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P14784

- IL2RB_HUMAN

UniProt

P14784 - IL2RB_HUMAN

Protein

Interleukin-2 receptor subunit beta

Gene

IL2RB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2.

    GO - Molecular functioni

    1. interleukin-2 binding Source: UniProtKB
    2. interleukin-2 receptor activity Source: MGI

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: MGI
    2. interleukin-2-mediated signaling pathway Source: GOC
    3. negative regulation of apoptotic process Source: MGI
    4. protein complex assembly Source: ProtInc
    5. signal transduction Source: ProtInc
    6. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.
    SignaLinkiP14784.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-2 receptor subunit beta
    Short name:
    IL-2 receptor subunit beta
    Short name:
    IL-2R subunit beta
    Short name:
    IL-2RB
    Alternative name(s):
    High affinity IL-2 receptor subunit beta
    p70-75
    Short name:
    p75
    CD_antigen: CD122
    Gene namesi
    Name:IL2RB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:6009. IL2RB.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: UniProtKB
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi418 – 4181Y → F: Partial loss of interaction with SHB; when associated with F-536. 1 Publication
    Mutagenesisi536 – 5361Y → F: Partial loss of interaction with SHB; when associated with F-418. 1 Publication

    Organism-specific databases

    Orphaneti85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    PharmGKBiPA29829.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 551525Interleukin-2 receptor subunit betaPRO_0000010878Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi36 ↔ 46
    Glycosylationi43 – 431N-linked (GlcNAc...)1 Publication
    Disulfide bondi59 ↔ 110
    Glycosylationi71 – 711N-linked (GlcNAc...)1 Publication
    Disulfide bondi74 ↔ 86
    Glycosylationi149 – 1491N-linked (GlcNAc...)2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP14784.
    PRIDEiP14784.

    PTM databases

    PhosphoSiteiP14784.

    Expressioni

    Gene expression databases

    ArrayExpressiP14784.
    BgeeiP14784.
    CleanExiHS_IL2RB.
    GenevestigatoriP14784.

    Organism-specific databases

    HPAiHPA062657.

    Interactioni

    Subunit structurei

    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. Interacts with HTLV-1 accessory protein p12I.4 Publications

    Protein-protein interaction databases

    BioGridi109775. 17 interactions.
    DIPiDIP-43N.
    IntActiP14784. 4 interactions.
    MINTiMINT-273361.
    STRINGi9606.ENSP00000216223.

    Structurei

    Secondary structure

    1
    551
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 386
    Beta strandi40 – 4910
    Beta strandi59 – 657
    Beta strandi72 – 754
    Beta strandi77 – 804
    Beta strandi84 – 896
    Beta strandi104 – 1107
    Beta strandi117 – 1248
    Helixi126 – 1283
    Beta strandi136 – 1438
    Beta strandi148 – 1536
    Helixi159 – 1613
    Beta strandi165 – 1728
    Helixi178 – 1803
    Beta strandi184 – 1863
    Beta strandi192 – 1954
    Beta strandi203 – 21311
    Beta strandi227 – 2304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ILMmodel-B31-230[»]
    1ILNmodel-B31-230[»]
    2B5IX-ray2.30B27-240[»]
    2ERJX-ray3.00B/F27-232[»]
    3QAZX-ray3.80B/E/H/K/N/Q/T/W/Z/c/f/i24-240[»]
    4GS7X-ray2.35B27-240[»]
    ProteinModelPortaliP14784.
    SMRiP14784. Positions 32-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14784.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 240214ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini266 – 551286CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei241 – 26525HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 234101Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi220 – 2245WSXWS motif
    Motifi278 – 2869Box 1 motif

    Domaini

    The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
    The box 1 motif is required for JAK interaction and/or activation.

