P14784 (IL2RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-2 receptor subunit beta
Short name=IL-2 receptor subunit beta
Short name=IL-2R subunit beta
Short name=IL-2RB

Alternative name(s):
High affinity IL-2 receptor subunit beta
p70-75
Short name=p75
CD_antigen=CD122

Gene names

Name:

IL2RB

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	551 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	Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2.
Subunit structure	Non-covalent dimer of an alpha and a beta subunit. IL2R exists in 3 different forms: a high affinity dimer, an intermediate affinity monomer (beta subunit), and a low affinity monomer (alpha subunit). The high and intermediate affinity forms also associate with a gamma subunit. Interacts with SHB upon interleukin stimulation. Interacts with HTLV-1 accessory protein p12I. Ref.8 Ref.9
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.
Sequence similarities	Belongs to the type I cytokine receptor family. Type 4 subfamily. Contains 1 fibronectin type-III domain.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of apoptotic process Inferred from direct assay PubMed 7736574. Source: MGI protein complex assembly Traceable author statement PubMed 2467293. Source: ProtInc 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 PubMed 8514792. Source: ProtInc
Molecular_function	interleukin-2 binding Inferred from sequence or structural similarity. Source: UniProtKB interleukin-2 receptor activity Inferred from direct assay PubMed 7736574. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Chain

27 – 551

525

Interleukin-2 receptor subunit beta

PRO_0000010878

Regions

Topological domain

27 – 240

214

Extracellular Potential

Transmembrane

241 – 265

25

Helical; Potential

Topological domain

266 – 551

286

Cytoplasmic Potential

Domain

131 – 229

99

Fibronectin type-III

Motif

220 – 224

5

WSXWS motif

Motif

278 – 286

9

Box 1 motif

Amino acid modifications

Glycosylation

29

1

N-linked (GlcNAc...) Potential

Glycosylation

43

1

N-linked (GlcNAc...) Ref.12

Glycosylation

71

1

N-linked (GlcNAc...) Ref.12

Glycosylation

149

1

N-linked (GlcNAc...) Ref.11 Ref.12

Disulfide bond

36 ↔ 46

Ref.11 Ref.12

Disulfide bond

59 ↔ 110

Ref.11 Ref.12

Disulfide bond

74 ↔ 86

Ref.11 Ref.12

Natural variations

Natural variant

10

1

L → V.
Corresponds to variant rs57770674 [ dbSNP | Ensembl ].

VAR_061186

Natural variant

83

1

S → F. Ref.3
Corresponds to variant rs2228143 [ dbSNP | Ensembl ].

VAR_021994

Natural variant

391

1

D → E. Ref.3
Corresponds to variant rs228942 [ dbSNP | Ensembl ].

VAR_019998

Experimental info

Mutagenesis

418

1

Y → F: Partial loss of interaction with SHB; when associated with F-536. Ref.9

Mutagenesis

536

1

Y → F: Partial loss of interaction with SHB; when associated with F-418. Ref.9

Secondary structure

1

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551

Helix Strand Turn

Details...

