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Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)

 I12R2_HUMAN             Reviewed;         862 AA.
Q99665; B1AN98; B7ZKL9; F5H7L6; Q2M3V3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
17-JUN-2020, entry version 190.
RecName: Full=Interleukin-12 receptor subunit beta-2;
Short=IL-12 receptor subunit beta-2;
Short=IL-12R subunit beta-2;
Short=IL-12R-beta-2;
Short=IL-12RB2;
Flags: Precursor;
Name=IL12RB2;
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=8943050; DOI=10.1073/pnas.93.24.14002;
Presky D.H., Yang H., Minetti L.J., Chua A.O., Nabavi N., Wu C.-Y.,
Gately M.K., Gubler U.;
"A functional interleukin 12 receptor complex is composed of two beta-type
cytokine receptor subunits.";
Proc. Natl. Acad. Sci. U.S.A. 93:14002-14007(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=T-cell;
PubMed=10663559; DOI=10.1007/s002510050005;
van Rietschoten J.G.I., Smits H.H., Westland R., Verweij C.L.,
den Hartog M.T., Wierenga E.A.;
"Genomic organization of the human interleukin-12 receptor beta2-chain
gene.";
Immunogenetics 51:30-36(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-13; GLN-149; HIS-426;
ASP-465 AND ARG-808.
SeattleSNPs variation discovery resource;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
HIS-426.
TISSUE=Brain;
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).
[7]
INTERACTION WITH STAT4, PHOSPHORYLATION AT TYR-800, AND MUTAGENESIS OF
LEU-801; PRO-802; SER-803 AND ASN-804.
PubMed=10415122; DOI=10.1006/abbi.1999.1302;
Yao B.B., Niu P., Surowy C.S., Faltynek C.R.;
"Direct interaction of STAT4 with the IL-12 receptor.";
Arch. Biochem. Biophys. 368:147-155(1999).
[8]
INTERACTION WITH JAK2, AND MUTAGENESIS OF TYR-678; TYR-767 AND TYR-800.
PubMed=10198225; DOI=10.1006/bbrc.1999.0479;
Yamamoto K., Shibata F., Miura O., Kamiyama R., Hirosawa S., Miyasaka N.;
"Physical interaction between interleukin-12 receptor beta 2 subunit and
Jak2 tyrosine kinase: Jak2 associates with cytoplasmic membrane-proximal
region of interleukin-12 receptor beta 2 via amino-terminus.";
Biochem. Biophys. Res. Commun. 257:400-404(1999).
[9]
INTERACTION WITH STAT4, AND MUTAGENESIS OF TYR-678; TYR-767 AND TYR-800.
PubMed=9890938; DOI=10.1074/jbc.274.4.1875;
Naeger L.K., McKinney J., Salvekar A., Hoey T.;
"Identification of a STAT4 binding site in the interleukin-12 receptor
required for signaling.";
J. Biol. Chem. 274:1875-1878(1999).
[10]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=9120388; DOI=10.1084/jem.185.5.825;
Rogge L., Barberis-Maino L., Biffi M., Passini N., Presky D.H., Gubler U.,
Sinigaglia F.;
"Selective expression of an interleukin-12 receptor component by human T
helper 1 cells.";
J. Exp. Med. 185:825-831(1997).
[11]
PHOSPHORYLATION, INTERACTION WITH SOCS3, AND MUTAGENESIS OF TYR-678;
TYR-767 AND TYR-800.
PubMed=14559241; DOI=10.1016/j.bbrc.2003.09.140;
Yamamoto K., Yamaguchi M., Miyasaka N., Miura O.;
"SOCS-3 inhibits IL-12-induced STAT4 activation by binding through its SH2
domain to the STAT4 docking site in the IL-12 receptor beta2 subunit.";
Biochem. Biophys. Res. Commun. 310:1188-1193(2003).
[12]
VARIANTS GLY-313 AND ARG-720.
PubMed=10600539; DOI=10.1006/bbrc.1999.1859;
Matsui E., Kaneko H., Fukao T., Teramoto T., Inoue R., Watanabe M.,
Kasahara K., Kondo N.;
"Mutations of the IL-12 receptor beta2 chain gene in atopic subjects.";
Biochem. Biophys. Res. Commun. 266:551-555(1999).
-!- FUNCTION: Receptor for interleukin-12. This subunit is the signaling
component coupling to the JAK2/STAT4 pathway. Promotes the
proliferation of T-cells as well as NK cells. Induces the promotion of
T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma
production.
-!- SUBUNIT: Heterodimer/heterooligomer; disulfide-linked. The functional
high affinity IL12 receptor is composed of I12RB1 and IL12RB2. Il12RB2
binds JAK2 (via its N-terminal) through a membrane-proximal region of
the cytoplasmic domain. Interaction, in vitro and in vivo, with SOCS3
(via its SH2 domain) inhibits the STAT4-mediated activation. Binds
STAT4 through a membrane-distal C-terminal region.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q99665-1; Sequence=Displayed;
Name=2;
IsoId=Q99665-2; Sequence=VSP_011112, VSP_011113;
Name=3;
IsoId=Q99665-3; Sequence=VSP_044784;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed at similar levels in both
naive and activated T-cells. {ECO:0000269|PubMed:9120388}.
-!- DEVELOPMENTAL STAGE: Maximum levels in Th1 cells between day 3 and day
8 of activation.
-!- INDUCTION: In vitro, up-regulated by IFN-alpha.
{ECO:0000269|PubMed:9120388}.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-surface
receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: On IL12 binding, phosphorylated on C-terminal tyrosine residues by
JAK2. Phosphorylation on Tyr-800 is required for STAT4 binding and
activation, and for SOCS3 binding. {ECO:0000269|PubMed:10415122,
ECO:0000269|PubMed:14559241}.
-!- POLYMORPHISM: Heterozygotic variants Gly-313 and Arg-720 are associated
with atopy, an immunological condition that can lead to clinical
symptoms such as allergic rhinitis, sinusitis, asthma and eczema.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il12rb2/";
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EMBL; U64198; AAB36675.1; -; mRNA.
EMBL; AY640177; AAT45456.1; -; Genomic_DNA.
EMBL; CH471059; EAX06499.1; -; Genomic_DNA.
EMBL; AL358512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL389925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC104772; AAI04773.1; -; mRNA.
EMBL; BC104774; AAI04775.1; -; mRNA.
EMBL; BC143249; AAI43250.1; -; mRNA.
CCDS; CCDS58006.1; -. [Q99665-2]
CCDS; CCDS58007.1; -. [Q99665-3]
CCDS; CCDS638.1; -. [Q99665-1]
RefSeq; NP_001245143.1; NM_001258214.1. [Q99665-2]
RefSeq; NP_001245144.1; NM_001258215.1. [Q99665-3]
RefSeq; NP_001245145.1; NM_001258216.1.
RefSeq; NP_001306162.1; NM_001319233.1. [Q99665-2]
RefSeq; NP_001550.1; NM_001559.2. [Q99665-1]
RefSeq; XP_005270882.1; XM_005270825.2.
RefSeq; XP_005270884.1; XM_005270827.2. [Q99665-1]
RefSeq; XP_005270885.1; XM_005270828.3. [Q99665-1]
RefSeq; XP_006710680.1; XM_006710617.2. [Q99665-3]
RefSeq; XP_011539685.1; XM_011541383.2. [Q99665-1]
RefSeq; XP_016856692.1; XM_017001203.1. [Q99665-2]
BioGRID; 109809; 4.
ComplexPortal; CPX-382; Interleukin-12-receptor complex.
CORUM; Q99665; -.
DIP; DIP-6011N; -.
IntAct; Q99665; 4.
MINT; Q99665; -.
STRING; 9606.ENSP00000262345; -.
iPTMnet; Q99665; -.
PhosphoSitePlus; Q99665; -.
BioMuta; IL12RB2; -.
DMDM; 12229836; -.
MassIVE; Q99665; -.
PaxDb; Q99665; -.
PeptideAtlas; Q99665; -.
PRIDE; Q99665; -.
ProteomicsDB; 27522; -.
ProteomicsDB; 78384; -. [Q99665-1]
ProteomicsDB; 78385; -. [Q99665-2]
ABCD; Q99665; 2 sequenced antibodies.
Antibodypedia; 19617; 331 antibodies.
