Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Interleukin-2 receptor subunit beta  

UniProtKB / Swiss-Prot ID :  IL2RB_HUMAN

Gene Name (Synonyms) : 
IL2RB  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Membrane; Single-pass type I membrane protein. 

Protein Function :  Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. 

Transmembrane Topology (topPTM) : IL2RB_HUMAN 

Protein Sequence MAAPALSWRLPLLILLLPLATSWASAAVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQVHAWPDRRRW...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHCCCCCCHHHCCCCCCEEEEEEEECEEEEEECCCCCCCCCCCCEEEEECCCCC...
Protein Variant
LocationDescription
10L -> V (in dbSNP:rs57770674). VAR_061186
83S -> F (in dbSNP:rs2228143). VAR_021994
391D -> E (in dbSNP:rs228942). VAR_019998
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
43N-linked (GlcNAc...).NSRANISCV
EEECEEEEE
26.12UniProtKB
Link
71N-linked (GlcNAc...).RRRWNQTCE
CCCCCCCEE
26.02UniProtKB
Link
149N-linked (GlcNAc...).THRCNISWE
CCEEEEEEC
31.14UniProtKB
Link
282PhosphothreonineLKCNTPDPS
ECCCCCCHH
38.24Phosphositeplus
Link-
293PhosphoserineFSQLSSEHG
CCCCCEEEC
26.50Phosphositeplus
Link-
364PhosphotyrosineTNQGYFFFH
ECCCEEEEE
6.35PhosphoELM
Link-
364PhosphotyrosineTNQGYFFFH
ECCCEEEEE
6.35Phosphositeplus
Link-
364Phosphotyrosine (JAK1)TNQGYFFFH
ECCCEEEEE
6.35HPRD
Link-
381PhosphotyrosineACQVYFTYD
EEEEEEEEC
2.43Phosphositeplus
Link-
381Phosphotyrosine (LCK)ACQVYFTYD
EEEEEEEEC
2.43HPRD
Link-
381Phosphotyrosine (Lck;Lck)ACQVYFTYD
EEEEEEEEC
2.43PhosphoELM
Link-
384PhosphotyrosineVYFTYDPYS
EEEEECCCC
12.67Phosphositeplus
Link-
384Phosphotyrosine (LCK)VYFTYDPYS
EEEEECCCC
12.67HPRD
Link-
384Phosphotyrosine (Lck;Lck)VYFTYDPYS
EEEEECCCC
12.67PhosphoELM
Link-
387PhosphotyrosineTYDPYSEED
EECCCCCCC
26.30Phosphositeplus
Link-
387Phosphotyrosine (LCK)TYDPYSEED
EECCCCCCC
26.30HPRD
Link-
387Phosphotyrosine (Lck;Lck)TYDPYSEED
EECCCCCCC
26.30PhosphoELM
Link-
418PhosphotyrosineEDDAYCTFP
CCCCEECCC
10.06Phosphositeplus
Link-
418Phosphotyrosine (LCK)EDDAYCTFP
CCCCEECCC
10.06HPRD
Link-
418Phosphotyrosine (Lck)EDDAYCTFP
CCCCEECCC
10.06PhosphoELM
Link-
536PhosphotyrosineNTDAYLSLQ
CCCCEEEHH
10.30Phosphositeplus
Link-
536Phosphotyrosine (LCK)NTDAYLSLQ
CCCCEEEHH
10.30HPRD
Link-
536Phosphotyrosine (Lck)NTDAYLSLQ
CCCCEEEHH
10.30PhosphoELM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GBLP_HUMANphysical interactionMINT-58667MINT12960323
IL2RG_HUMANphysical interaction
physical interaction
physical interaction
DIP:757EDIP8006584
10903799
10903799
IL2RA_HUMANphysical interactionDIP:758EDIP8006584
IL2_HUMANphysical interactionDIP:759EDIP8006584
STAT3_HUMANin vivoHPRD:00896HPRD10602027
GRB2_HUMANin vitroHPRD:00896HPRD10602027
SOCS3_HUMANin vitroHPRD:00896HPRD10373548
RAF1_HUMANin vitroHPRD:00896HPRD1639773
LYN_HUMANin vitro
in vivo
HPRD:00896HPRD1557373
PTN6_HUMANin vitroHPRD:00896HPRD9520455
KSYK_HUMANin vitroHPRD:00896HPRD7600304
CD4_HUMANENSP00000216223STRING
IL2_HUMANENSP00000216223STRING
IFNG_HUMANENSP00000216223STRING
IL4_HUMANENSP00000216223STRING
IL7_HUMANENSP00000216223STRING
IL2RG_HUMANENSP00000216223STRING
CD8A_HUMANENSP00000216223STRING
IL15_HUMANENSP00000216223STRING
STAT1_HUMANENSP00000216223STRING
STAT1_HUMANENSP00000216223STRING
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Disease Reference
Kegg disease
H00080 Systemic lupus erythematosus
There are no disease associations of PTM sites.
Drug Reference
Kegg drug
D00748 Aldesleukin (USAN/INN); Interleukin-2; Proleukin (TN)
D02743 Celmoleukin (genetical recombination) (JP16); Celmoleukin (INN); Celeuk (TN)
D02749 Teceleukin (genetical recombination) (JP16); Teceleukin (USAN); Imunace (TN)
D03682 Denileukin diftitox (USAN/INN); Ontak (TN)
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-240 IN COMPLEX WITH IL2;IL2RA AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-149.
"Crystal structure of the IL-2 signaling complex: paradigm for aheterotrimeric 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).
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-232 IN COMPLEX WITH IL2;IL2RA AND IL2RC, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-43; ASN-71AND ASN-149.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures