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P52630

- STAT2_HUMAN

UniProt

P52630 - STAT2_HUMAN

Protein

Signal transducer and activator of transcription 2

Gene

STAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. DNA binding Source: UniProtKB-KW
    3. identical protein binding Source: IntAct
    4. protein binding Source: IntAct
    5. sequence-specific DNA binding transcription factor activity Source: InterPro
    6. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. defense response to virus Source: UniProtKB-KW
    3. JAK-STAT cascade Source: ProtInc
    4. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    5. regulation of type I interferon-mediated signaling pathway Source: Reactome
    6. transcription, DNA-templated Source: UniProtKB-KW
    7. type I interferon signaling pathway Source: Reactome
    8. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    SignaLinkiP52630.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal transducer and activator of transcription 2
    Alternative name(s):
    p113
    Gene namesi
    Name:STAT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11363. STAT2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Translocated into the nucleus upon activation by IFN-alpha/beta.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi374 – 3741R → A: Prevents the nuclear import; when associated with A-375. 1 Publication
    Mutagenesisi375 – 3751K → A: Prevents the nuclear import; when associated with A-374. 1 Publication
    Mutagenesisi409 – 4091R → A: Prevents the nuclear import; when associated with A-415. 1 Publication
    Mutagenesisi415 – 4151K → A: Prevents the nuclear import; when associated with A-409. 1 Publication
    Mutagenesisi690 – 6901Y → F: Reduces phosphorylation of STAT1 in response to IFN-ALPHA. 1 Publication

    Organism-specific databases

    PharmGKBiPA36184.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 851851Signal transducer and activator of transcription 2PRO_0000182413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei283 – 2831Phosphoserine2 Publications
    Modified residuei287 – 2871Phosphoserine2 Publications
    Modified residuei294 – 2941Phosphothreonine2 Publications
    Modified residuei690 – 6901Phosphotyrosine; by JAK3 Publications

    Post-translational modificationi

    Tyrosine phosphorylated in response to IFN-alpha. Phosphorylation at Ser-287 negatively regulates the transcriptional response.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP52630.
    PaxDbiP52630.
    PeptideAtlasiP52630.
    PRIDEiP52630.

    PTM databases

    PhosphoSiteiP52630.

    Expressioni

    Gene expression databases

    ArrayExpressiP52630.
    BgeeiP52630.
    CleanExiHS_STAT2.
    GenevestigatoriP52630.

    Organism-specific databases

    HPAiCAB003858.
    HPA018888.

    Interactioni

    Subunit structurei

    Heterodimer with STAT1 upon IFN-alpha/beta induced phosphorylation. The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9; interacts with IRF9 in the cytoplasm. Interacts with CRSP2 and CRSP6. Can form a homodimer upon IFN-alpha induced phosphorylation. Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-466'. Interacts with IFNAR2. Interacts with ARL2BP. Interacts with dengue virus NS5; this interaction inhibits the phosphorylation of STAT2, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation. Interacts with human cytomegalovirus/HHV-5 protein UL123; this interaction promotes viral growth. Interacts with Simian virus 5 protein V and rabies virus phosphoprotein.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1546963,EBI-1546963
    IFNAR1P171814EBI-1546963,EBI-1547250
    IFNAR2P485512EBI-1546963,EBI-958408
    IRF9Q009786EBI-1546963,EBI-626526
    P/VP0C7744EBI-1546963,EBI-3650423From a different organism.
    P/VP112072EBI-1546963,EBI-6148694From a different organism.
    STAT1P4222414EBI-1546963,EBI-1057697

    Protein-protein interaction databases

    BioGridi112650. 21 interactions.
    DIPiDIP-38511N.
    IntActiP52630. 21 interactions.
    MINTiMINT-1526706.
    STRINGi9606.ENSP00000315768.

    Structurei

    Secondary structure

    1
    851
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi793 – 7964
    Helixi802 – 8065
    Turni812 – 8143
    Helixi824 – 8274
    Helixi831 – 8344

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KA4NMR-B786-838[»]
    ProteinModelPortaliP52630.
    SMRiP52630. Positions 2-699, 783-838.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52630.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini572 – 66796SH2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the transcription factor STAT family.Curated
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG303257.
    HOGENOMiHOG000220792.
    HOVERGENiHBG055669.
    InParanoidiP52630.
    KOiK11221.
    OMAiAFGRYYQ.
    OrthoDBiEOG71K62B.
    PhylomeDBiP52630.
    TreeFamiTF318648.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR022756. STAT2_C.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view]
    PANTHERiPTHR11801. PTHR11801. 1 hit.
    PfamiPF00017. SH2. 1 hit.
    PF12188. STAT2_C. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view]
    SMARTiSM00252. SH2. 1 hit.
    SM00964. STAT_int. 1 hit.
    [Graphical view]
    SUPFAMiSSF47655. SSF47655. 1 hit.
    SSF48092. SSF48092. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52630-3) [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

    MAQWEMLQNL DSPFQDQLHQ LYSHSLLPVD IRQYLAVWIE DQNWQEAALG    50
    SDDSKATMLF FHFLDQLNYE CGRCSQDPES LLLQHNLRKF CRDIQPFSQD 100
    PTQLAEMIFN LLLEEKRILI QAQRAQLEQG EPVLETPVES QQHEIESRIL 150
    DLRAMMEKLV KSISQLKDQQ DVFCFRYKIQ AKGKTPSLDP HQTKEQKILQ 200
    ETLNELDKRR KEVLDASKAL LGRLTTLIEL LLPKLEEWKA QQQKACIRAP 250
    IDHGLEQLET WFTAGAKLLF HLRQLLKELK GLSCLVSYQD DPLTKGVDLR 300
    NAQVTELLQR LLHRAFVVET QPCMPQTPHR PLILKTGSKF TVRTRLLVRL 350
    QEGNESLTVE VSIDRNPPQL QGFRKFNILT SNQKTLTPEK GQSQGLIWDF 400
    GYLTLVEQRS GGSGKGSNKG PLGVTEELHI ISFTVKYTYQ GLKQELKTDT 450
    LPVVIISNMN QLSIAWASVL WFNLLSPNLQ NQQFFSNPPK APWSLLGPAL 500
    SWQFSSYVGR GLNSDQLSML RNKLFGQNCR TEDPLLSWAD FTKRESPPGK 550
    LPFWTWLDKI LELVHDHLKD LWNDGRIMGF VSRSQERRLL KKTMSGTFLL 600
    RFSESSEGGI TCSWVEHQDD DKVLIYSVQP YTKEVLQSLP LTEIIRHYQL 650
    LTEENIPENP LRFLYPRIPR DEAFGCYYQE KVNLQERRKY LKHRLIVVSN 700
    RQVDELQQPL ELKPEPELES LELELGLVPE PELSLDLEPL LKAGLDLGPE 750
    LESVLESTLE PVIEPTLCMV SQTVPEPDQG PVSQPVPEPD LPCDLRHLNT 800
    EPMEIFRNCV KIEEIMPNGD PLLAGQNTVD EVYVSRPSHF YTDGPLMPSD 850
    F 851
    Length:851
    Mass (Da):97,916
    Last modified:October 1, 1996 - v1
    Checksum:iE4C74674CB7A3215
    GO
    Isoform 2 (identifier: P52630-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         96-99: Missing.

    Note: No experimental confirmation available. May be due to competing acceptor splice site.

    Show »
    Length:847
    Mass (Da):97,457
    Checksum:i3587443D40AF5E5B
    GO

    Sequence cautioni

    The sequence AAB36226.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAB36227.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti240 – 2401A → T in BAG59489. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti66 – 661Q → H.
    Corresponds to variant rs2066816 [ dbSNP | Ensembl ].
    VAR_014896
    Natural varianti220 – 2201L → P.
    Corresponds to variant rs2066817 [ dbSNP | Ensembl ].
    VAR_014897
    Natural varianti246 – 2461C → S.
    Corresponds to variant rs2228259 [ dbSNP | Ensembl ].
    VAR_052072
    Natural varianti448 – 4481T → M.1 Publication
    Corresponds to variant rs2066815 [ dbSNP | Ensembl ].
    VAR_014898
    Natural varianti464 – 4641I → V.1 Publication
    Corresponds to variant rs2066811 [ dbSNP | Ensembl ].
    VAR_014899
    Natural varianti501 – 5011S → I.
    Corresponds to variant rs2066809 [ dbSNP | Ensembl ].
    VAR_014900
    Natural varianti594 – 5941M → I.1 Publication
    Corresponds to variant rs2066807 [ dbSNP | Ensembl ].
    VAR_014901
    Natural varianti826 – 8261Q → H.1 Publication
    Corresponds to variant rs2229363 [ dbSNP | Ensembl ].
    VAR_019213

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei96 – 994Missing in isoform 2. 1 PublicationVSP_046705

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97934 mRNA. No translation available.
    U18671 Genomic DNA. Translation: AAA98760.1.
    S81491 Genomic DNA. Translation: AAB36226.1. Sequence problems.
    S81491 Genomic DNA. Translation: AAB36227.1. Sequence problems.
    AY525126 Genomic DNA. Translation: AAS00091.1.
    AK296939 mRNA. Translation: BAG59489.1.
    AC025574 Genomic DNA. No translation available.
    BC051284 mRNA. Translation: AAH51284.1.
    CCDSiCCDS55836.1. [P52630-4]
    CCDS8917.1. [P52630-3]
    PIRiA46160.
    RefSeqiNP_005410.1. NM_005419.3. [P52630-3]
    NP_938146.1. NM_198332.1. [P52630-4]
    UniGeneiHs.530595.

    Genome annotation databases

    EnsembliENST00000314128; ENSP00000315768; ENSG00000170581. [P52630-3]
    ENST00000557235; ENSP00000450751; ENSG00000170581. [P52630-4]
    GeneIDi6773.
    KEGGihsa:6773.
    UCSCiuc001slc.3. human. [P52630-3]

    Polymorphism databases

    DMDMi1711552.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97934 mRNA. No translation available.
    U18671 Genomic DNA. Translation: AAA98760.1 .
    S81491 Genomic DNA. Translation: AAB36226.1 . Sequence problems.
    S81491 Genomic DNA. Translation: AAB36227.1 . Sequence problems.
    AY525126 Genomic DNA. Translation: AAS00091.1 .
    AK296939 mRNA. Translation: BAG59489.1 .
    AC025574 Genomic DNA. No translation available.
    BC051284 mRNA. Translation: AAH51284.1 .
    CCDSi CCDS55836.1. [P52630-4 ]
    CCDS8917.1. [P52630-3 ]
    PIRi A46160.
    RefSeqi NP_005410.1. NM_005419.3. [P52630-3 ]
    NP_938146.1. NM_198332.1. [P52630-4 ]
    UniGenei Hs.530595.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KA4 NMR - B 786-838 [» ]
    ProteinModelPortali P52630.
    SMRi P52630. Positions 2-699, 783-838.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112650. 21 interactions.
    DIPi DIP-38511N.
    IntActi P52630. 21 interactions.
    MINTi MINT-1526706.
    STRINGi 9606.ENSP00000315768.

    PTM databases

    PhosphoSitei P52630.

    Polymorphism databases

    DMDMi 1711552.

    Proteomic databases

    MaxQBi P52630.
    PaxDbi P52630.
    PeptideAtlasi P52630.
    PRIDEi P52630.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314128 ; ENSP00000315768 ; ENSG00000170581 . [P52630-3 ]
    ENST00000557235 ; ENSP00000450751 ; ENSG00000170581 . [P52630-4 ]
    GeneIDi 6773.
    KEGGi hsa:6773.
    UCSCi uc001slc.3. human. [P52630-3 ]

    Organism-specific databases

    CTDi 6773.
    GeneCardsi GC12M056735.
    HGNCi HGNC:11363. STAT2.
    HPAi CAB003858.
    HPA018888.
    MIMi 600556. gene.
    neXtProti NX_P52630.
    PharmGKBi PA36184.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303257.
    HOGENOMi HOG000220792.
    HOVERGENi HBG055669.
    InParanoidi P52630.
    KOi K11221.
    OMAi AFGRYYQ.
    OrthoDBi EOG71K62B.
    PhylomeDBi P52630.
    TreeFami TF318648.

    Enzyme and pathway databases

    Reactomei REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    SignaLinki P52630.

