P31785 (IL2RG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

IL2RG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Common subunit for the receptors for a variety of interleukins.
Subunit structure	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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Membrane; Single-pass type I membrane protein.
Domain	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.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.26
Sequence similarities	Belongs to the type I cytokine receptor family. Type 5 subfamily. Contains 1 fibronectin type-III domain.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation SCID
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	immune response Traceable author statement Ref.7. Source: ProtInc interleukin-2-mediated signaling pathway Traceable author statement Ref.6. Source: GOC interleukin-4-mediated signaling pathway Traceable author statement Ref.7. Source: GOC interleukin-7-mediated signaling pathway Traceable author statement Ref.8. Source: GOC virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	external side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	cytokine receptor activity Inferred from electronic annotation. Source: InterPro interleukin-2 binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IL7	P13232	2	EBI-80475,EBI-80516

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 369

347

Cytokine receptor common subunit gamma

PRO_0000010866

Regions

Topological domain

23 – 262

240

Extracellular Potential

Transmembrane

263 – 283

21

Helical; Potential

Topological domain

284 – 369

86

Cytoplasmic Potential

Domain

154 – 241

88

Fibronectin type-III

Motif

237 – 241

5

WSXWS motif

Motif

286 – 294

9

Box 1 motif

Amino acid modifications

Modified residue

161

1

Phosphothreonine By similarity

Modified residue

292

1

Phosphothreonine Ref.11

Modified residue

325

1

Phosphotyrosine By similarity

Glycosylation

24

1

N-linked (GlcNAc...) Potential

Glycosylation

71

1

N-linked (GlcNAc...) Ref.13 Ref.14

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

84

1

N-linked (GlcNAc...) Ref.13 Ref.14

Glycosylation

159

1

N-linked (GlcNAc...) Ref.13 Ref.14

Glycosylation

249

1

N-linked (GlcNAc...) Potential

Disulfide bond

62 ↔ 72

Ref.13 Ref.14

Disulfide bond

102 ↔ 115

Ref.13 Ref.14

Disulfide bond

182 ↔ 231

Ref.13 Ref.14

Natural variations

Natural variant

39

1

D → N in XSCID. Ref.18

VAR_002668

Natural variant

44

1

T → S.
Corresponds to variant rs7885041 [ dbSNP | Ensembl ].

VAR_059301

Natural variant

62

1

C → G in XSCID.

VAR_002669

Natural variant

68

1

E → G in XSCID.

VAR_002670

Natural variant

68

1

E → K in XSCID. Ref.16

VAR_002671

Natural variant

84

1

N → K in XSCID.

VAR_002672

Natural variant

89

1

Y → C in XSCID.

VAR_002673

Natural variant

105

1

Y → C in XSCID.

VAR_002674

Natural variant

109

1

E → K. Ref.4
Corresponds to variant rs17875899 [ dbSNP | Ensembl ].

VAR_020611

Natural variant

114

1

G → D in XSCID. Ref.3

VAR_002675

Natural variant

115

1

C → F in XSCID. Ref.15

VAR_002676

Natural variant

115

1

C → R in XSCID; atypical. Ref.23

VAR_002677

Natural variant

123

1

H → P in XSCID.

VAR_002678

Natural variant

125

1

Y → N in XSCID.

VAR_002679

Natural variant

144

1

Q → P in XSCID.

VAR_002680

Natural variant

153

1

I → N in XSCID. Ref.3

VAR_002681

Natural variant

156

1

A → V in XSCID.

VAR_002682

Natural variant

162

1

L → H in XSCID. Ref.17

VAR_002683

Natural variant

172

1

L → P in XSCID.

VAR_002684

Natural variant

172

1

L → Q in XSCID.

VAR_002685

Natural variant

182

1

C → R in XSCID.

VAR_002686

Natural variant

183

1

L → S in XSCID. Ref.20

VAR_002687

Natural variant

222

1

R → C in XCID. Ref.26

VAR_002688

Natural variant

224

1

R → W in XSCID. Ref.25

VAR_002689

Natural variant

226

1

R → C in XSCID. Ref.19

VAR_002690

Natural variant

226

1

R → H in XSCID. Ref.19

VAR_002691

Natural variant

227

1

F → C in XSCID.

VAR_002692

Natural variant

230

1

L → P in XSCID.

VAR_002693

Natural variant

231

1

C → Y in XSCID.

VAR_002694

Natural variant

232

1

G → R in XSCID.

VAR_002695

Natural variant

237

1

W → WQHW in XSCID.

VAR_002696

Natural variant

240

1

W → C in XSCID. Ref.15

VAR_002697

Natural variant

241

1

S → I in XSCID. Ref.15

VAR_002698

Natural variant

270

1

M → R in XSCID.

VAR_002699

Natural variant

285

1

R → Q in XSCID. Ref.24

VAR_002701

Natural variant

293

1

L → Q in XCID. Ref.22

VAR_002702

Secondary structure

1

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369

Helix Strand Turn

Details...