    Sequence similaritiesi

    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46659.
    HOGENOMiHOG000038003.
    HOVERGENiHBG052110.
    KOiK05069.
    OMAiACQVYFT.
    OrthoDBiEOG72RMZ6.
    PhylomeDBiP14784.
    TreeFamiTF337874.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR003961. Fibronectin_type3.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR013783. Ig-like_fold.
    [Graphical view]
    SMARTiSM00060. FN3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    PROSITEiPS50853. FN3. 1 hit.
    PS01355. HEMATOPO_REC_S_F1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14784-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPALSWRL PLLILLLPLA TSWASAAVNG TSQFTCFYNS RANISCVWSQ    50
    DGALQDTSCQ VHAWPDRRRW NQTCELLPVS QASWACNLIL GAPDSQKLTT 100
    VDIVTLRVLC REGVRWRVMA IQDFKPFENL RLMAPISLQV VHVETHRCNI 150
    SWEISQASHY FERHLEFEAR TLSPGHTWEE APLLTLKQKQ EWICLETLTP 200
    DTQYEFQVRV KPLQGEFTTW SPWSQPLAFR TKPAALGKDT IPWLGHLLVG 250
    LSGAFGFIIL VYLLINCRNT GPWLKKVLKC NTPDPSKFFS QLSSEHGGDV 300
    QKWLSSPFPS SSFSPGGLAP EISPLEVLER DKVTQLLLQQ DKVPEPASLS 350
    SNHSLTSCFT NQGYFFFHLP DALEIEACQV YFTYDPYSEE DPDEGVAGAP 400
    TGSSPQPLQP LSGEDDAYCT FPSRDDLLLF SPSLLGGPSP PSTAPGGSGA 450
    GEERMPPSLQ ERVPRDWDPQ PLGPPTPGVP DLVDFQPPPE LVLREAGEEV 500
    PDAGPREGVS FPWSRPPGQG EFRALNARLP LNTDAYLSLQ ELQGQDPTHL 550
    V 551
    Length:551
    Mass (Da):61,117
    Last modified:April 1, 1990 - v1
    Checksum:i1A76FA1936BB7EE6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101L → V.
    Corresponds to variant rs57770674 [ dbSNP | Ensembl ].
    VAR_061186
    Natural varianti83 – 831S → F.1 Publication
    Corresponds to variant rs2228143 [ dbSNP | Ensembl ].
    VAR_021994
    Natural varianti391 – 3911D → E.1 Publication
    Corresponds to variant rs228942 [ dbSNP | Ensembl ].
    VAR_019998

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26062 mRNA. Translation: AAA59143.1.
    CR456506 mRNA. Translation: CAG30392.1.
    AF517934 Genomic DNA. Translation: AAM54040.1.
    AK312860 mRNA. Translation: BAG35712.1.
    AL022314 Genomic DNA. Translation: CAA18444.1.
    CH471095 Genomic DNA. Translation: EAW60144.1.
    BC025691 mRNA. Translation: AAH25691.1.
    CCDSiCCDS13942.1.
    PIRiA30342.
    RefSeqiNP_000869.1. NM_000878.3.
    UniGeneiHs.474787.

    Genome annotation databases

    EnsembliENST00000216223; ENSP00000216223; ENSG00000100385.
    GeneIDi3560.
    KEGGihsa:3560.
    UCSCiuc003aqv.1. human.

    Polymorphism databases

    DMDMi124321.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26062 mRNA. Translation: AAA59143.1 .
    CR456506 mRNA. Translation: CAG30392.1 .
    AF517934 Genomic DNA. Translation: AAM54040.1 .
    AK312860 mRNA. Translation: BAG35712.1 .
    AL022314 Genomic DNA. Translation: CAA18444.1 .
    CH471095 Genomic DNA. Translation: EAW60144.1 .
    BC025691 mRNA. Translation: AAH25691.1 .
    CCDSi CCDS13942.1.
    PIRi A30342.
    RefSeqi NP_000869.1. NM_000878.3.
    UniGenei Hs.474787.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ILM model - B 31-230 [» ]
    1ILN model - B 31-230 [» ]
    2B5I X-ray 2.30 B 27-240 [» ]
    2ERJ X-ray 3.00 B/F 27-232 [» ]
    3QAZ X-ray 3.80 B/E/H/K/N/Q/T/W/Z/c/f/i 24-240 [» ]
    4GS7 X-ray 2.35 B 27-240 [» ]
    ProteinModelPortali P14784.
    SMRi P14784. Positions 32-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109775. 17 interactions.
    DIPi DIP-43N.
    IntActi P14784. 4 interactions.
    MINTi MINT-273361.
    STRINGi 9606.ENSP00000216223.

