Full text data of IL2RB
IL2RB
[Confidence: high (a blood group or CD marker)]
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; p75; CD122; Flags: Precursor)
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; p75; CD122; Flags: Precursor)
UniProt
P14784
ID IL2RB_HUMAN Reviewed; 551 AA.
AC P14784; B2R765;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1990, sequence version 1.
DT 22-JAN-2014, entry version 165.
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=p70-75;
DE Short=p75;
DE AltName: CD_antigen=CD122;
DE Flags: Precursor;
GN Name=IL2RB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT forms 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
RX PubMed=8648694;
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
RT bind the interleukin-2 receptor beta and gammac chains and affects
RT their expression 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 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-240 IN COMPLEX WITH IL2;
RP IL2RA 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,
RT beta, and gammac receptors.";
RL Science 310:1159-1163(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-232 IN COMPLEX WITH IL2;
RP IL2RA AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-43; ASN-71
RP AND 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).
CC -!- FUNCTION: Receptor for interleukin-2. This beta subunit is
CC involved in receptor mediated endocytosis and transduces the
CC mitogenic signals of IL2.
CC -!- SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R
CC exists in 3 different forms: a high affinity dimer, an
CC intermediate affinity monomer (beta subunit), and a low affinity
CC monomer (alpha subunit). The high and intermediate affinity forms
CC also associate with a gamma subunit. Interacts with SHB upon
CC interleukin stimulation. Interacts with HTLV-1 accessory protein
CC p12I.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-
CC surface receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily.
CC -!- SIMILARITY: Contains 1 fibronectin type-III domain.
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; CAA18444.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60144.1; -; Genomic_DNA.
DR EMBL; BC025691; AAH25691.1; -; mRNA.
DR PIR; A30342; A30342.
DR RefSeq; NP_000869.1; NM_000878.3.
DR RefSeq; XP_005261656.1; XM_005261599.1.
DR UniGene; Hs.474787; -.
DR PDB; 1ILM; Model; -; B=31-230.
DR PDB; 1ILN; Model; -; B=31-230.
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=27-240.
DR PDB; 4GS7; X-ray; 2.35 A; B=27-240.
DR PDBsum; 1ILM; -.
DR PDBsum; 1ILN; -.
DR PDBsum; 2B5I; -.
DR PDBsum; 2ERJ; -.
DR PDBsum; 3QAZ; -.
DR PDBsum; 4GS7; -.
DR ProteinModelPortal; P14784; -.
DR SMR; P14784; 32-232.
DR DIP; DIP-43N; -.
DR IntAct; P14784; 4.
DR MINT; MINT-273361; -.
DR STRING; 9606.ENSP00000216223; -.
DR BindingDB; P14784; -.
DR ChEMBL; CHEMBL3276; -.
DR DrugBank; DB00041; Aldesleukin.
DR DrugBank; DB00074; Basiliximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00004; Denileukin diftitox.
DR PhosphoSite; P14784; -.
DR DMDM; 124321; -.
DR PaxDb; P14784; -.
DR PRIDE; P14784; -.
DR DNASU; 3560; -.
DR Ensembl; ENST00000216223; ENSP00000216223; ENSG00000100385.
DR GeneID; 3560; -.
DR KEGG; hsa:3560; -.
DR UCSC; uc003aqv.1; human.
DR CTD; 3560; -.
DR GeneCards; GC22M037515; -.
DR HGNC; HGNC:6009; IL2RB.
DR MIM; 146710; gene.
DR neXtProt; NX_P14784; -.
DR Orphanet; 85408; Juvenile rheumatoid factor-negative polyarthritis.
DR Orphanet; 85410; Oligoarticular juvenile arthritis.
DR PharmGKB; PA29829; -.
DR eggNOG; NOG46659; -.
DR HOGENOM; HOG000038003; -.
DR HOVERGEN; HBG052110; -.
DR KO; K05069; -.
DR OMA; ACQVYFT; -.
DR OrthoDB; EOG72RMZ6; -.
DR PhylomeDB; P14784; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P14784; -.
DR EvolutionaryTrace; P14784; -.
DR GeneWiki; IL2RB; -.
DR GenomeRNAi; 3560; -.
DR NextBio; 13904; -.
DR PRO; PR:P14784; -.
DR ArrayExpress; P14784; -.
DR Bgee; P14784; -.
DR CleanEx; HS_IL2RB; -.
DR Genevestigator; P14784; -.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0019976; F:interleukin-2 binding; ISS:UniProtKB.
DR GO; GO:0004911; F:interleukin-2 receptor activity; IDA:MGI.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Membrane; Polymorphism; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 26
FT CHAIN 27 551 Interleukin-2 receptor subunit beta.
FT /FTId=PRO_0000010878.
FT TOPO_DOM 27 240 Extracellular (Potential).
FT TRANSMEM 241 265 Helical; (Potential).
FT TOPO_DOM 266 551 Cytoplasmic (Potential).
FT DOMAIN 134 234 Fibronectin type-III.
FT MOTIF 220 224 WSXWS motif.
FT MOTIF 278 286 Box 1 motif.
FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 43 43 N-linked (GlcNAc...).
FT CARBOHYD 71 71 N-linked (GlcNAc...).
FT CARBOHYD 149 149 N-linked (GlcNAc...).
FT DISULFID 36 46
FT DISULFID 59 110
FT DISULFID 74 86
FT VARIANT 10 10 L -> V (in dbSNP:rs57770674).
FT /FTId=VAR_061186.
FT VARIANT 83 83 S -> F (in dbSNP:rs2228143).
FT /FTId=VAR_021994.
FT VARIANT 391 391 D -> E (in dbSNP:rs228942).
FT /FTId=VAR_019998.
FT MUTAGEN 418 418 Y->F: Partial loss of interaction with
FT SHB; when associated with F-536.
FT MUTAGEN 536 536 Y->F: Partial loss of interaction with
FT SHB; when associated with F-418.
FT STRAND 33 38
FT STRAND 40 49
FT STRAND 59 65
FT STRAND 72 75
FT STRAND 77 80
FT STRAND 84 89
FT STRAND 104 110
FT STRAND 117 124
FT HELIX 126 128
FT STRAND 136 143
FT STRAND 148 153
FT HELIX 159 161
FT STRAND 165 172
FT HELIX 178 180
FT STRAND 184 186
FT STRAND 192 195
FT STRAND 203 213
FT STRAND 227 230
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
//
ID IL2RB_HUMAN Reviewed; 551 AA.
AC P14784; B2R765;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1990, sequence version 1.
DT 22-JAN-2014, entry version 165.
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=p70-75;
DE Short=p75;
DE AltName: CD_antigen=CD122;
DE Flags: Precursor;
GN Name=IL2RB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT forms 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
RX PubMed=8648694;
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
RT bind the interleukin-2 receptor beta and gammac chains and affects
RT their expression 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 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-240 IN COMPLEX WITH IL2;
RP IL2RA 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,
RT beta, and gammac receptors.";
RL Science 310:1159-1163(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-232 IN COMPLEX WITH IL2;
RP IL2RA AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-43; ASN-71
RP AND 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).
CC -!- FUNCTION: Receptor for interleukin-2. This beta subunit is
CC involved in receptor mediated endocytosis and transduces the
CC mitogenic signals of IL2.
CC -!- SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R
CC exists in 3 different forms: a high affinity dimer, an
CC intermediate affinity monomer (beta subunit), and a low affinity
CC monomer (alpha subunit). The high and intermediate affinity forms
CC also associate with a gamma subunit. Interacts with SHB upon
CC interleukin stimulation. Interacts with HTLV-1 accessory protein
CC p12I.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-
CC surface receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily.
CC -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il2rb/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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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; CAA18444.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60144.1; -; Genomic_DNA.
DR EMBL; BC025691; AAH25691.1; -; mRNA.
DR PIR; A30342; A30342.
DR RefSeq; NP_000869.1; NM_000878.3.
DR RefSeq; XP_005261656.1; XM_005261599.1.
DR UniGene; Hs.474787; -.
DR PDB; 1ILM; Model; -; B=31-230.
DR PDB; 1ILN; Model; -; B=31-230.
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=27-240.
DR PDB; 4GS7; X-ray; 2.35 A; B=27-240.
DR PDBsum; 1ILM; -.
DR PDBsum; 1ILN; -.
DR PDBsum; 2B5I; -.
DR PDBsum; 2ERJ; -.
DR PDBsum; 3QAZ; -.
DR PDBsum; 4GS7; -.
DR ProteinModelPortal; P14784; -.
DR SMR; P14784; 32-232.
DR DIP; DIP-43N; -.
DR IntAct; P14784; 4.
DR MINT; MINT-273361; -.
DR STRING; 9606.ENSP00000216223; -.
DR BindingDB; P14784; -.
DR ChEMBL; CHEMBL3276; -.
DR DrugBank; DB00041; Aldesleukin.
DR DrugBank; DB00074; Basiliximab.
DR DrugBank; DB00111; Daclizumab.
DR DrugBank; DB00004; Denileukin diftitox.
DR PhosphoSite; P14784; -.
DR DMDM; 124321; -.
DR PaxDb; P14784; -.
DR PRIDE; P14784; -.
DR DNASU; 3560; -.
DR Ensembl; ENST00000216223; ENSP00000216223; ENSG00000100385.
DR GeneID; 3560; -.
DR KEGG; hsa:3560; -.
DR UCSC; uc003aqv.1; human.
DR CTD; 3560; -.
DR GeneCards; GC22M037515; -.
DR HGNC; HGNC:6009; IL2RB.
DR MIM; 146710; gene.
DR neXtProt; NX_P14784; -.
DR Orphanet; 85408; Juvenile rheumatoid factor-negative polyarthritis.
DR Orphanet; 85410; Oligoarticular juvenile arthritis.
DR PharmGKB; PA29829; -.
DR eggNOG; NOG46659; -.
DR HOGENOM; HOG000038003; -.
DR HOVERGEN; HBG052110; -.
DR KO; K05069; -.
DR OMA; ACQVYFT; -.
DR OrthoDB; EOG72RMZ6; -.
DR PhylomeDB; P14784; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P14784; -.
DR EvolutionaryTrace; P14784; -.
DR GeneWiki; IL2RB; -.
DR GenomeRNAi; 3560; -.
DR NextBio; 13904; -.
DR PRO; PR:P14784; -.
DR ArrayExpress; P14784; -.
DR Bgee; P14784; -.
DR CleanEx; HS_IL2RB; -.
DR Genevestigator; P14784; -.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0019976; F:interleukin-2 binding; ISS:UniProtKB.
DR GO; GO:0004911; F:interleukin-2 receptor activity; IDA:MGI.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Membrane; Polymorphism; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 26
FT CHAIN 27 551 Interleukin-2 receptor subunit beta.
FT /FTId=PRO_0000010878.
FT TOPO_DOM 27 240 Extracellular (Potential).
FT TRANSMEM 241 265 Helical; (Potential).
FT TOPO_DOM 266 551 Cytoplasmic (Potential).
FT DOMAIN 134 234 Fibronectin type-III.
FT MOTIF 220 224 WSXWS motif.
FT MOTIF 278 286 Box 1 motif.
FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 43 43 N-linked (GlcNAc...).
FT CARBOHYD 71 71 N-linked (GlcNAc...).
FT CARBOHYD 149 149 N-linked (GlcNAc...).
FT DISULFID 36 46
FT DISULFID 59 110
FT DISULFID 74 86
FT VARIANT 10 10 L -> V (in dbSNP:rs57770674).
FT /FTId=VAR_061186.
FT VARIANT 83 83 S -> F (in dbSNP:rs2228143).
FT /FTId=VAR_021994.
FT VARIANT 391 391 D -> E (in dbSNP:rs228942).
FT /FTId=VAR_019998.
FT MUTAGEN 418 418 Y->F: Partial loss of interaction with
FT SHB; when associated with F-536.
FT MUTAGEN 536 536 Y->F: Partial loss of interaction with
FT SHB; when associated with F-418.
FT STRAND 33 38
FT STRAND 40 49
FT STRAND 59 65
FT STRAND 72 75
FT STRAND 77 80
FT STRAND 84 89
FT STRAND 104 110
FT STRAND 117 124
FT HELIX 126 128
FT STRAND 136 143
FT STRAND 148 153
FT HELIX 159 161
FT STRAND 165 172
FT HELIX 178 180
FT STRAND 184 186
FT STRAND 192 195
FT STRAND 203 213
FT STRAND 227 230
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
//
MIM
146710
*RECORD*
*FIELD* NO
146710
*FIELD* TI
*146710 INTERLEUKIN 2 RECEPTOR, BETA; IL2RB
;;CD122 ANTIGEN; CD122
*FIELD* TX
CLONING
read more
Tsudo et al. (1989) characterized the interleukin-2 receptor beta chain
using 3 monoclonal antibodies, designated Mik-beta1, -beta2, and -beta3.
They showed by immunoprecipitation that the beta chain has a molecular
mass of 68,000-72,000 Da. Moreover, they found that the beta chain was
expressed on the surface of peripheral blood Leu-19+ natural killer
cells in the absence of alpha-chain expression. Also see IL2RA (147730).