Ensembl; ENST00000262345; ENSP00000262345; ENSG00000081985. [Q99665-1]
Ensembl; ENST00000371000; ENSP00000360039; ENSG00000081985. [Q99665-2]
Ensembl; ENST00000544434; ENSP00000442443; ENSG00000081985. [Q99665-3]
Ensembl; ENST00000648487; ENSP00000497959; ENSG00000081985. [Q99665-1]
GeneID; 3595; -.
KEGG; hsa:3595; -.
UCSC; uc001ddu.3; human. [Q99665-1]
CTD; 3595; -.
DisGeNET; 3595; -.
EuPathDB; HostDB:ENSG00000081985.10; -.
GeneCards; IL12RB2; -.
HGNC; HGNC:5972; IL12RB2.
HPA; ENSG00000081985; Tissue enhanced (blood, pancreas).
MIM; 601642; gene.
neXtProt; NX_Q99665; -.
OpenTargets; ENSG00000081985; -.
PharmGKB; PA29787; -.
eggNOG; ENOG410IHXG; Eukaryota.
eggNOG; ENOG41116V2; LUCA.
GeneTree; ENSGT00940000159829; -.
HOGENOM; CLU_016653_0_0_1; -.
InParanoid; Q99665; -.
KO; K05064; -.
OMA; SKWAKEC; -.
OrthoDB; 651627at2759; -.
PhylomeDB; Q99665; -.
TreeFam; TF338122; -.
Reactome; R-HSA-8984722; Interleukin-35 Signalling.
Reactome; R-HSA-9020591; Interleukin-12 signaling.
SIGNOR; Q99665; -.
BioGRID-ORCS; 3595; 26 hits in 780 CRISPR screens.
ChiTaRS; IL12RB2; human.
GeneWiki; Interleukin_12_receptor,_beta_2_subunit; -.
GenomeRNAi; 3595; -.
Pharos; Q99665; Tbio.
PRO; PR:Q99665; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; Q99665; protein.
Bgee; ENSG00000081985; Expressed in placenta and 109 other tissues.
ExpressionAtlas; Q99665; baseline and differential.
Genevisible; Q99665; HS.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0032609; P:interferon-gamma production; IEA:Ensembl.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0070757; P:interleukin-35-mediated signaling pathway; TAS:Reactome.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
Pfam; PF00041; fn3; 1.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 4.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 5.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1..23
/evidence="ECO:0000255"
CHAIN 24..862
/note="Interleukin-12 receptor subunit beta-2"
/id="PRO_0000010920"
TOPO_DOM 24..622
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 623..643
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 644..862
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 126..221
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 226..319
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 320..419
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 423..520
/note="Fibronectin type-III 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 521..620
/note="Fibronectin type-III 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
REGION 796..801
/note="Required for STAT4 binding"
MOTIF 305..309
/note="WSXWS motif"
MOTIF 662..670
/note="Box 1 motif"
COMPBIAS 208..211
/note="Poly-Ser"
COMPBIAS 750..753
/note="Poly-Pro"
MOD_RES 800
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:10415122"
CARBOHYD 48
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 129
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 166
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 195
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 271
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 347
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 376
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 480
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
VAR_SEQ 487..572
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_044784"
VAR_SEQ 650..659
/note="VFVLLAALRP -> RRHSCPWTGS (in isoform 2)"
/evidence="ECO:0000303|PubMed:10663559"
/id="VSP_011112"
VAR_SEQ 660..862
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:10663559"
/id="VSP_011113"
VARIANT 13
/note="M -> V (in dbSNP:rs17129772)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021278"
VARIANT 149
/note="R -> Q (in dbSNP:rs17129792)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021279"
VARIANT 185
/note="I -> V (in dbSNP:rs2307146)"
/id="VAR_014805"
VARIANT 201
/note="T -> I (in dbSNP:rs7526769)"
/id="VAR_019525"
VARIANT 313
/note="R -> G"
/evidence="ECO:0000269|PubMed:10600539"
/id="VAR_019526"
VARIANT 420
/note="G -> R (in dbSNP:rs2307148)"
/id="VAR_014806"
VARIANT 420
/note="G -> S (in dbSNP:rs2307148)"
/id="VAR_049169"
VARIANT 426
/note="Q -> H (in dbSNP:rs2307145)"
/evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
/id="VAR_014807"
VARIANT 465
/note="G -> D (in dbSNP:rs2307153)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_014808"
VARIANT 625
/note="A -> V (in dbSNP:rs2307154)"
/id="VAR_016097"
VARIANT 720
/note="H -> R (in dbSNP:rs1242019108)"
/evidence="ECO:0000269|PubMed:10600539"
/id="VAR_019527"
VARIANT 808
/note="L -> R (in dbSNP:rs17838066)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021280"
MUTAGEN 678
/note="Y->F: No loss of STAT4 activation. No loss of SOCS3
binding."
