Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Interleukin-7 receptor subunit alpha  

UniProtKB / Swiss-Prot ID :  IL7RA_HUMAN

Gene Name (Synonyms) : 
IL7R  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 3: Cell membrane; Single-pass type I membrane protein. Isoform 4: Secreted. 

Protein Function :  Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP). 

Transmembrane Topology (topPTM) : IL7RA_HUMAN 

Protein Sequence MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNTTNLE...
Predicted Secondary Structure CEEHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCEEEEEEEEEECCCCEEEEEEECCCCCCCCCCH...
Protein Variant
LocationDescription
66T -> I (in T(-)/B(+)/NK(+) SCID;dbSNP:rs1494558).
113E -> D (in dbSNP:rs11567735). VAR_021287
132P -> S (in T(-)/B(+)/NK(+) SCID). VAR_034870
138I -> V (in T(-)/B(+)/NK(+) SCID;dbSNP:rs1494555).
244T -> I (in dbSNP:rs6897932). VAR_021289
356I -> V (in dbSNP:rs3194051). VAR_021290
414T -> M (in dbSNP:rs2229232). VAR_047742
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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
49N-linked (GlcNAc...).QLEVNGSQH
EEEECCCCE
34.72UniProtKB
Link
65N-linked (GlcNAc...).DPDVNTTNL
CCCCCCCCC
48.87UniProtKB
Link
151N-linked (GlcNAc...).VVTFNTSHL
EEEEECCCC
31.16UniProtKB
Link
159PhosphotyrosineLQKKYVKVL
CCCCCEEEE
16.73HPRD
Link
159Phosphotyrosine.LQKKYVKVL
CCCCCEEEE
16.73UniProtKB
Link
169PhosphotyrosineHDVAYRQEK
EEEEEECCC
16.81HPRD
Link
169Phosphotyrosine.HDVAYRQEK
EEEEEECCC
16.81UniProtKB
Link
449PhosphotyrosineQEEAYVTMS
CCCEEEEEH
10.34HPRD
Link-
449PhosphotyrosineQEEAYVTMS
CCCEEEEEH
10.34PhosphoELM
Link-
449PhosphotyrosineQEEAYVTMS
CCCEEEEEH
10.34Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IL7_HUMANphysical interaction
physical interaction
DIP:4302EDIP1558969
8409434
IL7_HUMANphysical interaction
physical interaction
physical interaction
EBI-80504
EBI-80510
EBI-37159
intact8266077
8266077
8266077
FYN_HUMANin vitro
in vivo
HPRD:00893HPRD7515933
IL7_HUMANin vitro
in vivo
HPRD:00893HPRD11858939
10390077
JAK3_HUMANin vivoHPRD:00893HPRD15996891
7481769
P85A_HUMANin vivoHPRD:00893HPRD7522165
FAK2_HUMANin vivoHPRD:00893HPRD10702271
STA5A_HUMANin vivoHPRD:00893HPRD7719938
STA5B_HUMANin vivoHPRD:00893HPRD7719938
STAT3_HUMANin vivoHPRD:00893HPRD7719938
JAK1_HUMANin vivoHPRD:00893HPRD8647212
15996891
CD4_HUMANENSP00000306157STRING
IL4RA_HUMANENSP00000306157STRING
IL2_HUMANENSP00000306157STRING
IL4_HUMANENSP00000306157STRING
FLT3_HUMANENSP00000306157STRING
FLT3_HUMANENSP00000306157STRING
IL7_HUMANENSP00000306157STRING
IL2RG_HUMANENSP00000306157STRING
CD8A_HUMANENSP00000306157STRING
STA5B_HUMANENSP00000306157STRING
IL15_HUMANENSP00000306157STRING
RAG1_HUMANENSP00000306157STRING
STA5A_HUMANENSP00000306157STRING
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Disease Reference
Kegg disease
H00091 T-B+Severe combined immunodeficiencies (SCIDs), including the following eight diseases: X-linked SCI
OMIM disease
608971Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID)
612595Multiple sclerosis 3 (MS3)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural and biophysical studies of the human IL-7/IL-7Ralphacomplex.";
McElroy C.A., Dohm J.A., Walsh S.T.;
Structure 17:54-65(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-239 IN COMPLEX WITH IL7,SUBUNIT, GLYCOSYLATION AT ASN-49; ASN-65 AND ASN-151, AND DISULFIDEBONDS.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159 AND TYR-169, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures