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P24394

- IL4RA_HUMAN

UniProt

P24394 - IL4RA_HUMAN

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Protein

Interleukin-4 receptor subunit alpha

Gene

IL4R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2.1 Publication
Soluble IL4R (sIL4R) inhibits IL4-mediated cell proliferation and IL5 up-regulation by T-cells.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei38 – 381Major IL4 binding determinant
Sitei64 – 641Minor IL4 binding determinant
Sitei66 – 661Minor IL4 binding determinant
Sitei92 – 921Minor IL4 binding determinant
Sitei94 – 941Minor IL4 binding determinant
Sitei97 – 971Major IL4 binding determinant
Sitei152 – 1521Minor IL4 binding determinant
Sitei208 – 2081Major IL4 binding determinant

GO - Molecular functioni

  1. interleukin-4 receptor activity Source: ProtInc
  2. receptor signaling protein activity Source: ProtInc

GO - Biological processi

  1. defense response to protozoan Source: Ensembl
  2. immune response Source: ProtInc
  3. interleukin-4-mediated signaling pathway Source: GOC
  4. intracellular signal transduction Source: GOC
  5. negative regulation of T-helper 1 cell differentiation Source: Ensembl
  6. ovulation Source: Ensembl
  7. positive regulation of chemokine secretion Source: Ensembl
  8. positive regulation of macrophage activation Source: Ensembl
  9. positive regulation of T-helper 2 cell differentiation Source: Ensembl
  10. production of molecular mediator involved in inflammatory response Source: InterPro
  11. regulation of cell proliferation Source: Ensembl
  12. response to estrogen Source: Ensembl
  13. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity

Enzyme and pathway databases

SignaLinkiP24394.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-4 receptor subunit alpha
Short name:
IL-4 receptor subunit alpha
Short name:
IL-4R subunit alpha
Short name:
IL-4R-alpha
Short name:
IL-4RA
Alternative name(s):
CD_antigen: CD124
Cleaved into the following chain:
Soluble interleukin-4 receptor subunit alpha
Short name:
Soluble IL-4 receptor subunit alpha
Short name:
Soluble IL-4R-alpha
Short name:
sIL4Ralpha/prot
Alternative name(s):
IL-4-binding protein
Short name:
IL4-BP
Gene namesi
Name:IL4R
Synonyms:IL4RA
ORF Names:582J2.1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:6015. IL4R.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. integral component of plasma membrane Source: ProtInc
  3. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381Y → A: 700-fold reduction in IL4 binding. 1 Publication
Mutagenesisi38 – 381Y → F: 25-fold reduction in IL4 binding. 1 Publication
Mutagenesisi39 – 391M → A: No effect on IL4 binding. 1 Publication
Mutagenesisi40 – 401S → A: No effect on IL4 binding. 1 Publication
Mutagenesisi64 – 641L → A: 100-fold reduction in IL4 binding. 1 Publication
Mutagenesisi66 – 661F → A: 45-fold reduction in IL4 binding. 1 Publication
Mutagenesisi67 – 671L → A: No effect on IL4 binding. 1 Publication
Mutagenesisi68 – 681L → A: No effect on IL4 binding. 1 Publication
Mutagenesisi91 – 911D → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi92 – 921D → A: 50-fold reduction in IL4 binding. 1 Publication
Mutagenesisi93 – 931V → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi94 – 941V → A: 35-fold reduction in IL4 binding. 1 Publication
Mutagenesisi95 – 951S → A: No effect on IL4 binding. 1 Publication
Mutagenesisi97 – 971D → A or N: >150-fold reduction in IL4 binding. 1 Publication
Mutagenesisi98 – 981N → A: No effect on IL4 binding. 1 Publication
Mutagenesisi99 – 991Y → A: 10-fold reduction in IL4 binding. 1 Publication
Mutagenesisi116 – 1161K → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi117 – 1171P → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi118 – 1181S → A: No effect on IL4 binding. 1 Publication
Mutagenesisi119 – 1191E → A: No effect on IL4 binding. 1 Publication
Mutagenesisi150 – 1501D → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi151 – 1511N → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi152 – 1521Y → A: 40-fold reduction in IL4 binding. 1 Publication
Mutagenesisi152 – 1521Y → F: No effect on IL4 binding. 1 Publication
Mutagenesisi153 – 1531L → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi154 – 1541Y → A: Little effect on IL4 binding. 1 Publication
Mutagenesisi208 – 2081Y → A: 500-fold reduction in IL4 binding. 1 Publication
Mutagenesisi208 – 2081Y → F: 200-fold reduction in IL4 binding. 1 Publication
Mutagenesisi497 – 4971Y → F: Abolishes IRS1 tyrosine phosphorylation. No cell proliferation. 1 Publication
Mutagenesisi575 – 5751Y → F: Loss of CD23 gene induction; when associated with F-603 and F-631. 2 Publications
Mutagenesisi603 – 6031Y → F: Loss of CD23 gene induction; when associated with F-575 and F-631. 1 Publication
Mutagenesisi631 – 6311Y → F: Loss of CD23 gene induction; when associated with F-575 and F-603. 1 Publication
Mutagenesisi713 – 7131Y → F: Increased IL4-induced cell proliferation and STAT6 activation. 1 Publication

