Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32927

- IL3RB_HUMAN

UniProt

P32927 - IL3RB_HUMAN

Protein

Cytokine receptor common subunit beta

Gene

CSF2RB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor.

    GO - Molecular functioni

    1. cytokine receptor activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. receptor activity Source: ProtInc

    GO - Biological processi

    1. cellular response to interleukin-3 Source: GOC
    2. interleukin-3-mediated signaling pathway Source: GOC
    3. interleukin-5-mediated signaling pathway Source: GOC
    4. respiratory gaseous exchange Source: ProtInc
    5. response to lipopolysaccharide Source: Ensembl
    6. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinkiP32927.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytokine receptor common subunit beta
    Alternative name(s):
    CDw131
    GM-CSF/IL-3/IL-5 receptor common beta subunit
    CD_antigen: CD131
    Gene namesi
    Name:CSF2RB
    Synonyms:IL3RB, IL5RB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2436. CSF2RB.

    Subcellular locationi

    GO - Cellular componenti

    1. granulocyte macrophage colony-stimulating factor receptor complex Source: UniProtKB
    2. integral component of plasma membrane Source: UniProtKB
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Pulmonary surfactant metabolism dysfunction 5 (SMDP5) [MIM:614370]: A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi614370. phenotype.
    Orphaneti264675. Congenital pulmonary alveolar proteinosis.
    PharmGKBiPA26939.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 897881Cytokine receptor common subunit betaPRO_0000010862Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 45
    Glycosylationi58 – 581N-linked (GlcNAc...)2 Publications
    Disulfide bondi75 ↔ 96
    Disulfide bondi86 ↔ 91
    Glycosylationi191 – 1911N-linked (GlcNAc...)2 Publications
    Disulfide bondi250 ↔ 260
    Disulfide bondi289 ↔ 306
    Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis
    Modified residuei766 – 7661PhosphotyrosineBy similarity

    Post-translational modificationi

    May be phosphorylated by LYN.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP32927.
    PRIDEiP32927.

    PTM databases

    PhosphoSiteiP32927.

    Expressioni

    Gene expression databases

    ArrayExpressiP32927.
    BgeeiP32927.
    CleanExiHS_CSF2RB.
    GenevestigatoriP32927.

    Organism-specific databases

    HPAiCAB010251.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors. The signaling GM-CSF receptor complex is a dodecamer of two head-to-head hexamers of two alpha, two beta, and two ligand subunits. Interacts with TMEM102; this interaction occurs preferentially in the absence of CSF2. Interacts with LYN By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSF2P041412EBI-1809771,EBI-1809826
    IL5P051132EBI-1809771,EBI-2435811
    ITGB1P055565EBI-1809771,EBI-703066
    JAK2O606744EBI-1809771,EBI-518647

    Protein-protein interaction databases

    BioGridi107826. 15 interactions.
    DIPiDIP-127N.
    IntActiP32927. 14 interactions.
    MINTiMINT-105697.
    STRINGi9606.ENSP00000384053.

    Structurei

    Secondary structure

    1
    897
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 325
    Beta strandi34 – 374
    Beta strandi39 – 5012
    Helixi51 – 544
    Beta strandi59 – 668
    Beta strandi69 – 724
    Beta strandi75 – 773
    Beta strandi88 – 9912
    Beta strandi108 – 11710
    Beta strandi121 – 1266
    Helixi127 – 1293
    Beta strandi137 – 1448
    Beta strandi147 – 1537
    Helixi166 – 1683
    Beta strandi169 – 1779
    Helixi182 – 1843
    Beta strandi186 – 19712
    Turni199 – 2013
    Beta strandi207 – 21610
    Beta strandi218 – 2214
    Beta strandi233 – 2364
    Beta strandi242 – 2443
    Beta strandi246 – 2527
    Beta strandi254 – 26512
    Helixi266 – 2694
    Beta strandi274 – 2796
    Beta strandi292 – 2954
    Turni298 – 3003
    Beta strandi301 – 3099
    Turni313 – 3153
    Beta strandi318 – 3258
    Beta strandi330 – 3334
    Helixi334 – 3363
    Beta strandi337 – 3393
    Beta strandi344 – 3485
    Beta strandi350 – 3523
    Beta strandi355 – 3595
    Beta strandi365 – 3673
    Beta strandi370 – 3778
    Beta strandi379 – 3813
    Helixi383 – 3853
    Beta strandi388 – 3936
    Beta strandi395 – 3984
    Beta strandi405 – 4073
    Beta strandi409 – 4168
    Beta strandi418 – 4203
    Beta strandi432 – 4365

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C8PNMR-A338-438[»]
    1EGJX-ray2.80A338-438[»]
    1GH7X-ray3.00A/B25-437[»]
    2GYSX-ray2.70A/B25-437[»]
    3CXEX-ray3.30A25-438[»]
    ProteinModelPortaliP32927.
    SMRiP32927. Positions 25-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32927.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 443427ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini461 – 897437CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei444 – 46017HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini133 – 240108Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 43698Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi425 – 4295WSXWS motif
    Motifi474 – 4829Box 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

    eggNOGiNOG39324.
    HOGENOMiHOG000113049.
    HOVERGENiHBG052113.
    KOiK04738.
    OMAiCRWADTQ.
    OrthoDBiEOG7966FT.
    PhylomeDBiP32927.
    TreeFamiTF337996.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR013783. Ig-like_fold.
    IPR015321. IL-6_rcpt_alpha-bd.
    IPR011365. IL3_rcpt_beta.
    [Graphical view]
    PfamiPF00041. fn3. 1 hit.
    PF09240. IL6Ra-bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001956. IL3R_beta_c. 1 hit.
    SMARTiSM00060. FN3. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 4 hits.
    PROSITEiPS50853. FN3. 2 hits.
    PS01355. HEMATOPO_REC_S_F1. 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: P32927-1) [UniParc]FASTAAdd to Basket

    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

    MVLAQGLLSM ALLALCWERS LAGAEETIPL QTLRCYNDYT SHITCRWADT    50
    QDAQRLVNVT LIRRVNEDLL EPVSCDLSDD MPWSACPHPR CVPRRCVIPC 100
    QSFVVTDVDY FSFQPDRPLG TRLTVTLTQH VQPPEPRDLQ ISTDQDHFLL 150
    TWSVALGSPQ SHWLSPGDLE FEVVYKRLQD SWEDAAILLS NTSQATLGPE 200
    HLMPSSTYVA RVRTRLAPGS RLSGRPSKWS PEVCWDSQPG DEAQPQNLEC 250
    FFDGAAVLSC SWEVRKEVAS SVSFGLFYKP SPDAGEEECS PVLREGLGSL 300
    HTRHHCQIPV PDPATHGQYI VSVQPRRAEK HIKSSVNIQM APPSLNVTKD 350
    GDSYSLRWET MKMRYEHIDH TFEIQYRKDT ATWKDSKTET LQNAHSMALP 400
    ALEPSTRYWA RVRVRTSRTG YNGIWSEWSE ARSWDTESVL PMWVLALIVI 450
    FLTIAVLLAL RFCGIYGYRL RRKWEEKIPN PSKSHLFQNG SAELWPPGSM 500
    SAFTSGSPPH QGPWGSRFPE LEGVFPVGFG DSEVSPLTIE DPKHVCDPPS 550
    GPDTTPAASD LPTEQPPSPQ PGPPAASHTP EKQASSFDFN GPYLGPPHSR 600
    SLPDILGQPE PPQEGGSQKS PPPGSLEYLC LPAGGQVQLV PLAQAMGPGQ 650
    AVEVERRPSQ GAAGSPSLES GGGPAPPALG PRVGGQDQKD SPVAIPMSSG 700
    DTEDPGVASG YVSSADLVFT PNSGASSVSL VPSLGLPSDQ TPSLCPGLAS 750
    GPPGAPGPVK SGFEGYVELP PIEGRSPRSP RNNPVPPEAK SPVLNPGERP 800
    ADVSPTSPQP EGLLVLQQVG DYCFLPGLGP GPLSLRSKPS SPGPGPEIKN 850
    LDQAFQVKKP PGQAVPQVPV IQLFKALKQQ DYLSLPPWEV NKPGEVC 897
    Length:897
    Mass (Da):97,336
    Last modified:February 1, 1996 - v2
    Checksum:i3398E37FDB8F393A
    GO
    Isoform 2 (identifier: P32927-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         285-285: G → GSAVLLR

    Show »
    Length:903
    Mass (Da):97,976
    Checksum:iAE8FFF1721CD63F2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti249 – 2491E → Q.
    Corresponds to variant rs16845 [ dbSNP | Ensembl ].
    VAR_042521
    Natural varianti603 – 6031P → T.1 Publication
    Corresponds to variant rs1801122 [ dbSNP | Ensembl ].
    VAR_014801
    Natural varianti647 – 6471G → V.
    Corresponds to variant rs1801115 [ dbSNP | Ensembl ].
    VAR_014802
    Natural varianti652 – 6521V → M.
    Corresponds to variant rs1801114 [ dbSNP | Ensembl ].
    VAR_014803
    Natural varianti696 – 6961P → S.
    Corresponds to variant rs16997517 [ dbSNP | Ensembl ].
    VAR_042522

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei285 – 2851G → GSAVLLR in isoform 2. 1 PublicationVSP_032798

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59941 mRNA. Translation: AAA18171.1.
    CR456428 mRNA. Translation: CAG30314.1.
    AL008637, AL133392 Genomic DNA. Translation: CAI17999.1.
    AL008637, AL133392 Genomic DNA. Translation: CAQ10744.1.
    CH471095 Genomic DNA. Translation: EAW60125.1.
    CH471095 Genomic DNA. Translation: EAW60126.1.
    CCDSiCCDS13936.1. [P32927-1]
    PIRiA39255.
    RefSeqiNP_000386.1. NM_000395.2. [P32927-1]
    XP_005261397.1. XM_005261340.1. [P32927-2]
    UniGeneiHs.592192.

    Genome annotation databases

    EnsembliENST00000262825; ENSP00000262825; ENSG00000100368. [P32927-2]
    ENST00000403662; ENSP00000384053; ENSG00000100368. [P32927-1]
    ENST00000406230; ENSP00000385271; ENSG00000100368. [P32927-2]
    GeneIDi1439.
    KEGGihsa:1439.
    UCSCiuc003aqa.4. human. [P32927-1]
    uc003aqc.4. human. [P32927-2]

    Polymorphism databases

    DMDMi1345923.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59941 mRNA. Translation: AAA18171.1 .
    CR456428 mRNA. Translation: CAG30314.1 .
    AL008637 , AL133392 Genomic DNA. Translation: CAI17999.1 .
    AL008637 , AL133392 Genomic DNA. Translation: CAQ10744.1 .
    CH471095 Genomic DNA. Translation: EAW60125.1 .
    CH471095 Genomic DNA. Translation: EAW60126.1 .
    CCDSi CCDS13936.1. [P32927-1 ]
    PIRi A39255.
    RefSeqi NP_000386.1. NM_000395.2. [P32927-1 ]
    XP_005261397.1. XM_005261340.1. [P32927-2 ]
    UniGenei Hs.592192.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C8P NMR - A 338-438 [» ]
    1EGJ X-ray 2.80 A 338-438 [» ]
    1GH7 X-ray 3.00 A/B 25-437 [» ]
    2GYS X-ray 2.70 A/B 25-437 [» ]
    3CXE X-ray 3.30 A 25-438 [» ]
    ProteinModelPortali P32927.
    SMRi P32927. Positions 25-438.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107826. 15 interactions.
    DIPi DIP-127N.
    IntActi P32927. 14 interactions.
    MINTi MINT-105697.
    STRINGi 9606.ENSP00000384053.

    Chemistry

    ChEMBLi CHEMBL2364169.
    DrugBanki DB00020. Sargramostim.

    PTM databases

    PhosphoSitei P32927.

    Polymorphism databases

    DMDMi 1345923.

    Proteomic databases

    PaxDbi P32927.
    PRIDEi P32927.

    Protocols and materials databases

    DNASUi 1439.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262825 ; ENSP00000262825 ; ENSG00000100368 . [P32927-2 ]
    ENST00000403662 ; ENSP00000384053 ; ENSG00000100368 . [P32927-1 ]
    ENST00000406230 ; ENSP00000385271 ; ENSG00000100368 . [P32927-2 ]
    GeneIDi 1439.
    KEGGi hsa:1439.
    UCSCi uc003aqa.4. human. [P32927-1 ]
    uc003aqc.4. human. [P32927-2 ]

    Organism-specific databases

    CTDi 1439.
    GeneCardsi GC22P037309.
    HGNCi HGNC:2436. CSF2RB.
    HPAi CAB010251.
    MIMi 138981. gene.
    614370. phenotype.
    neXtProti NX_P32927.
    Orphaneti 264675. Congenital pulmonary alveolar proteinosis.
    PharmGKBi PA26939.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39324.
    HOGENOMi HOG000113049.
    HOVERGENi HBG052113.
    KOi K04738.
    OMAi CRWADTQ.
    OrthoDBi EOG7966FT.
    PhylomeDBi P32927.
    TreeFami TF337996.