Gnarra et al. (1990) characterized the IL2RB gene. They found that the
IL2 receptor is present in 3 forms with respect to binding ability to
IL2 (147680): high, intermediate, and low affinity forms. The alpha
chain constitutes the low affinity form and is not functional in IL2
internalization and signal transduction. The beta chain by itself
constitutes the intermediate affinity form. Hatakeyama et al. (1989)
presented evidence that coexpression of the IL2RA and IL2RB genes
results in the high affinity form of the receptor.
GENE FUNCTION
Giri et al. (1994) showed that IL2RB and IL2RG (308380), but not IL2RA,
transduce signals by IL15 (600554) in addition to IL2.
Kondo et al. (2000) showed that a clonogenic common lymphoid progenitor,
a bone marrow-resident cell that gives rise exclusively to lymphocytes
(T, B, and natural killer cells), can be redirected to the myeloid
lineage by stimulation through exogenously expressed interleukin-2
receptor and GMCSF receptor (138981, 306250). Analysis of mutants of the
beta chain of the IL2 receptor revealed that the granulocyte and
monocyte differentiation signals are triggered by different cytoplasmic
domains, showing that the signaling pathways responsible for these
unique developmental outcomes are separable. Finally, Kondo et al.
(2000) showed that the endogenous myelomonocytic cytokine receptors for
GM-CSF and macrophage colony-stimulating factor (CSF1R; 164770) are
expressed at low to moderate levels on the more primitive hematopoietic
stem cells, are absent on common lymphoid progenitors, and are
upregulated after myeloid lineage induction by IL2. Kondo et al. (2000)
concluded that cytokine signaling can regulate cell fate decisions and
proposed that a critical step in lymphoid commitment is downregulation
of cytokine receptors that drive myeloid cell development.
Lamaze et al. (2001) selectively blocked clathrin (see 118960)-dependent
endocytosis using dominant-negative mutants of EPS15 (600051) and showed
that clathrin-mediated endocytosis of transferrin (190000) was
inhibited, while endocytosis of the IL2Rs proceeded normally.
Ultrastructural and biochemical experiments showed that
clathrin-independent endocytosis of IL2Rs exists constitutively in
lymphocytes and is coupled to their association with detergent-resistant
membrane domains. The authors found that clathrin-independent
endocytosis requires dynamin (see 602377) and is specifically regulated
by Rho family GTPases (see 604980). These results defined novel
properties of receptor-mediated endocytosis and established that IL2R is
efficiently internalized through this clathrin-independent pathway.
Using flow cytometry, Corrigall et al. (2001) detected expression of a
functional IL2R of intermediate affinity composed solely of IL2RB and
IL2RG on fibroblast-like synoviocytes (FLS) obtained from rheumatoid
arthritis and osteoarthritis patients. Addition of recombinant IL2, IL1B
(147720), or TNFA (191160) independently did not upregulate expression
of the receptors on FLS, but IL2 or IL1B did significantly increase
expression of intracellular tyrosine-phosphorylated proteins and the
production of MCP1 (158105). Corrigall et al. (2001) proposed that MCP1
in the synovial membrane serves to recruit macrophages and perpetuate
inflammation in the joints of patients with rheumatoid arthritis.
Dai et al. (2010) noted that CD8 (see 186910)-positive/CD122-positive T
cells have been shown to function, paradoxically, as both regulatory and
memory T cells. Using flow cytometric analysis, they demonstrated that
mouse Cd8-positive/Cd122-positive T cells included both Pd1 (PDCD1;
600244)-positive and Pd1-negative subpopulations. Only the Pd1-positive
subpopulation suppressed T-cell responses in vitro and in vivo, and this
suppression occurred largely in an Il10 (124092)-dependent manner. Il10
production, in turn, was dependent on costimulatory signaling of both
Cd28 (186760) and Pd1. Cd8-positive/Cd122-positive/Pd1-negative T cells
mediated skin graft rejection. Dai et al. (2010) concluded that
CD8-positive/CD122-positive T cells can be either regulatory or memory T
cells, depending on their PD1 expression and antigen specificity.
BIOCHEMICAL FEATURES
- Crystal Structure
Wang et al. (2005) reported the crystal structure of the quaternary
complex of IL2 with IL2RA, IL2RB, and IL2RG at a resolution of 2.3
angstroms.
GENE STRUCTURE
Shibuya et al. (1990) found that the IL2RB gene contains 10 exons
spanning about 24.3 kb and that the gene product is encoded by exons
2-10. The cysteine-rich extracellular region, which displays a
significant evolutionary resemblance to other cytokine receptors, as
well as to growth hormone and prolactin receptors, is encoded primarily
by exons 3 and 4.
