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P31785

- IL2RG_HUMAN

UniProt

P31785 - IL2RG_HUMAN

Protein

Cytokine receptor common subunit gamma

Gene

IL2RG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Common subunit for the receptors for a variety of interleukins.

    GO - Molecular functioni

    1. cytokine receptor activity Source: InterPro
    2. interleukin-2 binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. immune response Source: ProtInc
    2. interleukin-2-mediated signaling pathway Source: GOC
    3. interleukin-4-mediated signaling pathway Source: GOC
    4. interleukin-7-mediated signaling pathway Source: GOC
    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_115529. Interleukin-7 signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.
    SignaLinkiP31785.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytokine receptor common subunit gamma
    Alternative name(s):
    Interleukin-2 receptor subunit gamma
    Short name:
    IL-2 receptor subunit gamma
    Short name:
    IL-2R subunit gamma
    Short name:
    IL-2RG
    gammaC
    p64
    CD_antigen: CD132
    Gene namesi
    Name:IL2RG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:6010. IL2RG.

    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

    Involvement in diseasei

    Severe combined immunodeficiency X-linked T-cell-negative/B-cell-positive/NK-cell-negative (XSCID) [MIM:300400]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development.11 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391D → N in XSCID. 1 Publication
    VAR_002668
    Natural varianti62 – 621C → G in XSCID.
    VAR_002669
    Natural varianti68 – 681E → G in XSCID.
    VAR_002670
    Natural varianti68 – 681E → K in XSCID. 1 Publication
    VAR_002671
    Natural varianti84 – 841N → K in XSCID.
    VAR_002672
    Natural varianti89 – 891Y → C in XSCID.
    VAR_002673
    Natural varianti105 – 1051Y → C in XSCID.
    VAR_002674
    Natural varianti114 – 1141G → D in XSCID. 1 Publication
    VAR_002675
    Natural varianti115 – 1151C → F in XSCID. 1 Publication
    VAR_002676
    Natural varianti115 – 1151C → R in XSCID; atypical. 1 Publication
    VAR_002677
    Natural varianti123 – 1231H → P in XSCID.
    VAR_002678
    Natural varianti125 – 1251Y → N in XSCID.
    VAR_002679
    Natural varianti144 – 1441Q → P in XSCID.
    VAR_002680
    Natural varianti153 – 1531I → N in XSCID. 1 Publication
    VAR_002681
    Natural varianti156 – 1561A → V in XSCID.
    VAR_002682
    Natural varianti162 – 1621L → H in XSCID. 1 Publication
    VAR_002683
    Natural varianti172 – 1721L → P in XSCID.
    VAR_002684
    Natural varianti172 – 1721L → Q in XSCID.
    VAR_002685
    Natural varianti182 – 1821C → R in XSCID.
    VAR_002686
    Natural varianti183 – 1831L → S in XSCID. 1 Publication
    VAR_002687
    Natural varianti224 – 2241R → W in XSCID. 1 Publication
    VAR_002689
    Natural varianti226 – 2261R → C in XSCID. 1 Publication
    VAR_002690
    Natural varianti226 – 2261R → H in XSCID. 1 Publication
    VAR_002691
    Natural varianti227 – 2271F → C in XSCID.
    VAR_002692
    Natural varianti230 – 2301L → P in XSCID.
    VAR_002693
    Natural varianti231 – 2311C → Y in XSCID.
    VAR_002694
    Natural varianti232 – 2321G → R in XSCID.
    VAR_002695
    Natural varianti237 – 2371W → WQHW in XSCID. 1 Publication
    VAR_002696
    Natural varianti240 – 2401W → C in XSCID. 1 Publication
    VAR_002697
    Natural varianti241 – 2411S → I in XSCID. 1 Publication
    VAR_002698
    Natural varianti270 – 2701M → R in XSCID.
    VAR_002699
    Natural varianti285 – 2851R → Q in XSCID. 1 Publication
    VAR_002701
    X-linked combined immunodeficiency (XCID) [MIM:312863]: Less severe form of X-linked immunodeficiency with a less severe degree of deficiency in cellular and humoral immunity than that seen in XSCID.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti222 – 2221R → C in XCID. 1 Publication
    VAR_002688
    Natural varianti293 – 2931L → Q in XCID. 1 Publication
    VAR_002702

    Keywords - Diseasei

    Disease mutation, SCID

    Organism-specific databases

    MIMi300400. phenotype.
    312863. phenotype.
    Orphaneti39041. Omenn syndrome.
    276. T-B+ severe combined immunodeficiency due to gamma chain deficiency.
    PharmGKBiPA196.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 369347Cytokine receptor common subunit gammaPRO_0000010866Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi62 ↔ 72
    Glycosylationi71 – 711N-linked (GlcNAc...)2 Publications
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi84 – 841N-linked (GlcNAc...)2 Publications
    Disulfide bondi102 ↔ 115
    Glycosylationi159 – 1591N-linked (GlcNAc...)2 Publications
    Disulfide bondi182 ↔ 231
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Modified residuei292 – 2921Phosphothreonine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP31785.
    PaxDbiP31785.
    PRIDEiP31785.

    PTM databases

    PhosphoSiteiP31785.

    Miscellaneous databases

    PMAP-CutDBP31785.

    Expressioni

    Gene expression databases

    ArrayExpressiP31785.
    BgeeiP31785.
    CleanExiHS_IL2RG.
    GenevestigatoriP31785.

    Organism-specific databases

    HPAiHPA046641.

    Interactioni

    Subunit structurei

    The gamma subunit is common to the IL2, IL4, IL7, IL15, IL21 and probably also the IL13 receptors. Interacts with SHB upon interleukin stimulation. Interacts with HTLV-1 accessory protein p12I.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IL7P132322EBI-80475,EBI-80516

    Protein-protein interaction databases

    BioGridi109776. 11 interactions.
    DIPiDIP-173N.
    IntActiP31785. 8 interactions.
    MINTiMINT-1524852.
    STRINGi9606.ENSP00000276110.

    Structurei

    Secondary structure

    1
    369
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 655
    Turni66 – 683
    Beta strandi69 – 735
    Beta strandi78 – 814
    Beta strandi86 – 916
    Beta strandi94 – 963
    Beta strandi103 – 1086
    Beta strandi111 – 1188
    Helixi119 – 1213
    Beta strandi124 – 1263
    Beta strandi128 – 1336
    Beta strandi135 – 1373
    Beta strandi141 – 1466
    Helixi148 – 1503
    Beta strandi151 – 1533
    Beta strandi158 – 1669
    Beta strandi169 – 1757
    Helixi180 – 1823
    Beta strandi184 – 1918
    Beta strandi198 – 2025
    Beta strandi207 – 2104
    Beta strandi215 – 2173
    Beta strandi219 – 2268
    Beta strandi229 – 2313
    Beta strandi244 – 2463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ILLmodel-G57-248[»]
    1ILMmodel-G57-248[»]
    1ILNmodel-G57-248[»]
    1ITEmodel-B23-254[»]
    2B5IX-ray2.30C56-254[»]
    2ERJX-ray3.00C/G23-255[»]
    3BPLX-ray2.93C56-254[»]
    3QAZX-ray3.80C/F/I/L/O/R/U/X/a/d/g/j56-254[»]
    3QB7X-ray3.24C/D55-254[»]
    4GS7X-ray2.35C55-254[»]
    ProteinModelPortaliP31785.
    SMRiP31785. Positions 56-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31785.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 262240ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini284 – 36986CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei263 – 28321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini156 – 25398Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi237 – 2415WSXWS motif
    Motifi286 – 2949Box 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

    eggNOGiNOG43995.
    HOGENOMiHOG000276891.
    HOVERGENiHBG052111.
    InParanoidiP31785.
    KOiK05070.
    OMAiDHSWTEQ.
    OrthoDBiEOG7H4DV0.
    PhylomeDBiP31785.
    TreeFamiTF333657.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR013783. Ig-like_fold.
    IPR015321. IL-6_rcpt_alpha-bd.
    [Graphical view]
    PfamiPF00041. fn3. 1 hit.
    PF09240. IL6Ra-bind. 1 hit.
    [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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P31785-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLKPSLPFTS LLFLQLPLLG VGLNTTILTP NGNEDTTADF FLTTMPTDSL    50
    SVSTLPLPEV QCFVFNVEYM NCTWNSSSEP QPTNLTLHYW YKNSDNDKVQ 100
    KCSHYLFSEE ITSGCQLQKK EIHLYQTFVV QLQDPREPRR QATQMLKLQN 150
    LVIPWAPENL TLHKLSESQL ELNWNNRFLN HCLEHLVQYR TDWDHSWTEQ 200
    SVDYRHKFSL PSVDGQKRYT FRVRSRFNPL CGSAQHWSEW SHPIHWGSNT 250
    SKENPFLFAL EAVVISVGSM GLIISLLCVY FWLERTMPRI PTLKNLEDLV 300
    TEYHGNFSAW SGVSKGLAES LQPDYSERLC LVSEIPPKGG ALGEGPGASP 350
    CNQHSPYWAP PCYTLKPET 369
    Length:369
    Mass (Da):42,287
    Last modified:July 1, 1993 - v1
    Checksum:i3B6215246D610215
    GO
    Isoform 2 (identifier: P31785-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: MLKPSLPF → MGMKTPQL
         9-198: Missing.

    Show »
    Length:179
    Mass (Da):20,088
    Checksum:i4A3D790462553D0A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391D → N in XSCID. 1 Publication
    VAR_002668
    Natural varianti44 – 441T → S.
    Corresponds to variant rs7885041 [ dbSNP | Ensembl ].
    VAR_059301
    Natural varianti62 – 621C → G in XSCID.
    VAR_002669
    Natural varianti68 – 681E → G in XSCID.
    VAR_002670
    Natural varianti68 – 681E → K in XSCID. 1 Publication
    VAR_002671
    Natural varianti84 – 841N → K in XSCID.
    VAR_002672
    Natural varianti89 – 891Y → C in XSCID.
    VAR_002673
    Natural varianti105 – 1051Y → C in XSCID.
    VAR_002674
    Natural varianti109 – 1091E → K.1 Publication
    Corresponds to variant rs17875899 [ dbSNP | Ensembl ].
    VAR_020611
    Natural varianti114 – 1141G → D in XSCID. 1 Publication
    VAR_002675
    Natural varianti115 – 1151C → F in XSCID. 1 Publication
    VAR_002676
    Natural varianti115 – 1151C → R in XSCID; atypical. 1 Publication
    VAR_002677
    Natural varianti123 – 1231H → P in XSCID.
    VAR_002678
    Natural varianti125 – 1251Y → N in XSCID.
    VAR_002679
    Natural varianti144 – 1441Q → P in XSCID.
    VAR_002680
    Natural varianti153 – 1531I → N in XSCID. 1 Publication
    VAR_002681
    Natural varianti156 – 1561A → V in XSCID.
    VAR_002682
    Natural varianti162 – 1621L → H in XSCID. 1 Publication
    VAR_002683
    Natural varianti172 – 1721L → P in XSCID.
    VAR_002684
    Natural varianti172 – 1721L → Q in XSCID.
    VAR_002685
    Natural varianti182 – 1821C → R in XSCID.
    VAR_002686
    Natural varianti183 – 1831L → S in XSCID. 1 Publication
    VAR_002687
    Natural varianti222 – 2221R → C in XCID. 1 Publication
    VAR_002688
    Natural varianti224 – 2241R → W in XSCID. 1 Publication
    VAR_002689
    Natural varianti226 – 2261R → C in XSCID. 1 Publication
    VAR_002690
    Natural varianti226 – 2261R → H in XSCID. 1 Publication
    VAR_002691
    Natural varianti227 – 2271F → C in XSCID.
    VAR_002692
    Natural varianti230 – 2301L → P in XSCID.
    VAR_002693
    Natural varianti231 – 2311C → Y in XSCID.
    VAR_002694
    Natural varianti232 – 2321G → R in XSCID.
    VAR_002695
    Natural varianti237 – 2371W → WQHW in XSCID. 1 Publication
    VAR_002696
    Natural varianti240 – 2401W → C in XSCID. 1 Publication
    VAR_002697
    Natural varianti241 – 2411S → I in XSCID. 1 Publication
    VAR_002698
    Natural varianti270 – 2701M → R in XSCID.
    VAR_002699
    Natural varianti285 – 2851R → Q in XSCID. 1 Publication
    VAR_002701
    Natural varianti293 – 2931L → Q in XCID. 1 Publication
    VAR_002702

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 88MLKPSLPF → MGMKTPQL in isoform 2. 1 PublicationVSP_047581
    Alternative sequencei9 – 198190Missing in isoform 2. 1 PublicationVSP_047582Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11086 mRNA. Translation: BAA01857.1.
    L12183
    , L12178, L12176, L12177, L12179, L12180, L12181, L12182 Genomic DNA. Translation: AAA59145.1.
    L19546 Genomic DNA. Translation: AAC37524.1.
    AB102794 mRNA. Translation: BAD89385.1.
    AY692262 Genomic DNA. Translation: AAT85803.1.
    AL590764 Genomic DNA. No translation available.
    BC014972 mRNA. Translation: AAH14972.1.
    CCDSiCCDS14406.1. [P31785-1]
    PIRiA42565.
    RefSeqiNP_000197.1. NM_000206.2. [P31785-1]
    UniGeneiHs.84.

    Genome annotation databases

    EnsembliENST00000374202; ENSP00000363318; ENSG00000147168. [P31785-1]
    ENST00000456850; ENSP00000388967; ENSG00000147168. [P31785-2]
    GeneIDi3561.
    KEGGihsa:3561.
    UCSCiuc004dyw.2. human. [P31785-1]

    Polymorphism databases

    DMDMi400048.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    IL2RGbase

    X-linked SCID mutation database

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11086 mRNA. Translation: BAA01857.1 .
    L12183
    , L12178 , L12176 , L12177 , L12179 , L12180 , L12181 , L12182 Genomic DNA. Translation: AAA59145.1 .
    L19546 Genomic DNA. Translation: AAC37524.1 .
    AB102794 mRNA. Translation: BAD89385.1 .
    AY692262 Genomic DNA. Translation: AAT85803.1 .
    AL590764 Genomic DNA. No translation available.
    BC014972 mRNA. Translation: AAH14972.1 .
    CCDSi CCDS14406.1. [P31785-1 ]
    PIRi A42565.
    RefSeqi NP_000197.1. NM_000206.2. [P31785-1 ]
    UniGenei Hs.84.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ILL model - G 57-248 [» ]
    1ILM model - G 57-248 [» ]
    1ILN model - G 57-248 [» ]
    1ITE model - B 23-254 [» ]
    2B5I X-ray 2.30 C 56-254 [» ]
    2ERJ X-ray 3.00 C/G 23-255 [» ]
    3BPL X-ray 2.93 C 56-254 [» ]
    3QAZ X-ray 3.80 C/F/I/L/O/R/U/X/a/d/g/j 56-254 [» ]
    3QB7 X-ray 3.24 C/D 55-254 [» ]
    4GS7 X-ray 2.35 C 55-254 [» ]
    ProteinModelPortali P31785.
    SMRi P31785. Positions 56-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109776. 11 interactions.
    DIPi DIP-173N.
    IntActi P31785. 8 interactions.
    MINTi MINT-1524852.
    STRINGi 9606.ENSP00000276110.

    Chemistry

    BindingDBi P31785.
    ChEMBLi CHEMBL2364167.
    DrugBanki DB00041. Aldesleukin.
    DB00004. Denileukin diftitox.

    PTM databases

    PhosphoSitei P31785.

    Polymorphism databases

    DMDMi 400048.

    Proteomic databases

    MaxQBi P31785.
    PaxDbi P31785.
    PRIDEi P31785.

    Protocols and materials databases

    DNASUi 3561.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374202 ; ENSP00000363318 ; ENSG00000147168 . [P31785-1 ]
    ENST00000456850 ; ENSP00000388967 ; ENSG00000147168 . [P31785-2 ]
    GeneIDi 3561.
    KEGGi hsa:3561.
    UCSCi uc004dyw.2. human. [P31785-1 ]

    Organism-specific databases

    CTDi 3561.
    GeneCardsi GC0XM070327.
    GeneReviewsi IL2RG.
    HGNCi HGNC:6010. IL2RG.
    HPAi HPA046641.
    MIMi 300400. phenotype.
    308380. gene.
    312863. phenotype.
    neXtProti NX_P31785.
    Orphaneti 39041. Omenn syndrome.
    276. T-B+ severe combined immunodeficiency due to gamma chain deficiency.
    PharmGKBi PA196.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43995.
    HOGENOMi HOG000276891.
    HOVERGENi HBG052111.
    InParanoidi P31785.
    KOi K05070.
    OMAi DHSWTEQ.
    OrthoDBi EOG7H4DV0.
    PhylomeDBi P31785.
    TreeFami TF333657.

    Enzyme and pathway databases

    Reactomei REACT_115529. Interleukin-7 signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_27283. Interleukin-2 signaling.
    SignaLinki P31785.

    Miscellaneous databases

    ChiTaRSi IL2RG. human.
    EvolutionaryTracei P31785.
    GeneWikii Common_gamma_chain.
    GenomeRNAii 3561.
    NextBioi 13908.
    PMAP-CutDB P31785.
    PROi P31785.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31785.
    Bgeei P31785.
    CleanExi HS_IL2RG.
    Genevestigatori P31785.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR013783. Ig-like_fold.
    IPR015321. IL-6_rcpt_alpha-bd.
    [Graphical view ]
    Pfami PF00041. fn3. 1 hit.
    PF09240. IL6Ra-bind. 1 hit.
    [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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "Characterization of the human interleukin-2 receptor gamma chain gene."
      Noguchi M., Adelstein S., Cao X., Leonard W.J.
      J. Biol. Chem. 268:13601-13608(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    3. "The interleukin-2 receptor gamma chain maps to Xq13.1 and is mutated in X-linked severe combined immunodeficiency, SCIDX1."
      Puck J.M., Deschenes S.M., Porter J.C., Dutra A.S., Brown C.J., Willard H., Henthorn P.S.
      Hum. Mol. Genet. 2:1099-1104(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XSCID ASP-114 AND ASN-153.
    4. "IL2RG mRNA, nirs splice variant 2."
      Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. SeattleSNPs variation discovery resource
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-109.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: B-cell.
    8. "Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4."
      Kondo M., Takeshita T., Ishii N., Nakamura M., Watanabe S., Arai K., Sugamura K.
      Science 262:1874-1877(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A IL4R SUBUNIT.
    9. "Interleukin-2 receptor gamma chain: a functional component of the interleukin-4 receptor."
      Russell S.M., Kkegan A.D., Harada N., Nakamura Y., Noguchi M., Leland P., Friedmann M.C., Miyajima A., Puri R.K., Paul W.E., Leonard W.J.
      Science 262:1880-1883(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A IL4R SUBUNIT.
    10. "Interleukin-2 receptor gamma chain: a functional component of the interleukin-7 receptor."
      Noguchi M., Nakamura Y., Russell S.M., Ziegler S.F., Tsang M., Cao X., Leonard W.J.
      Science 262:1877-1880(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A IL7R SUBUNIT.
    11. "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.
    12. "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.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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 57-248.
    15. "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 56-254 IN COMPLEX WITH IL2; IL2RA AND IL2RB, DISULFIDE BONDS, GLYCOSYLATION AT ASN-71; ASN-84 AND ASN-159.
    16. "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 23-255 IN COMPLEX WITH IL2; IL2RA AND IL2RB, DISULFIDE BONDS, GLYCOSYLATION AT ASN-71; ASN-84 AND ASN-159.
    17. "Interleukin-2 (IL-2) receptor gamma chain mutations in X-linked severe combined immunodeficiency disease result in the loss of high-affinity IL-2 receptor binding."
      Disanto J.P., Dautry-Varsat A., Certain S., Fischer A., de Saint Basile G.
      Eur. J. Immunol. 24:475-479(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XSCID PHE-115; CYS-240 AND ILE-241.
    18. "Detection of three nonsense mutations and one missense mutation in the interleukin-2 receptor gamma chain gene in SCIDX1 that differently affect the mRNA processing."
      Markiewicz S., Subtil A., Dautry-Varsat A., Fischer A., de Saint Basile G.
      Genomics 21:291-293(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID LYS-68.
    19. "Impairment of ligand binding and growth signaling of mutant IL-2 receptor gamma-chains in patients with X-linked severe combined immunodeficiency."
      Ishii N., Asao H., Kimura Y., Takeshita T., Nakamura M., Tsuchiya S., Konno T., Maeda M., Uchiyama T., Sugamura K.
      J. Immunol. 153:1310-1317(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID HIS-162.
    20. "Defective human interleukin 2 receptor gamma chain in an atypical X chromosome-linked severe combined immunodeficiency with peripheral T cells."
      Disanto J.P., Rieux-Laucat F., Dautry-Varsat A., Fischer A., de Saint Basile G.
      Proc. Natl. Acad. Sci. U.S.A. 91:9466-9470(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID ASN-39.
    21. "Two mutational hotspots in the interleukin-2 receptor gamma chain gene causing human X-linked severe combined immunodeficiency."
      Pepper A.E., Buckley R.H., Small T.N., Puck J.M.
      Am. J. Hum. Genet. 57:564-571(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XSCID CYS-226 AND HIS-226.
    22. "Screening for mutations causing X-linked severe combined immunodeficiency in the IL-2R gamma chain gene by single-strand conformation polymorphism analysis."
      Clark P.A., Lester T., Genet S., Jones A.M., Hendriks R., Levinsky R.L., Kinnon C.
      Hum. Genet. 96:427-432(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID SER-183.
    23. "Female germ line mosaicism as the origin of a unique IL-2 receptor gamma-chain mutation causing X-linked severe combined immunodeficiency."
      Puck J.M., Pepper A.E., Bedard P.-M., Laframboise R.
      J. Clin. Invest. 95:895-899(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID GLN-HIS-TRP-237 INS.
    24. "Missense mutation in exon 7 of the common gamma chain gene causes a moderate form of X-linked combined immunodeficiency."
      Schmalstieg F.C., Leonard W.J., Noguchi M., Berg M., Rudloff H.E., Denney R.M., Dave S.K., Brooks E.G., Goldman A.S.
      J. Clin. Invest. 95:1169-1173(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XCID GLN-293.
    25. "Atypical X-linked severe combined immunodeficiency due to possible spontaneous reversion of the genetic defect in T cells."
      Stephan V., Wahn V., Le Deist F., Dirksen U., Broeker B., Mueller-Fleckenstein I., Horneff G., Schroten H., Fischer A., de Saint Basile G.
      N. Engl. J. Med. 335:1563-1567(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID ARG-115.
    26. "B-cell-negative severe combined immunodeficiency associated with a common gamma chain mutation."
      Jones A.M., Clark P.A., Katz F., Genet S., McMahon C., Alterman L., Cant A., Kinnon C.
      Hum. Genet. 99:677-680(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID GLN-285.
    27. "Maternal mosaicism for a novel interleukin-2 receptor gamma-chain mutation causing X-linked severe combined immunodeficiency in a Navajo kindred."
      O'Marcaigh A.S., Puck J.M., Pepper A.E., De Santes K., Cowan M.J.
      J. Clin. Immunol. 17:29-33(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XSCID TRP-224.
    28. "An interleukin-2 receptor gamma chain mutation with normal thymus morphology."
      Sharfe N., Shahar M., Roifman C.M.
      J. Clin. Invest. 100:3036-3043(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XCID CYS-222.

    Entry informationi

    Entry nameiIL2RG_HUMAN
    AccessioniPrimary (citable) accession number: P31785
    Secondary accession number(s): Q5FC12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 174 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome X
      Human chromosome X: 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