ID IL2RB_HUMAN Reviewed; 551 AA.
AC P14784; B2R765;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 24-JAN-2024, entry version 237.
DE RecName: Full=Interleukin-2 receptor subunit beta;
DE Short=IL-2 receptor subunit beta;
DE Short=IL-2R subunit beta;
DE Short=IL-2RB;
DE AltName: Full=High affinity IL-2 receptor subunit beta;
DE AltName: Full=Interleukin-15 receptor subunit beta {ECO:0000312|HGNC:HGNC:6009};
DE AltName: Full=p70-75;
DE Short=p75;
DE AltName: CD_antigen=CD122;
DE Flags: Precursor;
GN Name=IL2RB {ECO:0000312|HGNC:HGNC:6009};
GN Synonyms=IL15RB {ECO:0000312|HGNC:HGNC:6009};
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].
RX PubMed=2785715; DOI=10.1126/science.2785715;
RA Hatakeyama M., Tsudo M., Minamoto S., Kono T., Doi T., Miyata T.,
RA Miyasaka M., Taniguchi T.;
RT "Interleukin-2 receptor beta chain gene: generation of three receptor forms
RT by cloned human alpha and beta chain cDNA's.";
RL Science 244:551-556(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-83 AND GLU-391.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
RX PubMed=8648694; DOI=10.1128/jvi.70.6.3599-3605.1996;
RA Mulloy J.C., Crownley R.W., Fullen J., Leonard W.J., Franchini G.;
RT "The human T-cell leukemia/lymphotropic virus type 1 p12I proteins bind the
RT interleukin-2 receptor beta and gammac chains and affects their expression
RT on the cell surface.";
RL J. Virol. 70:3599-3605(1996).
RN [9]
RP INTERACTION WITH SHB, AND MUTAGENESIS OF TYR-418 AND TYR-536.
RX PubMed=12200137; DOI=10.1016/s0006-291x(02)02016-8;
RA Lindholm C.K.;
RT "IL-2 receptor signaling through the Shb adapter protein in T and NK
RT cells.";
RL Biochem. Biophys. Res. Commun. 296:929-936(2002).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15123770; DOI=10.1189/jlb.0605298;
RA Ratthe C., Girard D.;
RT "Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent
RT mechanism: importance of the IL-15Ralpha chain.";
RL J. Leukoc. Biol. 76:162-168(2004).
RN [11]
RP 3D-STRUCTURE MODELING OF 31-230.
RX PubMed=7529123; DOI=10.1016/s0969-2126(94)00085-9;
RA Bamborough P., Hedgecock C.J., Richards W.G.;
RT "The interleukin-2 and interleukin-4 receptors studied by molecular
RT modelling.";
RL Structure 2:839-851(1994).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-240 IN COMPLEX WITH IL2; IL2RA
RP AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-149.
RX PubMed=16293754; DOI=10.1126/science.1117893;
RA Wang X., Rickert M., Garcia K.C.;
RT "Structure of the quaternary complex of interleukin-2 with its alpha, beta,
RT and gammac receptors.";
RL Science 310:1159-1163(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-232 IN COMPLEX WITH IL2; IL2RA
RP AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-43; ASN-71 AND
RP ASN-149.
RX PubMed=16477002; DOI=10.1073/pnas.0511161103;
RA Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.;
RT "Crystal structure of the IL-2 signaling complex: paradigm for a
RT heterotrimeric cytokine receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006).
RN [14]
RP INVOLVEMENT IN IMD63, VARIANT IMD63 222-PRO--SER-224 DEL, CHARACTERIZATION
RP OF VARIANT IMD63 222-PRO--SER-224 DEL, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31040184; DOI=10.1084/jem.20182015;
RA Fernandez I.Z., Baxter R.M., Garcia-Perez J.E., Vendrame E., Ranganath T.,
RA Kong D.S., Lundquist K., Nguyen T., Ogolla S., Black J., Galambos C.,
RA Gumbart J.C., Dawany N., Kelsen J.R., de Zoeten E.F., Quinones R.,
RA Eissa H., Verneris M.R., Sullivan K.E., Rochford R., Blish C.A., Kedl R.M.,
RA Dutmer C.M., Hsieh E.W.Y.;
RT "A novel human IL2RB mutation results in T and NK cell-driven immune
RT dysregulation.";
RL J. Exp. Med. 216:1255-1267(2019).
RN [15]
RP INVOLVEMENT IN IMD63, VARIANT IMD63 PRO-77, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=31040185; DOI=10.1084/jem.20182304;
RA Zhang Z., Gothe F., Pennamen P., James J.R., McDonald D., Mata C.P.,
RA Modis Y., Alazami A.M., Acres M., Haller W., Bowen C., Doeffinger R.,
RA Sinclair J., Brothers S., Zhang Y., Matthews H.F., Naudion S., Pelluard F.,
RA Alajlan H., Yamazaki Y., Notarangelo L.D., Thaventhiran J.E.,
RA Engelhardt K.R., Al-Mousa H., Hambleton S., Rooryck C., Smith K.G.C.,
RA Lenardo M.J.;
RT "Human interleukin-2 receptor beta mutations associated with defects in
RT immunity and peripheral tolerance.";
RL J. Exp. Med. 216:1311-1327(2019).
CC -!- FUNCTION: Receptor for interleukin-2. This beta subunit is involved in
CC receptor mediated endocytosis and transduces the mitogenic signals of
CC IL2. Probably in association with IL15RA, involved in the stimulation
CC of neutrophil phagocytosis by IL15 (PubMed:15123770, PubMed:31040185).
CC {ECO:0000269|PubMed:15123770, ECO:0000269|PubMed:31040184,
CC ECO:0000269|PubMed:31040185}.
CC -!- SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R exists
CC in 3 different forms: a high affinity dimer, an intermediate affinity
CC monomer (beta subunit), and a low affinity monomer (alpha subunit). The
CC high and intermediate affinity forms also associate with a gamma
CC subunit. Interacts with SHB upon interleukin stimulation.
CC {ECO:0000269|PubMed:12200137, ECO:0000269|PubMed:16293754,
CC ECO:0000269|PubMed:16477002}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein
CC p12I. {ECO:0000269|PubMed:8648694}.
CC -!- INTERACTION:
CC P14784; P40933: IL15; NbExp=3; IntAct=EBI-2866779, EBI-980274;
CC P14784; P60568: IL2; NbExp=5; IntAct=EBI-2866779, EBI-12508717;
CC P14784; Q15645: TRIP13; NbExp=3; IntAct=EBI-2866779, EBI-358993;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15123770,
CC ECO:0000269|PubMed:31040184, ECO:0000269|PubMed:31040185}; Single-pass
CC type I membrane protein {ECO:0000255}.
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 -!- DISEASE: Immunodeficiency 63 with lymphoproliferation and autoimmunity
CC (IMD63) [MIM:618495]: An autosomal recessive disorder characterized by
CC immune dysregulation resulting in lymphoid proliferation, dermatitis,
CC enteropathy, autoantibodies, hypergammaglobulinemia, and
CC immunodeficiency with recurrent infections. Patients show increased
CC susceptibility to viral infections, particularly cytomegalovirus
CC disease. {ECO:0000269|PubMed:31040184, ECO:0000269|PubMed:31040185}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il2rb/";
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DR EMBL; M26062; AAA59143.1; -; mRNA.
DR EMBL; CR456506; CAG30392.1; -; mRNA.
DR EMBL; AF517934; AAM54040.1; -; Genomic_DNA.
DR EMBL; AK312860; BAG35712.1; -; mRNA.
DR EMBL; AL022314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60144.1; -; Genomic_DNA.
DR EMBL; BC025691; AAH25691.1; -; mRNA.
DR CCDS; CCDS13942.1; -.
DR PIR; A30342; A30342.
DR RefSeq; NP_000869.1; NM_000878.4.
DR RefSeq; NP_001333151.1; NM_001346222.1.
DR RefSeq; NP_001333152.1; NM_001346223.1.
DR PDB; 2B5I; X-ray; 2.30 A; B=27-240.
DR PDB; 2ERJ; X-ray; 3.00 A; B/F=27-232.
DR PDB; 3QAZ; X-ray; 3.80 A; B/E/H/K/N/Q/T/W/Z/c/f/i=24-240.
DR PDB; 4GS7; X-ray; 2.35 A; B=27-240.
DR PDB; 5M5E; X-ray; 2.30 A; B=27-240.
DR PDB; 6E8K; X-ray; 1.71 A; B=381-393.
DR PDB; 7S2S; X-ray; 1.93 A; B/D=27-236.
DR PDBsum; 2B5I; -.
DR PDBsum; 2ERJ; -.
DR PDBsum; 3QAZ; -.
DR PDBsum; 4GS7; -.
DR PDBsum; 5M5E; -.
DR PDBsum; 6E8K; -.
DR PDBsum; 7S2S; -.
DR AlphaFoldDB; P14784; -.
DR SMR; P14784; -.
DR BioGRID; 109775; 25.
DR CORUM; P14784; -.
DR DIP; DIP-43N; -.
DR ELM; P14784; -.
DR IntAct; P14784; 8.
DR MINT; P14784; -.
DR STRING; 9606.ENSP00000216223; -.
DR ChEMBL; CHEMBL3276; -.
DR DrugBank; DB00041; Aldesleukin.
DR DrugBank; DB00074; Basiliximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00004; Denileukin diftitox.
DR DrugCentral; P14784; -.
DR GuidetoPHARMACOLOGY; 1696; -.
DR TCDB; 8.A.152.1.1; the interleukin receptor (ilr) family.
DR GlyCosmos; P14784; 4 sites, No reported glycans.
DR GlyGen; P14784; 4 sites.
DR iPTMnet; P14784; -.
DR PhosphoSitePlus; P14784; -.
DR BioMuta; IL2RB; -.
DR DMDM; 124321; -.
DR jPOST; P14784; -.
DR MassIVE; P14784; -.
DR PaxDb; 9606-ENSP00000216223; -.
DR PeptideAtlas; P14784; -.
DR ProteomicsDB; 53083; -.
DR ABCD; P14784; 1 sequenced antibody.
DR Antibodypedia; 11905; 1137 antibodies from 43 providers.
DR DNASU; 3560; -.
DR Ensembl; ENST00000216223.10; ENSP00000216223.5; ENSG00000100385.15.
DR Ensembl; ENST00000429622.6; ENSP00000402685.2; ENSG00000100385.15.
DR Ensembl; ENST00000445595.2; ENSP00000401020.2; ENSG00000100385.15.
DR Ensembl; ENST00000453962.6; ENSP00000403731.2; ENSG00000100385.15.
DR Ensembl; ENST00000698883.1; ENSP00000514005.1; ENSG00000100385.15.
DR Ensembl; ENST00000698890.1; ENSP00000514009.1; ENSG00000100385.15.
DR Ensembl; ENST00000698892.1; ENSP00000514011.1; ENSG00000100385.15.
DR Ensembl; ENST00000698893.1; ENSP00000514012.1; ENSG00000100385.15.
DR GeneID; 3560; -.
DR KEGG; hsa:3560; -.
DR MANE-Select; ENST00000216223.10; ENSP00000216223.5; NM_000878.5; NP_000869.1.
DR UCSC; uc003aqv.2; human.
DR AGR; HGNC:6009; -.
DR CTD; 3560; -.
DR DisGeNET; 3560; -.
DR GeneCards; IL2RB; -.
DR HGNC; HGNC:6009; IL2RB.
DR HPA; ENSG00000100385; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; IL2RB; -.
DR MIM; 146710; gene.
DR MIM; 618495; phenotype.
DR neXtProt; NX_P14784; -.
