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O75925

- PIAS1_HUMAN

UniProt

O75925 - PIAS1_HUMAN

Protein

E3 SUMO-protein ligase PIAS1

Gene

PIAS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (05 Mar 2002)
      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. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation By similarity. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation.By similarity3 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri320 – 39778SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. cytokine-mediated signaling pathway Source: Reactome
    3. interferon-gamma-mediated signaling pathway Source: Reactome
    4. JAK-STAT cascade Source: ProtInc
    5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    7. positive regulation of protein sumoylation Source: UniProtKB
    8. positive regulation of smooth muscle cell differentiation Source: Ensembl
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. protein-DNA complex assembly Source: Ensembl
    11. protein sumoylation Source: UniProtKB
    12. regulation of cell proliferation Source: UniProtKB
    13. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    14. spermatogenesis Source: Ensembl
    15. 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

    ReactomeiREACT_24980. Regulation of IFNG signaling.
    SignaLinkiO75925.
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 SUMO-protein ligase PIAS1 (EC:6.3.2.-)
    Alternative name(s):
    DEAD/H box-binding protein 1
    Gu-binding protein
    Short name:
    GBP
    Protein inhibitor of activated STAT protein 1
    RNA helicase II-binding protein
    Gene namesi
    Name:PIAS1
    Synonyms:DDXBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:2752. PIAS1.

    Subcellular locationi

    Nucleus speckle 3 Publications. NucleusPML body By similarity
    Note: Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi303 – 3031R → K: Partial loss of repression on STAT1 transcriptional activity. 1 Publication
    Mutagenesisi351 – 3511C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA33285.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 651650E3 SUMO-protein ligase PIAS1PRO_0000218974Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei303 – 3031Asymmetric dimethylarginine; by PRMT11 Publication
    Modified residuei485 – 4851PhosphoserineBy similarity
    Modified residuei487 – 4871PhosphothreonineBy similarity
    Modified residuei503 – 5031Phosphoserine3 Publications
    Modified residuei510 – 5101Phosphoserine1 Publication
    Modified residuei522 – 5221Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated.2 Publications
    Dimethylated by PRMT1 at Arg-303 in the late phase of interferon gamma (IFN-gamma) signaling, leading to preferential interaction with STAT1 and thus resulting in release of STAT1 from its target gene.

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO75925.
    PaxDbiO75925.
    PRIDEiO75925.

    PTM databases

    PhosphoSiteiO75925.

    Miscellaneous databases

    PMAP-CutDBO75925.

    Expressioni

    Tissue specificityi

    Expressed in numerous tissues with highest level in testis.2 Publications

    Gene expression databases

    ArrayExpressiO75925.
    BgeeiO75925.
    CleanExiHS_PIAS1.
    GenevestigatoriO75925.

    Organism-specific databases

    HPAiCAB012304.

    Interactioni

    Subunit structurei

    Interacts with NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation By similarity. Interacts with DDX21, CSRP2, AXIN1, JUN, UBE2I, SUMO1, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3 (preferentially when SUMO-modified). Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase. Interacts with STAT1. Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its sumoylation. Interacts with DDX5. Interacts with PML By similarity. Interacts with MTA1.By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P299913EBI-629434,EBI-8826488From a different organism.
    CASP8AP2Q9UKL34EBI-629434,EBI-2339650
    MBD1Q9UIS93EBI-629434,EBI-867196
    PRDM1O756262EBI-629434,EBI-948789
    TP53P046374EBI-629434,EBI-366083

    Protein-protein interaction databases

    BioGridi114124. 86 interactions.
    DIPiDIP-5970N.
    IntActiO75925. 35 interactions.
    MINTiMINT-132657.
    STRINGi9606.ENSP00000249636.