    Chemistry

    BindingDBi P14784.
    ChEMBLi CHEMBL3276.
    DrugBanki DB00041. Aldesleukin.
    DB00074. Basiliximab.
    DB00111. Daclizumab.
    DB00004. Denileukin diftitox.

    PTM databases

    PhosphoSitei P14784.

    Polymorphism databases

    DMDMi 124321.

    Proteomic databases

    PaxDbi P14784.
    PRIDEi P14784.

    Protocols and materials databases

    DNASUi 3560.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216223 ; ENSP00000216223 ; ENSG00000100385 .
    GeneIDi 3560.
    KEGGi hsa:3560.
    UCSCi uc003aqv.1. human.

    Organism-specific databases

    CTDi 3560.
    GeneCardsi GC22M037515.
    HGNCi HGNC:6009. IL2RB.
    HPAi HPA062657.
    MIMi 146710. gene.
    neXtProti NX_P14784.
    Orphaneti 85408. Juvenile rheumatoid factor-negative polyarthritis.
    85410. Oligoarticular juvenile arthritis.
    PharmGKBi PA29829.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46659.
    HOGENOMi HOG000038003.
    HOVERGENi HBG052110.
    KOi K05069.
    OMAi ACQVYFT.
    OrthoDBi EOG72RMZ6.
    PhylomeDBi P14784.
    TreeFami TF337874.

    Enzyme and pathway databases

    Reactomei REACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.
    SignaLinki P14784.

    Miscellaneous databases

    EvolutionaryTracei P14784.
    GeneWikii IL2RB.
    GenomeRNAii 3560.
    NextBioi 13904.
    PROi P14784.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14784.
    Bgeei P14784.
    CleanExi HS_IL2RB.
    Genevestigatori P14784.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR003961. Fibronectin_type3.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    SMARTi SM00060. FN3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 1 hit.
    PS01355. HEMATOPO_REC_S_F1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's."
      Hatakeyama M., Tsudo M., Minamoto S., Kono T., Doi T., Miyata T., Miyasaka M., Taniguchi T.
      Science 244:551-556(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. SeattleSNPs variation discovery resource
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-83 AND GLU-391.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Trachea.
    5. "The DNA sequence of human chromosome 22."
      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.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    8. "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."
      Mulloy J.C., Crownley R.W., Fullen J., Leonard W.J., Franchini G.
      J. Virol. 70:3599-3605(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
    9. "IL-2 receptor signaling through the Shb adapter protein in T and NK cells."
      Lindholm C.K.
      Biochem. Biophys. Res. Commun. 296:929-936(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB, MUTAGENESIS OF TYR-418 AND TYR-536.
    10. "The interleukin-2 and interleukin-4 receptors studied by molecular modelling."
      Bamborough P., Hedgecock C.J., Richards W.G.
      Structure 2:839-851(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 31-230.
    11. "Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors."
      Wang X., Rickert M., Garcia K.C.
      Science 310:1159-1163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-240 IN COMPLEX WITH IL2; IL2RA AND IL2RC, DISULFIDE BONDS, GLYCOSYLATION AT ASN-149.
    12. "Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor."
      Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-232 IN COMPLEX WITH IL2; IL2RA AND IL2RC, DISULFIDE BONDS, GLYCOSYLATION AT ASN-43; ASN-71 AND ASN-149.

    Entry informationi

    Entry nameiIL2RB_HUMAN
    AccessioniPrimary (citable) accession number: P14784
    Secondary accession number(s): B2R765
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 170 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3