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P14784 (IL2RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 551525Interleukin-2 receptor subunit beta
PRO_0000010878

Regions

Topological domain27 – 240214Extracellular Potential
Transmembrane241 – 26525Helical; Potential
Topological domain266 – 551286Cytoplasmic Potential
Domain134 – 234101Fibronectin type-III
Motif220 – 2245WSXWS motif
Motif278 – 2869Box 1 motif

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation431N-linked (GlcNAc...) Ref.12
Glycosylation711N-linked (GlcNAc...) Ref.12
Glycosylation1491N-linked (GlcNAc...) Ref.11 Ref.12
Disulfide bond36 ↔ 46 Ref.11 Ref.12
Disulfide bond59 ↔ 110 Ref.11 Ref.12
Disulfide bond74 ↔ 86 Ref.11 Ref.12

Natural variations

Natural variant101L → V.
Corresponds to variant rs57770674 [ dbSNP | Ensembl ].
VAR_061186
Natural variant831S → F. Ref.3
Corresponds to variant rs2228143 [ dbSNP | Ensembl ].
VAR_021994
Natural variant3911D → E. Ref.3
Corresponds to variant rs228942 [ dbSNP | Ensembl ].
VAR_019998

Experimental info

Mutagenesis4181Y → F: Partial loss of interaction with SHB; when associated with F-536. Ref.9
Mutagenesis5361Y → F: Partial loss of interaction with SHB; when associated with F-418. Ref.9

Secondary structure

..................................... 551
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14784 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 1A76FA1936BB7EE6

FASTA55161,117
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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

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.
CCDSCCDS13942.1.
PIRA30342.
RefSeqNP_000869.1. NM_000878.3.
UniGeneHs.474787.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILMmodel-B31-230[»]
1ILNmodel-B31-230[»]
2B5IX-ray2.30B27-240[»]
2ERJX-ray3.00B/F27-232[»]
3QAZX-ray3.80B/E/H/K/N/Q/T/W/Z/c/f/i24-240[»]
4GS7X-ray2.35B27-240[»]
ProteinModelPortalP14784.
SMRP14784. Positions 32-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109775. 17 interactions.
DIPDIP-43N.
IntActP14784. 4 interactions.
MINTMINT-273361.
STRING9606.ENSP00000216223.

Chemistry

BindingDBP14784.
ChEMBLCHEMBL3276.
DrugBankDB00041. Aldesleukin.
DB00074. Basiliximab.
DB00111. Daclizumab.
DB00004. Denileukin diftitox.

PTM databases

PhosphoSiteP14784.

Polymorphism databases

DMDM124321.

Proteomic databases

PaxDbP14784.
PRIDEP14784.

Protocols and materials databases

DNASU3560.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216223; ENSP00000216223; ENSG00000100385.
GeneID3560.
KEGGhsa:3560.
UCSCuc003aqv.1. human.

Organism-specific databases

CTD3560.
GeneCardsGC22M037515.
HGNCHGNC:6009. IL2RB.
HPAHPA062657.
MIM146710. gene.
neXtProtNX_P14784.
Orphanet85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
PharmGKBPA29829.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46659.
HOGENOMHOG000038003.
HOVERGENHBG052110.
KOK05069.
OMAACQVYFT.
OrthoDBEOG72RMZ6.
PhylomeDBP14784.
TreeFamTF337874.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP14784.

Gene expression databases

ArrayExpressP14784.
BgeeP14784.
CleanExHS_IL2RB.
GenevestigatorP14784.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR003961. Fibronectin_type3.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 1 hit.
PS01355. HEMATOPO_REC_S_F1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14784.
GeneWikiIL2RB.
GenomeRNAi3560.
NextBio13904.
PROP14784.
SOURCESearch...

Entry information

Entry nameIL2RB_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries