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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)

 IL2RB_HUMAN             Reviewed;         551 AA.
P14784; B2R765;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
12-AUG-2020, entry version 220.
RecName: Full=Interleukin-2 receptor subunit beta;
Short=IL-2 receptor subunit beta;
Short=IL-2R subunit beta;
Short=IL-2RB;
AltName: Full=High affinity IL-2 receptor subunit beta;
AltName: Full=Interleukin-15 receptor subunit beta {ECO:0000312|HGNC:HGNC:6009};
AltName: Full=p70-75;
Short=p75;
AltName: CD_antigen=CD122;
Flags: Precursor;
Name=IL2RB {ECO:0000312|HGNC:HGNC:6009};
Synonyms=IL15RB {ECO:0000312|HGNC:HGNC:6009};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2785715; DOI=10.1126/science.2785715;
Hatakeyama M., Tsudo M., Minamoto S., Kono T., Doi T., Miyata T.,
Miyasaka M., Taniguchi T.;
"Interleukin-2 receptor beta chain gene: generation of three receptor forms
by cloned human alpha and beta chain cDNA's.";
Science 244:551-556(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-83 AND GLU-391.
SeattleSNPs variation discovery resource;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Trachea;
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 [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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 HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
PubMed=8648694;
Mulloy J.C., Crownley R.W., Fullen J., Leonard W.J., Franchini G.;
"The human T-cell leukemia/lymphotropic virus type 1 p12I proteins bind the
interleukin-2 receptor beta and gammac chains and affects their expression
on the cell surface.";
J. Virol. 70:3599-3605(1996).
[9]
INTERACTION WITH SHB, AND MUTAGENESIS OF TYR-418 AND TYR-536.
PubMed=12200137; DOI=10.1016/s0006-291x(02)02016-8;
Lindholm C.K.;
"IL-2 receptor signaling through the Shb adapter protein in T and NK
cells.";
Biochem. Biophys. Res. Commun. 296:929-936(2002).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15123770; DOI=10.1189/jlb.0605298;
Ratthe C., Girard D.;
"Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent
mechanism: importance of the IL-15Ralpha chain.";
J. Leukoc. Biol. 76:162-168(2004).
[11]
3D-STRUCTURE MODELING OF 31-230.
PubMed=7529123; DOI=10.1016/s0969-2126(94)00085-9;
Bamborough P., Hedgecock C.J., Richards W.G.;
"The interleukin-2 and interleukin-4 receptors studied by molecular
modelling.";
Structure 2:839-851(1994).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-240 IN COMPLEX WITH IL2; IL2RA
AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-149.
PubMed=16293754; DOI=10.1126/science.1117893;
Wang X., Rickert M., Garcia K.C.;
"Structure of the quaternary complex of interleukin-2 with its alpha, beta,
and gammac receptors.";
Science 310:1159-1163(2005).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-232 IN COMPLEX WITH IL2; IL2RA
AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-43; ASN-71 AND
ASN-149.
PubMed=16477002; DOI=10.1073/pnas.0511161103;
Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.;
"Crystal structure of the IL-2 signaling complex: paradigm for a
heterotrimeric cytokine receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006).
[14]
INVOLVEMENT IN IMD63, VARIANT IMD63 222-PRO--SER-224 DEL, CHARACTERIZATION
OF VARIANT IMD63 222-PRO--SER-224 DEL, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=31040184; DOI=10.1084/jem.20182015;
Fernandez I.Z., Baxter R.M., Garcia-Perez J.E., Vendrame E., Ranganath T.,
Kong D.S., Lundquist K., Nguyen T., Ogolla S., Black J., Galambos C.,
Gumbart J.C., Dawany N., Kelsen J.R., de Zoeten E.F., Quinones R.,
Eissa H., Verneris M.R., Sullivan K.E., Rochford R., Blish C.A., Kedl R.M.,
Dutmer C.M., Hsieh E.W.Y.;
"A novel human IL2RB mutation results in T and NK cell-driven immune
dysregulation.";
J. Exp. Med. 216:1255-1267(2019).
[15]
INVOLVEMENT IN IMD63, VARIANT IMD63 PRO-77, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=31040185; DOI=10.1084/jem.20182304;
Zhang Z., Gothe F., Pennamen P., James J.R., McDonald D., Mata C.P.,
Modis Y., Alazami A.M., Acres M., Haller W., Bowen C., Doeffinger R.,
Sinclair J., Brothers S., Zhang Y., Matthews H.F., Naudion S., Pelluard F.,
Alajlan H., Yamazaki Y., Notarangelo L.D., Thaventhiran J.E.,
Engelhardt K.R., Al-Mousa H., Hambleton S., Rooryck C., Smith K.G.C.,
Lenardo M.J.;
"Human interleukin-2 receptor beta mutations associated with defects in
immunity and peripheral tolerance.";
J. Exp. Med. 216:1311-1327(2019).
-!- FUNCTION: Receptor for interleukin-2. This beta subunit is involved in
receptor mediated endocytosis and transduces the mitogenic signals of
IL2. Probably in association with IL15RA, involved in the stimulation
of neutrophil phagocytosis by IL15 (PubMed:15123770, PubMed:31040185).
{ECO:0000269|PubMed:15123770, ECO:0000269|PubMed:31040184,
ECO:0000269|PubMed:31040185}.
-!- SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R exists
in 3 different forms: a high affinity dimer, an intermediate affinity
monomer (beta subunit), and a low affinity monomer (alpha subunit). The
high and intermediate affinity forms also associate with a gamma
subunit. Interacts with SHB upon interleukin stimulation.
{ECO:0000269|PubMed:12200137, ECO:0000269|PubMed:16293754,
ECO:0000269|PubMed:16477002}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein
p12I. {ECO:0000269|PubMed:8648694}.
-!- INTERACTION:
P14784; P40933: IL15; NbExp=3; IntAct=EBI-2866779, EBI-980274;
P14784; P60568: IL2; NbExp=5; IntAct=EBI-2866779, EBI-12508717;
P14784; Q15645: TRIP13; NbExp=3; IntAct=EBI-2866779, EBI-358993;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15123770,
ECO:0000269|PubMed:31040184, ECO:0000269|PubMed:31040185}; Single-pass
type I membrane protein {ECO:0000255}.
-!- 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.
-!- DISEASE: Immunodeficiency 63 with lymphoproliferation and autoimmunity
(IMD63) [MIM:618495]: An autosomal recessive disorder characterized by
immune dysregulation resulting in lymphoid proliferation, dermatitis,
enteropathy, autoantibodies, hypergammaglobulinemia, and
immunodeficiency with recurrent infections. Patients show increased
susceptibility to viral infections, particularly cytomegalovirus
disease. {ECO:0000269|PubMed:31040184, ECO:0000269|PubMed:31040185}.
Note=The disease is caused by mutations affecting the gene represented
in this entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il2rb/";
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EMBL; M26062; AAA59143.1; -; mRNA.
EMBL; CR456506; CAG30392.1; -; mRNA.
EMBL; AF517934; AAM54040.1; -; Genomic_DNA.
EMBL; AK312860; BAG35712.1; -; mRNA.
EMBL; AL022314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60144.1; -; Genomic_DNA.
EMBL; BC025691; AAH25691.1; -; mRNA.
CCDS; CCDS13942.1; -.
PIR; A30342; A30342.
RefSeq; NP_000869.1; NM_000878.4.
RefSeq; NP_001333151.1; NM_001346222.1.
RefSeq; NP_001333152.1; NM_001346223.1.
PDB; 1ILM; Model; -; B=31-230.
PDB; 1ILN; Model; -; B=31-230.
PDB; 2B5I; X-ray; 2.30 A; B=27-240.
PDB; 2ERJ; X-ray; 3.00 A; B/F=27-232.
PDB; 3QAZ; X-ray; 3.80 A; B/E/H/K/N/Q/T/W/Z/c/f/i=24-240.
PDB; 4GS7; X-ray; 2.35 A; B=27-240.
PDB; 5M5E; X-ray; 2.30 A; B=27-240.
PDB; 6E8K; X-ray; 1.71 A; B=381-393.
PDBsum; 1ILM; -.
PDBsum; 1ILN; -.
PDBsum; 2B5I; -.
PDBsum; 2ERJ; -.
PDBsum; 3QAZ; -.
PDBsum; 4GS7; -.
PDBsum; 5M5E; -.
PDBsum; 6E8K; -.
SMR; P14784; -.
BioGRID; 109775; 24.
CORUM; P14784; -.
DIP; DIP-43N; -.
ELM; P14784; -.
IntAct; P14784; 8.
MINT; P14784; -.
STRING; 9606.ENSP00000216223; -.
ChEMBL; CHEMBL3276; -.
DrugBank; DB00041; Aldesleukin.
DrugBank; DB00074; Basiliximab.
DrugBank; DB00111; Daclizumab.
DrugBank; DB00004; Denileukin diftitox.
DrugCentral; P14784; -.
GuidetoPHARMACOLOGY; 1696; -.
TCDB; 9.B.281.1.1; the interleukin-2 receptor (il2r) family.
GlyGen; P14784; 4 sites.
iPTMnet; P14784; -.
PhosphoSitePlus; P14784; -.
BioMuta; IL2RB; -.
DMDM; 124321; -.
MassIVE; P14784; -.
PaxDb; P14784; -.
PeptideAtlas; P14784; -.
PRIDE; P14784; -.
ProteomicsDB; 53083; -.
ABCD; P14784; 1 sequenced antibody.
Antibodypedia; 11905; 910 antibodies.
DNASU; 3560; -.
Ensembl; ENST00000216223; ENSP00000216223; ENSG00000100385.
GeneID; 3560; -.
KEGG; hsa:3560; -.
UCSC; uc003aqv.2; human.
CTD; 3560; -.
DisGeNET; 3560; -.
EuPathDB; HostDB:ENSG00000100385.13; -.
GeneCards; IL2RB; -.
HGNC; HGNC:6009; IL2RB.
HPA; ENSG00000100385; Tissue enhanced (blood, lymphoid tissue, placenta).
MalaCards; IL2RB; -.
MIM; 146710; gene.
MIM; 618495; phenotype.
neXtProt; NX_P14784; -.
OpenTargets; ENSG00000100385; -.
Orphanet; 85410; Oligoarticular juvenile idiopathic arthritis.
Orphanet; 85408; Rheumatoid factor-negative polyarticular juvenile idiopathic arthritis.
PharmGKB; PA29829; -.
eggNOG; ENOG502S0MR; Eukaryota.
GeneTree; ENSGT00510000049239; -.
HOGENOM; CLU_035782_1_0_1; -.
InParanoid; P14784; -.
KO; K05069; -.
OMA; QFTCFYN; -.
OrthoDB; 1322475at2759; -.
PhylomeDB; P14784; -.
TreeFam; TF337874; -.
PathwayCommons; P14784; -.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-8983432; Interleukin-15 signaling.
Reactome; R-HSA-9020558; Interleukin-2 signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; P14784; -.
SIGNOR; P14784; -.
BioGRID-ORCS; 3560; 3 hits in 870 CRISPR screens.
ChiTaRS; IL2RB; human.
EvolutionaryTrace; P14784; -.
GeneWiki; IL2RB; -.
GenomeRNAi; 3560; -.
Pharos; P14784; Tclin.
PRO; PR:P14784; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; P14784; protein.
Bgee; ENSG00000100385; Expressed in granulocyte and 173 other tissues.
ExpressionAtlas; P14784; baseline and differential.
Genevisible; P14784; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005893; C:interleukin-2 receptor complex; TAS:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
GO; GO:0042010; F:interleukin-15 receptor activity; IDA:UniProtKB.
GO; GO:0019976; F:interleukin-2 binding; IMP:UniProtKB.
GO; GO:0004911; F:interleukin-2 receptor activity; IDA:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR040951; IL2RB_N1.
Pfam; PF18707; IL2RB_N1; 1.
SMART; SM00060; FN3; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Disease mutation; Disulfide bond;
Glycoprotein; Host-virus interaction; Membrane; Polymorphism; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1..26
CHAIN 27..551
/note="Interleukin-2 receptor subunit beta"
/id="PRO_0000010878"
TOPO_DOM 27..240
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 241..265
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 266..551
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 134..234
/note="Fibronectin type-III"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
MOTIF 220..224
/note="WSXWS motif"
MOTIF 278..286
/note="Box 1 motif"
CARBOHYD 29
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 43
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16477002"
CARBOHYD 71
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16477002"
CARBOHYD 149
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16293754,
ECO:0000269|PubMed:16477002"
DISULFID 36..46
DISULFID 59..110
DISULFID 74..86
VARIANT 10
/note="L -> V (in dbSNP:rs57770674)"
/id="VAR_061186"
VARIANT 77
/note="L -> P (in IMD63)"
/evidence="ECO:0000269|PubMed:31040185"
/id="VAR_083103"
VARIANT 83
/note="S -> F (in dbSNP:rs2228143)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_021994"
VARIANT 222..224
/note="Missing (in IMD63; decreased protein abundance;
changed IL-2 and IL-15 signaling pathways; plasma levels of
both IL2 and IL15 were increased; associated with increased
amounts of phosphorylated STAT5A)"
/evidence="ECO:0000269|PubMed:31040184"
/id="VAR_083104"
VARIANT 391
/note="D -> E (in dbSNP:rs228942)"
/evidence="ECO:0000269|Ref.3"
/id="VAR_019998"
MUTAGEN 418
/note="Y->F: Partial loss of interaction with SHB; when
associated with F-536."
/evidence="ECO:0000269|PubMed:12200137"
MUTAGEN 536
/note="Y->F: Partial loss of interaction with SHB; when
associated with F-418."
/evidence="ECO:0000269|PubMed:12200137"
STRAND 33..38
/evidence="ECO:0000244|PDB:2B5I"
STRAND 40..49
/evidence="ECO:0000244|PDB:2B5I"
STRAND 51..53
/evidence="ECO:0000244|PDB:5M5E"
STRAND 59..65
/evidence="ECO:0000244|PDB:2B5I"
STRAND 72..75
/evidence="ECO:0000244|PDB:2B5I"
STRAND 77..80
/evidence="ECO:0000244|PDB:2ERJ"
STRAND 84..89
/evidence="ECO:0000244|PDB:2B5I"
STRAND 104..110
/evidence="ECO:0000244|PDB:2B5I"
STRAND 117..124
/evidence="ECO:0000244|PDB:2B5I"
HELIX 126..128
/evidence="ECO:0000244|PDB:2B5I"
STRAND 136..143
/evidence="ECO:0000244|PDB:2B5I"
STRAND 148..153
/evidence="ECO:0000244|PDB:2B5I"
HELIX 159..161
/evidence="ECO:0000244|PDB:2B5I"
STRAND 165..172
/evidence="ECO:0000244|PDB:2B5I"
TURN 178..180
/evidence="ECO:0000244|PDB:5M5E"
STRAND 184..186
/evidence="ECO:0000244|PDB:2B5I"
STRAND 192..195
/evidence="ECO:0000244|PDB:2B5I"
STRAND 203..213
/evidence="ECO:0000244|PDB:2B5I"
STRAND 227..230
/evidence="ECO:0000244|PDB:2B5I"
SEQUENCE 551 AA; 61117 MW; 1A76FA1936BB7EE6 CRC64;
MAAPALSWRL PLLILLLPLA TSWASAAVNG TSQFTCFYNS RANISCVWSQ DGALQDTSCQ
VHAWPDRRRW NQTCELLPVS QASWACNLIL GAPDSQKLTT VDIVTLRVLC REGVRWRVMA
IQDFKPFENL RLMAPISLQV VHVETHRCNI SWEISQASHY FERHLEFEAR TLSPGHTWEE
APLLTLKQKQ EWICLETLTP DTQYEFQVRV KPLQGEFTTW SPWSQPLAFR TKPAALGKDT
IPWLGHLLVG LSGAFGFIIL VYLLINCRNT GPWLKKVLKC NTPDPSKFFS QLSSEHGGDV
QKWLSSPFPS SSFSPGGLAP EISPLEVLER DKVTQLLLQQ DKVPEPASLS SNHSLTSCFT
NQGYFFFHLP DALEIEACQV YFTYDPYSEE DPDEGVAGAP TGSSPQPLQP LSGEDDAYCT
FPSRDDLLLF SPSLLGGPSP PSTAPGGSGA GEERMPPSLQ ERVPRDWDPQ PLGPPTPGVP
DLVDFQPPPE LVLREAGEEV PDAGPREGVS FPWSRPPGQG EFRALNARLP LNTDAYLSLQ
ELQGQDPTHL V


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Pathways :
WP1655: Geraniol degradation
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP809: TGF-beta Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP2292: Chemokine signaling pathway
WP362: TGF-beta Receptor Signaling Pathway
WP1367: TGF-beta Receptor Signaling Pathway
WP2272: Pathogenic Escherichia coli infection
WP566: canonical wnt - zebrafish
WP1045: TGF-beta Receptor Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP2218: sGC
WP418: Beta Oxidation of Unsaturated Fatty Acids
WP143: Fatty Acid Beta Oxidation
WP560: TGF Beta Signaling Pathway
WP126: Fatty Acid Beta Oxidation 1
WP1680: Oxidative phosphorylation
WP1941: Peroxisomal beta-oxidation of tetracosanoyl-CoA
WP580: Dauer formation
WP943: Fatty Acid Beta Oxidation
WP1694: Pyrimidine metabolism
WP443: Beta Oxidation Meta MAPP
WP471: Beta Oxidation of Unsaturated Fatty Acids

Related Genes :
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[CSF2RB IL3RB IL5RB] Cytokine receptor common subunit beta (CDw131) (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)
[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)
[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)
[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)]
[Csf2rb Aic2b Csf2rb1 Il3rb1] Cytokine receptor common subunit beta (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)
[IL15RA] Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)]
[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)
[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)
[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)
[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)
[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)]
[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)
[IL6R] Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (Membrane glycoprotein 80) (gp80) (CD antigen CD126) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)]
[IL13RA1 IL13R IL13RA] Interleukin-13 receptor subunit alpha-1 (IL-13 receptor subunit alpha-1) (IL-13R subunit alpha-1) (IL-13R-alpha-1) (IL-13RA1) (Cancer/testis antigen 19) (CT19) (CD antigen CD213a1)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)

Bibliography :