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Q01344

- IL5RA_HUMAN

UniProt

Q01344 - IL5RA_HUMAN

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Protein

Interleukin-5 receptor subunit alpha

Gene

IL5RA

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

Functioni

This is the receptor for interleukin-5. The alpha chain binds to IL5.

GO - Molecular functioni

  1. interleukin-5 receptor activity Source: ProtInc

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. inflammatory response to antigenic stimulus Source: Ensembl
  3. interleukin-5-mediated signaling pathway Source: GOC
  4. regulation of interleukin-5 production Source: Ensembl
  5. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinkiQ01344.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-5 receptor subunit alpha
Short name:
IL-5 receptor subunit alpha
Short name:
IL-5R subunit alpha
Short name:
IL-5R-alpha
Short name:
IL-5RA
Alternative name(s):
CDw125
CD_antigen: CD125
Gene namesi
Name:IL5RA
Synonyms:IL5R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6017. IL5RA.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: ProtInc
  2. integral component of membrane Source: ProtInc
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 420400Interleukin-5 receptor subunit alphaPRO_0000010893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi134 ↔ 1551 Publication
Disulfide bondi182 ↔ 1961 Publication
Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi269 ↔ 3161 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ01344.
PaxDbiQ01344.
PRIDEiQ01344.

PTM databases

PhosphoSiteiQ01344.

Expressioni

Tissue specificityi

Expressed on eosinophils and basophils.

Gene expression databases

BgeeiQ01344.
CleanExiHS_IL5RA.
ExpressionAtlasiQ01344. baseline and differential.
GenevestigatoriQ01344.

Organism-specific databases

HPAiHPA013196.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors. Interacts with SDCBP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IL5P051132EBI-1759442,EBI-2435811

Protein-protein interaction databases

BioGridi109782. 6 interactions.
DIPiDIP-3510N.
IntActiQ01344. 3 interactions.
STRINGi9606.ENSP00000256452.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 429
Beta strandi45 – 517
Beta strandi59 – 613
Beta strandi64 – 7310
Beta strandi75 – 8713
Beta strandi94 – 10310
Beta strandi108 – 1103
Beta strandi114 – 1185
Beta strandi122 – 1243
Helixi125 – 1273
Beta strandi130 – 14011
Beta strandi144 – 1463
Beta strandi149 – 15810
Beta strandi168 – 1758
Beta strandi178 – 1814
Beta strandi185 – 1873
Beta strandi193 – 2008
Beta strandi209 – 21810
Beta strandi227 – 2326
Helixi233 – 2364
Beta strandi243 – 2508
Beta strandi253 – 2597
Beta strandi262 – 2654
Helixi267 – 2693
Beta strandi270 – 2789
Turni279 – 2813
Beta strandi284 – 29714
Beta strandi304 – 3129
Turni314 – 3163
Beta strandi329 – 3313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OBXX-ray1.35B413-420[»]
1OBZX-ray1.69P413-420[»]
3QT2X-ray2.55A/B20-335[»]
3VA2X-ray2.70C21-335[»]
ProteinModelPortaliQ01344.
SMRiQ01344. Positions 27-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01344.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 342322ExtracellularSequence AnalysisAdd
BLAST
Topological domaini363 – 42058CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei343 – 36220HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12392Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini241 – 33494Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi322 – 3265WSXWS motif
Motifi371 – 3799Box 1 motif

Domaini

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 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43089.
GeneTreeiENSGT00530000063295.
HOGENOMiHOG000070224.
HOVERGENiHBG052117.
InParanoidiQ01344.
KOiK05067.
OMAiAPEDTQY.
OrthoDBiEOG71P2B1.
PhylomeDBiQ01344.
TreeFamiTF331549.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015321. IL-6_rcpt_alpha-bd.
IPR003532. Short_hematopoietin_rcpt_2_CS.
[Graphical view]
PfamiPF09240. IL6Ra-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 2 hits.
PS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q01344-1) [UniParc]FASTAAdd to Basket

