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P42226

- STAT6_HUMAN

UniProt

P42226 - STAT6_HUMAN

Protein

Signal transducer and activator of transcription 6

Gene

STAT6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Carries out a dual function: signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. protein phosphatase binding Source: UniProtKB
    5. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. signal transducer activity Source: InterPro

    GO - Biological processi

    1. cellular response to hydrogen peroxide Source: Ensembl
    2. cellular response to reactive nitrogen species Source: Ensembl
    3. innate immune response Source: Reactome
    4. interleukin-4-mediated signaling pathway Source: UniProtKB
    5. mammary gland epithelial cell proliferation Source: Ensembl
    6. mammary gland morphogenesis Source: Ensembl
    7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    8. negative regulation of type 2 immune response Source: Ensembl
    9. positive regulation of isotype switching to IgE isotypes Source: Ensembl
    10. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    11. positive regulation of type I interferon production Source: Reactome
    12. regulation of cell proliferation Source: Ensembl
    13. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    14. signal transduction Source: ProtInc
    15. T-helper 1 cell lineage commitment Source: Ensembl
    16. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_163734. STAT6-mediated induction of chemokines.
    REACT_17025. Downstream signal transduction.
    SignaLinkiP42226.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal transducer and activator of transcription 6
    Alternative name(s):
    IL-4 Stat
    Gene namesi
    Name:STAT6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11368. STAT6.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Translocated into the nucleus in response to phosphorylation.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. membrane raft Source: Ensembl
    4. nuclear chromatin Source: Ensembl
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi802 – 8021L → A: Abolishes the interaction with NCOA1; when associated with A-805. 1 Publication
    Mutagenesisi805 – 8051L → A: Abolishes the interaction with NCOA1; when associated with A-802. 1 Publication

    Organism-specific databases

    Orphaneti2126. Solitary fibrous tumor.
    PharmGKBiPA339.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 847846Signal transducer and activator of transcription 6PRO_0000182433Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei641 – 6411Phosphotyrosine; by JAKBy similarity

    Post-translational modificationi

    Tyrosine phosphorylated following stimulation by IL4/interleukin-4 and IL3/interleukin-3 By similarity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates the IL4/interleukin-4 mediated signaling.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP42226.
    PaxDbiP42226.
    PRIDEiP42226.

    PTM databases

    PhosphoSiteiP42226.

    Expressioni

    Gene expression databases

    ArrayExpressiP42226.
    BgeeiP42226.
    CleanExiHS_STAT6.
    GenevestigatoriP42226.

    Organism-specific databases

    HPAiHPA001861.

    Interactioni

    Subunit structurei

    Forms a homodimer or a heterodimer with a related family member By similarity. Interacts with NCOA1 via its C-terminal LXXLL motif.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1186478,EBI-1186478
    EP300Q094722EBI-1186478,EBI-447295
    IL4RP243944EBI-1186478,EBI-367009
    TBK1Q9UHD27EBI-1186478,EBI-356402
    TMEM173Q86WV612EBI-1186478,EBI-2800345

    Protein-protein interaction databases

    BioGridi112655. 59 interactions.
    IntActiP42226. 31 interactions.
    MINTiMINT-8020389.
    STRINGi9606.ENSP00000300134.

    Structurei

    Secondary structure

    1
    847
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi799 – 8079

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OJ5X-ray2.20B795-808[»]
    ProteinModelPortaliP42226.
    SMRiP42226. Positions 13-631.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42226.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini517 – 632116SH2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi802 – 8065LXXLL motif

    Sequence similaritiesi

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

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG278979.
    HOGENOMiHOG000230988.
    HOVERGENiHBG107486.
    InParanoidiP42226.
    KOiK11225.
    OMAiKFQAGVR.
    OrthoDBiEOG73JKTT.
    PhylomeDBiP42226.
    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.
    IPR028187. STAT6_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.
    PF14596. STAT6_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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42226-1) [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

