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Database: UniProt
Entry: P42226
LinkDB: P42226
Original site: P42226 
ID   STAT6_HUMAN             Reviewed;         847 AA.
AC   P42226; A8K316; B7ZA27; F5GXI9; Q5FBW5; Q71UP4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-JUN-2021, entry version 210.
DE   RecName: Full=Signal transducer and activator of transcription 6;
DE   AltName: Full=IL-4 Stat;
GN   Name=STAT6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8085155; DOI=10.1126/science.8085155;
RA   Hou J., Schindler U., Henzel W.J., Ho T., Brasseur M., McKnight S.L.;
RT   "An interleukin-4-induced transcription factor: IL-4 Stat.";
RL   Science 265:1701-1706(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9782085; DOI=10.1006/geno.1998.5436;
RA   Patel B.K., Keck C.L., O'Leary R.S., Popescu N.C., LaRochelle W.J.;
RT   "Localization of the human stat6 gene to chromosome 12q13.3-q14.1, a region
RT   implicated in multiple solid tumors.";
RL   Genomics 52:192-200(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Tabata Y., Sameshima E., Hayashi A., Iida K., Mitsuyama M., Kanai S.,
RA   Furuya T., Saito T.;
RT   "STAT6 mRNA, nirs splice variant 2.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-181.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   INTERACTION WITH NCOA1, AND MUTAGENESIS OF LEU-802 AND LEU-805.
RX   PubMed=12138096; DOI=10.1074/jbc.m203556200;
RA   Litterst C.M., Pfitzner E.;
RT   "An LXXLL motif in the transactivation domain of STAT6 mediates recruitment
RT   of NCoA-1/SRC-1.";
RL   J. Biol. Chem. 277:36052-36060(2002).
RN   [9]
RP   FUNCTION IN IL4 SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
RX   PubMed=17210636; DOI=10.1128/mcb.01234-06;
RA   Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T.,
RA   Lossos I.S.;
RT   "T-cell protein tyrosine phosphatase, distinctively expressed in activated-
RT   B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of
RT   STAT6.";
RL   Mol. Cell. Biol. 27:2166-2179(2007).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
RP   PHOSPHORYLATION AT TYR-641, AND ADP-RIBOSYLATION.
RX   PubMed=27796300; DOI=10.1038/ncomms12849;
RA   Iwata H., Goettsch C., Sharma A., Ricchiuto P., Goh W.W., Halu A.,
RA   Yamada I., Yoshida H., Hara T., Wei M., Inoue N., Fukuda D., Mojcher A.,
RA   Mattson P.C., Barabasi A.L., Boothby M., Aikawa E., Singh S.A., Aikawa M.;
RT   "PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-
RT   ribosylation.";
RL   Nat. Commun. 7:12849-12849(2016).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 795-808 IN COMPLEX WITH 257-385 OF
RP   NCOA1.
RX   PubMed=14757047; DOI=10.1016/j.jmb.2003.12.057;
RA   Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C.,
RA   Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E., Becker S.;
RT   "Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the
RT   STAT6 transactivation domain.";
RL   J. Mol. Biol. 336:319-329(2004).
CC   -!- FUNCTION: Carries out a dual function: signal transduction and
CC       activation of transcription. Involved in IL4/interleukin-4- and
CC       IL3/interleukin-3-mediated signaling. {ECO:0000269|PubMed:17210636}.
CC   -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC       member (By similarity). Interacts with NCOA1 via its C-terminal LXXLL
CC       motif. {ECO:0000250, ECO:0000269|PubMed:12138096,
CC       ECO:0000269|PubMed:14757047}.
CC   -!- INTERACTION:
CC       P42226; Q09472: EP300; NbExp=2; IntAct=EBI-1186478, EBI-447295;
CC       P42226; P24394: IL4R; NbExp=4; IntAct=EBI-1186478, EBI-367009;
CC       P42226; Q13287: NMI; NbExp=2; IntAct=EBI-1186478, EBI-372942;
CC       P42226; P42226: STAT6; NbExp=2; IntAct=EBI-1186478, EBI-1186478;
CC       P42226; Q86WV6: STING1; NbExp=12; IntAct=EBI-1186478, EBI-2800345;
CC       P42226; Q9UHD2: TBK1; NbExp=7; IntAct=EBI-1186478, EBI-356402;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the
CC       nucleus in response to phosphorylation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P42226-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P42226-2; Sequence=VSP_031871, VSP_031872;
CC       Name=3;
CC         IsoId=P42226-3; Sequence=VSP_045282;
CC   -!- PTM: Tyrosine phosphorylated on Tyr-641 following stimulation by
CC       IL4/interleukin-4 (PubMed:27796300). Tyrosine phosphorylated following
CC       stimulation by IL3/interleukin-3 (By similarity). Dephosphorylation on
CC       tyrosine residues by PTPN2 negatively regulates the IL4/interleukin-4
CC       mediated signaling (PubMed:17210636). {ECO:0000250|UniProtKB:P52633,
CC       ECO:0000269|PubMed:17210636, ECO:0000269|PubMed:27796300}.
