P32927 (IL3RB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CSF2RB
Synonyms:	IL3RB, IL5RB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	897 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.10 Ref.11
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.
Sequence similarities	Belongs to the type I cytokine receptor family. Type 4 subfamily. Contains 2 fibronectin type-III domains.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to interleukin-3 Traceable author statement Ref.12. Source: GOC interleukin-5-mediated signaling pathway Traceable author statement Ref.12. Source: GOC respiratory gaseous exchange Traceable author statement. Source: ProtInc
Cellular component	granulocyte macrophage colony-stimulating factor receptor complex Traceable author statement Ref.12. Source: UniProtKB
Molecular function	cytokine receptor activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSF2	P04141	2	EBI-1809771,EBI-1809826
IL5	P05113	2	EBI-1809771,EBI-2435811
ITGB1	P05556	5	EBI-1809771,EBI-703066
JAK2	O60674	3	EBI-1809771,EBI-518647

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Chain

17 – 897

881

Cytokine receptor common subunit beta

PRO_0000010862

Regions

Topological domain

17 – 443

427

Extracellular Potential

Transmembrane

444 – 460

17

Helical; Potential

Topological domain

461 – 897

437

Cytoplasmic Potential

Domain

133 – 233

101

Fibronectin type-III 1

Domain

338 – 432

95

Fibronectin type-III 2

Motif

425 – 429

5

WSXWS motif

Motif

474 – 482

9

Box 1 motif

Amino acid modifications

Modified residue

766

1

Phosphotyrosine By similarity

Glycosylation

58

1

N-linked (GlcNAc...) Ref.10 Ref.11

Glycosylation

191

1

N-linked (GlcNAc...) Ref.10 Ref.11

Glycosylation

346

1

N-linked (GlcNAc...) Potential

Disulfide bond

35 ↔ 45

Ref.10 Ref.11

Disulfide bond

75 ↔ 96

Ref.10 Ref.11

Disulfide bond

86 ↔ 91

Ref.10 Ref.11

Disulfide bond

250 ↔ 260

Ref.10 Ref.11

Disulfide bond

289 ↔ 306

Ref.10 Ref.11

Natural variations

Alternative sequence

285

1

G → GSAVLLR in isoform 2.

VSP_032798

Natural variant

249

1

E → Q.
Corresponds to variant rs16845 [ dbSNP | Ensembl ].

VAR_042521

Natural variant

603

1

P → T. Ref.12
Corresponds to variant rs1801122 [ dbSNP | Ensembl ].

VAR_014801

Natural variant

647

1

G → V.
Corresponds to variant rs1801115 [ dbSNP | Ensembl ].

VAR_014802

Natural variant

652

1

V → M.
Corresponds to variant rs1801114 [ dbSNP | Ensembl ].

VAR_014803

Natural variant

696

1

P → S.
Corresponds to variant rs16997517 [ dbSNP | Ensembl ].

VAR_042522

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

897

Helix Strand Turn

Details...

Helix

28 – 31

4

Beta strand

33 – 38

6

Turn

39 – 41

3

Beta strand

42 – 47

6

Helix

51 – 54

4

Beta strand

59 – 68

10

Beta strand

70 – 72

3

Beta strand

75 – 77

3

Beta strand

88 – 91

4

Beta strand

94 – 98

5

Beta strand

108 – 117

10

Beta strand

121 – 126

6

Helix

127 – 130

4

Beta strand

136 – 143

8

Beta strand

148 – 154

7

Helix

166 – 168

3

Beta strand

169 – 180

12

Helix

182 – 184

3

Beta strand

186 – 197

12

Turn

199 – 201

3

Beta strand

207 – 216

10

Beta strand

218 – 221

4

Beta strand

233 – 236

4

Beta strand

249 – 253

5

Turn

254 – 256

3

Beta strand

257 – 261

5

Helix

268 – 270

3

Beta strand

274 – 279

6

Beta strand

294 – 296

3

Beta strand

298 – 309

12

Turn

313 – 315

3

Beta strand

318 – 325

8

Beta strand

330 – 333

4

Helix

334 – 336

3

Beta strand

337 – 339

3

Beta strand

350 – 352

3

Beta strand

370 – 375

6

Helix

383 – 385

3

Beta strand

388 – 393

6

Beta strand

405 – 407

3

Beta strand

412 – 416

5

Beta strand

418 – 420

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 3398E37FDB8F393A	FASTA	897	97,336
	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
	Isoform 2 [UniParc]. Checksum: AE8FFF1721CD63F2	FASTA	903	97,976
	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 SPDAGSAVLL REEECSPVLR 310 320 330 340 350 360 EGLGSLHTRH HCQIPVPDPA THGQYIVSVQ PRRAEKHIKS SVNIQMAPPS LNVTKDGDSY 370 380 390 400 410 420 SLRWETMKMR YEHIDHTFEI QYRKDTATWK DSKTETLQNA HSMALPALEP STRYWARVRV 430 440 450 460 470 480 RTSRTGYNGI WSEWSEARSW DTESVLPMWV LALIVIFLTI AVLLALRFCG IYGYRLRRKW 490 500 510 520 530 540 EEKIPNPSKS HLFQNGSAEL WPPGSMSAFT SGSPPHQGPW GSRFPELEGV FPVGFGDSEV 550 560 570 580 590 600 SPLTIEDPKH VCDPPSGPDT TPAASDLPTE QPPSPQPGPP AASHTPEKQA SSFDFNGPYL 610 620 630 640 650 660 GPPHSRSLPD ILGQPEPPQE GGSQKSPPPG SLEYLCLPAG GQVQLVPLAQ AMGPGQAVEV 670 680 690 700 710 720 ERRPSQGAAG SPSLESGGGP APPALGPRVG GQDQKDSPVA IPMSSGDTED PGVASGYVSS 730 740 750 760 770 780 ADLVFTPNSG ASSVSLVPSL GLPSDQTPSL CPGLASGPPG APGPVKSGFE GYVELPPIEG 790 800 810 820 830 840 RSPRSPRNNP VPPEAKSPVL NPGERPADVS PTSPQPEGLL VLQQVGDYCF LPGLGPGPLS 850 860 870 880 890 900 LRSKPSSPGP GPEIKNLDQA FQVKKPPGQA VPQVPVIQLF KALKQQDYLS LPPWEVNKPG EVC

References

	« Hide 'large scale' referencesShow '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: 1702217] [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: 15461802] [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. , 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: 10591208] [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. , 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: 17828305] [Abstract] Cited for: INTERACTION WITH TMEM102.
[7]	"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: 10736232] [Abstract] Cited for: STRUCTURE BY NMR OF 338-438.
[8]	"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: 10753826] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 338-438.
[9]	"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: 11207369] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-437.
[10]	"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: 16754968] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 25-443, DISULFIDE BONDS, SUBUNIT, GLYCOSYLATION AT ASN-58 AND ASN-191.
[11]	"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: 18692472] [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.
[12]	"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: 9410898] [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.

IPI

IPI00465234.
IPI00879222.

PIR

A39255.

RefSeq

NP_000386.1. NM_000395.2.

UniGene

Hs.592192.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P32927.

SMR

P32927. Positions 25-438.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-127N.

IntAct

P32927. 7 interactions.

STRING

P32927.

PTM databases

PhosphoSite

P32927.

Polymorphism databases

DMDM

1345923.

Proteomic databases

PRIDE

P32927.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000403662; ENSP00000384053; ENSG00000100368.

GeneID

1439.

KEGG

hsa:1439.

UCSC

uc003aqa.2. human.
uc003aqc.2. human.

Organism-specific databases

CTD

1439.

GeneCards

GC22P037309.

H-InvDB

HIX0041183.

HGNC

HGNC:2436. CSF2RB.

HPA

CAB010251.

MIM

138981. gene.

neXtProt

NX_P32927.

Orphanet

264675. Congenital pulmonary alveolar proteinosis.

PharmGKB

PA26939.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08018.

HOVERGEN

HBG052113.

OMA

CRWADTQ.

OrthoDB

EOG40CHH2.

PhylomeDB

P32927.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P32927.

Bgee

P32927.

CleanEx

HS_CSF2RB.

Genevestigator

P32927.

GermOnline

ENSG00000100368. Homo sapiens.

Family and domain databases

InterPro

IPR003961. Fibronectin_type3.
IPR003531. Hempt_rcpt_S_F1_CS.
IPR013783. Ig-like_fold.
IPR011365. IL3_rcpt_beta.
IPR015321. IL6_recept-bd.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 4 hits.

KO

K04738.

Pfam

PF00041. fn3. 1 hit.
PF09240. IL6Ra-bind. 1 hit.
[Graphical view]

PIRSF

PIRSF001956. IL3R_beta_c. 1 hit.

SMART

SM00060. FN3. 2 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 4 hits.

PROSITE

PS50853. FN3. 2 hits.
PS01355. HEMATOPO_REC_S_F1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00020. Sargramostim.

NextBio

5889.

SOURCE

Search...

Entry information

Entry name

IL3RB_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.