Beta strand

61 – 65

5

Turn

66 – 68

3

Beta strand

69 – 73

5

Beta strand

78 – 81

4

Beta strand

86 – 91

6

Beta strand

94 – 96

3

Beta strand

103 – 108

6

Beta strand

111 – 118

8

Helix

119 – 121

3

Beta strand

124 – 126

3

Beta strand

128 – 133

6

Beta strand

135 – 137

3

Beta strand

141 – 146

6

Helix

148 – 150

3

Beta strand

151 – 153

3

Beta strand

158 – 166

9

Beta strand

169 – 175

7

Helix

180 – 182

3

Beta strand

184 – 191

8

Beta strand

198 – 202

5

Beta strand

207 – 210

4

Beta strand

215 – 217

3

Beta strand

219 – 226

8

Beta strand

229 – 231

3

Beta strand

244 – 246

3

Sequences

	Sequence		Length	Mass (Da)
	P31785 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 3B6215246D610215	FASTA	369	42,287
	10 20 30 40 50 60 MLKPSLPFTS LLFLQLPLLG VGLNTTILTP NGNEDTTADF FLTTMPTDSL SVSTLPLPEV 70 80 90 100 110 120 QCFVFNVEYM NCTWNSSSEP QPTNLTLHYW YKNSDNDKVQ KCSHYLFSEE ITSGCQLQKK 130 140 150 160 170 180 EIHLYQTFVV QLQDPREPRR QATQMLKLQN LVIPWAPENL TLHKLSESQL ELNWNNRFLN 190 200 210 220 230 240 HCLEHLVQYR TDWDHSWTEQ SVDYRHKFSL PSVDGQKRYT FRVRSRFNPL CGSAQHWSEW 250 260 270 280 290 300 SHPIHWGSNT SKENPFLFAL EAVVISVGSM GLIISLLCVY FWLERTMPRI PTLKNLEDLV 310 320 330 340 350 360 TEYHGNFSAW SGVSKGLAES LQPDYSERLC LVSEIPPKGG ALGEGPGASP CNQHSPYWAP PCYTLKPET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the gamma chain of the human IL-2 receptor." Takeshita T., Asao H., Ohtani K., Ishii N., Kumaki S., Tanaka N., Munakata H., Nakamura M., Sugamura K. Science 257:379-382(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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]	SeattleSNPs variation discovery resource Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-109.
[5]	"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: B-cell.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
+	Additional computationally mapped references.

Web resources

IL2RGbase

X-linked SCID mutation database

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D11086 mRNA. Translation: BAA01857.1.
L12183 , L12178, L12176, L12177, L12179, L12180, L12181, L12182 Genomic DNA. Translation: AAA59145.1.
L19546 Genomic DNA. Translation: AAC37524.1.
AY692262 Genomic DNA. Translation: AAT85803.1.
BC014972 mRNA. Translation: AAH14972.1.

IPI

IPI00012899.

PIR

A42565.

RefSeq

NP_000197.1. NM_000206.2.

UniGene

Hs.84.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P31785.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-173N.

IntAct

P31785. 8 interactions.

MINT

MINT-1524852.

STRING

9606.ENSP00000276110.

PTM databases

PhosphoSite

P31785.

Polymorphism databases

DMDM

400048.

Proteomic databases

PaxDb

P31785.

PRIDE

P31785.

Protocols and materials databases

DNASU

3561.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374202; ENSP00000363318; ENSG00000147168.

GeneID

3561.

KEGG

hsa:3561.

UCSC

uc004dyw.2. human.

Organism-specific databases

CTD

3561.

GeneCards

GC0XM070327.

HGNC

HGNC:6010. IL2RG.

HPA

HPA046641.

MIM

300400. phenotype.
308380. gene.
312863. phenotype.

neXtProt

NX_P31785.

Orphanet

39041. Omenn syndrome.
276. Severe combined immunodeficiency T- B+ due to gamma chain deficiency.

PharmGKB

PA196.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43995.

HOGENOM

HOG000276891.

HOVERGEN

HBG052111.

InParanoid

P31785.

KO

K05070.

OMA

WTEQSVD.

OrthoDB

EOG43FGZ6.

PhylomeDB

P31785.

Enzyme and pathway databases

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
il12_2pathway. IL12-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il2_1pathway. IL2-mediated signaling events.
il4_2pathway. IL4-mediated signaling events.

Reactome

REACT_6900. Immune System.

SignaLink

P31785.

Gene expression databases

ArrayExpress

P31785.

Bgee

P31785.

CleanEx

HS_IL2RG.

Genevestigator

P31785.

GermOnline

ENSG00000147168. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
IPR015321. IL6_recept-bd.
[Graphical view]

Pfam

PF00041. fn3. 1 hit.
PF09240. IL6Ra-bind. 1 hit.
[Graphical view]

SMART

SM00060. FN3. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.

PROSITE

PS50853. FN3. 1 hit.
PS01355. HEMATOPO_REC_S_F1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P31785.

ChEMBL

CHEMBL2166.

ChiTaRS

IL2RG. human.

DrugBank

DB00041. Aldesleukin.
DB00004. Denileukin diftitox.

EvolutionaryTrace

P31785.

GenomeRNAi

3561.

NextBio

13908.

PMAP-CutDB

P31785.

SOURCE

Search...

Entry information

Entry name

IL2RG_HUMAN

Accession

Primary (citable) accession number: P31785

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 29, 2013
This is version 159 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.