DR OpenTargets; ENSG00000100385; -.
DR Orphanet; 85410; Oligoarticular juvenile idiopathic arthritis.
DR Orphanet; 85408; Rheumatoid factor-negative polyarticular juvenile idiopathic arthritis.
DR PharmGKB; PA29829; -.
DR VEuPathDB; HostDB:ENSG00000100385; -.
DR eggNOG; ENOG502S0MR; Eukaryota.
DR GeneTree; ENSGT00510000049239; -.
DR HOGENOM; CLU_035782_1_0_1; -.
DR InParanoid; P14784; -.
DR OMA; QTSCFTN; -.
DR OrthoDB; 4609144at2759; -.
DR PhylomeDB; P14784; -.
DR TreeFam; TF337874; -.
DR PathwayCommons; P14784; -.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR Reactome; R-HSA-9020558; Interleukin-2 signaling.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR SignaLink; P14784; -.
DR SIGNOR; P14784; -.
DR BioGRID-ORCS; 3560; 11 hits in 1153 CRISPR screens.
DR ChiTaRS; IL2RB; human.
DR EvolutionaryTrace; P14784; -.
DR GeneWiki; IL2RB; -.
DR GenomeRNAi; 3560; -.
DR Pharos; P14784; Tclin.
DR PRO; PR:P14784; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P14784; Protein.
DR Bgee; ENSG00000100385; Expressed in granulocyte and 154 other cell types or tissues.
DR ExpressionAtlas; P14784; baseline and differential.
DR Genevisible; P14784; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005893; C:interleukin-2 receptor complex; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; IDA:UniProt.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0042010; F:interleukin-15 receptor activity; IDA:UniProtKB.
DR GO; GO:0019976; F:interleukin-2 binding; IMP:UniProtKB.
DR GO; GO:0004911; F:interleukin-2 receptor activity; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IDA:UniProt.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040951; IL2RB_N1.
DR PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR23037:SF30; INTERLEUKIN-2 RECEPTOR SUBUNIT BETA; 1.
DR Pfam; PF18707; IL2RB_N1; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disease variant; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT CHAIN 27..551
FT /note="Interleukin-2 receptor subunit beta"
FT /id="PRO_0000010878"
FT TOPO_DOM 27..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 134..234
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 389..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 220..224
FT /note="WSXWS motif"
FT MOTIF 278..286
FT /note="Box 1 motif"
FT COMPBIAS 468..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16477002"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16477002"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16293754,
FT ECO:0000269|PubMed:16477002"
FT DISULFID 36..46
FT DISULFID 59..110
FT DISULFID 74..86
FT VARIANT 10
FT /note="L -> V (in dbSNP:rs57770674)"
FT /id="VAR_061186"
FT VARIANT 77
FT /note="L -> P (in IMD63; dbSNP:rs934523851)"
FT /evidence="ECO:0000269|PubMed:31040185"
FT /id="VAR_083103"
FT VARIANT 83
FT /note="S -> F (in dbSNP:rs2228143)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_021994"
FT VARIANT 222..224
FT /note="Missing (in IMD63; decreased protein abundance;
FT changed IL-2 and IL-15 signaling pathways; plasma levels of
FT both IL2 and IL15 were increased; associated with increased
FT amounts of phosphorylated STAT5A)"
FT /evidence="ECO:0000269|PubMed:31040184"
FT /id="VAR_083104"
FT VARIANT 391
FT /note="D -> E (in dbSNP:rs228942)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019998"
FT MUTAGEN 418
FT /note="Y->F: Partial loss of interaction with SHB; when
FT associated with F-536."
FT /evidence="ECO:0000269|PubMed:12200137"
FT MUTAGEN 536
FT /note="Y->F: Partial loss of interaction with SHB; when
FT associated with F-418."
FT /evidence="ECO:0000269|PubMed:12200137"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5M5E"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 77..89
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:7S2S"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:7S2S"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:7S2S"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:5M5E"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:7S2S"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:7S2S"
SQ 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
//