    Enzyme and pathway databases

    Reactomei REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    SignaLinki P32927.

    Miscellaneous databases

    EvolutionaryTracei P32927.
    GenomeRNAii 1439.
    NextBioi 5889.
    PROi P32927.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P32927.
    Bgeei P32927.
    CleanExi HS_CSF2RB.
    Genevestigatori P32927.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR003531. Hempt_rcpt_S_F1_CS.
    IPR013783. Ig-like_fold.
    IPR015321. IL-6_rcpt_alpha-bd.
    IPR011365. IL3_rcpt_beta.
    [Graphical view ]
    Pfami PF00041. fn3. 1 hit.
    PF09240. IL6Ra-bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001956. IL3R_beta_c. 1 hit.
    SMARTi SM00060. FN3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 4 hits.
    PROSITEi PS50853. FN3. 2 hits.
    PS01355. HEMATOPO_REC_S_F1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a second subunit of the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF): reconstitution of a high-affinity GM-CSF receptor."
      Hayashida K., Kitamura T., Gorman D.M., Arai K., Yokota T., Miyajima A.
      Proc. Natl. Acad. Sci. U.S.A. 87:9655-9659(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Kitamura T.
      Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 454.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "CBAP interacts with the un-liganded common beta-subunit of the GM-CSF/IL-3/IL-5 receptor and induces apoptosis via mitochondrial dysfunction."
      Kao C.J., Chiang Y.J., Chen P.H., Lin K.R., Hwang P.I., Yang-Yen H.F., Yen J.J.
      Oncogene 27:1397-1403(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM102.
    7. "Adult-onset hereditary pulmonary alveolar proteinosis caused by a single-base deletion in CSF2RB."
      Tanaka T., Motoi N., Tsuchihashi Y., Tazawa R., Kaneko C., Nei T., Yamamoto T., Hayashi T., Tagawa T., Nagayasu T., Kuribayashi F., Ariyoshi K., Nakata K., Morimoto K.
      J. Med. Genet. 48:205-209(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SMDP5.
    8. "The solution structure of the cytokine-binding domain of the common beta-chain of the receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3 and interleukin-5."
      Mulhern T.D., Lopez A.F., D'Andrea R.J., Gaunt C., Vandeleur L., Vadas M.A., Booker G.W., Bagley C.J.
      J. Mol. Biol. 297:989-1001(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 338-438.
    9. "Structure of the activation domain of the GM-CSF/IL-3/IL-5 receptor common beta-chain bound to an antagonist."
      Rossjohn J., McKinstry W.J., Woodcock J.M., McClure B.J., Hercus T.R., Parker M.W., Lopez A.F., Bagley C.J.
      Blood 95:2491-2498(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 338-438.
    10. "Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration."
      Carr P.D., Gustin S.E., Church A.P., Murphy J.M., Ford S.C., Mann D.A., Woltring D.M., Walker I., Ollis D.L., Young I.G.
      Cell 104:291-300(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-437.
    11. "An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope."
      Carr P.D., Conlan F., Ford S., Ollis D.L., Young I.G.
      Acta Crystallogr. F 62:509-513(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 25-443, DISULFIDE BONDS, SUBUNIT, GLYCOSYLATION AT ASN-58 AND ASN-191.
    12. "The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation."
      Hansen G., Hercus T.R., McClure B.J., Stomski F.C., Dottore M., Powell J., Ramshaw H., Woodcock J.M., Xu Y., Guthridge M., McKinstry W.J., Lopez A.F., Parker M.W.
      Cell 134:496-507(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-438 IN COMPLEX WITH CSF2RA AND CSF2, SUBUNIT, GLYCOSYLATION AT ASN-58 AND ASN-191, DISULFIDE BONDS.
    13. "Human pulmonary alveolar proteinosis associated with a defect in GM-CSF/IL-3/IL-5 receptor common beta chain expression."
      Dirksen U., Nishinakamura R., Groneck P., Hattenhorst U., Nogee L., Murray R., Burdach S.
      J. Clin. Invest. 100:2211-2217(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THR-603.

    Entry informationi

    Entry nameiIL3RB_HUMAN
    AccessioniPrimary (citable) accession number: P32927
    Secondary accession number(s): Q5JZI1, Q6ICE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 156 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 22
      Human chromosome 22: 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