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Signal transducer and activator of transcription 6 (IL-4 Stat)

 STAT6_HUMAN             Reviewed;         847 AA.
P42226; A8K316; B7ZA27; F5GXI9; Q5FBW5; Q71UP4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
18-JUL-2018, entry version 187.
RecName: Full=Signal transducer and activator of transcription 6;
AltName: Full=IL-4 Stat;
Name=STAT6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8085155; DOI=10.1126/science.8085155;
Hou J., Schindler U., Henzel W.J., Ho T., Brasseur M., McKnight S.L.;
"An interleukin-4-induced transcription factor: IL-4 Stat.";
Science 265:1701-1706(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9782085; DOI=10.1006/geno.1998.5436;
Patel B.K., Keck C.L., O'Leary R.S., Popescu N.C., LaRochelle W.J.;
"Localization of the human stat6 gene to chromosome 12q13.3-q14.1, a
region implicated in multiple solid tumors.";
Genomics 52:192-200(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tabata Y., Sameshima E., Hayashi A., Iida K., Mitsuyama M., Kanai S.,
Furuya T., Saito T.;
"STAT6 mRNA, nirs splice variant 2.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-181.
SeattleSNPs variation discovery resource;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH NCOA1, AND MUTAGENESIS OF LEU-802 AND LEU-805.
PubMed=12138096; DOI=10.1074/jbc.M203556200;
Litterst C.M., Pfitzner E.;
"An LXXLL motif in the transactivation domain of STAT6 mediates
recruitment of NCoA-1/SRC-1.";
J. Biol. Chem. 277:36052-36060(2002).
[9]
FUNCTION IN IL4 SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION BY
PTPN2.
PubMed=17210636; DOI=10.1128/MCB.01234-06;
Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T.,
Lossos I.S.;
"T-cell protein tyrosine phosphatase, distinctively expressed in
activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear
phosphatase of STAT6.";
Mol. Cell. Biol. 27:2166-2179(2007).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[11]
PHOSPHORYLATION AT TYR-641, AND ADP-RIBOSYLATION.
PubMed=27796300; DOI=10.1038/ncomms12849;
Iwata H., Goettsch C., Sharma A., Ricchiuto P., Goh W.W., Halu A.,
Yamada I., Yoshida H., Hara T., Wei M., Inoue N., Fukuda D.,
Mojcher A., Mattson P.C., Barabasi A.L., Boothby M., Aikawa E.,
Singh S.A., Aikawa M.;
"PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-
ribosylation.";
Nat. Commun. 7:12849-12849(2016).
[12]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 795-808 IN COMPLEX WITH
257-385 OF NCOA1.
PubMed=14757047; DOI=10.1016/j.jmb.2003.12.057;
Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C.,
Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E.,
Becker S.;
"Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif
of the STAT6 transactivation domain.";
J. Mol. Biol. 336:319-329(2004).
-!- FUNCTION: Carries out a dual function: signal transduction and
activation of transcription. Involved in IL4/interleukin-4- and
IL3/interleukin-3-mediated signaling.
{ECO:0000269|PubMed:17210636}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member (By similarity). Interacts with NCOA1 via its C-terminal
LXXLL motif. {ECO:0000250, ECO:0000269|PubMed:12138096,
ECO:0000269|PubMed:14757047}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1186478, EBI-1186478;
Q09472:EP300; NbExp=2; IntAct=EBI-1186478, EBI-447295;
P24394:IL4R; NbExp=4; IntAct=EBI-1186478, EBI-367009;
Q9UHD2:TBK1; NbExp=7; IntAct=EBI-1186478, EBI-356402;
Q86WV6:TMEM173; NbExp=12; IntAct=EBI-1186478, EBI-2800345;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into
the nucleus in response to phosphorylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P42226-1; Sequence=Displayed;
Name=2;
IsoId=P42226-2; Sequence=VSP_031871, VSP_031872;
Name=3;
IsoId=P42226-3; Sequence=VSP_045282;
Note=No experimental confirmation available.;
-!- PTM: Tyrosine phosphorylated on Tyr-641 following stimulation by
IL4/interleukin-4 (PubMed:27796300). Tyrosine phosphorylated
following stimulation by IL3/interleukin-3 (By similarity).
Dephosphorylation on tyrosine residues by PTPN2 negatively
regulates the IL4/interleukin-4 mediated signaling
(PubMed:17210636). {ECO:0000250|UniProtKB:P52633,
ECO:0000269|PubMed:17210636, ECO:0000269|PubMed:27796300}.
-!- PTM: Mono-ADP-ribosylated by PARP14.
{ECO:0000269|PubMed:27796300}.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/stat6/";
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EMBL; U16031; AAA57193.1; -; mRNA.
EMBL; AF067575; AAC67525.1; -; Genomic_DNA.
EMBL; AF067572; AAC67525.1; JOINED; Genomic_DNA.
EMBL; AF067573; AAC67525.1; JOINED; Genomic_DNA.
EMBL; AB103089; BAD89432.1; -; mRNA.
EMBL; AK290431; BAF83120.1; -; mRNA.
EMBL; AK316142; BAH14513.1; -; mRNA.
EMBL; AF417842; AAL06595.1; -; Genomic_DNA.
EMBL; AC023237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC075852; AAH75852.1; -; mRNA.
CCDS; CCDS53804.1; -. [P42226-3]
CCDS; CCDS8931.1; -. [P42226-1]
PIR; A54740; A54740.
RefSeq; NP_001171549.1; NM_001178078.1. [P42226-1]
RefSeq; NP_001171550.1; NM_001178079.1. [P42226-1]
RefSeq; NP_001171551.1; NM_001178080.1. [P42226-3]
RefSeq; NP_003144.3; NM_003153.4. [P42226-1]
RefSeq; XP_006719638.1; XM_006719575.2. [P42226-1]
UniGene; Hs.524518; -.
PDB; 1OJ5; X-ray; 2.20 A; B=795-808.
PDB; 4Y5U; X-ray; 2.71 A; A/B=113-658.
PDB; 4Y5W; X-ray; 3.10 A; A/B/C/D=113-658.
PDB; 5D39; X-ray; 3.20 A; A/B/C/D=123-658.
PDB; 5NWM; NMR; -; B=783-814.
PDB; 5NWX; X-ray; 2.51 A; B=783-814.
PDBsum; 1OJ5; -.
PDBsum; 4Y5U; -.
PDBsum; 4Y5W; -.
PDBsum; 5D39; -.
PDBsum; 5NWM; -.
PDBsum; 5NWX; -.
ProteinModelPortal; P42226; -.
SMR; P42226; -.
BioGrid; 112655; 61.
CORUM; P42226; -.
DIP; DIP-39855N; -.
IntAct; P42226; 35.
MINT; P42226; -.
STRING; 9606.ENSP00000300134; -.
BindingDB; P42226; -.
ChEMBL; CHEMBL5401; -.
GuidetoPHARMACOLOGY; 2993; -.
iPTMnet; P42226; -.
PhosphoSitePlus; P42226; -.
BioMuta; STAT6; -.
DMDM; 1174459; -.
EPD; P42226; -.
MaxQB; P42226; -.
PaxDb; P42226; -.
PeptideAtlas; P42226; -.
PRIDE; P42226; -.
ProteomicsDB; 55493; -.
ProteomicsDB; 55494; -. [P42226-2]
DNASU; 6778; -.
Ensembl; ENST00000300134; ENSP00000300134; ENSG00000166888. [P42226-1]
Ensembl; ENST00000454075; ENSP00000401486; ENSG00000166888. [P42226-1]
Ensembl; ENST00000537215; ENSP00000444530; ENSG00000166888. [P42226-3]
Ensembl; ENST00000538913; ENSP00000445409; ENSG00000166888. [P42226-3]
Ensembl; ENST00000543873; ENSP00000438451; ENSG00000166888. [P42226-1]
Ensembl; ENST00000556155; ENSP00000451742; ENSG00000166888. [P42226-1]
GeneID; 6778; -.
KEGG; hsa:6778; -.
UCSC; uc001sna.5; human. [P42226-1]
CTD; 6778; -.
DisGeNET; 6778; -.
EuPathDB; HostDB:ENSG00000166888.10; -.
GeneCards; STAT6; -.
HGNC; HGNC:11368; STAT6.
HPA; HPA001861; -.
MalaCards; STAT6; -.
MIM; 601512; gene.
neXtProt; NX_P42226; -.
OpenTargets; ENSG00000166888; -.
Orphanet; 2126; Solitary fibrous tumor.
PharmGKB; PA339; -.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOGENOM; HOG000230988; -.
HOVERGEN; HBG107486; -.
InParanoid; P42226; -.
KO; K11225; -.
OMA; ENSIPGN; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P42226; -.
TreeFam; TF318648; -.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-3249367; STAT6-mediated induction of chemokines.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; P42226; -.
SIGNOR; P42226; -.
ChiTaRS; STAT6; human.
EvolutionaryTrace; P42226; -.
GeneWiki; STAT6; -.
GenomeRNAi; 6778; -.
PRO; PR:P42226; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000166888; -.
CleanEx; HS_STAT6; -.
ExpressionAtlas; P42226; baseline and differential.
Genevisible; P42226; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:1902170; P:cellular response to reactive nitrogen species; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:0060443; P:mammary gland morphogenesis; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0002829; P:negative regulation of type 2 immune response; IEA:Ensembl.
GO; GO:0048295; P:positive regulation of isotype switching to IgE isotypes; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002296; P:T-helper 1 cell lineage commitment; IEA:Ensembl.
CDD; cd10377; SH2_STAT6; 1.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001217; STAT.
InterPro; IPR028187; STAT6_C.
InterPro; IPR035857; STAT6_SH2.
