STAT6_MOUSE
ID STAT6_MOUSE Reviewed; 837 AA.
AC P52633; Q8R2F1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Signal transducer and transcription activator 6;
GN Name=Stat6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7760829; DOI=10.1128/mcb.15.6.3336;
RA Quelle F.W., Shimoda K., Thierfelder W., Fischer C.L., Kim A., Ruben S.M.,
RA Cleveland J.L., Pierce J.H., Keegan A.D., Nelms K., Paul W.E., Ihle J.N.;
RT "Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine
RT phosphorylated in responses to IL-4 and IL-3 but are not required for
RT mitogenesis.";
RL Mol. Cell. Biol. 15:3336-3343(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Leyva F.J., Evans C.M., Tuvim M.J., Dickey B.F.;
RT "Murine signal transducer and activator of transcription 6 (mSTAT6).";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION IN IL4/INTERLEUKIN-4 SIGNALING, PHOSPHORYLATION, AND
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Interacts with NCOA1 via its C-terminal LXXLL motif (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P52633; Q2EMV9: Parp14; NbExp=3; IntAct=EBI-647085, EBI-1534943;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the
CC nucleus in response to phosphorylation.
CC -!- PTM: Tyrosine phosphorylated on Tyr-641 following stimulation by
CC IL4/interleukin-4. Tyrosine phosphorylated following stimulation by
CC IL3/interleukin-3. Dephosphorylation on tyrosine residues by PTPN2
CC negatively regulates the IL4/interleukin-4 mediated signaling.
CC {ECO:0000269|PubMed:17210636}.
CC -!- PTM: Mono-ADP-ribosylated by PARP14. {ECO:0000250|UniProtKB:P42226}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
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DR EMBL; L47650; AAA79006.1; -; mRNA.
DR EMBL; AF481809; AAL82638.1; -; mRNA.
DR EMBL; AK163053; BAE37172.1; -; mRNA.
DR EMBL; CH466578; EDL24514.1; -; Genomic_DNA.
DR EMBL; BC127054; AAI27055.1; -; mRNA.
DR CCDS; CCDS36082.1; -.
DR PIR; I57557; I57557.
DR RefSeq; NP_033310.2; NM_009284.2.
DR AlphaFoldDB; P52633; -.
DR SMR; P52633; -.
DR BioGRID; 203527; 6.
DR DIP; DIP-49680N; -.
DR IntAct; P52633; 9.
DR STRING; 10090.ENSMUSP00000089708; -.
DR BindingDB; P52633; -.
DR ChEMBL; CHEMBL2189147; -.
DR iPTMnet; P52633; -.
DR PhosphoSitePlus; P52633; -.
DR EPD; P52633; -.
DR MaxQB; P52633; -.
DR PaxDb; P52633; -.
DR PeptideAtlas; P52633; -.
DR PRIDE; P52633; -.
DR ProteomicsDB; 254580; -.
DR Antibodypedia; 662; 1481 antibodies from 50 providers.
DR DNASU; 20852; -.
DR Ensembl; ENSMUST00000092074; ENSMUSP00000089708; ENSMUSG00000002147.
DR GeneID; 20852; -.
DR KEGG; mmu:20852; -.
DR UCSC; uc007hka.1; mouse.
DR CTD; 6778; -.
DR MGI; MGI:103034; Stat6.
DR VEuPathDB; HostDB:ENSMUSG00000002147; -.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244952; -.
DR HOGENOM; CLU_014189_2_1_1; -.
DR InParanoid; P52633; -.
DR OMA; EPQMPAM; -.
DR OrthoDB; 327469at2759; -.
DR PhylomeDB; P52633; -.
DR TreeFam; TF318648; -.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-3249367; STAT6-mediated induction of chemokines.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR BioGRID-ORCS; 20852; 3 hits in 114 CRISPR screens.
DR ChiTaRS; Stat6; mouse.
DR PRO; PR:P52633; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P52633; protein.
DR Bgee; ENSMUSG00000002147; Expressed in granulocyte and 236 other tissues.
DR ExpressionAtlas; P52633; baseline and differential.
DR Genevisible; P52633; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:1902170; P:cellular response to reactive nitrogen species; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
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; IGI:MGI.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060443; P:mammary gland morphogenesis; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0002829; P:negative regulation of type 2 immune response; IGI:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0048295; P:positive regulation of isotype switching to IgE isotypes; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
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; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IMP:MGI.
DR GO; GO:0002296; P:T-helper 1 cell lineage commitment; IGI:MGI.
DR CDD; cd10377; SH2_STAT6; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
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 Acetylation; Activator; ADP-ribosylation; Cytoplasm; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P42226"
FT CHAIN 2..837
FT /note="Signal transducer and transcription activator 6"
FT /id="PRO_0000182434"
FT DOMAIN 517..632
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 802..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 793..797
FT /note="LXXLL motif"
FT COMPBIAS 804..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P42226"
FT MOD_RES 641
FT /note="Phosphotyrosine; by JAK"
FT /evidence="ECO:0000250|UniProtKB:P42226"
FT CONFLICT 133
FT /note="A -> P (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="Q -> H (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..155
FT /note="QQGA -> HLGP (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="V -> L (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..182
FT /note="ATM -> PTI (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> T (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> P (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="K -> L (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="Q -> H (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> T (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> S (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="P -> S (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> G (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="A -> V (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="C -> W (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="M -> L (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 804
FT /note="A -> G (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="Q -> K (in Ref. 1; AAA79006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 93497 MW; 082E0A15C7457307 CRC64;
MSLWGLISKM SPEKLQRLYV DFPQRLRHLL ADWLESQPWE FLVGSDAFCY NMASALLSAT
VQRLQATAGE QGKGNSILPH ISTLESIYQR DPLKLVATIR QILQGEKKAV IEEFRHLPGP
FHRKQEELKF TTALGRLQHR VRETRLLRES LQQGAKTGQV SLQNLIDPPV NGPGPSEDLA
TMLQGTVGDL EATQALVLKR IQIWKRQQQL AGNGTPFEES LAGLQERCES LVEIYSQLQQ
EIGAASGELE PKTRASLISR LDEVLRTLVT SSFLVEKQPP QVLKTQTKFQ AGVRFLLGLQ
FLGTSAKPPM VRADMVTEKQ ARELSLAQGP GTGVESTGEI MNNTVPLENS IPSNCCSALF
KNLLLKKIKR CERKGTESVT EEKCAVLFST SFTLGPNKLL IQLQALSLPL VVIVHGNQDN
NAKATILWDN AFSEMDRVPF VVAERVPWEK MCETLNLKFM AEVGTSRGLL PEHFLFLAQK
IFNDNSLSVE AFQHRCVSWS QFNKEILLGR GFTFWQWFDG VLDLTKRCLR SYWSDRLIIG
FISKQYVTSL LLNEPDGTFL LRFSDSEIGG ITIAHVIRGQ DGSSQIENIQ PFSAKDLSIR
SLGDRIRDLA QLKNLYPKKP KDEAFRSHYK PEQMGKDGRG YVSTTIKMTV ERDQPLPTPE
PQMPAMVPPY DLGMAPDASM QLSSDMGYPP QSIHSFQSLE ESMSVLPSFQ EPHLQMPPNM
SQITMPFDQP HPQGLLQCQS QEHAVSSPEP MLCSDVTMVE DSCLTQPVGG FPQGTWVSED
MYPPLMPPTE QDLTKLLLEN QGEAGGSLGS QPLLQPSPYG QSGISLSHLD LRTNPSW
