I12R2_HUMAN
ID I12R2_HUMAN Reviewed; 862 AA.
AC Q99665; B1AN98; B7ZKL9; F5H7L6; Q2M3V3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Interleukin-12 receptor subunit beta-2;
DE Short=IL-12 receptor subunit beta-2;
DE Short=IL-12R subunit beta-2;
DE Short=IL-12R-beta-2;
DE Short=IL-12RB2;
DE Flags: Precursor;
GN Name=IL12RB2;
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=8943050; DOI=10.1073/pnas.93.24.14002;
RA Presky D.H., Yang H., Minetti L.J., Chua A.O., Nabavi N., Wu C.-Y.,
RA Gately M.K., Gubler U.;
RT "A functional interleukin 12 receptor complex is composed of two beta-type
RT cytokine receptor subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14002-14007(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RX PubMed=10663559; DOI=10.1007/s002510050005;
RA van Rietschoten J.G.I., Smits H.H., Westland R., Verweij C.L.,
RA den Hartog M.T., Wierenga E.A.;
RT "Genomic organization of the human interleukin-12 receptor beta2-chain
RT gene.";
RL Immunogenetics 51:30-36(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-13; GLN-149; HIS-426;
RP ASP-465 AND ARG-808.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP HIS-426.
RC TISSUE=Brain;
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 [7]
RP INTERACTION WITH STAT4, PHOSPHORYLATION AT TYR-800, AND MUTAGENESIS OF
RP LEU-801; PRO-802; SER-803 AND ASN-804.
RX PubMed=10415122; DOI=10.1006/abbi.1999.1302;
RA Yao B.B., Niu P., Surowy C.S., Faltynek C.R.;
RT "Direct interaction of STAT4 with the IL-12 receptor.";
RL Arch. Biochem. Biophys. 368:147-155(1999).
RN [8]
RP INTERACTION WITH JAK2, AND MUTAGENESIS OF TYR-678; TYR-767 AND TYR-800.
RX PubMed=10198225; DOI=10.1006/bbrc.1999.0479;
RA Yamamoto K., Shibata F., Miura O., Kamiyama R., Hirosawa S., Miyasaka N.;
RT "Physical interaction between interleukin-12 receptor beta 2 subunit and
RT Jak2 tyrosine kinase: Jak2 associates with cytoplasmic membrane-proximal
RT region of interleukin-12 receptor beta 2 via amino-terminus.";
RL Biochem. Biophys. Res. Commun. 257:400-404(1999).
RN [9]
RP INTERACTION WITH STAT4, AND MUTAGENESIS OF TYR-678; TYR-767 AND TYR-800.
RX PubMed=9890938; DOI=10.1074/jbc.274.4.1875;
RA Naeger L.K., McKinney J., Salvekar A., Hoey T.;
RT "Identification of a STAT4 binding site in the interleukin-12 receptor
RT required for signaling.";
RL J. Biol. Chem. 274:1875-1878(1999).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9120388; DOI=10.1084/jem.185.5.825;
RA Rogge L., Barberis-Maino L., Biffi M., Passini N., Presky D.H., Gubler U.,
RA Sinigaglia F.;
RT "Selective expression of an interleukin-12 receptor component by human T
RT helper 1 cells.";
RL J. Exp. Med. 185:825-831(1997).
RN [11]
RP PHOSPHORYLATION, INTERACTION WITH SOCS3, AND MUTAGENESIS OF TYR-678;
RP TYR-767 AND TYR-800.
RX PubMed=14559241; DOI=10.1016/j.bbrc.2003.09.140;
RA Yamamoto K., Yamaguchi M., Miyasaka N., Miura O.;
RT "SOCS-3 inhibits IL-12-induced STAT4 activation by binding through its SH2
RT domain to the STAT4 docking site in the IL-12 receptor beta2 subunit.";
RL Biochem. Biophys. Res. Commun. 310:1188-1193(2003).
RN [12]
RP VARIANTS GLY-313 AND ARG-720.
RX PubMed=10600539; DOI=10.1006/bbrc.1999.1859;
RA Matsui E., Kaneko H., Fukao T., Teramoto T., Inoue R., Watanabe M.,
RA Kasahara K., Kondo N.;
RT "Mutations of the IL-12 receptor beta2 chain gene in atopic subjects.";
RL Biochem. Biophys. Res. Commun. 266:551-555(1999).