InterPro; IPR036535; STAT_N_sf.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_N.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF14596; STAT6_C; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00252; SH2; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; ADP-ribosylation;
Alternative splicing; Complete proteome; Cytoplasm; DNA-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; SH2 domain;
Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 847 Signal transducer and activator of
transcription 6.
/FTId=PRO_0000182433.
DOMAIN 517 632 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOTIF 802 806 LXXLL motif.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 641 641 Phosphotyrosine; by JAK.
{ECO:0000269|PubMed:27796300}.
VAR_SEQ 1 174 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_031871.
VAR_SEQ 1 110 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045282.
VAR_SEQ 175 177 PSE -> MEQ (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_031872.
VARIANT 181 181 M -> R (in dbSNP:rs3024952).
{ECO:0000269|Ref.5}.
/FTId=VAR_013094.
VARIANT 419 419 D -> N (in dbSNP:rs11172102).
/FTId=VAR_059812.
MUTAGEN 802 802 L->A: Abolishes the interaction with
NCOA1; when associated with A-805.
{ECO:0000269|PubMed:12138096}.
MUTAGEN 805 805 L->A: Abolishes the interaction with
NCOA1; when associated with A-802.
{ECO:0000269|PubMed:12138096}.
CONFLICT 149 149 E -> Q (in Ref. 2; AAC67525).
{ECO:0000305}.
CONFLICT 246 246 G -> D (in Ref. 4; BAH14513).
{ECO:0000305}.
CONFLICT 733 733 S -> N (in Ref. 2; AAC67525).
{ECO:0000305}.
HELIX 132 147 {ECO:0000244|PDB:4Y5U}.
HELIX 148 150 {ECO:0000244|PDB:5D39}.
HELIX 186 211 {ECO:0000244|PDB:4Y5U}.
TURN 212 214 {ECO:0000244|PDB:4Y5U}.
HELIX 222 241 {ECO:0000244|PDB:4Y5U}.
STRAND 244 246 {ECO:0000244|PDB:4Y5W}.
HELIX 256 271 {ECO:0000244|PDB:4Y5U}.
STRAND 272 277 {ECO:0000244|PDB:4Y5U}.
STRAND 281 284 {ECO:0000244|PDB:4Y5U}.
STRAND 288 295 {ECO:0000244|PDB:4Y5U}.
HELIX 298 301 {ECO:0000244|PDB:4Y5U}.
STRAND 310 316 {ECO:0000244|PDB:4Y5U}.
TURN 318 321 {ECO:0000244|PDB:4Y5U}.
STRAND 340 342 {ECO:0000244|PDB:4Y5U}.
STRAND 344 346 {ECO:0000244|PDB:4Y5U}.
STRAND 348 350 {ECO:0000244|PDB:4Y5U}.
TURN 351 354 {ECO:0000244|PDB:4Y5U}.
STRAND 355 365 {ECO:0000244|PDB:4Y5U}.
HELIX 379 381 {ECO:0000244|PDB:4Y5W}.
STRAND 384 392 {ECO:0000244|PDB:4Y5U}.
STRAND 401 406 {ECO:0000244|PDB:4Y5U}.
STRAND 410 413 {ECO:0000244|PDB:4Y5U}.
STRAND 415 417 {ECO:0000244|PDB:4Y5U}.
HELIX 420 431 {ECO:0000244|PDB:4Y5U}.
STRAND 444 447 {ECO:0000244|PDB:4Y5U}.
HELIX 448 463 {ECO:0000244|PDB:4Y5U}.
HELIX 471 482 {ECO:0000244|PDB:4Y5U}.
TURN 489 494 {ECO:0000244|PDB:4Y5U}.
STRAND 496 498 {ECO:0000244|PDB:4Y5U}.
HELIX 499 503 {ECO:0000244|PDB:4Y5U}.
STRAND 510 512 {ECO:0000244|PDB:4Y5U}.
HELIX 514 528 {ECO:0000244|PDB:4Y5U}.
HELIX 530 534 {ECO:0000244|PDB:4Y5U}.
HELIX 544 551 {ECO:0000244|PDB:4Y5U}.
STRAND 558 563 {ECO:0000244|PDB:4Y5U}.
STRAND 565 569 {ECO:0000244|PDB:4Y5U}.
STRAND 571 578 {ECO:0000244|PDB:4Y5U}.
STRAND 584 589 {ECO:0000244|PDB:4Y5U}.
HELIX 594 599 {ECO:0000244|PDB:4Y5U}.
HELIX 602 607 {ECO:0000244|PDB:4Y5U}.
TURN 616 618 {ECO:0000244|PDB:4Y5U}.
HELIX 621 624 {ECO:0000244|PDB:4Y5U}.
TURN 625 628 {ECO:0000244|PDB:4Y5W}.
STRAND 638 640 {ECO:0000244|PDB:4Y5W}.
STRAND 644 650 {ECO:0000244|PDB:4Y5U}.
HELIX 786 789 {ECO:0000244|PDB:5NWM}.
HELIX 799 807 {ECO:0000244|PDB:1OJ5}.
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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