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Q8C5D8

- PIAS2_MOUSE

UniProt

Q8C5D8 - PIAS2_MOUSE

Protein

E3 SUMO-protein ligase PIAS2

Gene

Pias2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      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 coregulation 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 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 PIASx-beta, but not isoform PIASx-alpha, promotes MDM2 sumoylation. Isoform PIASx-alpha promotes PARK7 sumoylation. Isoform PIASx-beta promotes NCOA2 sumoylation more efficiently than isoform PIASx-alpha By similarity. Sumoylates PML at'Lys-65' and 'Lys-160' By similarity.By similarity

    Pathwayi

    Regions

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

    GO - Molecular functioni

    1. androgen receptor binding Source: MGI
    2. DNA binding Source: MGI
    3. protein binding Source: IntAct
    4. SUMO ligase activity Source: MGI
    5. ubiquitin protein ligase binding Source: BHF-UCL
    6. zinc ion binding Source: InterPro

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    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
    Protein inhibitor of activated STAT x
    Protein inhibitor of activated STAT2
    Gene namesi
    Name:Pias2
    Synonyms:Miz1, Piasx
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1096566. Pias2.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 621621E3 SUMO-protein ligase PIAS2PRO_0000218977Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Sumoylated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ8C5D8.
    PRIDEiQ8C5D8.

    PTM databases

    PhosphoSiteiQ8C5D8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8C5D8.
    BgeeiQ8C5D8.
    CleanExiMM_PIAS2.
    GenevestigatoriQ8C5D8.

    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. Sumoylation of a target protein seems to enhance the interaction. Binds to sumoylated ELK1. Interacts with PLAG1 By similarity. Binds DNA, such as CDKN1A promoter, in a sequence-specific manner. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase By similarity. Interacts with IFIH1/MDA5 By similarity. Interacts with PML By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dab2P980782EBI-6305825,EBI-1391846
    Dab2P98078-33EBI-6305825,EBI-6305891
    Egr2P081525EBI-8064899,EBI-7070449

    Protein-protein interaction databases

    BioGridi201429. 10 interactions.
    IntActiQ8C5D8. 5 interactions.
    MINTiMINT-1782012.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C5D8.
    SMRiQ8C5D8. Positions 1-65, 147-426.
    ModBaseiSearch...
    MobiDBiSearch...

    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-bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 235LXXLL motif
    Motifi484 – 4929Nuclear localization signal1 Publication

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi571 – 61040Ser-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.
    GeneTreeiENSGT00550000074410.
    HOVERGENiHBG053598.
    InParanoidiQ8C5D8.
    KOiK16063.
    OMAiPHESSTH.
    OrthoDBiEOG7HF1JB.
    PhylomeDBiQ8C5D8.
    TreeFamiTF323787.

    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8C5D8-1) [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 GLCDLSTIKS SVFSLDGSSS PVEPDLPVAG 100
    IHSLPSTSIT 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 KEAMKVTSQP CTKVESSSVF 450
    SKPCSVTVAS DASKKKIDVI DLTIESSSDE EEDPPAKRKC IFMSETQSSP 500
    TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP VSSMSSDLPG 550
    LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSPHE SSTHVSSSSS 600
    RSETGVITSS GRNIPDIISL D 621
    Length:621
    Mass (Da):68,426
    Last modified:December 7, 2004 - v2
    Checksum:iE980B834C2A9C58E
    GO
    Isoform 2 (identifier: Q8C5D8-2) [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 → EQRRNDINNEVQLGASSDTVQQ
         573-621: Missing.

    Show »
    Length:572
    Mass (Da):63,458
    Checksum:i70668C1CEB3702EE
    GO
    Isoform 3 (identifier: Q8C5D8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: Missing.
         551-572: LDFLSLIPVDPQYCPPMFLDSL → EQRRNDINNEVQLGASSDTVQQ
         573-621: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:563
    Mass (Da):62,352
    Checksum:i25D6D636E852AA07
    GO
    Isoform 4 (identifier: Q8C5D8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         563-580: YCPPMFLDSLTSPLTASS → SHLTLNSKQYVCHHHQPP
         581-621: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:580
    Mass (Da):64,421
    Checksum:i4461E5438EC68633
    GO
    Isoform 5 (identifier: Q8C5D8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:612
    Mass (Da):67,320
    Checksum:i98EA1B83556CDE86
    GO

    Sequence cautioni

    The sequence BAB29594.1 differs from that shown. Reason: Frameshift at position 34.
    The sequence AAB96678.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731C → S in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti97 – 971P → A in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti110 – 1101T → A in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti119 – 1191G → E in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti150 – 1501N → T in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti158 – 1581D → E in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti173 – 1731R → G in BAC26579. (PubMed:16141072)Curated
    Sequence conflicti243 – 2431G → A in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti288 – 2881N → Q in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti320 – 3201R → K in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti327 – 3271L → P in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti375 – 3751Q → R in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti413 – 4131V → A in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti438 – 4381S → I in BAC37407. (PubMed:16141072)Curated
    Sequence conflicti458 – 4581V → G in AAF12825. (PubMed:11104669)Curated
    Sequence conflicti464 – 4663KKK → GTR in AAF12825. (PubMed:11104669)Curated
    Isoform 2 (identifier: Q8C5D8-2)
    Sequence conflicti555 – 5551N → T in AAF12825. (PubMed:11104669)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 99Missing in isoform 3 and isoform 5. 1 PublicationVSP_012198
    Alternative sequencei551 – 57222LDFLS…FLDSL → EQRRNDINNEVQLGASSDTV QQ in isoform 2 and isoform 3. 3 PublicationsVSP_012199Add
    BLAST
    Alternative sequencei563 – 58018YCPPM…LTASS → SHLTLNSKQYVCHHHQPP in isoform 4. 1 PublicationVSP_012200Add
    BLAST
    Alternative sequencei573 – 62149Missing in isoform 2 and isoform 3. 3 PublicationsVSP_012201Add
    BLAST
    Alternative sequencei581 – 62141Missing in isoform 4. 1 PublicationVSP_012202Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF201391 mRNA. Translation: AAF12825.1.
    AK029716 mRNA. Translation: BAC26579.1.
    AK014871 mRNA. Translation: BAB29594.1. Frameshift.
    AK078813 mRNA. Translation: BAC37407.1.
    AK086653 mRNA. Translation: BAC39710.1.
    BC005596 mRNA. Translation: AAH05596.1.
    BC034711 mRNA. Translation: AAH34711.1.
    AF039567 mRNA. Translation: AAB96678.1. Different initiation.
    CCDSiCCDS37866.1. [Q8C5D8-1]
    RefSeqiNP_001157639.1. NM_001164167.1. [Q8C5D8-4]
    NP_001157640.1. NM_001164168.1.
    NP_001157641.1. NM_001164169.1. [Q8C5D8-2]
    NP_001157642.1. NM_001164170.1.
    NP_032628.3. NM_008602.4. [Q8C5D8-1]
    UniGeneiMm.6370.