    MSLWGLVSKM PPEKVQRLYV DFPQHLRHLL GDWLESQPWE FLVGSDAFCC    50
    NLASALLSDT VQHLQASVGE QGEGSTILQH ISTLESIYQR DPLKLVATFR 100
    QILQGEKKAV MEQFRHLPMP FHWKQEELKF KTGLRRLQHR VGEIHLLREA 150
    LQKGAEAGQV SLHSLIETPA NGTGPSEALA MLLQETTGEL EAAKALVLKR 200
    IQIWKRQQQL AGNGAPFEES LAPLQERCES LVDIYSQLQQ EVGAAGGELE 250
    PKTRASLTGR LDEVLRTLVT SCFLVEKQPP QVLKTQTKFQ AGVRFLLGLR 300
    FLGAPAKPPL VRADMVTEKQ ARELSVPQGP GAGAESTGEI INNTVPLENS 350
    IPGNCCSALF KNLLLKKIKR CERKGTESVT EEKCAVLFSA SFTLGPGKLP 400
    IQLQALSLPL VVIVHGNQDN NAKATILWDN AFSEMDRVPF VVAERVPWEK 450
    MCETLNLKFM AEVGTNRGLL PEHFLFLAQK IFNDNSLSME AFQHRSVSWS 500
    QFNKEILLGR GFTFWQWFDG VLDLTKRCLR SYWSDRLIIG FISKQYVTSL 550
    LLNEPDGTFL LRFSDSEIGG ITIAHVIRGQ DGSPQIENIQ PFSAKDLSIR 600
    SLGDRIRDLA QLKNLYPKKP KDEAFRSHYK PEQMGKDGRG YVPATIKMTV 650
    ERDQPLPTPE LQMPTMVPSY DLGMAPDSSM SMQLGPDMVP QVYPPHSHSI 700
    PPYQGLSPEE SVNVLSAFQE PHLQMPPSLG QMSLPFDQPH PQGLLPCQPQ 750
    EHAVSSPDPL LCSDVTMVED SCLSQPVTAF PQGTWIGEDI FPPLLPPTEQ 800
    DLTKLLLEGQ GESGGGSLGA QPLLQPSHYG QSGISMSHMD LRANPSW 847
    Length:847
    Mass (Da):94,135
    Last modified:November 1, 1995 - v1
    Checksum:iF35075F1C1F2A677
    GO
    Isoform 2 (identifier: P42226-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-174: Missing.
         175-177: PSE → MEQ

    Show »
    Length:673
    Mass (Da):74,456
    Checksum:i7A050ADF43A669BB
    GO
    Isoform 3 (identifier: P42226-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-110: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:737
    Mass (Da):81,748
    Checksum:i8A076ABC6053A831
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491E → Q in AAC67525. (PubMed:9782085)Curated
    Sequence conflicti246 – 2461G → D in BAH14513. (PubMed:14702039)Curated
    Sequence conflicti733 – 7331S → N in AAC67525. (PubMed:9782085)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti181 – 1811M → R.1 Publication
    Corresponds to variant rs3024952 [ dbSNP | Ensembl ].
    VAR_013094
    Natural varianti419 – 4191D → N.
    Corresponds to variant rs11172102 [ dbSNP | Ensembl ].
    VAR_059812

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 174174Missing in isoform 2. 1 PublicationVSP_031871Add
    BLAST
    Alternative sequencei1 – 110110Missing in isoform 3. 1 PublicationVSP_045282Add
    BLAST
    Alternative sequencei175 – 1773PSE → MEQ in isoform 2. 1 PublicationVSP_031872

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U16031 mRNA. Translation: AAA57193.1.
    AF067575, AF067572, AF067573 Genomic DNA. Translation: AAC67525.1.
    AB103089 mRNA. Translation: BAD89432.1.
    AK290431 mRNA. Translation: BAF83120.1.
    AK316142 mRNA. Translation: BAH14513.1.
    AF417842 Genomic DNA. Translation: AAL06595.1.
    AC023237 Genomic DNA. No translation available.
    BC075852 mRNA. Translation: AAH75852.1.
    CCDSiCCDS53804.1. [P42226-3]
    CCDS8931.1. [P42226-1]
    PIRiA54740.
    RefSeqiNP_001171549.1. NM_001178078.1. [P42226-1]
    NP_001171550.1. NM_001178079.1. [P42226-1]
    NP_001171551.1. NM_001178080.1. [P42226-3]
    NP_003144.3. NM_003153.4. [P42226-1]
    XP_006719636.1. XM_006719573.1. [P42226-1]
    XP_006719637.1. XM_006719574.1. [P42226-1]
    XP_006719638.1. XM_006719575.1. [P42226-1]
    UniGeneiHs.524518.

    Genome annotation databases

    EnsembliENST00000300134; ENSP00000300134; ENSG00000166888. [P42226-1]
    ENST00000454075; ENSP00000401486; ENSG00000166888. [P42226-1]
    ENST00000537215; ENSP00000444530; ENSG00000166888. [P42226-3]
    ENST00000538913; ENSP00000445409; ENSG00000166888. [P42226-3]
    ENST00000543873; ENSP00000438451; ENSG00000166888. [P42226-1]
    ENST00000556155; ENSP00000451742; ENSG00000166888. [P42226-1]
    GeneIDi6778.
    KEGGihsa:6778.
    UCSCiuc001sna.3. human. [P42226-1]

    Polymorphism databases

    DMDMi1174459.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U16031 mRNA. Translation: AAA57193.1 .
    AF067575 , AF067572 , AF067573 Genomic DNA. Translation: AAC67525.1 .
    AB103089 mRNA. Translation: BAD89432.1 .
    AK290431 mRNA. Translation: BAF83120.1 .
    AK316142 mRNA. Translation: BAH14513.1 .
    AF417842 Genomic DNA. Translation: AAL06595.1 .
    AC023237 Genomic DNA. No translation available.
    BC075852 mRNA. Translation: AAH75852.1 .
    CCDSi CCDS53804.1. [P42226-3 ]
    CCDS8931.1. [P42226-1 ]
    PIRi A54740.
    RefSeqi NP_001171549.1. NM_001178078.1. [P42226-1 ]
    NP_001171550.1. NM_001178079.1. [P42226-1 ]
    NP_001171551.1. NM_001178080.1. [P42226-3 ]
    NP_003144.3. NM_003153.4. [P42226-1 ]
    XP_006719636.1. XM_006719573.1. [P42226-1 ]
    XP_006719637.1. XM_006719574.1. [P42226-1 ]
    XP_006719638.1. XM_006719575.1. [P42226-1 ]
    UniGenei Hs.524518.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OJ5 X-ray 2.20 B 795-808 [» ]
    ProteinModelPortali P42226.
    SMRi P42226. Positions 13-631.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112655. 59 interactions.
    IntActi P42226. 31 interactions.
    MINTi MINT-8020389.
    STRINGi 9606.ENSP00000300134.

    Chemistry

    BindingDBi P42226.
    ChEMBLi CHEMBL5401.

    PTM databases

    PhosphoSitei P42226.

    Polymorphism databases

    DMDMi 1174459.

    Proteomic databases

    MaxQBi P42226.
    PaxDbi P42226.
    PRIDEi P42226.

    Protocols and materials databases

    DNASUi 6778.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300134 ; ENSP00000300134 ; ENSG00000166888 . [P42226-1 ]
    ENST00000454075 ; ENSP00000401486 ; ENSG00000166888 . [P42226-1 ]
    ENST00000537215 ; ENSP00000444530 ; ENSG00000166888 . [P42226-3 ]
    ENST00000538913 ; ENSP00000445409 ; ENSG00000166888 . [P42226-3 ]
    ENST00000543873 ; ENSP00000438451 ; ENSG00000166888 . [P42226-1 ]
    ENST00000556155 ; ENSP00000451742 ; ENSG00000166888 . [P42226-1 ]
    GeneIDi 6778.
    KEGGi hsa:6778.
    UCSCi uc001sna.3. human. [P42226-1 ]

    Organism-specific databases

    CTDi 6778.
    GeneCardsi GC12M057489.
    HGNCi HGNC:11368. STAT6.
    HPAi HPA001861.
    MIMi 601512. gene.
    neXtProti NX_P42226.
    Orphaneti 2126. Solitary fibrous tumor.
    PharmGKBi PA339.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278979.
    HOGENOMi HOG000230988.
    HOVERGENi HBG107486.
    InParanoidi P42226.
    KOi K11225.
    OMAi KFQAGVR.
    OrthoDBi EOG73JKTT.
    PhylomeDBi P42226.
    TreeFami TF318648.

    Enzyme and pathway databases

    Reactomei REACT_163734. STAT6-mediated induction of chemokines.
    REACT_17025. Downstream signal transduction.
    SignaLinki P42226.

    Miscellaneous databases

    ChiTaRSi STAT6. human.
    EvolutionaryTracei P42226.
    GeneWikii STAT6.
    GenomeRNAii 6778.
    NextBioi 26458.
    PROi P42226.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42226.
    Bgeei P42226.
    CleanExi HS_STAT6.
    Genevestigatori P42226.

    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.
    IPR028187. STAT6_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.
    PF14596. STAT6_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. "An interleukin-4-induced transcription factor: IL-4 Stat."
      Hou J., Schindler U., Henzel W.J., Ho T., Brasseur M., McKnight S.L.
      Science 265:1701-1706(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Localization of the human stat6 gene to chromosome 12q13.3-q14.1, a region implicated in multiple solid tumors."
      Patel B.K., Keck C.L., O'Leary R.S., Popescu N.C., LaRochelle W.J.
      Genomics 52:192-200(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "STAT6 mRNA, nirs splice variant 2."
      Tabata Y., Sameshima E., Hayashi A., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    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] (ISOFORMS 1 AND 3).
      Tissue: Tongue.
    5. SeattleSNPs variation discovery resource
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-181.
    6. "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].
    7. "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: Uterus.
    8. "An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1."
      Litterst C.M., Pfitzner E.
      J. Biol. Chem. 277:36052-36060(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA1, MUTAGENESIS OF LEU-802 AND LEU-805.
    9. "T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6."
      Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T., Lossos I.S.
      Mol. Cell. Biol. 27:2166-2179(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN IL4 SIGNALING, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain."
      Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C., Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E., Becker S.
      J. Mol. Biol. 336:319-329(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 795-808 IN COMPLEX WITH 257-385 OF NCOA1.

    Entry informationi

    Entry nameiSTAT6_HUMAN
    AccessioniPrimary (citable) accession number: P42226
    Secondary accession number(s): A8K316
    , B7ZA27, F5GXI9, Q5FBW5, Q71UP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 149 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, 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