    Structurei

    Secondary structure

    1
    651
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 116
    Helixi16 – 249
    Helixi34 – 4613
    Helixi51 – 6313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V66NMR-A1-65[»]
    ProteinModelPortaliO75925.
    SMRiO75925. Positions 1-65, 135-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75925.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini124 – 288165PINITPROSITE-ProRule annotationAdd
    BLAST
    Repeati520 – 52341
    Repeati557 – 56042
    Repeati598 – 60143; approximate
    Repeati612 – 61544; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni462 – 47312SUMO1-bindingBy similarityAdd
    BLAST
    Regioni520 – 615964 X 4 AA repeats of N-T-S-LAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 235LXXLL motif
    Motifi56 – 649Nuclear localization signalSequence Analysis
    Motifi368 – 38013Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi577 – 63458Ser-richAdd
    BLAST

    Domaini

    The LXXLL motif is a transcriptional coregulator signature.
    The SP-RING-type domain is required for promoting EKLF sumoylation.By similarity

    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 fingeri320 – 39778SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG125513.
    HOVERGENiHBG053598.
    InParanoidiO75925.
    KOiK04706.
    OrthoDBiEOG7HF1JB.
    PhylomeDBiO75925.
    TreeFamiTF323787.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    InterProiIPR027227. PIAS1.
    IPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view]
    PANTHERiPTHR10782:SF11. PTHR10782:SF11. 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 (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75925-1) [UniParc]FASTAAdd to Basket

    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

    MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS    50
    PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD 100
    GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 150
    IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 200
    RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 250
    NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 300
    GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT 350
    CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT 400
    DCDEIQFKED GTWAPMRSKK EVQEVSASYN GVDGCLSSTL EHQVASHHQS 450
    SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT CPSLSPTSPL NNKGILSLPH 500
    QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS 550
    GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 600
    LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL 650
    D 651
    Length:651
    Mass (Da):71,836
    Last modified:March 5, 2002 - v2
    Checksum:iAA69338221124119
    GO
    Isoform 2 (identifier: O75925-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: MADSAEL → MFTLQDSYV

    Note: No experimental confirmation available.

    Show »
    Length:653
    Mass (Da):72,203
    Checksum:i585370DA0FBDC926
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191E → K in AAC36702. (PubMed:9724754)Curated
    Sequence conflicti266 – 2683IVV → MC in AAC36702. (PubMed:9724754)Curated
    Sequence conflicti613 – 6131S → T in AAB58488. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 77MADSAEL → MFTLQDSYV in isoform 2. 1 PublicationVSP_056219

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077951 mRNA. Translation: AAC36702.1.
    AF167160 mRNA. Translation: AAD49722.1.
    AK094641 mRNA. Translation: BAG52901.1.
    AK314515 mRNA. Translation: BAG37114.1.
    AC107871 Genomic DNA. No translation available.
    AC135628 Genomic DNA. No translation available.
    BC118587 mRNA. Translation: AAI18588.1.
    BC121797 mRNA. Translation: AAI21798.1.
    U78524 mRNA. Translation: AAB58488.1.
    CCDSiCCDS45290.1.
    RefSeqiNP_057250.1. NM_016166.1.
    UniGeneiHs.162458.

    Genome annotation databases

    EnsembliENST00000249636; ENSP00000249636; ENSG00000033800.
    ENST00000545237; ENSP00000438574; ENSG00000033800.
    GeneIDi8554.
    KEGGihsa:8554.
    UCSCiuc002aqz.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077951 mRNA. Translation: AAC36702.1 .
    AF167160 mRNA. Translation: AAD49722.1 .
    AK094641 mRNA. Translation: BAG52901.1 .
    AK314515 mRNA. Translation: BAG37114.1 .
    AC107871 Genomic DNA. No translation available.
    AC135628 Genomic DNA. No translation available.
    BC118587 mRNA. Translation: AAI18588.1 .
    BC121797 mRNA. Translation: AAI21798.1 .
    U78524 mRNA. Translation: AAB58488.1 .
    CCDSi CCDS45290.1.
    RefSeqi NP_057250.1. NM_016166.1.
    UniGenei Hs.162458.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V66 NMR - A 1-65 [» ]
    ProteinModelPortali O75925.
    SMRi O75925. Positions 1-65, 135-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114124. 86 interactions.
    DIPi DIP-5970N.
    IntActi O75925. 35 interactions.
    MINTi MINT-132657.
    STRINGi 9606.ENSP00000249636.

    PTM databases

    PhosphoSitei O75925.

    Proteomic databases

    MaxQBi O75925.
    PaxDbi O75925.
    PRIDEi O75925.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249636 ; ENSP00000249636 ; ENSG00000033800 .
    ENST00000545237 ; ENSP00000438574 ; ENSG00000033800 .
    GeneIDi 8554.
    KEGGi hsa:8554.
    UCSCi uc002aqz.3. human.