CC   -!- PTM: Mono-ADP-ribosylated by PARP14. {ECO:0000269|PubMed:27796300}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/stat6/";
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DR   EMBL; U16031; AAA57193.1; -; mRNA.
DR   EMBL; AF067575; AAC67525.1; -; Genomic_DNA.
DR   EMBL; AF067572; AAC67525.1; JOINED; Genomic_DNA.
DR   EMBL; AF067573; AAC67525.1; JOINED; Genomic_DNA.
DR   EMBL; AB103089; BAD89432.1; -; mRNA.
DR   EMBL; AK290431; BAF83120.1; -; mRNA.
DR   EMBL; AK316142; BAH14513.1; -; mRNA.
DR   EMBL; AF417842; AAL06595.1; -; Genomic_DNA.
DR   EMBL; AC023237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC075852; AAH75852.1; -; mRNA.
DR   CCDS; CCDS53804.1; -. [P42226-3]
DR   CCDS; CCDS8931.1; -. [P42226-1]
DR   PIR; A54740; A54740.
DR   RefSeq; NP_001171549.1; NM_001178078.1. [P42226-1]
DR   RefSeq; NP_001171550.1; NM_001178079.1. [P42226-1]
DR   RefSeq; NP_001171551.1; NM_001178080.1. [P42226-3]
DR   RefSeq; NP_003144.3; NM_003153.4. [P42226-1]
DR   RefSeq; XP_006719638.1; XM_006719575.2.
DR   PDB; 1OJ5; X-ray; 2.20 A; B=795-808.
DR   PDB; 4Y5U; X-ray; 2.71 A; A/B=113-658.
DR   PDB; 4Y5W; X-ray; 3.10 A; A/B/C/D=113-658.
DR   PDB; 5D39; X-ray; 3.20 A; A/B/C/D=123-658.
DR   PDB; 5NWM; NMR; -; B=783-814.
DR   PDB; 5NWX; X-ray; 2.51 A; B=783-814.
DR   PDBsum; 1OJ5; -.
DR   PDBsum; 4Y5U; -.
DR   PDBsum; 4Y5W; -.
DR   PDBsum; 5D39; -.
DR   PDBsum; 5NWM; -.
DR   PDBsum; 5NWX; -.
DR   SMR; P42226; -.
DR   BioGRID; 112655; 65.
DR   ComplexPortal; CPX-6047; STAT2/STAT6 complex.
DR   ComplexPortal; CPX-6051; STAT6 homodimer.
DR   CORUM; P42226; -.
DR   DIP; DIP-39855N; -.
DR   IntAct; P42226; 58.
DR   MINT; P42226; -.
DR   STRING; 9606.ENSP00000300134; -.
DR   BindingDB; P42226; -.
DR   ChEMBL; CHEMBL5401; -.
DR   GuidetoPHARMACOLOGY; 2993; -.
DR   iPTMnet; P42226; -.
DR   MetOSite; P42226; -.
DR   PhosphoSitePlus; P42226; -.
DR   BioMuta; STAT6; -.
DR   DMDM; 1174459; -.
DR   CPTAC; CPTAC-1639; -.
DR   EPD; P42226; -.
DR   jPOST; P42226; -.
DR   MassIVE; P42226; -.
DR   MaxQB; P42226; -.
DR   PaxDb; P42226; -.
DR   PeptideAtlas; P42226; -.
DR   PRIDE; P42226; -.
DR   ProteomicsDB; 24436; -.
DR   ProteomicsDB; 55493; -. [P42226-1]
DR   ProteomicsDB; 55494; -. [P42226-2]
DR   Antibodypedia; 662; 1428 antibodies.
DR   DNASU; 6778; -.