MAPPING
By Southern analysis of somatic cell hybrid DNA and in situ
hybridization, Gnarra et al. (1990) localized the IL2RB gene to
chromosome 22q11.2-q12, a region that is associated with several
lymphoid neoplasias. By RFLP linkage analysis, Shibuya et al. (1990)
assigned the IL2RB gene to 22q12-q13. By in situ hybridization, Campbell
et al. (1992) mapped the Il2rb gene to band E of mouse chromosome 15.
ANIMAL MODEL
Suzuki et al. (1995) generated mice defective in Il2rb expression by
insertion of a neomycin resistance cassette into the IL2RB gene at exon
6, which encodes a region of the extracellular domain proximal to the
transmembrane region. Mice from 2 independent embryonic stem cell lines
were separately bred homozygous for the defect, with both lineages
showing identical gross appearances. The mice showed normal growth until
approximately 3 weeks after birth. After 4 weeks of age, they were
generally smaller than normal or heterozygous littermates and had
abnormal appearances characterized by fuzzy hair, slow movement, and
fully developed external genitals. Death occurred at approximately 12
weeks. In mice lacking the IL2R beta chain, T cells were shown to be
spontaneously activated, resulting in exhaustive differentiation of B
cells into plasma cells and the appearance of high serum concentrations
of immunoglobulins G1 and E, as well as autoantibodies that cause
hemolytic anemia. Marked infiltrated granulocytopoiesis was also
apparent. Depletion of CD4+ T cells in mutant mice rescued B cells
without reversion of granulocyte abnormalities. T cells did not
proliferate in response to polyclonal activators, nor could
antigen-specific immune responses be elicited. Thus, Suzuki et al.
(1995) concluded that Il2rb is required to keep the activation programs
of T cells under control, to maintain homeostasis, and to prevent
autoimmunity.
*FIELD* RF
1. Campbell, H. D.; Webb, G. C.; Kono, T.; Taniguchi, T.; Ford, J.
H.; Young, I. G.: Assignment of the interleukin-2 receptor beta chain
gene (Il-2rb) to band E on mouse chromosome 15. Genomics 12: 179-180,
1992.
2. Corrigall, V. M.; Arastu, M.; Khan, S.; Shah, C.; Fife, M.; Smeets,
T.; Tak, P.-P.; Panayi, G. S.: Functional IL-2 receptor beta (CD122)
and gamma (CD132) chains are expressed by fibroblast-like synoviocytes:
activation by IL-2 stimulates monocyte chemoattractant protein-1 production. J.
Immun. 166: 4141-4147, 2001.
3. Dai, H.; Wan, N.; Zhang, S.; Moore, Y.; Wan, F.; Dai, Z.: Cutting
edge: programmed death-1 defines CD8+CD122+ T cells as regulatory
versus memory T cells. J. Immun. 185: 803-807, 2010.
4. Giri, J. G.; Ahdieh, M.; Eisenman, J.; Shanebeck, K.; Grabstein,
K.; Kumaki, S.; Namen, A.; Park, L. S.; Cosman, D.; Anderson, D.:
Utilization of the beta and gamma chains of the IL-2 receptor by the
novel cytokine IL-15. EMBO J. 13: 2822-2830, 1994.
5. Gnarra, J. R.; Otani, H.; Wang, M. G.; McBride, O. W.; Sharon,
M.; Leonard, W. J.: Human interleukin 2 receptor beta-chain gene:
chromosomal localization and identification of 5-prime regulatory
sequences. Proc. Nat. Acad. Sci. 87: 3440-3444, 1990.
6. 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.
7. Kondo, M.; Scherer, D. C.; Miyamoto, T.; King, A. G.; Akashi, K.;
Sugamura, K.; Weissman, I. L.: Cell-fate conversion of lymphoid-committed
progenitors by instructive actions of cytokines. Nature 407: 383-386,
2000.
8. Lamaze, C.; Dujeancourt, A.; Baba, T.; Lo, C. G.; Benmerah, A.;
Dautry-Varsat, A.: Interleukin 2 receptors and detergent-resistant
membrane domains define a clathrin-independent endocytic pathway. Molec.
Cell 7: 661-671, 2001.
9. Shibuya, H.; Yoneyama, M.; Nakamura, Y.; Harada, H.; Hatakeyama,
M.; Minamoto, S.; Kono, T.; Doi, T.; White, R.; Taniguchi, T.: The
human interleukin-2 receptor beta-chain gene: genomic organization,
promoter analysis and chromosomal assignment. Nucleic Acids Res. 18:
3697-3703, 1990.