Also known as: Membrane-bound

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
MIIVAHVLLI LLGATEILQA DLLPDEKISL LPPVNFTIKV TGLAQVLLQW
60 70 80 90 100
KPNPDQEQRN VNLEYQVKIN APKEDDYETR ITESKCVTIL HKGFSASVRT
110 120 130 140 150
ILQNDHSLLA SSWASAELHA PPGSPGTSIV NLTCTTNTTE DNYSRLRSYQ
160 170 180 190 200
VSLHCTWLVG TDAPEDTQYF LYYRYGSWTE ECQEYSKDTL GRNIACWFPR
210 220 230 240 250
TFILSKGRDW LAVLVNGSSK HSAIRPFDQL FALHAIDQIN PPLNVTAEIE
260 270 280 290 300
GTRLSIQWEK PVSAFPIHCF DYEVKIHNTR NGYLQIEKLM TNAFISIIDD
310 320 330 340 350
LSKYDVQVRA AVSSMCREAG LWSEWSQPIY VGNDEHKPLR EWFVIVIMAT
360 370 380 390 400
ICFILLILSL ICKICHLWIK LFPPIPAPKS NIKDLFVTTN YEKAGSSETE
410 420
IEVICYIEKP GVETLEDSVF
Length:420
Mass (Da):47,685
Last modified:October 17, 2006 - v2
Checksum:i4E0A5F2838B9C4FE
GO
Isoform 2 (identifier: Q01344-2) [UniParc]FASTAAdd to Basket

Also known as: Soluble-S1

The sequence of this isoform differs from the canonical sequence as follows:
     333-335: NDE → FSR
     336-420: Missing.

Show »
Length:335
Mass (Da):37,984
Checksum:iBAED076239845E16
GO
Isoform 3 (identifier: Q01344-3) [UniParc]FASTAAdd to Basket

Also known as: Soluble-S2

The sequence of this isoform differs from the canonical sequence as follows:
     333-333: N → K
     334-420: Missing.

Show »
Length:333
Mass (Da):37,722
Checksum:i8D9239845E16985B
GO
Isoform 4 (identifier: Q01344-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     365-420: CHLWIKLFPPIPAPKSNIKDLFVTTNYEKAGSSETEIEVICYIEKPGVETLEDSVF → KLGPVRRKLKSSVI

Show »
Length:378
Mass (Da):42,924
Checksum:i3044C8640A83F586
GO
Isoform 5 (identifier: Q01344-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-331: Missing.

Show »
Length:211
Mass (Da):23,737
Checksum:i475CB1AB3BF8D2B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121A → S in AAA36110. (PubMed:1833065)Curated
Sequence conflicti212 – 2121A → S in AAA59151. (PubMed:1732409)Curated
Sequence conflicti212 – 2121A → S in AAA59152. (PubMed:1732409)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291I → V.2 Publications
Corresponds to variant rs2290610 [ dbSNP | Ensembl ].
VAR_020654
Natural varianti262 – 2621V → A.1 Publication
Corresponds to variant rs17879690 [ dbSNP | Ensembl ].
VAR_020655

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei123 – 331209Missing in isoform 5. 1 PublicationVSP_047762Add
BLAST
Alternative sequencei333 – 3353NDE → FSR in isoform 2. 1 PublicationVSP_001678
Alternative sequencei333 – 3331N → K in isoform 3. 2 PublicationsVSP_001680
Alternative sequencei334 – 42087Missing in isoform 3. 2 PublicationsVSP_001681Add
BLAST
Alternative sequencei336 – 42085Missing in isoform 2. 1 PublicationVSP_001679Add
BLAST
Alternative sequencei365 – 42056CHLWI…EDSVF → KLGPVRRKLKSSVI in isoform 4. 1 PublicationVSP_046742Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M75914 mRNA. Translation: AAA36110.1.
X61176 mRNA. Translation: CAA43483.1.
X62156 mRNA. Translation: CAA44081.1.
M96651 mRNA. Translation: AAA59151.1.
M96652 mRNA. Translation: AAA59152.1.
AB288090 mRNA. Translation: BAG49562.1.
AK304256 mRNA. Translation: BAG65122.1.
AY642135 Genomic DNA. Translation: AAT45457.1.
AC022002 Genomic DNA. No translation available.
AC024060 Genomic DNA. No translation available.
CCDSiCCDS2559.1. [Q01344-1]
CCDS2560.1. [Q01344-2]
CCDS46739.1. [Q01344-3]
CCDS58813.1. [Q01344-4]
PIRiA40267.
RefSeqiNP_000555.2. NM_000564.4. [Q01344-1]
NP_001230028.1. NM_001243099.1. [Q01344-4]
NP_783851.1. NM_175724.2. [Q01344-3]
NP_783852.1. NM_175725.2. [Q01344-2]
NP_783853.1. NM_175726.3. [Q01344-1]
NP_783854.1. NM_175727.2. [Q01344-3]
NP_783855.1. NM_175728.2. [Q01344-2]
UniGeneiHs.68876.

Genome annotation databases

EnsembliENST00000256452; ENSP00000256452; ENSG00000091181. [Q01344-1]
ENST00000311981; ENSP00000309196; ENSG00000091181. [Q01344-2]
ENST00000383846; ENSP00000373358; ENSG00000091181. [Q01344-2]
ENST00000430514; ENSP00000400400; ENSG00000091181. [Q01344-3]
ENST00000438560; ENSP00000390753; ENSG00000091181. [Q01344-4]
ENST00000446632; ENSP00000412209; ENSG00000091181. [Q01344-1]
ENST00000456302; ENSP00000392059; ENSG00000091181. [Q01344-3]
GeneIDi3568.
KEGGihsa:3568.
UCSCiuc010hbr.3. human.
uc010hbs.3. human. [Q01344-1]
uc010hbt.2. human. [Q01344-2]
uc010hbu.2. human. [Q01344-3]
uc011asl.2. human.

Polymorphism databases

DMDMi116242525.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M75914 mRNA. Translation: AAA36110.1 .
X61176 mRNA. Translation: CAA43483.1 .
X62156 mRNA. Translation: CAA44081.1 .
M96651 mRNA. Translation: AAA59151.1 .
M96652 mRNA. Translation: AAA59152.1 .
AB288090 mRNA. Translation: BAG49562.1 .
AK304256 mRNA. Translation: BAG65122.1 .
AY642135 Genomic DNA. Translation: AAT45457.1 .
AC022002 Genomic DNA. No translation available.
AC024060 Genomic DNA. No translation available.
CCDSi CCDS2559.1. [Q01344-1 ]
CCDS2560.1. [Q01344-2 ]
CCDS46739.1. [Q01344-3 ]
CCDS58813.1. [Q01344-4 ]
PIRi A40267.
RefSeqi NP_000555.2. NM_000564.4. [Q01344-1 ]
NP_001230028.1. NM_001243099.1. [Q01344-4 ]
NP_783851.1. NM_175724.2. [Q01344-3 ]
NP_783852.1. NM_175725.2. [Q01344-2 ]
NP_783853.1. NM_175726.3. [Q01344-1 ]
NP_783854.1. NM_175727.2. [Q01344-3 ]
NP_783855.1. NM_175728.2. [Q01344-2 ]
UniGenei Hs.68876.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OBX X-ray 1.35 B 413-420 [» ]
1OBZ X-ray 1.69 P 413-420 [» ]
3QT2 X-ray 2.55 A/B 20-335 [» ]
3VA2 X-ray 2.70 C 21-335 [» ]
ProteinModelPortali Q01344.
SMRi Q01344. Positions 27-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109782. 6 interactions.
DIPi DIP-3510N.
IntActi Q01344. 3 interactions.
STRINGi 9606.ENSP00000256452.

Chemistry

GuidetoPHARMACOLOGYi 1706.

PTM databases

PhosphoSitei Q01344.

Polymorphism databases

DMDMi 116242525.