DR   Ensembl; ENST00000300134; ENSP00000300134; ENSG00000166888. [P42226-1]
DR   Ensembl; ENST00000454075; ENSP00000401486; ENSG00000166888. [P42226-1]
DR   Ensembl; ENST00000537215; ENSP00000444530; ENSG00000166888. [P42226-3]
DR   Ensembl; ENST00000538913; ENSP00000445409; ENSG00000166888. [P42226-3]
DR   Ensembl; ENST00000543873; ENSP00000438451; ENSG00000166888. [P42226-1]
DR   Ensembl; ENST00000556155; ENSP00000451742; ENSG00000166888. [P42226-1]
DR   GeneID; 6778; -.
DR   KEGG; hsa:6778; -.
DR   UCSC; uc001sna.5; human. [P42226-1]
DR   CTD; 6778; -.
DR   DisGeNET; 6778; -.
DR   GeneCards; STAT6; -.
DR   HGNC; HGNC:11368; STAT6.
DR   HPA; ENSG00000166888; Low tissue specificity.
DR   MalaCards; STAT6; -.
DR   MIM; 601512; gene.
DR   neXtProt; NX_P42226; -.
DR   OpenTargets; ENSG00000166888; -.
DR   Orphanet; 2126; Solitary fibrous tumor/hemangiopericytoma.
DR   PharmGKB; PA339; -.
DR   VEuPathDB; HostDB:ENSG00000166888.10; -.
DR   eggNOG; KOG3667; Eukaryota.
DR   GeneTree; ENSGT01030000234663; -.
DR   HOGENOM; CLU_014189_2_1_1; -.
DR   InParanoid; P42226; -.
DR   OMA; FPQGTWI; -.
DR   OrthoDB; 327469at2759; -.
DR   PhylomeDB; P42226; -.
DR   TreeFam; TF318648; -.
DR   PathwayCommons; P42226; -.
DR   Reactome; R-HSA-186763; Downstream signal transduction.
DR   Reactome; R-HSA-3249367; STAT6-mediated induction of chemokines.
DR   Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   SignaLink; P42226; -.
DR   SIGNOR; P42226; -.
DR   BioGRID-ORCS; 6778; 6 hits in 1020 CRISPR screens.
DR   ChiTaRS; STAT6; human.
DR   EvolutionaryTrace; P42226; -.
DR   GeneWiki; STAT6; -.
DR   GenomeRNAi; 6778; -.
DR   Pharos; P42226; Tchem.
DR   PRO; PR:P42226; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P42226; protein.
DR   Bgee; ENSG00000166888; Expressed in granulocyte and 240 other tissues.
DR   ExpressionAtlas; P42226; baseline and differential.
DR   Genevisible; P42226; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd10377; SH2_STAT6; 1.
DR   DisProt; DP02262; -.
DR   Gene3D; 1.10.532.10; -; 1.
DR   Gene3D; 2.60.40.630; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   IDEAL; IID00047; -.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR028187; STAT6_C.
DR   InterPro; IPR035857; STAT6_SH2.
DR   InterPro; IPR036535; STAT_N_sf.
DR   InterPro; IPR013800; STAT_TF_alpha.
DR   InterPro; IPR015988; STAT_TF_coiled-coil.
DR   InterPro; IPR013801; STAT_TF_DNA-bd.
DR   InterPro; IPR012345; STAT_TF_DNA-bd_N.
DR   InterPro; IPR013799; STAT_TF_prot_interaction.
DR   PANTHER; PTHR11801; PTHR11801; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF14596; STAT6_C; 1.
DR   Pfam; PF01017; STAT_alpha; 1.
DR   Pfam; PF02864; STAT_bind; 1.
DR   Pfam; PF02865; STAT_int; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00964; STAT_int; 1.
DR   SUPFAM; SSF47655; SSF47655; 1.
DR   SUPFAM; SSF48092; SSF48092; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; ADP-ribosylation;
KW   Alternative splicing; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; SH2 domain; Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..847
FT                   /note="Signal transducer and activator of transcription 6"
FT                   /id="PRO_0000182433"
FT   DOMAIN          517..632
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          809..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           802..806
FT                   /note="LXXLL motif"
FT   COMPBIAS        824..847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         641
FT                   /note="Phosphotyrosine; by JAK"
FT                   /evidence="ECO:0000269|PubMed:27796300"
FT   VAR_SEQ         1..174
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_031871"
FT   VAR_SEQ         1..110
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045282"
FT   VAR_SEQ         175..177
FT                   /note="PSE -> MEQ (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_031872"
FT   VARIANT         181
FT                   /note="M -> R (in dbSNP:rs3024952)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_013094"
FT   VARIANT         419
FT                   /note="D -> N (in dbSNP:rs11172102)"
FT                   /id="VAR_059812"
FT   MUTAGEN         802
FT                   /note="L->A: Abolishes the interaction with NCOA1; when
FT                   associated with A-805."
