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P32927

- IL3RB_HUMAN

UniProt

P32927 - IL3RB_HUMAN

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Protein
Cytokine receptor common subunit beta
Gene
CSF2RB, IL3RB, IL5RB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
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.
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 443427Extracellular Reviewed prediction
Add
BLAST
Transmembranei444 – 46017Helical; Reviewed prediction
Add
BLAST
Topological domaini461 – 897437Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Chaini17 – 897881Cytokine receptor common subunit beta
PRO_0000010862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 452 Publications
Glycosylationi58 – 581N-linked (GlcNAc...)2 Publications
Disulfide bondi75 ↔ 962 Publications
Disulfide bondi86 ↔ 912 Publications
Glycosylationi191 – 1911N-linked (GlcNAc...)2 Publications
Disulfide bondi250 ↔ 2602 Publications
Disulfide bondi289 ↔ 3062 Publications
Glycosylationi346 – 3461N-linked (GlcNAc...) Reviewed prediction
Modified residuei766 – 7661Phosphotyrosine By 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.3 Publications

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

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.

Miscellaneous databases

EvolutionaryTraceiP32927.

Family & Domainsi

Domains and Repeats

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

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.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 155 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

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