    Genome annotation databases

    EnsembliENSMUST00000114777; ENSMUSP00000110425; ENSMUSG00000025423. [Q8C5D8-1]
    GeneIDi17344.
    KEGGimmu:17344.
    UCSCiuc008frb.1. mouse. [Q8C5D8-2]
    uc008frc.2. mouse. [Q8C5D8-1]
    uc012bfb.1. mouse. [Q8C5D8-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF201391 mRNA. Translation: AAF12825.1 .
    AK029716 mRNA. Translation: BAC26579.1 .
    AK014871 mRNA. Translation: BAB29594.1 . Frameshift.
    AK078813 mRNA. Translation: BAC37407.1 .
    AK086653 mRNA. Translation: BAC39710.1 .
    BC005596 mRNA. Translation: AAH05596.1 .
    BC034711 mRNA. Translation: AAH34711.1 .
    AF039567 mRNA. Translation: AAB96678.1 . Different initiation.
    CCDSi CCDS37866.1. [Q8C5D8-1 ]
    RefSeqi NP_001157639.1. NM_001164167.1. [Q8C5D8-4 ]
    NP_001157640.1. NM_001164168.1.
    NP_001157641.1. NM_001164169.1. [Q8C5D8-2 ]
    NP_001157642.1. NM_001164170.1.
    NP_032628.3. NM_008602.4. [Q8C5D8-1 ]
    UniGenei Mm.6370.

    3D structure databases

    ProteinModelPortali Q8C5D8.
    SMRi Q8C5D8. Positions 1-65, 147-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201429. 10 interactions.
    IntActi Q8C5D8. 5 interactions.
    MINTi MINT-1782012.

    PTM databases

    PhosphoSitei Q8C5D8.

    Proteomic databases

    PaxDbi Q8C5D8.
    PRIDEi Q8C5D8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000114777 ; ENSMUSP00000110425 ; ENSMUSG00000025423 . [Q8C5D8-1 ]
    GeneIDi 17344.
    KEGGi mmu:17344.
    UCSCi uc008frb.1. mouse. [Q8C5D8-2 ]
    uc008frc.2. mouse. [Q8C5D8-1 ]
    uc012bfb.1. mouse. [Q8C5D8-4 ]

    Organism-specific databases

    CTDi 9063.
    MGIi MGI:1096566. Pias2.

    Phylogenomic databases

    eggNOGi NOG125513.
    GeneTreei ENSGT00550000074410.
    HOVERGENi HBG053598.
    InParanoidi Q8C5D8.
    KOi K16063.
    OMAi PHESSTH.
    OrthoDBi EOG7HF1JB.
    PhylomeDBi Q8C5D8.
    TreeFami TF323787.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .

    Miscellaneous databases

    NextBioi 291922.
    PROi Q8C5D8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C5D8.
    Bgeei Q8C5D8.
    CleanExi MM_PIAS2.
    Genevestigatori Q8C5D8.

    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. "p67 isoform of mouse disabled 2 protein acts as a transcriptional activator during the differentiation of F9 cells."
      Cho S.-Y., Jeon J.W., Lee S.H., Park S.-S.
      Biochem. J. 352:645-650(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH DAB2.
      Strain: 129.
      Tissue: Teratocarcinoma.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
      Strain: C57BL/6J.
      Tissue: Embryonic lung and Testis.
    3. "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] (ISOFORMS 3 AND 5).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    4. "Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA."
      Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R.
      Mech. Dev. 65:3-17(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-621 (ISOFORM 1), INTERACTION WITH MSX2.
      Tissue: Embryo.
    5. Erratum
      Wu L., Wu H., Ma L., Sangiorgi F., Wu N., Bell J.R., Lyons G.E., Maxson R.
      Mech. Dev. 69:219-219(1997)
    6. "The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta/Siz2 is a transcriptional cofactor for TFII-I."
      Tussie-Luna M.I., Michel B., Hakre S., Roy A.L.
      J. Biol. Chem. 277:43185-43193(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH GTF2I AND GTF2IRD1.
    7. "PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases."
      Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.
      Mol. Cell. Biol. 22:5222-5234(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATION.
    8. Cited for: INTERACTION WITH IKFZ1.

    Entry informationi

    Entry nameiPIAS2_MOUSE
    AccessioniPrimary (citable) accession number: Q8C5D8
    Secondary accession number(s): O54987
    , Q8C384, Q8CDQ8, Q8K208, Q99JX5, Q9D5W7, Q9QZ63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3