Organism-specific databases

PharmGKBiPA29832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525By similarityAdd
BLAST
Chaini26 – 825800Interleukin-4 receptor subunit alphaPRO_0000010887Add
BLAST
Chaini26 – ?Soluble interleukin-4 receptor subunit alphaPRO_0000010888

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 44By similarity
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi74 ↔ 86By similarity
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Modified residuei497 – 4971Phosphotyrosine1 Publication
Modified residuei575 – 5751Phosphotyrosine1 Publication
Modified residuei603 – 6031Phosphotyrosine1 Publication
Modified residuei631 – 6311Phosphotyrosine1 Publication

Post-translational modificationi

On IL4 binding, phosphorylated on C-terminal tyrosine residues. Phosphorylation on any one of tyrosine residues, Tyr-575, Tyr-603 or Tyr-631, is required for STAT6-induced gene induction.1 Publication
The soluble form (sIL4R/IL4BP) can also be produced by proteolytic cleavage at the cell surface (shedding) by a metalloproteinase.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP24394.
PaxDbiP24394.
PRIDEiP24394.

PTM databases

PhosphoSiteiP24394.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are highly expressed in activated T-cells.

Gene expression databases

BgeeiP24394.
ExpressionAtlasiP24394. baseline and differential.
GenevestigatoriP24394.

Organism-specific databases

HPAiCAB004451.
HPA050124.

Interactioni

Subunit structurei

The functional IL4 receptor is formed by initial binding of IL4 to IL4R. Subsequent recruitment to the complex of the common gamma chain, in immune cells, creates a type I receptor and, in non-immune cells, of IL13RA1 forms a type II receptor. IL4R can also interact with the IL13/IL13RA1 complex to form a similar type II receptor. Interacts with PIK3C3 (By similarity). Interacts with the SH2-containing phosphatases, PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP (By similarity). Interacts with JAK1 through a Box 1-containing region; inhibited by SOCS5. Interacts with SOCS5; inhibits IL4 signaling (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
IL4P051127EBI-367009,EBI-367025
STAT6P422264EBI-367009,EBI-1186478

Protein-protein interaction databases

BioGridi109780. 18 interactions.
DIPiDIP-3223N.
IntActiP24394. 10 interactions.
MINTiMINT-90363.

Structurei

Secondary structure

1
825
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 369
Beta strandi38 – 5013
Helixi54 – 574
Beta strandi58 – 6811
Beta strandi72 – 743
Beta strandi77 – 8913
Beta strandi99 – 1057
Beta strandi108 – 1158
Helixi117 – 1193
Beta strandi127 – 1326
Turni135 – 1373
Beta strandi139 – 1446
Helixi154 – 1563
Beta strandi158 – 16811
Beta strandi172 – 1776
Beta strandi183 – 1864
Helixi188 – 1903
Beta strandi193 – 1953
Beta strandi197 – 2048
Helixi206 – 2083
Beta strandi219 – 2213
Helixi495 – 4973

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IARX-ray2.30B26-232[»]
1IRSNMR-B489-499[»]
1ITEmodel-C26-232[»]
3BPLX-ray2.93B27-227[»]
3BPNX-ray3.02B27-227[»]
3BPOX-ray3.00B27-227[»]
ProteinModelPortaliP24394.
SMRiP24394. Positions 27-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24394.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 232207ExtracellularSequence AnalysisAdd
BLAST
Topological domaini257 – 825569CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei233 – 25624HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 224100Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni437 – 557121Required for IRS1 activation and IL4-induced cell growthAdd
BLAST
Regioni558 – 657100Required for IL4-induced gene expressionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi212 – 2165WSXWS motif
Motifi262 – 2709Box 1 motif
Motifi711 – 7166ITIM motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi370 – 38011Poly-GluAdd
BLAST
Compositional biasi563 – 5664Poly-Ala
Compositional biasi789 – 7946Poly-Ser

Domaini

The extracellular domain represents the IL4 binding protein (IL4BP).
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 similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46569.
GeneTreeiENSGT00510000049182.
HOVERGENiHBG052116.
InParanoidiP24394.
KOiK05071.
OMAiSPCCGCC.
OrthoDBiEOG73RBCJ.
PhylomeDBiP24394.
TreeFamiTF337996.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
IPR015319. IL-4_rcpt-alpha_N.
[Graphical view]
PfamiPF09238. IL4Ra_N. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 1 hit.
PS01355. HEMATOPO_REC_S_F1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P24394-1) [UniParc]FASTAAdd to Basket

Also known as: Membrane-bound form

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGWLCSGLLF PVSCLVLLQV ASSGNMKVLQ EPTCVSDYMS ISTCEWKMNG
60 70 80 90 100
PTNCSTELRL LYQLVFLLSE AHTCIPENNG GAGCVCHLLM DDVVSADNYT
110 120 130 140 150
LDLWAGQQLL WKGSFKPSEH VKPRAPGNLT VHTNVSDTLL LTWSNPYPPD
160 170 180 190 200
NYLYNHLTYA VNIWSENDPA DFRIYNVTYL EPSLRIAAST LKSGISYRAR
210 220 230 240 250
VRAWAQCYNT TWSEWSPSTK WHNSYREPFE QHLLLGVSVS CIVILAVCLL
260 270 280 290 300
CYVSITKIKK EWWDQIPNPA RSRLVAIIIQ DAQGSQWEKR SRGQEPAKCP
310 320 330 340 350
HWKNCLTKLL PCFLEHNMKR DEDPHKAAKE MPFQGSGKSA WCPVEISKTV
360 370 380 390 400
LWPESISVVR CVELFEAPVE CEEEEEVEEE KGSFCASPES SRDDFQEGRE
410 420 430 440 450
GIVARLTESL FLDLLGEENG GFCQQDMGES CLLPPSGSTS AHMPWDEFPS
460 470 480 490 500
AGPKEAPPWG KEQPLHLEPS PPASPTQSPD NLTCTETPLV IAGNPAYRSF
510 520 530 540 550
SNSLSQSPCP RELGPDPLLA RHLEEVEPEM PCVPQLSEPT TVPQPEPETW
560 570 580 590 600
EQILRRNVLQ HGAAAAPVSA PTSGYQEFVH AVEQGGTQAS AVVGLGPPGE
610 620 630 640 650
AGYKAFSSLL ASSAVSPEKC GFGASSGEEG YKPFQDLIPG CPGDPAPVPV
660 670 680 690 700
PLFTFGLDRE PPRSPQSSHL PSSSPEHLGL EPGEKVEDMP KPPLPQEQAT
710 720 730 740 750
DPLVDSLGSG IVYSALTCHL CGHLKQCHGQ EDGGQTPVMA SPCCGCCCGD
760 770 780 790 800
RSSPPTTPLR APDPSPGGVP LEASLCPASL APSGISEKSK SSSSFHPAPG
810 820
NAQSSSQTPK IVNFVSVGPT YMRVS
Length:825
Mass (Da):89,658
Last modified:March 1, 1992 - v1
Checksum:i9F886DF5612297F8
GO
Isoform 2 (identifier: P24394-2) [UniParc]FASTAAdd to Basket

Also known as: Soluble form, sIL4Ralpha/splice

The sequence of this isoform differs from the canonical sequence as follows:
     225-227: YRE → NIC
     228-825: Missing.

Show »
Length:227
Mass (Da):25,553
Checksum:i9FE8FCC827717CC5
GO
Isoform 3 (identifier: P24394-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MGWLCSGLLFPVSCLVLLQVASS → MQKDARRE

Note: No experimental confirmation available.

Show »
Length:810
Mass (Da):88,267
Checksum:i234ADCAA655651CB
GO

Polymorphismi

Allelic variants in IL4RA are associated with a susceptibility to atopy, an immunological condition that can lead to clinical symptoms such as allergic rhinitis, sinusitis, asthma and eczema.
Allelic variants in IL4RA are associated with cedar pollen sensitization. Individuals develop Japanese cedar pollinosis with increased exposure to cedar pollen. Japanese cedar pollinosis is a type I allergic disease with ocular and nasal symptoms that develop paroxysmally on contact with Japanese cedar pollen. These symptoms, which occur seasonally each year, are typical features of allergic rhinitis, such as sneezing, excessive nasal secretion, nasal congestion, and conjunctival itching.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751I → F.
Corresponds to variant rs1805010 [ dbSNP | Ensembl ].
VAR_059302
Natural varianti75 – 751I → L.
Corresponds to variant rs1805010 [ dbSNP | Ensembl ].
VAR_059303
Natural varianti75 – 751I → V Associated with atopic asthma and cedar pollen sensitization. 5 Publications
Corresponds to variant rs1805010 [ dbSNP | Ensembl ].
VAR_008034
Natural varianti387 – 3871S → L.
Corresponds to variant rs6413500 [ dbSNP | Ensembl ].
VAR_019999
Natural varianti400 – 4001E → A Associated with cedar pollen sensitization. 4 Publications
Corresponds to variant rs1805011 [ dbSNP | Ensembl ].
VAR_011657
Natural varianti431 – 4311C → R.3 Publications
Corresponds to variant rs1805012 [ dbSNP | Ensembl ].
VAR_011658
Natural varianti436 – 4361S → L.3 Publications
Corresponds to variant rs1805013 [ dbSNP | Ensembl ].
VAR_011659
Natural varianti492 – 4921A → T.
Corresponds to variant rs35606110 [ dbSNP | Ensembl ].
VAR_049164
Natural varianti492 – 4921A → V.
Corresponds to variant rs34727572 [ dbSNP | Ensembl ].
VAR_049165
Natural varianti503 – 5031S → P Lowered total IgE concentration. 3 Publications
Corresponds to variant rs1805015 [ dbSNP | Ensembl ].
VAR_011660
Natural varianti576 – 5761Q → R Associated with atopic dermatitis; lowered total IgE concentration; no effect on IL4-induced signal transduction. 5 Publications
Corresponds to variant rs1801275 [ dbSNP | Ensembl ].
VAR_008035
Natural varianti579 – 5791V → I.2 Publications
Corresponds to variant rs3024677 [ dbSNP | Ensembl ].
VAR_011661
Natural varianti675 – 6751P → S.1 Publication
Corresponds to variant rs3024678 [ dbSNP | Ensembl ].
VAR_020000
Natural varianti752 – 7521S → A.2 Publications
Corresponds to variant rs1805016 [ dbSNP | Ensembl ].
VAR_011662
Natural varianti786 – 7861S → P in 1.8% of the population. 2 Publications
Corresponds to variant rs1805014 [ dbSNP | Ensembl ].
VAR_011663