Beta strand

33 – 38

6

Beta strand

40 – 49

10

Beta strand

59 – 65

7

Beta strand

72 – 75

4

Beta strand

77 – 80

4

Beta strand

84 – 89

6

Beta strand

104 – 110

7

Beta strand

117 – 124

8

Helix

126 – 128

3

Beta strand

136 – 143

8

Beta strand

148 – 153

6

Helix

159 – 161

3

Beta strand

165 – 172

8

Helix

178 – 180

3

Beta strand

184 – 186

3

Beta strand

192 – 195

4

Beta strand

203 – 213

11

Beta strand

227 – 230

4

Sequences

	Sequence		Length	Mass (Da)
	P14784 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 1A76FA1936BB7EE6	FASTA	551	61,117
	10 20 30 40 50 60 MAAPALSWRL PLLILLLPLA TSWASAAVNG TSQFTCFYNS RANISCVWSQ DGALQDTSCQ 70 80 90 100 110 120 VHAWPDRRRW NQTCELLPVS QASWACNLIL GAPDSQKLTT VDIVTLRVLC REGVRWRVMA 130 140 150 160 170 180 IQDFKPFENL RLMAPISLQV VHVETHRCNI SWEISQASHY FERHLEFEAR TLSPGHTWEE 190 200 210 220 230 240 APLLTLKQKQ EWICLETLTP DTQYEFQVRV KPLQGEFTTW SPWSQPLAFR TKPAALGKDT 250 260 270 280 290 300 IPWLGHLLVG LSGAFGFIIL VYLLINCRNT GPWLKKVLKC NTPDPSKFFS QLSSEHGGDV 310 320 330 340 350 360 QKWLSSPFPS SSFSPGGLAP EISPLEVLER DKVTQLLLQQ DKVPEPASLS SNHSLTSCFT 370 380 390 400 410 420 NQGYFFFHLP DALEIEACQV YFTYDPYSEE DPDEGVAGAP TGSSPQPLQP LSGEDDAYCT 430 440 450 460 470 480 FPSRDDLLLF SPSLLGGPSP PSTAPGGSGA GEERMPPSLQ ERVPRDWDPQ PLGPPTPGVP 490 500 510 520 530 540 DLVDFQPPPE LVLREAGEEV PDAGPREGVS FPWSRPPGQG EFRALNARLP LNTDAYLSLQ 550 ELQGQDPTHL V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's." Hatakeyama M., Tsudo M., Minamoto S., Kono T., Doi T., Miyata T., Miyasaka M., Taniguchi T. Science 244:551-556(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	SeattleSNPs variation discovery resource Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-83 AND GLU-391.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[5]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[8]	"The human T-cell leukemia/lymphotropic virus type 1 p12I proteins bind the interleukin-2 receptor beta and gammac chains and affects their expression on the cell surface." Mulloy J.C., Crownley R.W., Fullen J., Leonard W.J., Franchini G. J. Virol. 70:3599-3605(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
[9]	"IL-2 receptor signaling through the Shb adapter protein in T and NK cells." Lindholm C.K. Biochem. Biophys. Res. Commun. 296:929-936(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SHB, MUTAGENESIS OF TYR-418 AND TYR-536.
[10]	"The interleukin-2 and interleukin-4 receptors studied by molecular modelling." Bamborough P., Hedgecock C.J., Richards W.G. Structure 2:839-851(1994) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 31-230.
[11]	"Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors." Wang X., Rickert M., Garcia K.C. Science 310:1159-1163(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-240 IN COMPLEX WITH IL2; IL2RA AND IL2RC, DISULFIDE BONDS, GLYCOSYLATION AT ASN-149.
[12]	"Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor." Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A. Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-232 IN COMPLEX WITH IL2; IL2RA AND IL2RC, DISULFIDE BONDS, GLYCOSYLATION AT ASN-43; ASN-71 AND ASN-149.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M26062 mRNA. Translation: AAA59143.1.
CR456506 mRNA. Translation: CAG30392.1.
AF517934 Genomic DNA. Translation: AAM54040.1.
AK312860 mRNA. Translation: BAG35712.1.
AL022314 Genomic DNA. Translation: CAA18444.1.
CH471095 Genomic DNA. Translation: EAW60144.1.
BC025691 mRNA. Translation: AAH25691.1.

IPI

IPI00878728.

PIR

A30342.

RefSeq

NP_000869.1. NM_000878.3.

UniGene

Hs.474787.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ILM	model	-	B	31-230	[»]
1ILN	model	-	B	31-230	[»]
2B5I	X-ray	2.30	B	27-240	[»]
2ERJ	X-ray	3.00	B/F	27-232	[»]
3QAZ	X-ray	3.80	B/E/H/K/N/Q/T/W/Z/c/f/i	27-240	[»]
4GS7	X-ray	2.35	B	27-240	[»]

ProteinModelPortal

P14784.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-43N.

IntAct

P14784. 1 interaction.

STRING

9606.ENSP00000216223.

PTM databases

PhosphoSite

P14784.

Polymorphism databases

DMDM

124321.

Proteomic databases

PaxDb

P14784.

PRIDE

P14784.

Protocols and materials databases

DNASU

3560.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216223; ENSP00000216223; ENSG00000100385.

GeneID

3560.

KEGG

hsa:3560.

UCSC

uc003aqv.1. human.

Organism-specific databases

CTD

3560.

GeneCards

GC22M037515.

HGNC

HGNC:6009. IL2RB.

MIM

146710. gene.

neXtProt

NX_P14784.

PharmGKB

PA29829.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG46659.

HOGENOM

HOG000038003.

HOVERGEN

HBG052110.

KO

K05069.

OMA

LAFRTKP.

OrthoDB

EOG42Z4Q0.

PhylomeDB

P14784.

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.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P14784.

Bgee

P14784.

CleanEx

HS_IL2RB.

Genevestigator

P14784.

GermOnline

ENSG00000100385. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.

InterPro

IPR003961. Fibronectin_type3.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
[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

P14784.

ChEMBL

CHEMBL3276.

DrugBank

DB00041. Aldesleukin.
DB00074. Basiliximab.
DB00111. Daclizumab.
DB00004. Denileukin diftitox.

EvolutionaryTrace

P14784.

GenomeRNAi

3560.

NextBio

13904.

SOURCE

Search...

Entry information

Entry name

IL2RB_HUMAN

Accession

Primary (citable) accession number: P14784
Secondary accession number(s): B2R765

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 158 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.