    Organism-specific databases

    CTDi 8554.
    GeneCardsi GC15P068346.
    HGNCi HGNC:2752. PIAS1.
    HPAi CAB012304.
    MIMi 603566. gene.
    neXtProti NX_O75925.
    PharmGKBi PA33285.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG125513.
    HOVERGENi HBG053598.
    InParanoidi O75925.
    KOi K04706.
    OrthoDBi EOG7HF1JB.
    PhylomeDBi O75925.
    TreeFami TF323787.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    Reactomei REACT_24980. Regulation of IFNG signaling.
    SignaLinki O75925.

    Miscellaneous databases

    EvolutionaryTracei O75925.
    GeneWikii PIAS1.
    GenomeRNAii 8554.
    NextBioi 32053.
    PMAP-CutDB O75925.
    PROi O75925.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75925.
    Bgeei O75925.
    CleanExi HS_PIAS1.
    Genevestigatori O75925.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    InterProi IPR027227. PIAS1.
    IPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view ]
    PANTHERi PTHR10782:SF11. PTHR10782:SF11. 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] (ISOFORM 1), INTERACTION WITH STAT1.
      Tissue: B-cell.
    2. "Protein inhibitor of activated STAT-1 (signal transducer and activator of transcription-1) is a nuclear receptor coregulator expressed in human testis."
      Tan J., Hall S.H., Hamil K.G., Grossman G., Petrusz P., Liao J., Shuai K., French F.S.
      Mol. Endocrinol. 14:14-26(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Amygdala and Trachea.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-651 (ISOFORM 1), INTERACTION WITH DDX21, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: B-cell.
    7. "LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of activated STAT1."
      Weiskirchen R., Moser M., Weiskirchen S., Erdel M., Dahmen S., Buettner R., Gressner A.M.
      Biochem. J. 359:485-496(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSRP2.
    8. "Involvement of PIAS1 in the sumoylation of tumor suppressor p53."
      Kahyo T., Nishida T., Yasuda H.
      Mol. Cell 8:713-718(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I; SUMO1 AND TP53, MUTAGENESIS OF CYS-351.
    9. "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.
    10. "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.
    11. "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.
    12. "Transcription factor Sp3 is silenced through SUMO modification by PIAS1."
      Sapetschnig A., Rischitor G., Braun H., Doll A., Schergaut M., Melchior F., Suske G.
      EMBO J. 21:5206-5215(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SP3 AND UBE2I.
    13. "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 AND TP53, SUMOYLATION.
    14. "SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression."
      Dobreva G., Dambacher J., Grosschedl R.
      Genes Dev. 17:3048-3061(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SATB2.
    15. "PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation."
      Kadare G., Toutant M., Formstecher E., Corvol J.C., Carnaud M., Boutterin M.C., Girault J.A.
      J. Biol. Chem. 278:47434-47440(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1.
    16. "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.
    17. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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.
    19. "Proinflammatory stimuli induce IKKalpha-mediated phosphorylation of PIAS1 to restrict inflammation and immunity."
      Liu B., Yang Y., Chernishof V., Loo R.R., Jang H., Tahk S., Yang R., Mink S., Shultz D., Bellone C.J., Loo J.A., Shuai K.
      Cell 129:903-914(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHUK.
    20. "SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1."
      Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V.
      Oncogene 26:5866-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX5.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling."
      Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.
      Genes Dev. 23:118-132(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STAT1, METHYLATION AT ARG-303 BY PRMT1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-303.
    23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
      Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
      J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MTA1.
    26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    27. "NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers."
      Okubo S., Hara F., Tsuchida Y., Shimotakahara S., Suzuki S., Hatanaka H., Yokoyama S., Tanaka H., Yasuda H., Shindo H.
      J. Biol. Chem. 279:31455-31461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-65, INTERACTION WITH TP53 AND DNA-BINDING.

    Entry informationi

    Entry nameiPIAS1_HUMAN
    AccessioniPrimary (citable) accession number: O75925
    Secondary accession number(s): B2RB67
    , B3KSY9, Q147X4, Q99751, Q9UN02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: March 5, 2002
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3