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323MGWLC…QVASS → MQKDARRE in isoform 3. 1 PublicationVSP_053738Add
BLAST
Alternative sequencei225 – 2273YRE → NIC in isoform 2. CuratedVSP_011116
Alternative sequencei228 – 825598Missing in isoform 2. CuratedVSP_011117Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52425 mRNA. Translation: CAA36672.1.
AC004525 Genomic DNA. Translation: AAC23495.1.
AF421855 Genomic DNA. Translation: AAL12163.1.
AJ293647 Genomic DNA. Translation: CAC20445.1.
AJ293648 Genomic DNA. Translation: CAC20446.1.
AJ293649 Genomic DNA. Translation: CAC20447.1.
AJ293650 Genomic DNA. Translation: CAC20448.1.
AJ293651 Genomic DNA. Translation: CAC20449.1.
AJ293652 Genomic DNA. Translation: CAC20450.1.
AJ293653 Genomic DNA. Translation: CAC20451.1.
AK303255 mRNA. Translation: BAG64338.1.
AC106739 Genomic DNA. No translation available.
BC151131 mRNA. Translation: AAI51132.1.
AJ293654 Genomic DNA. Translation: CAC20452.1.
CCDSiCCDS10629.1. [P24394-1]
CCDS58441.1. [P24394-3]
PIRiA60386.
RefSeqiNP_000409.1. NM_000418.3. [P24394-1]
NP_001244335.1. NM_001257406.1. [P24394-1]
NP_001244336.1. NM_001257407.1. [P24394-3]
UniGeneiHs.513457.
Hs.742121.

Genome annotation databases

EnsembliENST00000170630; ENSP00000170630; ENSG00000077238. [P24394-3]
ENST00000395762; ENSP00000379111; ENSG00000077238. [P24394-1]
ENST00000543915; ENSP00000441667; ENSG00000077238. [P24394-1]
GeneIDi3566.
KEGGihsa:3566.
UCSCiuc002don.4. human. [P24394-1]

Polymorphism databases

DMDMi124335.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52425 mRNA. Translation: CAA36672.1 .
AC004525 Genomic DNA. Translation: AAC23495.1 .
AF421855 Genomic DNA. Translation: AAL12163.1 .
AJ293647 Genomic DNA. Translation: CAC20445.1 .
AJ293648 Genomic DNA. Translation: CAC20446.1 .
AJ293649 Genomic DNA. Translation: CAC20447.1 .
AJ293650 Genomic DNA. Translation: CAC20448.1 .
AJ293651 Genomic DNA. Translation: CAC20449.1 .
AJ293652 Genomic DNA. Translation: CAC20450.1 .
AJ293653 Genomic DNA. Translation: CAC20451.1 .
AK303255 mRNA. Translation: BAG64338.1 .
AC106739 Genomic DNA. No translation available.
BC151131 mRNA. Translation: AAI51132.1 .
AJ293654 Genomic DNA. Translation: CAC20452.1 .
CCDSi CCDS10629.1. [P24394-1 ]
CCDS58441.1. [P24394-3 ]
PIRi A60386.
RefSeqi NP_000409.1. NM_000418.3. [P24394-1 ]
NP_001244335.1. NM_001257406.1. [P24394-1 ]
NP_001244336.1. NM_001257407.1. [P24394-3 ]
UniGenei Hs.513457.
Hs.742121.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IAR X-ray 2.30 B 26-232 [» ]
1IRS NMR - B 489-499 [» ]
1ITE model - C 26-232 [» ]
3BPL X-ray 2.93 B 27-227 [» ]
3BPN X-ray 3.02 B 27-227 [» ]
3BPO X-ray 3.00 B 27-227 [» ]
ProteinModelPortali P24394.
SMRi P24394. Positions 27-224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109780. 18 interactions.
DIPi DIP-3223N.
IntActi P24394. 10 interactions.
MINTi MINT-90363.

PTM databases

PhosphoSitei P24394.

Polymorphism databases

DMDMi 124335.

Proteomic databases

MaxQBi P24394.
PaxDbi P24394.
PRIDEi P24394.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000170630 ; ENSP00000170630 ; ENSG00000077238 . [P24394-3 ]
ENST00000395762 ; ENSP00000379111 ; ENSG00000077238 . [P24394-1 ]
ENST00000543915 ; ENSP00000441667 ; ENSG00000077238 . [P24394-1 ]
GeneIDi 3566.
KEGGi hsa:3566.
UCSCi uc002don.4. human. [P24394-1 ]

Organism-specific databases

CTDi 3566.
GeneCardsi GC16P027325.
HGNCi HGNC:6015. IL4R.
HPAi CAB004451.
HPA050124.
MIMi 147781. gene.
neXtProti NX_P24394.
PharmGKBi PA29832.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46569.
GeneTreei ENSGT00510000049182.
HOVERGENi HBG052116.
InParanoidi P24394.
KOi K05071.
OMAi SPCCGCC.
OrthoDBi EOG73RBCJ.
PhylomeDBi P24394.
TreeFami TF337996.

Enzyme and pathway databases

SignaLinki P24394.

Miscellaneous databases

ChiTaRSi IL4R. human.
EvolutionaryTracei P24394.
GeneWikii Interleukin-4_receptor.
GenomeRNAii 3566.
NextBioi 13926.
PROi P24394.
SOURCEi Search...

Gene expression databases

Bgeei P24394.
ExpressionAtlasi P24394. baseline and differential.
Genevestigatori P24394.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
IPR015319. IL-4_rcpt-alpha_N.
[Graphical view ]
Pfami PF09238. IL4Ra_N. 1 hit.
[Graphical view ]
SMARTi SM00060. FN3. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
PROSITEi PS50853. FN3. 1 hit.
PS01355. HEMATOPO_REC_S_F1. 1 hit.
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Publicationsi