FT                   /evidence="ECO:0000269|PubMed:12138096"
FT   MUTAGEN         805
FT                   /note="L->A: Abolishes the interaction with NCOA1; when
FT                   associated with A-802."
FT                   /evidence="ECO:0000269|PubMed:12138096"
FT   CONFLICT        149
FT                   /note="E -> Q (in Ref. 2; AAC67525)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="G -> D (in Ref. 4; BAH14513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        733
FT                   /note="S -> N (in Ref. 2; AAC67525)"
FT                   /evidence="ECO:0000305"
FT   HELIX           132..147
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:5D39"
FT   HELIX           186..211
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   TURN            212..214
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           222..241
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          244..246
FT                   /evidence="ECO:0007829|PDB:4Y5W"
FT   HELIX           256..271
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          272..277
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          281..284
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          288..295
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           298..301
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          310..316
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   TURN            318..321
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          340..342
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   TURN            351..354
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          355..365
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           379..381
FT                   /evidence="ECO:0007829|PDB:4Y5W"
FT   STRAND          384..392
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          401..406
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          410..413
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           420..431
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          444..447
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           448..463
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           471..482
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   TURN            489..494
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          496..498
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           499..503
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          510..512
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           514..528
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           530..534
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           544..551
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          558..563
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          565..569
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          571..578
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   STRAND          584..589
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           594..599
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           602..607
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   TURN            616..618
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           621..624
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   TURN            625..628
FT                   /evidence="ECO:0007829|PDB:4Y5W"
FT   STRAND          638..640
FT                   /evidence="ECO:0007829|PDB:4Y5W"
FT   STRAND          644..650
FT                   /evidence="ECO:0007829|PDB:4Y5U"
FT   HELIX           786..789
FT                   /evidence="ECO:0007829|PDB:5NWM"
FT   HELIX           799..807
FT                   /evidence="ECO:0007829|PDB:1OJ5"
SQ   SEQUENCE   847 AA;  94135 MW;  F35075F1C1F2A677 CRC64;
     MSLWGLVSKM PPEKVQRLYV DFPQHLRHLL GDWLESQPWE FLVGSDAFCC NLASALLSDT
     VQHLQASVGE QGEGSTILQH ISTLESIYQR DPLKLVATFR QILQGEKKAV MEQFRHLPMP
     FHWKQEELKF KTGLRRLQHR VGEIHLLREA LQKGAEAGQV SLHSLIETPA NGTGPSEALA
     MLLQETTGEL EAAKALVLKR IQIWKRQQQL AGNGAPFEES LAPLQERCES LVDIYSQLQQ
     EVGAAGGELE PKTRASLTGR LDEVLRTLVT SCFLVEKQPP QVLKTQTKFQ AGVRFLLGLR
     FLGAPAKPPL VRADMVTEKQ ARELSVPQGP GAGAESTGEI INNTVPLENS IPGNCCSALF
     KNLLLKKIKR CERKGTESVT EEKCAVLFSA SFTLGPGKLP IQLQALSLPL VVIVHGNQDN
     NAKATILWDN AFSEMDRVPF VVAERVPWEK MCETLNLKFM AEVGTNRGLL PEHFLFLAQK
     IFNDNSLSME AFQHRSVSWS QFNKEILLGR GFTFWQWFDG VLDLTKRCLR SYWSDRLIIG
     FISKQYVTSL LLNEPDGTFL LRFSDSEIGG ITIAHVIRGQ DGSPQIENIQ PFSAKDLSIR
     SLGDRIRDLA QLKNLYPKKP KDEAFRSHYK PEQMGKDGRG YVPATIKMTV ERDQPLPTPE
     LQMPTMVPSY DLGMAPDSSM SMQLGPDMVP QVYPPHSHSI PPYQGLSPEE SVNVLSAFQE
     PHLQMPPSLG QMSLPFDQPH PQGLLPCQPQ EHAVSSPDPL LCSDVTMVED SCLSQPVTAF
     PQGTWIGEDI FPPLLPPTEQ DLTKLLLEGQ GESGGGSLGA QPLLQPSHYG QSGISMSHMD
     LRANPSW
//
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