Proteomic databases

MaxQBi Q01344.
PaxDbi Q01344.
PRIDEi Q01344.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256452 ; ENSP00000256452 ; ENSG00000091181 . [Q01344-1 ]
ENST00000311981 ; ENSP00000309196 ; ENSG00000091181 . [Q01344-2 ]
ENST00000383846 ; ENSP00000373358 ; ENSG00000091181 . [Q01344-2 ]
ENST00000430514 ; ENSP00000400400 ; ENSG00000091181 . [Q01344-3 ]
ENST00000438560 ; ENSP00000390753 ; ENSG00000091181 . [Q01344-4 ]
ENST00000446632 ; ENSP00000412209 ; ENSG00000091181 . [Q01344-1 ]
ENST00000456302 ; ENSP00000392059 ; ENSG00000091181 . [Q01344-3 ]
GeneIDi 3568.
KEGGi hsa:3568.
UCSCi uc010hbr.3. human.
uc010hbs.3. human. [Q01344-1 ]
uc010hbt.2. human. [Q01344-2 ]
uc010hbu.2. human. [Q01344-3 ]
uc011asl.2. human.

Organism-specific databases

CTDi 3568.
GeneCardsi GC03M003111.
HGNCi HGNC:6017. IL5RA.
HPAi HPA013196.
MIMi 147851. gene.
neXtProti NX_Q01344.
PharmGKBi PA29834.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43089.
GeneTreei ENSGT00530000063295.
HOGENOMi HOG000070224.
HOVERGENi HBG052117.
InParanoidi Q01344.
KOi K05067.
OMAi APEDTQY.
OrthoDBi EOG71P2B1.
PhylomeDBi Q01344.
TreeFami TF331549.

Enzyme and pathway databases

Reactomei REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinki Q01344.

Miscellaneous databases

EvolutionaryTracei Q01344.
GeneWikii Interleukin_5_receptor_alpha_subunit.
GenomeRNAii 3568.
NextBioi 13936.
PROi Q01344.
SOURCEi Search...

Gene expression databases

Bgeei Q01344.
CleanExi HS_IL5RA.
ExpressionAtlasi Q01344. baseline and differential.
Genevestigatori Q01344.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015321. IL-6_rcpt_alpha-bd.
IPR003532. Short_hematopoietin_rcpt_2_CS.
[Graphical view ]
Pfami PF09240. IL6Ra-bind. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
PROSITEi PS50853. FN3. 2 hits.
PS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF."
    Tavernier J., Devos R., Cornelis S., Tuypens T., van der Heyden J., Fiers W., Plaetinck G.
    Cell 66:1175-1184(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Molecular cloning and expression of the human interleukin 5 receptor."
    Murata Y., Takaki S., Migita M., Kikuchi Y., Tominaga A., Takatsu K.
    J. Exp. Med. 175:341-351(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT VAL-129.
    Tissue: Peripheral blood.
  3. "Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit."
    Tavernier J., Tuypens T., Plaetinck G., Verhee A., Fiers W., Devos R.
    Proc. Natl. Acad. Sci. U.S.A. 89:7041-7045(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
  4. "Isolation of the variants for human interleukin-5 receptor alpha subunit."
    Ishihara K., Yamada M., Hirasawa N., Ohuchi K.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  5. "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 4).
    Tissue: Trachea.
  6. SeattleSNPs variation discovery resource
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-129 AND ALA-262.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm."
    Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.
    Structure 11:845-853(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-420 IN COMPLEX WITH SDCBP.
  9. "Structure analysis of the IL-5 ligand-receptor complex reveals a wrench-like architecture for IL-5Ralpha."
    Patino E., Kotzsch A., Saremba S., Nickel J., Schmitz W., Sebald W., Mueller T.D.
    Structure 19:1864-1875(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 20-332 IN COMPLEX WITH IL5, DISULFIDE BONDS.

Entry informationi

Entry nameiIL5RA_HUMAN
AccessioniPrimary (citable) accession number: Q01344
Secondary accession number(s): B3IU77
, B4E2G0, Q14633, Q15469, Q6ISX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 152 of the entry and version 2 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 3
    Human chromosome 3: 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

Dasty 3