10. Suzuki, H.; Kundig, T. M.; Furlonger, C.; Wakeham, A.; Timms,
E.; Matsuyama, T.; Schmits, R.; Simard, J. J. L.; Ohashi, P. S.; Griesser,
H.; Taniguchi, T.; Paige, C. J.; Mak, T. W.: Deregulated T cell activation
and autoimmunity in mice lacking interleukin-2 receptor beta. Science 268:
1472-1476, 1995.
11. Tsudo, M.; Kitamura, F.; Miyasaka, M.: Characterization of the
interleukin 2 receptor beta chain using three distinct monoclonal
antibodies. Proc. Nat. Acad. Sci. 86: 1982-1986, 1989.
12. Wang, X.; Rickert, M.; Garcia, K. C.: Structure of the quaternary
complex of interleukin-2 with its alpha, beta, and gamma-c receptors. Science 310:
1159-1163, 2005.
*FIELD* CN
Paul J. Converse - updated: 10/12/2010
Paul J. Converse - updated: 2/9/2006
Paul J. Converse - updated: 1/10/2006
Jane Kelly - updated: 1/25/2002
Paul J. Converse - updated: 4/27/2001
Stylianos E. Antonarakis - updated: 4/17/2001
Ada Hamosh - updated: 9/20/2000
*FIELD* CD
Victor A. McKusick: 10/10/1988
*FIELD* ED
mgross: 10/18/2010
terry: 10/12/2010
mgross: 2/9/2006
mgross: 1/10/2006
ckniffin: 10/27/2004
carol: 2/15/2002
terry: 1/25/2002
mgross: 4/27/2001
mgross: 4/17/2001
alopez: 9/20/2000
dkim: 7/2/1998
mark: 7/11/1995
carol: 5/16/1994
supermim: 3/16/1992
carol: 1/6/1992
carol: 9/27/1990
carol: 8/15/1990
*RECORD*
*FIELD* NO
146710
*FIELD* TI
*146710 INTERLEUKIN 2 RECEPTOR, BETA; IL2RB
;;CD122 ANTIGEN; CD122
*FIELD* TX
CLONING
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Tsudo et al. (1989) characterized the interleukin-2 receptor beta chain
using 3 monoclonal antibodies, designated Mik-beta1, -beta2, and -beta3.
They showed by immunoprecipitation that the beta chain has a molecular
mass of 68,000-72,000 Da. Moreover, they found that the beta chain was
expressed on the surface of peripheral blood Leu-19+ natural killer
cells in the absence of alpha-chain expression. Also see IL2RA (147730).
Gnarra et al. (1990) characterized the IL2RB gene. They found that the
IL2 receptor is present in 3 forms with respect to binding ability to
IL2 (147680): high, intermediate, and low affinity forms. The alpha
chain constitutes the low affinity form and is not functional in IL2
internalization and signal transduction. The beta chain by itself
constitutes the intermediate affinity form. Hatakeyama et al. (1989)
presented evidence that coexpression of the IL2RA and IL2RB genes
results in the high affinity form of the receptor.
GENE FUNCTION
Giri et al. (1994) showed that IL2RB and IL2RG (308380), but not IL2RA,
transduce signals by IL15 (600554) in addition to IL2.
Kondo et al. (2000) showed that a clonogenic common lymphoid progenitor,
a bone marrow-resident cell that gives rise exclusively to lymphocytes
(T, B, and natural killer cells), can be redirected to the myeloid
lineage by stimulation through exogenously expressed interleukin-2
receptor and GMCSF receptor (138981, 306250). Analysis of mutants of the
beta chain of the IL2 receptor revealed that the granulocyte and
monocyte differentiation signals are triggered by different cytoplasmic
domains, showing that the signaling pathways responsible for these
unique developmental outcomes are separable. Finally, Kondo et al.
(2000) showed that the endogenous myelomonocytic cytokine receptors for
GM-CSF and macrophage colony-stimulating factor (CSF1R; 164770) are
expressed at low to moderate levels on the more primitive hematopoietic
stem cells, are absent on common lymphoid progenitors, and are
upregulated after myeloid lineage induction by IL2. Kondo et al. (2000)
concluded that cytokine signaling can regulate cell fate decisions and
proposed that a critical step in lymphoid commitment is downregulation
of cytokine receptors that drive myeloid cell development.
Lamaze et al. (2001) selectively blocked clathrin (see 118960)-dependent
endocytosis using dominant-negative mutants of EPS15 (600051) and showed
that clathrin-mediated endocytosis of transferrin (190000) was
inhibited, while endocytosis of the IL2Rs proceeded normally.
Ultrastructural and biochemical experiments showed that
clathrin-independent endocytosis of IL2Rs exists constitutively in
lymphocytes and is coupled to their association with detergent-resistant
membrane domains. The authors found that clathrin-independent
endocytosis requires dynamin (see 602377) and is specifically regulated
by Rho family GTPases (see 604980). These results defined novel
properties of receptor-mediated endocytosis and established that IL2R is
efficiently internalized through this clathrin-independent pathway.
Using flow cytometry, Corrigall et al. (2001) detected expression of a
functional IL2R of intermediate affinity composed solely of IL2RB and
IL2RG on fibroblast-like synoviocytes (FLS) obtained from rheumatoid
arthritis and osteoarthritis patients. Addition of recombinant IL2, IL1B
(147720), or TNFA (191160) independently did not upregulate expression
of the receptors on FLS, but IL2 or IL1B did significantly increase
expression of intracellular tyrosine-phosphorylated proteins and the
production of MCP1 (158105). Corrigall et al. (2001) proposed that MCP1
in the synovial membrane serves to recruit macrophages and perpetuate
inflammation in the joints of patients with rheumatoid arthritis.
Dai et al. (2010) noted that CD8 (see 186910)-positive/CD122-positive T
cells have been shown to function, paradoxically, as both regulatory and
memory T cells. Using flow cytometric analysis, they demonstrated that
mouse Cd8-positive/Cd122-positive T cells included both Pd1 (PDCD1;
600244)-positive and Pd1-negative subpopulations. Only the Pd1-positive
subpopulation suppressed T-cell responses in vitro and in vivo, and this
suppression occurred largely in an Il10 (124092)-dependent manner. Il10
production, in turn, was dependent on costimulatory signaling of both
Cd28 (186760) and Pd1. Cd8-positive/Cd122-positive/Pd1-negative T cells
mediated skin graft rejection. Dai et al. (2010) concluded that
CD8-positive/CD122-positive T cells can be either regulatory or memory T
cells, depending on their PD1 expression and antigen specificity.
BIOCHEMICAL FEATURES
- Crystal Structure
Wang et al. (2005) reported the crystal structure of the quaternary
complex of IL2 with IL2RA, IL2RB, and IL2RG at a resolution of 2.3
angstroms.
GENE STRUCTURE
Shibuya et al. (1990) found that the IL2RB gene contains 10 exons
spanning about 24.3 kb and that the gene product is encoded by exons
2-10. The cysteine-rich extracellular region, which displays a
significant evolutionary resemblance to other cytokine receptors, as
well as to growth hormone and prolactin receptors, is encoded primarily
by exons 3 and 4.
MAPPING
By Southern analysis of somatic cell hybrid DNA and in situ
hybridization, Gnarra et al. (1990) localized the IL2RB gene to
chromosome 22q11.2-q12, a region that is associated with several
lymphoid neoplasias. By RFLP linkage analysis, Shibuya et al. (1990)
assigned the IL2RB gene to 22q12-q13. By in situ hybridization, Campbell
et al. (1992) mapped the Il2rb gene to band E of mouse chromosome 15.
ANIMAL MODEL
Suzuki et al. (1995) generated mice defective in Il2rb expression by
insertion of a neomycin resistance cassette into the IL2RB gene at exon
6, which encodes a region of the extracellular domain proximal to the
transmembrane region. Mice from 2 independent embryonic stem cell lines
were separately bred homozygous for the defect, with both lineages
showing identical gross appearances. The mice showed normal growth until
approximately 3 weeks after birth. After 4 weeks of age, they were
generally smaller than normal or heterozygous littermates and had
abnormal appearances characterized by fuzzy hair, slow movement, and
fully developed external genitals. Death occurred at approximately 12
weeks. In mice lacking the IL2R beta chain, T cells were shown to be
spontaneously activated, resulting in exhaustive differentiation of B
cells into plasma cells and the appearance of high serum concentrations
of immunoglobulins G1 and E, as well as autoantibodies that cause
hemolytic anemia. Marked infiltrated granulocytopoiesis was also
apparent. Depletion of CD4+ T cells in mutant mice rescued B cells
without reversion of granulocyte abnormalities. T cells did not
proliferate in response to polyclonal activators, nor could
antigen-specific immune responses be elicited. Thus, Suzuki et al.
(1995) concluded that Il2rb is required to keep the activation programs
of T cells under control, to maintain homeostasis, and to prevent
autoimmunity.
*FIELD* RF
1. Campbell, H. D.; Webb, G. C.; Kono, T.; Taniguchi, T.; Ford, J.
H.; Young, I. G.: Assignment of the interleukin-2 receptor beta chain
gene (Il-2rb) to band E on mouse chromosome 15. Genomics 12: 179-180,
1992.
2. Corrigall, V. M.; Arastu, M.; Khan, S.; Shah, C.; Fife, M.; Smeets,
T.; Tak, P.-P.; Panayi, G. S.: Functional IL-2 receptor beta (CD122)
and gamma (CD132) chains are expressed by fibroblast-like synoviocytes:
activation by IL-2 stimulates monocyte chemoattractant protein-1 production. J.
Immun. 166: 4141-4147, 2001.
3. Dai, H.; Wan, N.; Zhang, S.; Moore, Y.; Wan, F.; Dai, Z.: Cutting
edge: programmed death-1 defines CD8+CD122+ T cells as regulatory
versus memory T cells. J. Immun. 185: 803-807, 2010.
4. Giri, J. G.; Ahdieh, M.; Eisenman, J.; Shanebeck, K.; Grabstein,
K.; Kumaki, S.; Namen, A.; Park, L. S.; Cosman, D.; Anderson, D.:
Utilization of the beta and gamma chains of the IL-2 receptor by the
novel cytokine IL-15. EMBO J. 13: 2822-2830, 1994.
5. Gnarra, J. R.; Otani, H.; Wang, M. G.; McBride, O. W.; Sharon,
M.; Leonard, W. J.: Human interleukin 2 receptor beta-chain gene:
chromosomal localization and identification of 5-prime regulatory
sequences. Proc. Nat. Acad. Sci. 87: 3440-3444, 1990.
6. 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.
7. Kondo, M.; Scherer, D. C.; Miyamoto, T.; King, A. G.; Akashi, K.;
Sugamura, K.; Weissman, I. L.: Cell-fate conversion of lymphoid-committed
progenitors by instructive actions of cytokines. Nature 407: 383-386,
2000.
8. Lamaze, C.; Dujeancourt, A.; Baba, T.; Lo, C. G.; Benmerah, A.;
Dautry-Varsat, A.: Interleukin 2 receptors and detergent-resistant
membrane domains define a clathrin-independent endocytic pathway. Molec.
Cell 7: 661-671, 2001.
9. Shibuya, H.; Yoneyama, M.; Nakamura, Y.; Harada, H.; Hatakeyama,
M.; Minamoto, S.; Kono, T.; Doi, T.; White, R.; Taniguchi, T.: The
human interleukin-2 receptor beta-chain gene: genomic organization,
promoter analysis and chromosomal assignment. Nucleic Acids Res. 18:
3697-3703, 1990.
10. Suzuki, H.; Kundig, T. M.; Furlonger, C.; Wakeham, A.; Timms,
E.; Matsuyama, T.; Schmits, R.; Simard, J. J. L.; Ohashi, P. S.; Griesser,
H.; Taniguchi, T.; Paige, C. J.; Mak, T. W.: Deregulated T cell activation
and autoimmunity in mice lacking interleukin-2 receptor beta. Science 268:
1472-1476, 1995.
11. Tsudo, M.; Kitamura, F.; Miyasaka, M.: Characterization of the
interleukin 2 receptor beta chain using three distinct monoclonal
antibodies. Proc. Nat. Acad. Sci. 86: 1982-1986, 1989.
12. Wang, X.; Rickert, M.; Garcia, K. C.: Structure of the quaternary
complex of interleukin-2 with its alpha, beta, and gamma-c receptors. Science 310:
1159-1163, 2005.
*FIELD* CN
Paul J. Converse - updated: 10/12/2010
Paul J. Converse - updated: 2/9/2006
Paul J. Converse - updated: 1/10/2006
Jane Kelly - updated: 1/25/2002
Paul J. Converse - updated: 4/27/2001
Stylianos E. Antonarakis - updated: 4/17/2001
Ada Hamosh - updated: 9/20/2000
*FIELD* CD
Victor A. McKusick: 10/10/1988
*FIELD* ED
mgross: 10/18/2010
terry: 10/12/2010
mgross: 2/9/2006
mgross: 1/10/2006
ckniffin: 10/27/2004
carol: 2/15/2002
terry: 1/25/2002
mgross: 4/27/2001
mgross: 4/17/2001
alopez: 9/20/2000
dkim: 7/2/1998
mark: 7/11/1995
carol: 5/16/1994
supermim: 3/16/1992
carol: 1/6/1992
carol: 9/27/1990
carol: 8/15/1990