IL2RG_HUMAN
ID IL2RG_HUMAN Reviewed; 369 AA.
AC P31785; Q5FC12;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Cytokine receptor common subunit gamma;
DE AltName: Full=Interleukin-2 receptor subunit gamma;
DE Short=IL-2 receptor subunit gamma;
DE Short=IL-2R subunit gamma;
DE Short=IL-2RG;
DE AltName: Full=gammaC;
DE AltName: Full=p64;
DE AltName: CD_antigen=CD132;
DE Flags: Precursor;
GN Name=IL2RG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1631559; DOI=10.1126/science.1631559;
RA Takeshita T., Asao H., Ohtani K., Ishii N., Kumaki S., Tanaka N.,
RA Munakata H., Nakamura M., Sugamura K.;
RT "Cloning of the gamma chain of the human IL-2 receptor.";
RL Science 257:379-382(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8514792; DOI=10.1016/s0021-9258(19)38691-0;
RA Noguchi M., Adelstein S., Cao X., Leonard W.J.;
RT "Characterization of the human interleukin-2 receptor gamma chain gene.";
RL J. Biol. Chem. 268:13601-13608(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS XSCID ASP-114 AND ASN-153.
RX PubMed=8401490; DOI=10.1093/hmg/2.8.1099;
RA Puck J.M., Deschenes S.M., Porter J.C., Dutra A.S., Brown C.J., Willard H.,
RA Henthorn P.S.;
RT "The interleukin-2 receptor gamma chain maps to Xq13.1 and is mutated in X-
RT linked severe combined immunodeficiency, SCIDX1.";
RL Hum. Mol. Genet. 2:1099-1104(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S.,
RA Furuya T., Saito T.;
RT "IL2RG mRNA, nirs splice variant 2.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-109.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION AS A IL4R SUBUNIT.
RX PubMed=8266076; DOI=10.1126/science.8266076;
RA Kondo M., Takeshita T., Ishii N., Nakamura M., Watanabe S., Arai K.,
RA Sugamura K.;
RT "Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors
RT for IL-2 and IL-4.";
RL Science 262:1874-1877(1993).
RN [9]
RP IDENTIFICATION AS A IL4R SUBUNIT.
RX PubMed=8266078; DOI=10.1126/science.8266078;
RA Russell S.M., Kkegan A.D., Harada N., Nakamura Y., Noguchi M., Leland P.,
RA Friedmann M.C., Miyajima A., Puri R.K., Paul W.E., Leonard W.J.;
RT "Interleukin-2 receptor gamma chain: a functional component of the
RT interleukin-4 receptor.";
RL Science 262:1880-1883(1993).
RN [10]
RP IDENTIFICATION AS A IL7R SUBUNIT.
RX PubMed=8266077; DOI=10.1126/science.8266077;
RA Noguchi M., Nakamura Y., Russell S.M., Ziegler S.F., Tsang M., Cao X.,
RA Leonard W.J.;
RT "Interleukin-2 receptor gamma chain: a functional component of the
RT interleukin-7 receptor.";
RL Science 262:1877-1880(1993).
RN [11]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
RX PubMed=8648694; DOI=10.1128/jvi.70.6.3599-3605.1996;
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 bind the
RT interleukin-2 receptor beta and gammac chains and affects their expression
RT on the cell surface.";
RL J. Virol. 70:3599-3605(1996).
RN [12]
RP INTERACTION WITH SHB.
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 [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15123770; DOI=10.1189/jlb.0605298;
RA Ratthe C., Girard D.;
RT "Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent
RT mechanism: importance of the IL-15Ralpha chain.";
RL J. Leukoc. Biol. 76:162-168(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP 3D-STRUCTURE MODELING OF 57-248.
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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 56-254 IN COMPLEX WITH IL2; IL2RA
RP AND IL2RB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71; ASN-84 AND
RP ASN-159.
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, beta,
RT and gammac receptors.";
RL Science 310:1159-1163(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 23-255 IN COMPLEX WITH IL2; IL2RA
RP AND IL2RB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71; ASN-84 AND
RP ASN-159.
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).
RN [18]
RP VARIANTS XSCID PHE-115; CYS-240 AND ILE-241.
RX PubMed=8299698; DOI=10.1002/eji.1830240232;
RA Disanto J.P., Dautry-Varsat A., Certain S., Fischer A., de Saint Basile G.;
RT "Interleukin-2 (IL-2) receptor gamma chain mutations in X-linked severe
RT combined immunodeficiency disease result in the loss of high-affinity IL-2
RT receptor binding.";
RL Eur. J. Immunol. 24:475-479(1994).
RN [19]
RP VARIANT XSCID LYS-68.
RX PubMed=8088810; DOI=10.1006/geno.1994.1265;
RA Markiewicz S., Subtil A., Dautry-Varsat A., Fischer A., de Saint Basile G.;
RT "Detection of three nonsense mutations and one missense mutation in the
RT interleukin-2 receptor gamma chain gene in SCIDX1 that differently affect
RT the mRNA processing.";
RL Genomics 21:291-293(1994).
RN [20]
RP VARIANT XSCID HIS-162.
RX PubMed=8027558;
RA Ishii N., Asao H., Kimura Y., Takeshita T., Nakamura M., Tsuchiya S.,
RA Konno T., Maeda M., Uchiyama T., Sugamura K.;
RT "Impairment of ligand binding and growth signaling of mutant IL-2 receptor
RT gamma-chains in patients with X-linked severe combined immunodeficiency.";
RL J. Immunol. 153:1310-1317(1994).
RN [21]
RP VARIANT XSCID ASN-39.
RX PubMed=7937790; DOI=10.1073/pnas.91.20.9466;
RA Disanto J.P., Rieux-Laucat F., Dautry-Varsat A., Fischer A.,
RA de Saint Basile G.;
RT "Defective human interleukin 2 receptor gamma chain in an atypical X
RT chromosome-linked severe combined immunodeficiency with peripheral T
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9466-9470(1994).
RN [22]
RP VARIANTS XSCID CYS-226 AND HIS-226.
RX PubMed=7668284;
RA Pepper A.E., Buckley R.H., Small T.N., Puck J.M.;
RT "Two mutational hotspots in the interleukin-2 receptor gamma chain gene
RT causing human X-linked severe combined immunodeficiency.";
RL Am. J. Hum. Genet. 57:564-571(1995).
RN [23]
RP VARIANT XSCID SER-183.
RX PubMed=7557965; DOI=10.1007/bf00191801;
RA Clark P.A., Lester T., Genet S., Jones A.M., Hendriks R., Levinsky R.L.,
RA Kinnon C.;
RT "Screening for mutations causing X-linked severe combined immunodeficiency
RT in the IL-2R gamma chain gene by single-strand conformation polymorphism
RT analysis.";
RL Hum. Genet. 96:427-432(1995).
RN [24]
RP VARIANT XSCID GLN-HIS-TRP-237 INS.
RX PubMed=7860773; DOI=10.1172/jci117740;
RA Puck J.M., Pepper A.E., Bedard P.-M., Laframboise R.;
RT "Female germ line mosaicism as the origin of a unique IL-2 receptor gamma-
RT chain mutation causing X-linked severe combined immunodeficiency.";
RL J. Clin. Invest. 95:895-899(1995).
RN [25]
RP VARIANT XCID GLN-293.
RX PubMed=7883965; DOI=10.1172/jci117765;
RA Schmalstieg F.C., Leonard W.J., Noguchi M., Berg M., Rudloff H.E.,
RA Denney R.M., Dave S.K., Brooks E.G., Goldman A.S.;
RT "Missense mutation in exon 7 of the common gamma chain gene causes a
RT moderate form of X-linked combined immunodeficiency.";
RL J. Clin. Invest. 95:1169-1173(1995).
RN [26]
RP VARIANT XSCID ARG-115.
RX PubMed=8900089; DOI=10.1056/nejm199611213352104;
RA Stephan V., Wahn V., Le Deist F., Dirksen U., Broeker B.,
RA Mueller-Fleckenstein I., Horneff G., Schroten H., Fischer A.,
RA de Saint Basile G.;
RT "Atypical X-linked severe combined immunodeficiency due to possible
RT spontaneous reversion of the genetic defect in T cells.";
RL N. Engl. J. Med. 335:1563-1567(1996).
RN [27]
RP VARIANT XSCID GLN-285.
RX PubMed=9150740; DOI=10.1007/s004390050428;
RA Jones A.M., Clark P.A., Katz F., Genet S., McMahon C., Alterman L.,
RA Cant A., Kinnon C.;
RT "B-cell-negative severe combined immunodeficiency associated with a common
RT gamma chain mutation.";
RL Hum. Genet. 99:677-680(1997).
RN [28]
RP VARIANT XSCID TRP-224.
RX PubMed=9049783; DOI=10.1023/a:1027332327827;
RA O'Marcaigh A.S., Puck J.M., Pepper A.E., De Santes K., Cowan M.J.;
RT "Maternal mosaicism for a novel interleukin-2 receptor gamma-chain mutation
RT causing X-linked severe combined immunodeficiency in a Navajo kindred.";
RL J. Clin. Immunol. 17:29-33(1997).
RN [29]
RP VARIANT XCID CYS-222.
RX PubMed=9399950; DOI=10.1172/jci119858;
RA Sharfe N., Shahar M., Roifman C.M.;
RT "An interleukin-2 receptor gamma chain mutation with normal thymus
RT morphology.";
RL J. Clin. Invest. 100:3036-3043(1997).
CC -!- FUNCTION: Common subunit for the receptors for a variety of
CC interleukins. Probably in association with IL15RA, involved in the
CC stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770).
CC {ECO:0000269|PubMed:15123770}.
CC -!- SUBUNIT: The gamma subunit is common to the IL2, IL4, IL7, IL15, IL21
CC and probably also the IL13 receptors. Interacts with SHB upon
CC interleukin stimulation. Interacts with IL9 (By similarity).
CC {ECO:0000250|UniProtKB:P34902, ECO:0000269|PubMed:12200137,
CC ECO:0000269|PubMed:16293754, ECO:0000269|PubMed:16477002}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein
CC p12I. {ECO:0000269|PubMed:8648694}.
CC -!- INTERACTION:
CC P31785; P13232: IL7; NbExp=2; IntAct=EBI-80475, EBI-80516;
CC P31785; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-80475, EBI-10171774;
CC P31785; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-80475, EBI-11987425;
CC P31785; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-80475, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15123770};
CC Single-pass type I membrane protein {ECO:0000255}. Cell surface
CC {ECO:0000269|PubMed:15123770}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31785-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31785-2; Sequence=VSP_047581, VSP_047582;
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- DISEASE: Severe combined immunodeficiency X-linked T-cell-negative/B-
CC cell-positive/NK-cell-negative (XSCID) [MIM:300400]: A form of severe
CC combined immunodeficiency (SCID), a genetically and clinically
CC heterogeneous group of rare congenital disorders characterized by
CC impairment of both humoral and cell-mediated immunity, leukopenia, and
CC low or absent antibody levels. Patients present in infancy recurrent,
CC persistent infections by opportunistic organisms. The common
CC characteristic of all types of SCID is absence of T-cell-mediated
CC cellular immunity due to a defect in T-cell development.
CC {ECO:0000269|PubMed:7557965, ECO:0000269|PubMed:7668284,
CC ECO:0000269|PubMed:7860773, ECO:0000269|PubMed:7937790,
CC ECO:0000269|PubMed:8027558, ECO:0000269|PubMed:8088810,
CC ECO:0000269|PubMed:8299698, ECO:0000269|PubMed:8401490,
CC ECO:0000269|PubMed:8900089, ECO:0000269|PubMed:9049783,
CC ECO:0000269|PubMed:9150740}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: X-linked combined immunodeficiency (XCID) [MIM:312863]: Less
CC severe form of X-linked immunodeficiency with a less severe degree of
CC deficiency in cellular and humoral immunity than that seen in XSCID.
CC {ECO:0000269|PubMed:7883965, ECO:0000269|PubMed:9399950}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=IL2RGbase; Note=X-linked SCID mutation database;
CC URL="http://research.nhgri.nih.gov/scid/";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il2rg/";
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DR EMBL; D11086; BAA01857.1; -; mRNA.
DR EMBL; L12183; AAA59145.1; -; Genomic_DNA.
DR EMBL; L12178; AAA59145.1; JOINED; Genomic_DNA.
DR EMBL; L12176; AAA59145.1; JOINED; Genomic_DNA.
DR EMBL; L12177; AAA59145.1; JOINED; Genomic_DNA.
DR EMBL; L12179; AAA59145.1; JOINED; Genomic_DNA.
DR EMBL; L12180; AAA59145.1; JOINED; Genomic_DNA.
DR EMBL; L12181; AAA59145.1; JOINED; Genomic_DNA.
DR EMBL; L12182; AAA59145.1; JOINED; Genomic_DNA.
DR EMBL; L19546; AAC37524.1; -; Genomic_DNA.
