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P26951

- IL3RA_HUMAN

UniProt

P26951 - IL3RA_HUMAN

Protein

Interleukin-3 receptor subunit alpha

Gene

IL3RA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    This is a receptor for interleukin-3.

    GO - Molecular functioni

    1. interleukin-3 receptor activity Source: ProtInc

    GO - Biological processi

    1. cellular response to interleukin-3 Source: GOC
    2. interleukin-3-mediated signaling pathway Source: GOC

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinkiP26951.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interleukin-3 receptor subunit alpha
    Short name:
    IL-3 receptor subunit alpha
    Short name:
    IL-3R subunit alpha
    Short name:
    IL-3R-alpha
    Short name:
    IL-3RA
    Alternative name(s):
    CD_antigen: CD123
    Gene namesi
    Name:IL3RA
    Synonyms:IL3R
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:6012. IL3RA.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29831.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 378360Interleukin-3 receptor subunit alphaPRO_0000010883Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP26951.
    PRIDEiP26951.

    PTM databases

    PhosphoSiteiP26951.

    Expressioni

    Gene expression databases

    ArrayExpressiP26951.
    BgeeiP26951.
    CleanExiHS_IL3RA.
    GenevestigatoriP26951.

    Organism-specific databases

    HPAiCAB018374.
    HPA003539.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi109778. 11 interactions.
    DIPiDIP-3293N.
    IntActiP26951. 12 interactions.
    MINTiMINT-7241956.
    STRINGi9606.ENSP00000327890.

    Structurei

    Secondary structure

    1
    378
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 338
    Turni34 – 374
    Beta strandi38 – 458
    Beta strandi50 – 545
    Turni55 – 573
    Beta strandi58 – 614
    Turni64 – 663
    Beta strandi67 – 693
    Beta strandi75 – 773
    Beta strandi79 – 857
    Turni86 – 894
    Beta strandi90 – 978
    Beta strandi106 – 11510
    Turni116 – 1183
    Beta strandi119 – 1268
    Beta strandi135 – 1428
    Turni143 – 1453
    Beta strandi147 – 1504
    Beta strandi153 – 1564
    Beta strandi162 – 1687
    Helixi170 – 1734
    Turni174 – 1763
    Beta strandi178 – 18710
    Beta strandi189 – 1913
    Beta strandi196 – 2016
    Helixi202 – 2054
    Beta strandi212 – 2143
    Beta strandi223 – 2275
    Beta strandi236 – 2427
    Beta strandi250 – 2567
    Beta strandi258 – 2614
    Beta strandi270 – 2767
    Turni277 – 2793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JZJX-ray2.80C/D20-307[»]
    ProteinModelPortaliP26951.
    SMRiP26951. Positions 101-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 305287ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini326 – 37853CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei306 – 32520HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi282 – 2865WSXWS motif
    Motifi334 – 3429Box 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

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG44788.
    HOGENOMiHOG000201004.
    HOVERGENiHBG107484.
    InParanoidiP26951.
    KOiK04737.
    OMAiKNLRMEP.
    OrthoDBiEOG7TJ3J7.
    PhylomeDBiP26951.
    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.
    PROSITEiPS01356. HEMATOPO_REC_S_F2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P26951-1) [UniParc]FASTAAdd to Basket

    Also known as: SP1

    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

    MVLLWLTLLL IALPCLLQTK EDPNPPITNL RMKAKAQQLT WDLNRNVTDI    50
    ECVKDADYSM PAVNNSYCQF GAISLCEVTN YTVRVANPPF STWILFPENS 100
    GKPWAGAENL TCWIHDVDFL SCSWAVGPGA PADVQYDLYL NVANRRQQYE 150
    CLHYKTDAQG TRIGCRFDDI SRLSSGSQSS HILVRGRSAA FGIPCTDKFV 200
    VFSQIEILTP PNMTAKCNKT HSFMHWKMRS HFNRKFRYEL QIQKRMQPVI 250
    TEQVRDRTSF QLLNPGTYTV QIRARERVYE FLSAWSTPQR FECDQEEGAN 300
    TRAWRTSLLI ALGTLLALVC VFVICRRYLV MQRLFPRIPH MKDPIGDSFQ 350
    NDKLVVWEAG KAGLEECLVT EVQVVQKT 378
    Length:378
    Mass (Da):43,330
    Last modified:October 1, 1993 - v1
    Checksum:i716CE1803F2E5FC0
    GO
    Isoform 2 (identifier: P26951-2) [UniParc]FASTAAdd to Basket

    Also known as: SP2

    The sequence of this isoform differs from the canonical sequence as follows:
         22-100: DPNPPITNLR...STWILFPENS → G

    Show »
    Length:300
    Mass (Da):34,466
    Checksum:iD90ED8C49F3BD8CC
    GO

    Sequence cautioni

    The sequence BAA08393.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121A → T.2 Publications
    Corresponds to variant rs6647004 [ dbSNP | Ensembl ].
    VAR_021113
    Natural varianti77 – 771E → G.1 Publication
    Corresponds to variant rs17886756 [ dbSNP | Ensembl ].
    VAR_021114
    Natural varianti123 – 1231S → T.1 Publication
    Corresponds to variant rs17883572 [ dbSNP | Ensembl ].
    VAR_021115
    Natural varianti323 – 3231V → L.1 Publication
    Corresponds to variant rs17883366 [ dbSNP | Ensembl ].
    VAR_021116

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei22 – 10079DPNPP…FPENS → G in isoform 2. 1 PublicationVSP_040622Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74782 mRNA. Translation: AAA59148.1.
    D49410 Genomic DNA. Translation: BAA08393.1. Sequence problems.
    FJ550347 mRNA. Translation: ACM24116.1.
    AK290568 mRNA. Translation: BAF83257.1.
    AY789109 Genomic DNA. Translation: AAV40832.1.
    BX296563, AL683870, BX119906 Genomic DNA. Translation: CAI39694.1.
    BX296563, BX119906 Genomic DNA. Translation: CAI39695.1.
    BX901885 Genomic DNA. No translation available.
    BC035407 mRNA. Translation: AAH35407.1.
    CCDSiCCDS14113.1. [P26951-1]
    CCDS59158.1. [P26951-2]
    PIRiA40266.
    RefSeqiNP_001254642.1. NM_001267713.1.
    NP_002174.1. NM_002183.3. [P26951-1]
    XP_005274488.1. XM_005274431.2. [P26951-1]
    XP_005274837.1. XM_005274780.2. [P26951-1]
    UniGeneiHs.632790.

    Genome annotation databases

    EnsembliENST00000331035; ENSP00000327890; ENSG00000185291. [P26951-1]
    ENST00000381469; ENSP00000370878; ENSG00000185291. [P26951-2]
    GeneIDi3563.
    KEGGihsa:3563.
    UCSCiuc004cps.3. human. [P26951-1]

    Polymorphism databases

    DMDMi417184.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74782 mRNA. Translation: AAA59148.1 .
    D49410 Genomic DNA. Translation: BAA08393.1 . Sequence problems.
    FJ550347 mRNA. Translation: ACM24116.1 .
    AK290568 mRNA. Translation: BAF83257.1 .
    AY789109 Genomic DNA. Translation: AAV40832.1 .
    BX296563 , AL683870 , BX119906 Genomic DNA. Translation: CAI39694.1 .
    BX296563 , BX119906 Genomic DNA. Translation: CAI39695.1 .
    BX901885 Genomic DNA. No translation available.
    BC035407 mRNA. Translation: AAH35407.1 .
    CCDSi CCDS14113.1. [P26951-1 ]
    CCDS59158.1. [P26951-2 ]
    PIRi A40266.
    RefSeqi NP_001254642.1. NM_001267713.1.
    NP_002174.1. NM_002183.3. [P26951-1 ]
    XP_005274488.1. XM_005274431.2. [P26951-1 ]
    XP_005274837.1. XM_005274780.2. [P26951-1 ]
    UniGenei Hs.632790.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JZJ X-ray 2.80 C/D 20-307 [» ]
    ProteinModelPortali P26951.
    SMRi P26951. Positions 101-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109778. 11 interactions.
    DIPi DIP-3293N.
    IntActi P26951. 12 interactions.
    MINTi MINT-7241956.
    STRINGi 9606.ENSP00000327890.

    Chemistry

    DrugBanki DB00020. Sargramostim.
    GuidetoPHARMACOLOGYi 1705.

    PTM databases

    PhosphoSitei P26951.

    Polymorphism databases

    DMDMi 417184.

    Proteomic databases

    PaxDbi P26951.
    PRIDEi P26951.

    Protocols and materials databases

    DNASUi 3563.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331035 ; ENSP00000327890 ; ENSG00000185291 . [P26951-1 ]
    ENST00000381469 ; ENSP00000370878 ; ENSG00000185291 . [P26951-2 ]
    GeneIDi 3563.
    KEGGi hsa:3563.
    UCSCi uc004cps.3. human. [P26951-1 ]

    Organism-specific databases

    CTDi 3563.
    GeneCardsi GC0XP001455.
    HGNCi HGNC:6012. IL3RA.
    HPAi CAB018374.
    HPA003539.
    MIMi 308385. gene.
    430000. gene.
    neXtProti NX_P26951.
    PharmGKBi PA29831.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44788.
    HOGENOMi HOG000201004.
    HOVERGENi HBG107484.
    InParanoidi P26951.
    KOi K04737.
    OMAi KNLRMEP.
    OrthoDBi EOG7TJ3J7.
    PhylomeDBi P26951.
    TreeFami TF331549.

    Enzyme and pathway databases

    Reactomei REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinki P26951.

    Miscellaneous databases

    GeneWikii IL3RA.
    GenomeRNAii 3563.
    NextBioi 13916.
    PROi P26951.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26951.
    Bgeei P26951.
    CleanExi HS_IL3RA.
    Genevestigatori P26951.

    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 PS01356. HEMATOPO_REC_S_F2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors."
      Kitamura T., Sato N., Arai K., Miyajima A.
      Cell 66:1165-1174(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure of the gene encoding the alpha subunit of the human interleukin 3 receptor."
      Kosugi H., Nakagawa Y., Hotta T., Saito H., Miyajima A., Arai K., Yokota T.
      Biochem. Biophys. Res. Commun. 208:360-367(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "A new isoform of IL-3 receptor alpha with novel differentiation activity and high affinity binding mode."
      Chen J., Olsen J., Ford S., Mirza S., Walker A., Murphy J.M., Young I.G.
      J. Biol. Chem. 284:5763-5773(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    4. "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 1).
      Tissue: Lung.
    5. SeattleSNPs variation discovery resource
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-12; GLY-77; THR-123 AND LEU-323.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-12.
    7. "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: Brain.

    Entry informationi

    Entry nameiIL3RA_HUMAN
    AccessioniPrimary (citable) accession number: P26951
    Secondary accession number(s): A8K3F3
    , B9VI81, Q5HYQ7, Q5HYQ8, Q9UEH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 138 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

    Miscellaneous

    The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.

    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 X
      Human chromosome X: 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