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Q01344

- IL5RA_HUMAN

UniProt

Q01344 - IL5RA_HUMAN

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
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. interleukin-5 receptor activity Source: ProtInc
    2. protein binding Source: IntAct

    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

    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

    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

    PaxDbiQ01344.
    PRIDEiQ01344.

    PTM databases

    PhosphoSiteiQ01344.

    Expressioni

    Tissue specificityi

    Expressed on eosinophils and basophils.

    Gene expression databases

    ArrayExpressiQ01344.
    BgeeiQ01344.
    CleanExiHS_IL5RA.
    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.
    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

    MIIVAHVLLI LLGATEILQA DLLPDEKISL LPPVNFTIKV TGLAQVLLQW    50
    KPNPDQEQRN VNLEYQVKIN APKEDDYETR ITESKCVTIL HKGFSASVRT 100
    ILQNDHSLLA SSWASAELHA PPGSPGTSIV NLTCTTNTTE DNYSRLRSYQ 150
    VSLHCTWLVG TDAPEDTQYF LYYRYGSWTE ECQEYSKDTL GRNIACWFPR 200
    TFILSKGRDW LAVLVNGSSK HSAIRPFDQL FALHAIDQIN PPLNVTAEIE 250
    GTRLSIQWEK PVSAFPIHCF DYEVKIHNTR NGYLQIEKLM TNAFISIIDD 300
    LSKYDVQVRA AVSSMCREAG LWSEWSQPIY VGNDEHKPLR EWFVIVIMAT 350
    ICFILLILSL ICKICHLWIK LFPPIPAPKS NIKDLFVTTN YEKAGSSETE 400
    IEVICYIEKP GVETLEDSVF 420
    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.
    UCSCiuc010hbs.3. human. [Q01344-1]
    uc010hbt.2. human. [Q01344-2]
    uc010hbu.2. human. [Q01344-3]

    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

    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 uc010hbs.3. human. [Q01344-1 ]
    uc010hbt.2. human. [Q01344-2 ]
    uc010hbu.2. human. [Q01344-3 ]

    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.
    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

    ArrayExpressi Q01344.
    Bgeei Q01344.
    CleanExi HS_IL5RA.
    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

    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 1, 2014
    This is version 151 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