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  1. "Human interleukin 4 receptor confers biological responsiveness and defines a novel receptor superfamily."
    Idzerda R.L., March C.J., Mosley B., Lyman S.D., Bos T.V., Gimpel S.D., Din W.S., Grabstein K.H., Widmer M.B., Park L.S., Cosman D., Beckmann M.P.
    J. Exp. Med. 171:861-873(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Peripheral blood.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Myeloid leukemia cell.
  3. "Characterization of the membrane-bound and a soluble form of human IL-4 receptor alpha produced by alternative splicing."
    Kruse S., Forster J., Kuehr J., Deichmann K.A.
    Int. Immunol. 11:1965-1970(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    Tissue: Blood.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
  5. SeattleSNPs variation discovery resource
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-75; ALA-400; ARG-431; LEU-436; PRO-503; ARG-576; ILE-579; SER-675 AND ALA-752.
  6. "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] (ISOFORM 3).
    Tissue: Thymus.
  7. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Testis.
  9. "Identification of a novel single-nucleotide polymorphism (Val554Ile) and definition of eight common alleles for human IL4RA exon 11."
    Lozano F., Places L., Vila J.-M., Padilla O., Arman M., Gimferrer I., Suarez B., Lopez de la Iglesia A., Miserachs N., Vives J.
    Tissue Antigens 57:216-220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-825 (ISOFORM 1), VARIANTS ALA-400; ARG-431; LEU-436; PRO-503; ARG-576 AND ILE-579.
  10. "An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth."
    Keegan A.D., Nelms K., White M., Wang L.-M., Pierce J.H., Paul W.E.
    Cell 76:811-820(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IRS1 ACTIVATION, MUTAGENESIS OF TYR-497.
  11. "Activation of JAK3, but not JAK1, is critical to interleukin-4 (IL4) stimulated proliferation and requires a membrane-proximal region of IL4 receptor alpha."
    Malabarba M.G., Kirken R.A., Rui H., Koettnitz K., Kawamura M., O'Shea J.J., Kalthoff F.S., Farrar W.L.
    J. Biol. Chem. 270:9630-9637(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN JAK3 ACTIVATION.
  12. "The primary binding subunit of the human interleukin-4 receptor is also a component of the interleukin-13 receptor."
    Zurawski S.M., Chomarat P., Djossou O., Bidaud C., McKenzie A.N., Miossec P., Banchereau J., Zurawski G.
    J. Biol. Chem. 270:13869-13878(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IL13RA1.
  13. "JAK3 associates with the human interleukin 4 receptor and is tyrosine phosphorylated following receptor triggering."
    Rolling C., Treton D., Beckmann P., Galanaud P., Richard Y.
    Oncogene 10:1757-1761(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JAK3.
  14. "IL4 and IL13 receptors share the gamma c chain and activate STAT6, STAT3 and STAT5 proteins in normal human B cells."
    Rolling C., Treton D., Pellegrini S., Galanaud P., Richard Y.
    FEBS Lett. 393:53-56(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IL13RA1, PHOSPHORYLATION.
  15. "Growth and gene expression are predominantly controlled by distinct regions of the human IL-4 receptor."
    Ryan J.J., McReynolds L.J., Keegan A., Wang L.-H., Garfein E., Rothman P., Nelms K., Paul W.E.
    Immunity 4:123-132(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN STAT6 ACTIVATION, MUTAGENESIS OF TYR-575; TYR-603 AND TYR-631.
  16. "Soluble human interleukin-4 receptor is produced by activated T cells under the control of metalloproteinases."
    Jung T., Schrader N., Hellwig M., Enssle K.H., Neumann C.
    Int. Arch. Allergy Immunol. 119:23-30(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  17. "Immunoreceptor tyrosine-based inhibitory motif of the IL-4 receptor associates with SH2-containing phosphatases and regulates IL-4-induced proliferation."
    Kashiwada M., Giallourakis C.C., Pan P.-Y., Rothman P.B.
    J. Immunol. 167:6382-6387(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN6; PTPN11 AND INPP5D, STAT6 ACTIVATION, MUTAGENESIS OF TYR-713.
  18. "The high-affinity interaction of human IL-4 and the receptor alpha chain is constituted by two independent binding clusters."
    Zhang J.-L., Simeonowa I., Wang Y., Sebald W.