DR EMBL; AB102794; BAD89385.1; -; mRNA.
DR EMBL; AY692262; AAT85803.1; -; Genomic_DNA.
DR EMBL; AL590764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014972; AAH14972.1; -; mRNA.
DR CCDS; CCDS14406.1; -. [P31785-1]
DR PIR; A42565; A42565.
DR RefSeq; NP_000197.1; NM_000206.2. [P31785-1]
DR PDB; 2B5I; X-ray; 2.30 A; C=56-254.
DR PDB; 2ERJ; X-ray; 3.00 A; C/G=23-255.
DR PDB; 3BPL; X-ray; 2.93 A; C=56-254.
DR PDB; 3QAZ; X-ray; 3.80 A; C/F/I/L/O/R/U/X/a/d/g/j=56-254.
DR PDB; 3QB7; X-ray; 3.24 A; C/D=55-254.
DR PDB; 4GS7; X-ray; 2.35 A; C=55-254.
DR PDB; 5M5E; X-ray; 2.30 A; C=23-262.
DR PDB; 6OEL; X-ray; 3.10 A; C=61-249.
DR PDB; 7S2R; X-ray; 2.49 A; A=54-254.
DR PDBsum; 2B5I; -.
DR PDBsum; 2ERJ; -.
DR PDBsum; 3BPL; -.
DR PDBsum; 3QAZ; -.
DR PDBsum; 3QB7; -.
DR PDBsum; 4GS7; -.
DR PDBsum; 5M5E; -.
DR PDBsum; 6OEL; -.
DR PDBsum; 7S2R; -.
DR AlphaFoldDB; P31785; -.
DR SMR; P31785; -.
DR BioGRID; 109776; 26.
DR CORUM; P31785; -.
DR DIP; DIP-173N; -.
DR IntAct; P31785; 18.
DR STRING; 9606.ENSP00000363318; -.
DR ChEMBL; CHEMBL2364167; -.
DR ChEMBL; CHEMBL4665588; -.
DR ChEMBL; CHEMBL4665592; -.
DR DrugBank; DB00041; Aldesleukin.
DR DrugBank; DB00004; Denileukin diftitox.
DR DrugBank; DB05943; Resatorvid.
DR DrugCentral; P31785; -.
DR GuidetoPHARMACOLOGY; 2303; -.
DR GlyGen; P31785; 8 sites.
DR iPTMnet; P31785; -.
DR PhosphoSitePlus; P31785; -.
DR BioMuta; IL2RG; -.
DR DMDM; 400048; -.
DR EPD; P31785; -.
DR MassIVE; P31785; -.
DR MaxQB; P31785; -.
DR PaxDb; P31785; -.
DR PeptideAtlas; P31785; -.
DR PRIDE; P31785; -.
DR ProteomicsDB; 54802; -. [P31785-1]
DR ProteomicsDB; 62802; -.
DR ABCD; P31785; 1 sequenced antibody.
DR Antibodypedia; 27479; 640 antibodies from 36 providers.
DR CPTC; P31785; 1 antibody.
DR DNASU; 3561; -.
DR Ensembl; ENST00000374202.7; ENSP00000363318.3; ENSG00000147168.13. [P31785-1]
DR Ensembl; ENST00000456850.6; ENSP00000388967.2; ENSG00000147168.13. [P31785-2]
DR GeneID; 3561; -.
DR KEGG; hsa:3561; -.
DR MANE-Select; ENST00000374202.7; ENSP00000363318.3; NM_000206.3; NP_000197.1.
DR UCSC; uc004dyw.4; human. [P31785-1]
DR CTD; 3561; -.
DR DisGeNET; 3561; -.
DR GeneCards; IL2RG; -.
DR GeneReviews; IL2RG; -.
DR HGNC; HGNC:6010; IL2RG.
DR HPA; ENSG00000147168; Tissue enhanced (intestine, lymphoid tissue).
DR MalaCards; IL2RG; -.
DR MIM; 300400; phenotype.
DR MIM; 308380; gene.
DR MIM; 312863; phenotype.
DR neXtProt; NX_P31785; -.
DR OpenTargets; ENSG00000147168; -.
DR Orphanet; 39041; Omenn syndrome.
DR Orphanet; 276; T-B+ severe combined immunodeficiency due to gamma chain deficiency.
DR PharmGKB; PA196; -.
DR VEuPathDB; HostDB:ENSG00000147168; -.
DR eggNOG; ENOG502S289; Eukaryota.
DR GeneTree; ENSGT00510000048979; -.
DR HOGENOM; CLU_060544_1_0_1; -.
DR InParanoid; P31785; -.
DR OMA; NKDTSWT; -.
DR OrthoDB; 753404at2759; -.
DR PhylomeDB; P31785; -.
DR TreeFam; TF333657; -.
DR PathwayCommons; P31785; -.
DR Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR Reactome; R-HSA-8985947; Interleukin-9 signaling.
DR Reactome; R-HSA-9020558; Interleukin-2 signaling.
DR Reactome; R-HSA-9020958; Interleukin-21 signaling.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling.
DR SignaLink; P31785; -.
DR SIGNOR; P31785; -.
DR BioGRID-ORCS; 3561; 11 hits in 706 CRISPR screens.
DR ChiTaRS; IL2RG; human.
DR EvolutionaryTrace; P31785; -.
DR GeneWiki; Common_gamma_chain; -.
DR GenomeRNAi; 3561; -.
DR Pharos; P31785; Tclin.
DR PRO; PR:P31785; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P31785; protein.
DR Bgee; ENSG00000147168; Expressed in granulocyte and 149 other tissues.
DR ExpressionAtlas; P31785; baseline and differential.
DR Genevisible; P31785; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0042010; F:interleukin-15 receptor activity; IDA:UniProtKB.
DR GO; GO:0019976; F:interleukin-2 binding; ISS:UniProtKB.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IEA:GOC.
DR GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IEA:GOC.
DR GO; GO:0038111; P:interleukin-7-mediated signaling pathway; IEA:GOC.
DR GO; GO:0002335; P:mature B cell differentiation; IEA:Ensembl.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF09240; IL6Ra-bind; 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; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; SCID; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT CHAIN 23..369
FT /note="Cytokine receptor common subunit gamma"
FT /id="PRO_0000010866"
FT TOPO_DOM 23..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 156..253
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 237..241
FT /note="WSXWS motif"
FT MOTIF 286..294
FT /note="Box 1 motif"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16293754,
FT ECO:0000269|PubMed:16477002"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16293754,
FT ECO:0000269|PubMed:16477002"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16293754,
FT ECO:0000269|PubMed:16477002"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..72
FT DISULFID 102..115
FT DISULFID 182..231
FT VAR_SEQ 1..8
FT /note="MLKPSLPF -> MGMKTPQL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047581"
FT VAR_SEQ 9..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047582"
FT VARIANT 39
FT /note="D -> N (in XSCID)"
FT /evidence="ECO:0000269|PubMed:7937790"
FT /id="VAR_002668"
FT VARIANT 44
FT /note="T -> S (in dbSNP:rs7885041)"
FT /id="VAR_059301"
FT VARIANT 62
FT /note="C -> G (in XSCID)"
FT /id="VAR_002669"
FT VARIANT 68
FT /note="E -> G (in XSCID)"
FT /id="VAR_002670"
FT VARIANT 68
FT /note="E -> K (in XSCID; dbSNP:rs1057520644)"
FT /evidence="ECO:0000269|PubMed:8088810"
FT /id="VAR_002671"
FT VARIANT 84
FT /note="N -> K (in XSCID)"
FT /id="VAR_002672"
FT VARIANT 89
FT /note="Y -> C (in XSCID)"
FT /id="VAR_002673"
FT VARIANT 105
FT /note="Y -> C (in XSCID; dbSNP:rs193922347)"
FT /id="VAR_002674"
FT VARIANT 109
FT /note="E -> K (in dbSNP:rs17875899)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020611"
FT VARIANT 114
FT /note="G -> D (in XSCID; dbSNP:rs111033620)"
FT /evidence="ECO:0000269|PubMed:8401490"
FT /id="VAR_002675"
FT VARIANT 115
FT /note="C -> F (in XSCID)"
FT /evidence="ECO:0000269|PubMed:8299698"
FT /id="VAR_002676"
FT VARIANT 115
FT /note="C -> R (in XSCID; atypical; dbSNP:rs111033622)"
FT /evidence="ECO:0000269|PubMed:8900089"
FT /id="VAR_002677"
FT VARIANT 123
FT /note="H -> P (in XSCID)"
FT /id="VAR_002678"
FT VARIANT 125
FT /note="Y -> N (in XSCID)"
FT /id="VAR_002679"
FT VARIANT 144
FT /note="Q -> P (in XSCID)"
FT /id="VAR_002680"
FT VARIANT 153
FT /note="I -> N (in XSCID; dbSNP:rs111033621)"
FT /evidence="ECO:0000269|PubMed:8401490"
FT /id="VAR_002681"
FT VARIANT 156
FT /note="A -> V (in XSCID; dbSNP:rs1057521062)"
FT /id="VAR_002682"
FT VARIANT 162
FT /note="L -> H (in XSCID)"
FT /evidence="ECO:0000269|PubMed:8027558"
FT /id="VAR_002683"
FT VARIANT 172
FT /note="L -> P (in XSCID)"
FT /id="VAR_002684"
FT VARIANT 172
FT /note="L -> Q (in XSCID)"
FT /id="VAR_002685"
FT VARIANT 182
FT /note="C -> R (in XSCID)"
FT /id="VAR_002686"
FT VARIANT 183
FT /note="L -> S (in XSCID)"
FT /evidence="ECO:0000269|PubMed:7557965"
FT /id="VAR_002687"
FT VARIANT 222
FT /note="R -> C (in XCID; dbSNP:rs111033618)"
FT /evidence="ECO:0000269|PubMed:9399950"
FT /id="VAR_002688"
FT VARIANT 224
FT /note="R -> W (in XSCID; dbSNP:rs869320658)"
FT /evidence="ECO:0000269|PubMed:9049783"
FT /id="VAR_002689"
FT VARIANT 226
FT /note="R -> C (in XSCID; dbSNP:rs869320659)"
FT /evidence="ECO:0000269|PubMed:7668284"
FT /id="VAR_002690"
FT VARIANT 226
FT /note="R -> H (in XSCID; dbSNP:rs869320660)"
FT /evidence="ECO:0000269|PubMed:7668284"
FT /id="VAR_002691"
FT VARIANT 227
FT /note="F -> C (in XSCID)"
FT /id="VAR_002692"
FT VARIANT 230
FT /note="L -> P (in XSCID)"
FT /id="VAR_002693"
FT VARIANT 231
FT /note="C -> Y (in XSCID)"
FT /id="VAR_002694"
FT VARIANT 232
FT /note="G -> R (in XSCID; dbSNP:rs1569479909)"
FT /id="VAR_002695"
FT VARIANT 237
FT /note="W -> WQHW (in XSCID)"
FT /evidence="ECO:0000269|PubMed:7860773"
FT /id="VAR_002696"
FT VARIANT 240
FT /note="W -> C (in XSCID)"
FT /evidence="ECO:0000269|PubMed:8299698"
FT /id="VAR_002697"
FT VARIANT 241
FT /note="S -> I (in XSCID)"
FT /evidence="ECO:0000269|PubMed:8299698"
FT /id="VAR_002698"
FT VARIANT 270
FT /note="M -> R (in XSCID)"
FT /id="VAR_002699"
FT VARIANT 285
FT /note="R -> Q (in XSCID; dbSNP:rs111033617)"
FT /evidence="ECO:0000269|PubMed:9150740"
FT /id="VAR_002701"
FT VARIANT 293
FT /note="L -> Q (in XCID; dbSNP:rs137852510)"
FT /evidence="ECO:0000269|PubMed:7883965"
FT /id="VAR_002702"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2B5I"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4GS7"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:2B5I"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3BPL"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4GS7"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2B5I"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2B5I"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5M5E"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3QB7"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2B5I"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2B5I"
SQ SEQUENCE 369 AA; 42287 MW; 3B6215246D610215 CRC64;
MLKPSLPFTS LLFLQLPLLG VGLNTTILTP NGNEDTTADF FLTTMPTDSL SVSTLPLPEV
QCFVFNVEYM NCTWNSSSEP QPTNLTLHYW YKNSDNDKVQ KCSHYLFSEE ITSGCQLQKK
EIHLYQTFVV QLQDPREPRR QATQMLKLQN LVIPWAPENL TLHKLSESQL ELNWNNRFLN
HCLEHLVQYR TDWDHSWTEQ SVDYRHKFSL PSVDGQKRYT FRVRSRFNPL CGSAQHWSEW
SHPIHWGSNT SKENPFLFAL EAVVISVGSM GLIISLLCVY FWLERTMPRI PTLKNLEDLV
TEYHGNFSAW SGVSKGLAES LQPDYSERLC LVSEIPPKGG ALGEGPGASP CNQHSPYWAP
PCYTLKPET