CC -!- FUNCTION: Receptor for interleukin-12. This subunit is the signaling
CC component coupling to the JAK2/STAT4 pathway. Promotes the
CC proliferation of T-cells as well as NK cells. Induces the promotion of
CC T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma
CC production.
CC -!- SUBUNIT: Heterodimer/heterooligomer; disulfide-linked. The functional
CC high affinity IL12 receptor is composed of I12RB1 and IL12RB2. Il12RB2
CC binds JAK2 (via its N-terminal) through a membrane-proximal region of
CC the cytoplasmic domain. Interaction, in vitro and in vivo, with SOCS3
CC (via its SH2 domain) inhibits the STAT4-mediated activation. Binds
CC STAT4 through a membrane-distal C-terminal region.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99665-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99665-2; Sequence=VSP_011112, VSP_011113;
CC Name=3;
CC IsoId=Q99665-3; Sequence=VSP_044784;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed at similar levels in both
CC naive and activated T-cells. {ECO:0000269|PubMed:9120388}.
CC -!- DEVELOPMENTAL STAGE: Maximum levels in Th1 cells between day 3 and day
CC 8 of activation.
CC -!- INDUCTION: In vitro, up-regulated by IFN-alpha.
CC {ECO:0000269|PubMed:9120388}.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- PTM: On IL12 binding, phosphorylated on C-terminal tyrosine residues by
CC JAK2. Phosphorylation on Tyr-800 is required for STAT4 binding and
CC activation, and for SOCS3 binding. {ECO:0000269|PubMed:10415122,
CC ECO:0000269|PubMed:14559241}.
CC -!- POLYMORPHISM: Heterozygotic variants Gly-313 and Arg-720 are associated
CC with atopy, an immunological condition that can lead to clinical
CC symptoms such as allergic rhinitis, sinusitis, asthma and eczema.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il12rb2/";
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DR EMBL; U64198; AAB36675.1; -; mRNA.
DR EMBL; AY640177; AAT45456.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06499.1; -; Genomic_DNA.
DR EMBL; AL358512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL389925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104772; AAI04773.1; -; mRNA.
DR EMBL; BC104774; AAI04775.1; -; mRNA.
DR EMBL; BC143249; AAI43250.1; -; mRNA.
DR CCDS; CCDS58006.1; -. [Q99665-2]
DR CCDS; CCDS58007.1; -. [Q99665-3]
DR CCDS; CCDS638.1; -. [Q99665-1]
DR RefSeq; NP_001245143.1; NM_001258214.1. [Q99665-2]
DR RefSeq; NP_001245144.1; NM_001258215.1. [Q99665-3]
DR RefSeq; NP_001245145.1; NM_001258216.1.
DR RefSeq; NP_001306162.1; NM_001319233.1. [Q99665-2]
DR RefSeq; NP_001550.1; NM_001559.2. [Q99665-1]
DR RefSeq; XP_005270882.1; XM_005270825.2.
DR RefSeq; XP_005270884.1; XM_005270827.2. [Q99665-1]
DR RefSeq; XP_005270885.1; XM_005270828.3. [Q99665-1]
DR RefSeq; XP_006710680.1; XM_006710617.2. [Q99665-3]
DR RefSeq; XP_011539685.1; XM_011541383.2. [Q99665-1]
DR RefSeq; XP_016856692.1; XM_017001203.1. [Q99665-2]
DR AlphaFoldDB; Q99665; -.
DR SMR; Q99665; -.
DR BioGRID; 109809; 15.
DR ComplexPortal; CPX-382; Interleukin-12-receptor complex.
DR CORUM; Q99665; -.
DR DIP; DIP-6011N; -.
DR IntAct; Q99665; 5.
DR MINT; Q99665; -.
DR STRING; 9606.ENSP00000262345; -.
DR GlyGen; Q99665; 8 sites.
DR iPTMnet; Q99665; -.
DR PhosphoSitePlus; Q99665; -.
DR BioMuta; IL12RB2; -.
DR DMDM; 12229836; -.
DR PaxDb; Q99665; -.
DR PeptideAtlas; Q99665; -.
DR PRIDE; Q99665; -.
DR ProteomicsDB; 27522; -.
DR ProteomicsDB; 78384; -. [Q99665-1]
DR ABCD; Q99665; 2 sequenced antibodies.
DR Antibodypedia; 19617; 371 antibodies from 35 providers.
DR DNASU; 3595; -.
DR Ensembl; ENST00000262345.5; ENSP00000262345.1; ENSG00000081985.13. [Q99665-1]
DR Ensembl; ENST00000371000.5; ENSP00000360039.1; ENSG00000081985.13. [Q99665-2]
DR Ensembl; ENST00000544434.5; ENSP00000442443.1; ENSG00000081985.13. [Q99665-3]
DR Ensembl; ENST00000648487.1; ENSP00000497959.1; ENSG00000081985.13. [Q99665-1]
DR Ensembl; ENST00000674203.2; ENSP00000501329.1; ENSG00000081985.13. [Q99665-1]
DR GeneID; 3595; -.
DR KEGG; hsa:3595; -.
DR MANE-Select; ENST00000674203.2; ENSP00000501329.1; NM_001374259.2; NP_001361188.1.
DR UCSC; uc001ddu.3; human. [Q99665-1]
DR CTD; 3595; -.
DR DisGeNET; 3595; -.
DR GeneCards; IL12RB2; -.
DR HGNC; HGNC:5972; IL12RB2.
DR HPA; ENSG00000081985; Tissue enhanced (brain, placenta).
DR MIM; 601642; gene.
DR neXtProt; NX_Q99665; -.
DR OpenTargets; ENSG00000081985; -.
DR PharmGKB; PA29787; -.
DR VEuPathDB; HostDB:ENSG00000081985; -.
DR eggNOG; ENOG502QRRE; Eukaryota.
DR GeneTree; ENSGT00940000159829; -.
DR HOGENOM; CLU_016653_0_0_1; -.
DR InParanoid; Q99665; -.
DR OMA; KWAKECT; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; Q99665; -.
DR TreeFam; TF338122; -.
DR PathwayCommons; Q99665; -.
DR Reactome; R-HSA-8984722; Interleukin-35 Signalling.
DR Reactome; R-HSA-9020591; Interleukin-12 signaling.
DR SignaLink; Q99665; -.
DR SIGNOR; Q99665; -.
DR BioGRID-ORCS; 3595; 32 hits in 1060 CRISPR screens.
DR ChiTaRS; IL12RB2; human.
DR GeneWiki; Interleukin_12_receptor,_beta_2_subunit; -.
DR GenomeRNAi; 3595; -.
DR Pharos; Q99665; Tbio.
DR PRO; PR:Q99665; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99665; protein.
DR Bgee; ENSG00000081985; Expressed in hindlimb stylopod muscle and 111 other tissues.
DR ExpressionAtlas; Q99665; baseline and differential.
DR Genevisible; Q99665; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0042022; C:interleukin-12 receptor complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IC:ComplexPortal.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:ComplexPortal.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:ComplexPortal.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:ComplexPortal.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:ComplexPortal.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR010457; IgC2-like_lig-bd.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF06328; Lep_receptor_Ig; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..862
FT /note="Interleukin-12 receptor subunit beta-2"
FT /id="PRO_0000010920"
FT TOPO_DOM 24..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..221
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 226..319
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 320..419
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 423..520
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 521..620
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 725..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..801
FT /note="Required for STAT4 binding"
FT MOTIF 305..309
FT /note="WSXWS motif"
FT MOTIF 662..670
FT /note="Box 1 motif"
FT MOD_RES 800
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10415122"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 487..572
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044784"
FT VAR_SEQ 650..659
FT /note="VFVLLAALRP -> RRHSCPWTGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10663559"
FT /id="VSP_011112"
FT VAR_SEQ 660..862
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10663559"
FT /id="VSP_011113"
FT VARIANT 13
FT /note="M -> V (in dbSNP:rs17129772)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_021278"
FT VARIANT 149
FT /note="R -> Q (in dbSNP:rs17129792)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_021279"
FT VARIANT 185
FT /note="I -> V (in dbSNP:rs2307146)"
FT /id="VAR_014805"
FT VARIANT 201
FT /note="T -> I (in dbSNP:rs7526769)"
FT /id="VAR_019525"
FT VARIANT 313
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:10600539"
FT /id="VAR_019526"
FT VARIANT 420
FT /note="G -> R (in dbSNP:rs2307148)"
FT /id="VAR_014806"
FT VARIANT 420
FT /note="G -> S (in dbSNP:rs2307148)"
FT /id="VAR_049169"
FT VARIANT 426
FT /note="Q -> H (in dbSNP:rs2307145)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_014807"
FT VARIANT 465
FT /note="G -> D (in dbSNP:rs2307153)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_014808"
FT VARIANT 625
FT /note="A -> V (in dbSNP:rs2307154)"
FT /id="VAR_016097"
FT VARIANT 720
FT /note="H -> R (in dbSNP:rs1242019108)"
FT /evidence="ECO:0000269|PubMed:10600539"
FT /id="VAR_019527"
FT VARIANT 808
FT /note="L -> R (in dbSNP:rs17838066)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_021280"
FT MUTAGEN 678
FT /note="Y->F: No loss of STAT4 activation. No loss of SOCS3
FT binding."
