomeDBi O75928.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    SignaLinki O75928.

    Miscellaneous databases

    EvolutionaryTracei O75928.
    GeneWikii Protein_inhibitor_of_activated_STAT2.
    GenomeRNAii 9063.
    NextBioi 33959.
    PROi O75928.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75928.
    Bgeei O75928.
    CleanExi HS_PIAS2.
    Genevestigatori O75928.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    InterProi IPR027228. PIAS2.
    IPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view ]
    PANTHERi PTHR10782:SF12. PTHR10782:SF12. 1 hit.
    Pfami PF14324. PINIT. 1 hit.
    PF02891. zf-MIZ. 1 hit.
    [Graphical view ]
    SMARTi SM00513. SAP. 1 hit.
    [Graphical view ]
    PROSITEi PS51466. PINIT. 1 hit.
    PS50800. SAP. 1 hit.
    PS51044. ZF_SP_RING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PIAS2-ALPHA AND PIAS2-BETA).
      Tissue: B-cell.
    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]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PIAS2-ALPHA).
      Tissue: Brain.
    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]
      Cited for: TISSUE SPECIFICITY.
    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]
      Cited for: INTERACTION WITH SUMO1; TP73 AND TP53.
    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]
      Cited for: INTERACTION WITH PARK7, SUBCELLULAR LOCATION.
    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.
      Oncogene 20:3880-3887(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    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]
      Cited for: INTERACTION WITH AXIN1.
    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]
      Cited for: SUMOYLATION OF MDM2, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-362.
    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]
      Cited for: INTERACTION WITH JUN; TP53 AND UBE2I, SUMOYLATION, MUTAGENESIS OF CYS-362.
    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]
      Cited for: INTERACTION WITH STAT4, SUBCELLULAR LOCATION.
    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]
      Cited for: INTERACTION WITH PLAG1.
    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]
      Cited for: FUNCTION, INTERACTION WITH ELK1.
    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]
      Cited for: FUNCTION IN PARK7 SUMOYLATION.
    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]
      Cited for: INTERACTION WITH KLF8.
    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]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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]
      Cited for: INTERACTION WITH IFIH1/MDA5.
    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]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-477 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
    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]
      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.

    Entry informationi

    Entry nameiPIAS2_HUMAN
    AccessioniPrimary (citable) accession number: O75928
    Secondary accession number(s): O75927, Q96BT5, Q96KE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3