ID IL2B_HUMAN STANDARD; PRT; 551 AA. AC P14784; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Interleukin-2 receptor beta chain precursor (IL-2 receptor) (P70-75) DE (High affinity IL-2 receptor beta subunit) (CD122 antigen). GN IL2RB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89242117; PubMed=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 SEQUENCE FROM N.A. RA Rieder M.J., Armel T.Z., Carrington D.P., Ozuna M., Kuldanek S.A., RA Rajkumar N., Toth E.J., Yi Q., Nickerson D.A.; RT "SeattleSNPs. NHLBI HL66682 program for genomic applications, UW- RT FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu)."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=20057165; PubMed=10591208; 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 [4] RP SEQUENCE FROM N.A. RC TISSUE=Lung; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP 3D-STRUCTURE MODELING OF 31-230. RX MEDLINE=95111955; PubMed=7529123; 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). 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: Noncovalent dimer of an alpha and a beta chains. IL2R CC exists in 3 different forms: a high affinity dimer, an CC intermediate affinity monomer (beta chain), and a low affinity CC monomer (alpha chain). The high and intermediate affinity forms CC also associate with a gamma chain. CC -!- SUBCELLULAR LOCATION: Type I membrane 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 family of receptors. CC Subfamily 4. CC -!- SIMILARITY: Contains 1 fibronectin type III domain. CC -!- DATABASE: NAME=PROW; NOTE=CD guide CD122 entry; CC WWW="http://www.ncbi.nlm.nih.gov/prow/cd/cd122.htm". CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M26062; AAA59143.1; -. DR EMBL; AF517934; AAM54040.1; -. DR EMBL; AL022314; -; NOT_ANNOTATED_CDS. DR EMBL; BC025691; AAH25691.1; -. DR PIR; A30342; A30342. DR PDB; 1ILM; 26-JAN-95. DR PDB; 1ILN; 26-JAN-95. DR Genew; HGNC:6009; IL2RB. DR MIM; 146710; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0004911; F:interleukin-2 receptor activity; TAS. DR GO; GO:0006461; P:protein complex assembly; TAS. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR002996; CR1A. DR InterPro; IPR003961; FN_III. DR InterPro; IPR008957; FN_III-like. DR InterPro; IPR003531; Hemtopoptn_S_F1. DR InterPro; IPR007110; Ig-like. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1. KW Receptor; Transmembrane; Glycoprotein; Signal; 3D-structure. FT SIGNAL 1 26 FT CHAIN 27 551 Interleukin-2 receptor beta chain. FT DOMAIN 27 240 Extracellular (Potential). FT TRANSMEM 241 265 Potential. FT DOMAIN 266 551 Cytoplasmic (Potential). FT DOMAIN 131 229 Fibronectin type-III. FT SITE 220 224 WSXWS motif. FT SITE 278 286 Box 1 motif. FT DISULFID 36 46 By similarity. FT DISULFID 74 86 By similarity. FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential). FT CARBOHYD 43 43 N-linked (GlcNAc...) (Potential). FT CARBOHYD 71 71 N-linked (GlcNAc...) (Potential). FT CARBOHYD 149 149 N-linked (GlcNAc...) (Potential). FT STRAND 35 37 FT STRAND 45 47 FT STRAND 52 52 FT STRAND 56 56 FT STRAND 60 64 FT HELIX 68 70 FT STRAND 72 73 FT TURN 80 82 FT STRAND 85 86 FT TURN 90 92 FT HELIX 93 95 FT STRAND 99 104 FT STRAND 112 116 FT STRAND 132 133 FT HELIX 139 142 FT STRAND 149 150 FT TURN 159 160 FT STRAND 163 169 FT STRAND 178 180 FT STRAND 185 186 FT TURN 200 201 FT STRAND 205 206 FT STRAND 208 210 FT TURN 215 216 FT STRAND 221 221 FT STRAND 227 228 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 //