STAT6_HUMAN
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 03-AUG-2022, entry version 214.
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/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P42226; -.
DR SMR; P42226; -.
DR BioGRID; 112655; 69.
DR ComplexPortal; CPX-6047; STAT2/STAT6 complex.
DR ComplexPortal; CPX-6051; STAT6 homodimer.
DR CORUM; P42226; -.
DR DIP; DIP-39855N; -.
DR IntAct; P42226; 59.
DR MINT; P42226; -.
DR STRING; 9606.ENSP00000300134; -.
DR BindingDB; P42226; -.
DR ChEMBL; CHEMBL5401; -.
DR GuidetoPHARMACOLOGY; 2993; -.
DR GlyGen; P42226; 1 site, 1 O-linked glycan (1 site).
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; 1481 antibodies from 50 providers.
DR CPTC; P42226; 1 antibody.
DR DNASU; 6778; -.
DR Ensembl; ENST00000300134.8; ENSP00000300134.3; ENSG00000166888.12. [P42226-1]
DR Ensembl; ENST00000454075.7; ENSP00000401486.3; ENSG00000166888.12. [P42226-1]
DR Ensembl; ENST00000537215.6; ENSP00000444530.2; ENSG00000166888.12. [P42226-3]
DR Ensembl; ENST00000538913.6; ENSP00000445409.2; ENSG00000166888.12. [P42226-3]
DR Ensembl; ENST00000543873.6; ENSP00000438451.2; ENSG00000166888.12. [P42226-1]
DR Ensembl; ENST00000556155.5; ENSP00000451742.1; ENSG00000166888.12. [P42226-1]
DR GeneID; 6778; -.
DR KEGG; hsa:6778; -.
DR MANE-Select; ENST00000300134.8; ENSP00000300134.3; NM_003153.5; NP_003144.3.
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; -.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244952; -.
DR HOGENOM; CLU_014189_2_1_1; -.
DR InParanoid; P42226; -.
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; 12 hits in 1105 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 199 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:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
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:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:1902170; P:cellular response to reactive nitrogen species; IEA:Ensembl.
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:0048289; P:isotype switching to IgE isotypes; IEA:Ensembl.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0060443; P:mammary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0002829; P:negative regulation of type 2 immune response; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0048295; P:positive regulation of isotype switching to IgE isotypes; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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:0070666; P:regulation of mast cell proliferation; IEA:Ensembl.
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 GO; GO:0002296; P:T-helper 1 cell lineage commitment; IEA:Ensembl.
DR CDD; cd10377; SH2_STAT6; 1.
DR DisProt; DP02262; -.
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
