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P32927 (IL3RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytokine receptor common subunit beta
Alternative name(s):
CDw131
GM-CSF/IL-3/IL-5 receptor common beta subunit
CD_antigen=CD131
Gene names
Name:CSF2RB
Synonyms:IL3RB, IL5RB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length897 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.6 Ref.11 Ref.12

Subcellular location

Membrane; Single-pass type I membrane protein.

Domain

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.

Post-translational modification

May be phosphorylated by LYN By similarity.

Involvement in disease

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. Ref.7

Sequence similarities

Belongs to the type I cytokine receptor family. Type 4 subfamily.

Contains 2 fibronectin type-III domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P32927-1)

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.
Isoform 2 (identifier: P32927-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 897881Cytokine receptor common subunit beta
PRO_0000010862

Regions

Topological domain17 – 443427Extracellular Potential
Transmembrane444 – 46017Helical; Potential
Topological domain461 – 897437Cytoplasmic Potential
Domain133 – 240108Fibronectin type-III 1
Domain339 – 43698Fibronectin type-III 2
Motif425 – 4295WSXWS motif
Motif474 – 4829Box 1 motif

Amino acid modifications

Modified residue7661Phosphotyrosine By similarity
Glycosylation581N-linked (GlcNAc...) Ref.11 Ref.12
Glycosylation1911N-linked (GlcNAc...) Ref.11 Ref.12
Glycosylation3461N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 45 Ref.11 Ref.12
Disulfide bond75 ↔ 96 Ref.11 Ref.12
Disulfide bond86 ↔ 91 Ref.11 Ref.12
Disulfide bond250 ↔ 260 Ref.11 Ref.12
Disulfide bond289 ↔ 306 Ref.11 Ref.12

Natural variations

Alternative sequence2851G → GSAVLLR in isoform 2.
VSP_032798
Natural variant2491E → Q.
Corresponds to variant rs16845 [ dbSNP | Ensembl ].
VAR_042521
Natural variant6031P → T. Ref.13
Corresponds to variant rs1801122 [ dbSNP | Ensembl ].
VAR_014801
Natural variant6471G → V.
Corresponds to variant rs1801115 [ dbSNP | Ensembl ].
VAR_014802
Natural variant6521V → M.
Corresponds to variant rs1801114 [ dbSNP | Ensembl ].
VAR_014803
Natural variant6961P → S.
Corresponds to variant rs16997517 [ dbSNP | Ensembl ].
VAR_042522

Secondary structure

........................................................................................ 897
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 3398E37FDB8F393A

FASTA89797,336
        10         20         30         40         50         60 
MVLAQGLLSM ALLALCWERS LAGAEETIPL QTLRCYNDYT SHITCRWADT QDAQRLVNVT 

        70         80         90        100        110        120 
LIRRVNEDLL EPVSCDLSDD MPWSACPHPR CVPRRCVIPC QSFVVTDVDY FSFQPDRPLG 

       130        140        150        160        170        180 
TRLTVTLTQH VQPPEPRDLQ ISTDQDHFLL TWSVALGSPQ SHWLSPGDLE FEVVYKRLQD 

       190        200        210        220        230        240 
SWEDAAILLS NTSQATLGPE HLMPSSTYVA RVRTRLAPGS RLSGRPSKWS PEVCWDSQPG 

       250        260        270        280        290        300 
DEAQPQNLEC FFDGAAVLSC SWEVRKEVAS SVSFGLFYKP SPDAGEEECS PVLREGLGSL 

       310        320        330        340        350        360 
HTRHHCQIPV PDPATHGQYI VSVQPRRAEK HIKSSVNIQM APPSLNVTKD GDSYSLRWET 

       370        380        390        400        410        420 
MKMRYEHIDH TFEIQYRKDT ATWKDSKTET LQNAHSMALP ALEPSTRYWA RVRVRTSRTG 

       430        440        450        460        470        480 
YNGIWSEWSE ARSWDTESVL PMWVLALIVI FLTIAVLLAL RFCGIYGYRL RRKWEEKIPN 

       490        500        510        520        530        540 
PSKSHLFQNG SAELWPPGSM SAFTSGSPPH QGPWGSRFPE LEGVFPVGFG DSEVSPLTIE 