/evidence="ECO:0000269|PubMed:10198225,
ECO:0000269|PubMed:14559241, ECO:0000269|PubMed:9890938"
MUTAGEN 767
/note="Y->F: No loss of STAT4 activation. No loss of SOCS3
binding."
/evidence="ECO:0000269|PubMed:10198225,
ECO:0000269|PubMed:14559241, ECO:0000269|PubMed:9890938"
MUTAGEN 800
/note="Y->F: Loss of STAT4 activation. Abolishes SOCS3
binding."
/evidence="ECO:0000269|PubMed:10198225,
ECO:0000269|PubMed:14559241, ECO:0000269|PubMed:9890938"
MUTAGEN 801
/note="L->A: Abolishes in vitro STAT4 binding to a
phosphorylated Y-800 peptide."
/evidence="ECO:0000269|PubMed:10415122"
MUTAGEN 802
/note="P->A: No effect on in vitro STAT4 binding to a
phosphorylated Y-800 peptide."
/evidence="ECO:0000269|PubMed:10415122"
MUTAGEN 803
/note="S->A: No effect on in vitro STAT4 binding to a
phosphorylated Y-800 peptide."
/evidence="ECO:0000269|PubMed:10415122"
MUTAGEN 804
/note="N->A: No effect on in vitro STAT4 binding to a
phosphorylated Y-800 peptide."
/evidence="ECO:0000269|PubMed:10415122"
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


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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1566: Citrate cycle (TCA cycle)
WP566: canonical wnt - zebrafish
WP1161: TGF-beta Receptor Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP809: TGF-beta Receptor Signaling Pathway
WP1367: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1434: Osteopontin Signaling
WP930: TGF Beta Signaling Pathway
WP126: Fatty Acid Beta Oxidation 1
WP169: Fatty Acid Beta Oxidation 3
WP419: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP230: TGF Beta Signaling Pathway
WP148: Fatty Acid Beta Oxidation 2
WP305: Glucocorticoid Metabolism
WP1982: SREBP signalling
WP668: Octadecanoid Pathway
WP1048: TGF Beta Signaling Pathway
WP1177: Fatty Acid Beta Oxidation

Related Genes :
[Il12rb2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)
[Il12rb1 Il12rb] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[OSMR OSMRB] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[CSF2RB IL3RB IL5RB] Cytokine receptor common subunit beta (CDw131) (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)
[Osmr Osmrb] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[Il2rb] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (p70-75) (CD antigen CD122)
[Csf2rb Aic2b Csf2rb1 Il3rb1] Cytokine receptor common subunit beta (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)
[IL4R IL4RA 582J2.1] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[Il2rb] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (p70-75) (CD antigen CD122)
[Il2rg] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL13RA2 IL13R] Interleukin-13 receptor subunit alpha-2 (IL-13 receptor subunit alpha-2) (IL-13R subunit alpha-2) (IL-13R-alpha-2) (IL-13RA2) (Interleukin-13-binding protein) (CD antigen CD213a2)
[Il3ra Sut-1] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (Interleukin-3 receptor class II alpha chain) (CD antigen CD123)
[Csf2rb2 Ai2ca Il3r Il3rb2] Interleukin-3 receptor class 2 subunit beta (IL-3 receptor class 2 subunit beta) (IL-3R class 2 subunit beta) (Colony-stimulating factor 2 receptor subunit beta-2) (Interleukin-3 receptor class II beta chain)
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il1b] Interleukin-1 beta (IL-1 beta)
[IL10RA IL10R] Interleukin-10 receptor subunit alpha (IL-10 receptor subunit alpha) (IL-10R subunit alpha) (IL-10RA) (CDw210a) (Interleukin-10 receptor subunit 1) (IL-10R subunit 1) (IL-10R1) (CD antigen CD210)

Bibliography :
No related Items