    J. Mol. Biol. 315:399-407(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIGAND-BINDING SITES, MUTAGENESIS OF TYR-38; MET-39; SER-40; LEU-64; PHE-66; LEU-67; LEU-68; ASP-91; ASP-92; VAL-93; VAL-94; SER-95; ASP-97; ASN-98; TYR-99; LYS-116; PRO-117; SER-118; GLU-119; ASP-150; ASN-151; TYR-152; LEU-153; TYR-154 AND TYR-208.
  19. "Regulation of the dephosphorylation of Stat6. Participation of Tyr-713 in the interleukin-4 receptor alpha, the tyrosine phosphatase SHP-1, and the proteasome."
    Hanson E.M., Dickensheets H., Qu C.K., Donnelly R.P., Keegan A.D.
    J. Biol. Chem. 278:3903-3911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STAT6 ACTIVATION, INHIBITION BY TYROSINE PHOSPHATASE SHP1.
  20. "Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface."
    Hage T., Sebald W., Reinemer P.
    Cell 97:271-281(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-232 IN COMPLEX WITH IL4.
  21. "Common polymorphisms in the coding part of the IL4-receptor gene."
    Deichmann K., Bardutzky J., Forster J., Heinzmann A., Kuehr J.
    Biochem. Biophys. Res. Commun. 231:696-697(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-75; ALA-400; ARG-431; LEU-436 AND PRO-786.
  22. "The association of atopy with a gain-of-function mutation in the alpha subunit of the interleukin-4 receptor."
    Hershey G.K.K., Friedrich M.F., Esswein L.A., Thomas M.L., Chatila T.A.
    N. Engl. J. Med. 337:1720-1725(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-576.
  23. "Ile50Val variant of IL4R alpha upregulates IgE synthesis and associates with atopic asthma."
    Mitsuyasu H., Izuhara K., Mao X.-Q., Gao P.S., Arinobu Y., Enomoto T., Kawai M., Sasaki S., Dake Y., Hamasaki N., Shirakawa T., Hopkin J.M.
    Nat. Genet. 19:119-120(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-75.
  24. Cited for: VARIANT VAL-75.
  25. "The polymorphisms S503P and Q576R in the interleukin-4 receptor alpha gene are associated with atopy and influence the signal transduction."
    Kruse S., Japha T., Tedner M., Sparholt S.H., Forster J., Kuehr J., Deichmann K.A.
    Immunology 96:365-371(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRO-503 AND ARG-576.
  26. "Effects of an allergy-associated mutation in the human IL-4R alpha (Q576R) on human IL-4-induced signal transduction."
    Wang H.Y., Shelburne C.P., Zamorano J., Kelly A.E., Ryan J.J., Keegan A.D.
    J. Immunol. 162:4385-4389(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT ARG-576, MUTAGENESIS OF TYR-575.
  27. "Variation in the interleukin 4-receptor alpha gene confers susceptibility to asthma and atopy in ethnically diverse populations."
    Ober C., Leavitt S.A., Tsalenko A., Howard T.D., Hoki D.M., Daniel R., Newman D.L., Wu X., Parry R., Lester L.A., Solway J., Blumenthal M., King R.A., Xu J., Meyers D.A., Bleecker E.R., Cox N.J.
    Am. J. Hum. Genet. 66:517-526(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-752.
  28. "Interleukin 4 receptor alpha chain polymorphism Gln551Arg is associated with adult atopic dermatitis in Japan."
    Oiso N., Fukai K., Ishii M.
    Br. J. Dermatol. 142:1003-1006(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-576.
  29. "Analysis of the Ser786Pro interleukin-4 receptor alpha allelic variant in allergic and nonallergic asthma and its functional consequences."
    Andrews R.P., Burrell L., Rosa-Rosa L., Cunningham C.M., Brzezinski J.L., Bernstein J.A., Khurana Hershey G.K.
    Clin. Immunol. 100:298-304(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-786.
  30. "High contribution contrast between the genes of eosinophil peroxidase and IL-4 receptor alpha-chain in Japanese cedar pollinosis."
    Nakamura H., Miyagawa K., Ogino K., Endo T., Imai T., Ozasa K., Motohashi Y., Matsuzaki I., Sasahara S., Hatta K., Eboshida A.
    J. Allergy Clin. Immunol. 112:1127-1131(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-75 AND ALA-400, POLYMORPHISM.

Entry informationi

Entry nameiIL4RA_HUMAN
AccessioniPrimary (citable) accession number: P24394
Secondary accession number(s): B4E076
, B9EKU8, H3BSY5, Q96P01, Q9H181, Q9H182, Q9H183, Q9H184, Q9H185, Q9H186, Q9H187, Q9H188
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: October 29, 2014
This is version 175 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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