    Miscellaneous databases

    ChiTaRSi STAT2. human.
    EvolutionaryTracei P52630.
    GeneWikii STAT2.
    GenomeRNAii 6773.
    NextBioi 26434.
    PROi P52630.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52630.
    Bgeei P52630.
    CleanExi HS_STAT2.
    Genevestigatori P52630.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR022756. STAT2_C.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view ]
    PANTHERi PTHR11801. PTHR11801. 1 hit.
    Pfami PF00017. SH2. 1 hit.
    PF12188. STAT2_C. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view ]
    SMARTi SM00252. SH2. 1 hit.
    SM00964. STAT_int. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47655. SSF47655. 1 hit.
    SSF48092. SSF48092. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The proteins of ISGF-3, the interferon alpha-induced transcriptional activator, define a gene family involved in signal transduction."
      Fu X.-Y., Schindler C., Improta T., Aebersold R., Darnell J.E. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 89:7840-7843(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "The genomic structure of the STAT genes: multiple exons in coincident sites in Stat1 and Stat2."
      Yan R., Qureshi S., Zhong Z., Wen Z., Darnell J.E. Jr.
      Nucleic Acids Res. 23:459-463(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. NIEHS SNPs program
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-448; VAL-464; ILE-594 AND HIS-826.
    4. "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] (ISOFORM 2).
      Tissue: Tongue.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Lung.
    7. "A transcription factor with SH2 and SH3 domains is directly activated by an interferon alpha-induced cytoplasmic protein tyrosine kinase(s)."
      Fu X.Y.
      Cell 70:323-335(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO IFN-ALPHA.
    8. "Role of STAT2 in the alpha interferon signaling pathway."
      Leung S., Qureshi S.A., Kerr I.M., Darnell J.E. Jr., Stark G.R.
      Mol. Cell. Biol. 15:1312-1317(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-690, MUTAGENESIS OF TYR-690.
    9. "Identification of alternative splicing form of Stat2."
      Sugiyama T., Nishio Y., Kishimoto T., Akira S.
      FEBS Lett. 381:191-194(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: POTENTIAL ALTERNATIVE SPLICING.
    10. "Stat2 is a transcriptional activator that requires sequence-specific contacts provided by stat1 and p48 for stable interaction with DNA."
      Bluyssen H.A., Levy D.E.
      J. Biol. Chem. 272:4600-4605(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    11. "Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling."
      Li X., Leung S., Kerr I.M., Stark G.R.
      Mol. Cell. Biol. 17:2048-2056(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFNAR1 AND IFNAR2, PHOSPHORYLATION AT TYR-690.
    12. "Viral inhibition of interferon signal transduction."
      Cebulla C.M., Miller D.M., Sedmak D.D.
      Intervirology 42:325-330(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. "Arginine/lysine-rich structural element is involved in interferon-induced nuclear import of STATs."
      Melen K., Kinnunen L., Julkunen I.
      J. Biol. Chem. 276:16447-16455(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-374; LYS-375; ARG-409 AND LYS-415.
    14. "Role of metazoan mediator proteins in interferon-responsive transcription."
      Lau J.F., Nusinzon I., Burakov D., Freedman L.P., Horvath C.M.
      Mol. Cell. Biol. 23:620-628(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRSP2 AND CRSP6.
    15. "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1."
      Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E.
      J. Virol. 79:13434-13441(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V.
    16. "Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO."
      Huh Y.H., Kim Y.E., Kim E.T., Park J.J., Song M.J., Zhu H., Hayward G.S., Ahn J.H.
      J. Virol. 82:10444-10454(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL123.
    17. "NS5 of dengue virus mediates STAT2 binding and degradation."
      Ashour J., Laurent-Rolle M., Shi P.Y., Garcia-Sastre A.
      J. Virol. 83:5408-5418(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DENGUE VIRUS NS5.
    18. "Dengue virus NS5 inhibits interferon-alpha signaling by blocking signal transducer and activator of transcription 2 phosphorylation."
      Mazzon M., Jones M., Davidson A., Chain B., Jacobs M.
      J. Infect. Dis. 200:1261-1270(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DENGUE VIRUS NS5.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Identification of STAT2 serine 287 as a novel regulatory phosphorylation site in type I interferon-induced cellular responses."
      Steen H.C., Nogusa S., Thapa R.J., Basagoudanavar S.H., Gill A.L., Merali S., Barrero C.A., Balachandran S., Gamero A.M.
      J. Biol. Chem. 288:747-758(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-283; SER-287 AND THR-294, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSTAT2_HUMAN
    AccessioniPrimary (citable) accession number: P52630
    Secondary accession number(s): B4DLC7
    , G3V2M6, Q16430, Q16431, Q9UDL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3