       550        560        570        580        590        600 
DPKHVCDPPS GPDTTPAASD LPTEQPPSPQ PGPPAASHTP EKQASSFDFN GPYLGPPHSR 

       610        620        630        640        650        660 
SLPDILGQPE PPQEGGSQKS PPPGSLEYLC LPAGGQVQLV PLAQAMGPGQ AVEVERRPSQ 

       670        680        690        700        710        720 
GAAGSPSLES GGGPAPPALG PRVGGQDQKD SPVAIPMSSG DTEDPGVASG YVSSADLVFT 

       730        740        750        760        770        780 
PNSGASSVSL VPSLGLPSDQ TPSLCPGLAS GPPGAPGPVK SGFEGYVELP PIEGRSPRSP 

       790        800        810        820        830        840 
RNNPVPPEAK SPVLNPGERP ADVSPTSPQP EGLLVLQQVG DYCFLPGLGP GPLSLRSKPS 

       850        860        870        880        890 
SPGPGPEIKN LDQAFQVKKP PGQAVPQVPV IQLFKALKQQ DYLSLPPWEV NKPGEVC 

« Hide

Isoform 2 [UniParc].

Checksum: AE8FFF1721CD63F2
Show »

FASTA90397,976

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA39255.
RefSeqNP_000386.1. NM_000395.2.
XP_005261397.1. XM_005261340.1.
UniGeneHs.592192.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C8PNMR-A338-438[»]
1EGJX-ray2.80A338-438[»]
1GH7X-ray3.00A/B25-437[»]
2GYSX-ray2.70A/B25-437[»]
3CXEX-ray3.30A25-438[»]
ProteinModelPortalP32927.
SMRP32927. Positions 25-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107826. 15 interactions.
DIPDIP-127N.
IntActP32927. 14 interactions.
MINTMINT-105697.
STRING9606.ENSP00000384053.

Chemistry

ChEMBLCHEMBL2364169.
DrugBankDB00020. Sargramostim.

PTM databases

PhosphoSiteP32927.

Polymorphism databases

DMDM1345923.

Proteomic databases

PaxDbP32927.
PRIDEP32927.

Protocols and materials databases

DNASU1439.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262825; ENSP00000262825; ENSG00000100368. [P32927-2]
ENST00000403662; ENSP00000384053; ENSG00000100368. [P32927-1]
ENST00000406230; ENSP00000385271; ENSG00000100368. [P32927-2]
GeneID1439.
KEGGhsa:1439.
UCSCuc003aqa.4. human. [P32927-1]
uc003aqc.4. human. [P32927-2]

Organism-specific databases

CTD1439.
GeneCardsGC22P037309.
HGNCHGNC:2436. CSF2RB.
HPACAB010251.
MIM138981. gene.
614370. phenotype.
neXtProtNX_P32927.
Orphanet264675. Congenital pulmonary alveolar proteinosis.
PharmGKBPA26939.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39324.
HOGENOMHOG000113049.
HOVERGENHBG052113.
KOK04738.
OMACRWADTQ.
OrthoDBEOG7966FT.
PhylomeDBP32927.
TreeFamTF337996.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP32927.

Gene expression databases

ArrayExpressP32927.
BgeeP32927.
CleanExHS_CSF2RB.
GenevestigatorP32927.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR003961. Fibronectin_type3.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
IPR015321. IL-6_rcpt_alpha-bd.
IPR011365. IL3_rcpt_beta.
[Graphical view]
PfamPF00041. fn3. 1 hit.
PF09240. IL6Ra-bind. 1 hit.
[Graphical view]
PIRSFPIRSF001956. IL3R_beta_c. 1 hit.
SMARTSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 4 hits.
PROSITEPS50853. FN3. 2 hits.
PS01355. HEMATOPO_REC_S_F1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32927.
GenomeRNAi1439.
NextBio5889.
PROP32927.
SOURCESearch...

Entry information

Entry nameIL3RB_HUMAN
AccessionPrimary (citable) accession number: P32927
Secondary accession number(s): Q5JZI1, Q6ICE0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries