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P16297

- IL2RB_MOUSE

UniProt

P16297 - IL2RB_MOUSE

Protein

Interleukin-2 receptor subunit beta

Gene

Il2rb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Aug 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: MGI
    2. interleukin-2 receptor activity Source: Ensembl

    GO - Biological processi

    1. negative regulation of apoptotic process Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_210793. Interleukin receptor SHC signaling.

    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
    CD_antigen: CD122
    Gene namesi
    Name:Il2rb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:96550. Il2rb.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 539513Interleukin-2 receptor subunit betaPRO_0000010879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi36 ↔ 46By similarity
    Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi71 – 711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi74 ↔ 86By similarity
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiP16297.

    PTM databases

    PhosphoSiteiP16297.

    Expressioni

    Gene expression databases

    BgeeiP16297.
    CleanExiMM_IL2RB.
    GenevestigatoriP16297.

    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 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP16297. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP16297.
    SMRiP16297. Positions 32-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 240214ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini269 – 539271CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei241 – 26828HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 235101Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi221 – 2255WSXWS motif
    Motifi281 – 2899Box 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.
    GeneTreeiENSGT00510000049239.
    HOGENOMiHOG000038003.
    HOVERGENiHBG052110.
    InParanoidiP16297.
    KOiK05069.
    OMAiACQVYFT.
    OrthoDBiEOG72RMZ6.
    PhylomeDBiP16297.
    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.

    P16297-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATIALPWSL SLYVFLLLLA TPWASAAVKN CSHLECFYNS RANVSCMWSH    50
    EEALNVTTCH VHAKSNLRHW NKTCELTLVR QASWACNLIL GSFPESQSLT 100
    SVDLLDINVV CWEEKGWRRV KTCDFHPFDN LRLVAPHSLQ VLHIDTQRCN 150
    ISWKVSQVSH YIEPYLEFEA RRRLLGHSWE DASVLSLKQR QQWLFLEMLI 200
    PSTSYEVQVR VKAQRNNTGT WSPWSQPLTF RTRPADPMKE ILPMSWLRYL 250
    LLVLGCFSGF FSCVYILVKC RYLGPWLKTV LKCHIPDPSE FFSQLSSQHG 300
    GDLQKWLSSP VPLSFFSPSG PAPEISPLEV LDGDSKAVQL LLLQKDSAPL 350
    PSPSGHSQAS CFTNQGYFFF HLPNALEIES CQVYFTYDPC VEEEVEEDGS 400
    RLPEGSPHPP LLPLAGEQDD YCAFPPRDDL LLFSPSLSTP NTAYGGSRAP 450
    EERSPLSLHE GLPSLASRDL MGLQRPLERM PEGDGEGLSA NSSGEQASVP 500
    EGNLHGQDQD RGQGPILTLN TDAYLSLQEL QAQDSVHLI 539
    Length:539
    Mass (Da):60,539
    Last modified:August 1, 1990 - v1
    Checksum:i365C9D206E86FE14
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28052 mRNA. Translation: AAA39283.1.
    AK017288 mRNA. Translation: BAB30674.1.
    AK157572 mRNA. Translation: BAE34125.1.
    CCDSiCCDS27616.1.
    PIRiA35052.
    RefSeqiNP_032394.1. NM_008368.4.
    XP_006520540.1. XM_006520477.1.
    XP_006520541.1. XM_006520478.1.
    XP_006520542.1. XM_006520479.1.
    XP_006520543.1. XM_006520480.1.
    XP_006520544.1. XM_006520481.1.
    UniGeneiMm.35287.
    Mm.384038.

    Genome annotation databases

    EnsembliENSMUST00000089398; ENSMUSP00000086820; ENSMUSG00000068227.
    ENSMUST00000163494; ENSMUSP00000127006; ENSMUSG00000068227.
    GeneIDi16185.
    KEGGimmu:16185.
    UCSCiuc007wpk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28052 mRNA. Translation: AAA39283.1 .
    AK017288 mRNA. Translation: BAB30674.1 .
    AK157572 mRNA. Translation: BAE34125.1 .
    CCDSi CCDS27616.1.
    PIRi A35052.
    RefSeqi NP_032394.1. NM_008368.4.
    XP_006520540.1. XM_006520477.1.
    XP_006520541.1. XM_006520478.1.
    XP_006520542.1. XM_006520479.1.
    XP_006520543.1. XM_006520480.1.
    XP_006520544.1. XM_006520481.1.
    UniGenei Mm.35287.
    Mm.384038.

    3D structure databases

    ProteinModelPortali P16297.
    SMRi P16297. Positions 32-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P16297. 1 interaction.

    PTM databases

    PhosphoSitei P16297.

    Proteomic databases

    PRIDEi P16297.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089398 ; ENSMUSP00000086820 ; ENSMUSG00000068227 .
    ENSMUST00000163494 ; ENSMUSP00000127006 ; ENSMUSG00000068227 .
    GeneIDi 16185.
    KEGGi mmu:16185.
    UCSCi uc007wpk.2. mouse.

    Organism-specific databases

    CTDi 3560.
    MGIi MGI:96550. Il2rb.

    Phylogenomic databases

    eggNOGi NOG46659.
    GeneTreei ENSGT00510000049239.
    HOGENOMi HOG000038003.
    HOVERGENi HBG052110.
    InParanoidi P16297.
    KOi K05069.
    OMAi ACQVYFT.
    OrthoDBi EOG72RMZ6.
    PhylomeDBi P16297.
    TreeFami TF337874.

    Enzyme and pathway databases

    Reactomei REACT_210793. Interleukin receptor SHC signaling.

    Miscellaneous databases

    NextBioi 289077.
    PROi P16297.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16297.
    CleanExi MM_IL2RB.
    Genevestigatori P16297.

    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. "Murine interleukin 2 receptor beta chain: dysregulated gene expression in lymphoma line EL-4 caused by a promoter insertion."
      Kono T., Doi T., Yamada G., Hatakeyama M., Minamoto S., Tsudo M., Miyasaka M., Miyata T., Taniguchi T.
      Proc. Natl. Acad. Sci. U.S.A. 87:1806-1810(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Head and Spleen.

    Entry informationi

    Entry nameiIL2RB_MOUSE
    AccessioniPrimary (citable) accession number: P16297
    Secondary accession number(s): Q3TZT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3