FT /evidence="ECO:0000269|PubMed:10198225,
FT ECO:0000269|PubMed:14559241, ECO:0000269|PubMed:9890938"
FT MUTAGEN 767
FT /note="Y->F: No loss of STAT4 activation. No loss of SOCS3
FT binding."
FT /evidence="ECO:0000269|PubMed:10198225,
FT ECO:0000269|PubMed:14559241, ECO:0000269|PubMed:9890938"
FT MUTAGEN 800
FT /note="Y->F: Loss of STAT4 activation. Abolishes SOCS3
FT binding."
FT /evidence="ECO:0000269|PubMed:10198225,
FT ECO:0000269|PubMed:14559241, ECO:0000269|PubMed:9890938"
FT MUTAGEN 801
FT /note="L->A: Abolishes in vitro STAT4 binding to a
FT phosphorylated Y-800 peptide."
FT /evidence="ECO:0000269|PubMed:10415122"
FT MUTAGEN 802
FT /note="P->A: No effect on in vitro STAT4 binding to a
FT phosphorylated Y-800 peptide."
FT /evidence="ECO:0000269|PubMed:10415122"
FT MUTAGEN 803
FT /note="S->A: No effect on in vitro STAT4 binding to a
FT phosphorylated Y-800 peptide."
FT /evidence="ECO:0000269|PubMed:10415122"
FT MUTAGEN 804
FT /note="N->A: No effect on in vitro STAT4 binding to a
FT phosphorylated Y-800 peptide."
FT /evidence="ECO:0000269|PubMed:10415122"
SQ SEQUENCE 862 AA; 97135 MW; 67C0E0D946B8DD58 CRC64;
MAHTFRGCSL AFMFIITWLL IKAKIDACKR GDVTVKPSHV ILLGSTVNIT CSLKPRQGCF
HYSRRNKLIL YKFDRRINFH HGHSLNSQVT GLPLGTTLFV CKLACINSDE IQICGAEIFV
GVAPEQPQNL SCIQKGEQGT VACTWERGRD THLYTEYTLQ LSGPKNLTWQ KQCKDIYCDY
LDFGINLTPE SPESNFTAKV TAVNSLGSSS SLPSTFTFLD IVRPLPPWDI RIKFQKASVS
RCTLYWRDEG LVLLNRLRYR PSNSRLWNMV NVTKAKGRHD LLDLKPFTEY EFQISSKLHL
YKGSWSDWSE SLRAQTPEEE PTGMLDVWYM KRHIDYSRQQ ISLFWKNLSV SEARGKILHY
QVTLQELTGG KAMTQNITGH TSWTTVIPRT GNWAVAVSAA NSKGSSLPTR INIMNLCEAG
LLAPRQVSAN SEGMDNILVT WQPPRKDPSA VQEYVVEWRE LHPGGDTQVP LNWLRSRPYN
VSALISENIK SYICYEIRVY ALSGDQGGCS SILGNSKHKA PLSGPHINAI TEEKGSILIS
WNSIPVQEQM GCLLHYRIYW KERDSNSQPQ LCEIPYRVSQ NSHPINSLQP RVTYVLWMTA
LTAAGESSHG NEREFCLQGK ANWMAFVAPS ICIAIIMVGI FSTHYFQQKV FVLLAALRPQ
WCSREIPDPA NSTCAKKYPI AEEKTQLPLD RLLIDWPTPE DPEPLVISEV LHQVTPVFRH
PPCSNWPQRE KGIQGHQASE KDMMHSASSP PPPRALQAES RQLVDLYKVL ESRGSDPKPE
NPACPWTVLP AGDLPTHDGY LPSNIDDLPS HEAPLADSLE ELEPQHISLS VFPSSSLHPL
TFSCGDKLTL DQLKMRCDSL ML
