Reviewed, UniProtKB/Swiss-Prot P09619 (PGFRB_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-type platelet-derived growth factor receptor
    EC=2.7.10.1
Alternative name(s):
    PDGF-R-beta
    CD140 antigen-like family member B
    CD_antigen=CD140b

Gene names

Name:

PDGFRB

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	1106 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	Receptor that binds specifically to PDGFB and PDGFD and has a tyrosine-protein kinase activity. Phosphorylates Tyr residues at the C-terminus of PTPN11 creating a binding site for the SH2 domain of GRB2. Ref.12
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Homodimer, and heterodimer with PDGFRA. Interacts with APS. The autophosphorylated form interacts directly with SHB and with PIK3C2B, maybe indirectly. Ref.8 Ref.10 Ref.11
Subcellular location	Membrane; Single-pass type I membrane protein.
Involvement in disease	A chromosomal aberration involving PDGFRB is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;12)(q33;p13) with EVT6/TEL. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML). A chromosomal aberration involving PDGFRB may be a cause of acute myelogenous leukemia. Translocation t(5;14)(q33;q32) with TRIP11. The fusion protein may be involved in clonal evolution of leukemia and eosinophilia. A chromosomal aberration involving PDGFRB may be a cause of juvenile myelomonocytic leukemia. Translocation t(5;17)(q33;p11.2) with SPECC1. A chromosomal aberration involving PDGFRB is a cause in many instances of chronic myeloproliferative disorder with eosinophilia (MPE) [MIM:131440]. Translocation t(5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein. A chromosomal aberration involving PDGFRB may be the cause of a myeloproliferative disorder (MBD) associated with eosinophilia. Translocation t(1;5)(q23;q33) that forms a PDE4DIP-PDGFRB fusion protein.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. Contains 5 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell chemotaxis Inferred from direct assay. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay. Source: UniProtKB platelet-derived growth factor receptor signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of cell migration Inferred from direct assay. Source: UniProtKB positive regulation of cell proliferation Inferred from direct assay. Source: UniProtKB protein amino acid autophosphorylation Inferred from direct assay. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred by curator. Source: UniProtKB platelet activating factor receptor activity Traceable author statement. Source: ProtInc platelet-derived growth factor beta-receptor activity Inferred from direct assay. Source: UniProtKB platelet-derived growth factor binding Inferred from physical interaction. Source: UniProtKB platelet-derived growth factor receptor binding Inferred from physical interaction. Source: UniProtKB vascular endothelial growth factor receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDGFB	P01127	1	EBI-641237,EBI-1554925
PIK3C2B	O00750	1	EBI-641237,EBI-641107
PTPN1	P18031	1	EBI-641237,EBI-968788
PTPN12	Q05209	1	EBI-641237,EBI-2266035
PTPN22	Q9Y2R2	1	EBI-641237,EBI-1211241
PTPN6	P29350	1	EBI-641237,EBI-78260
PTPRB	P23467	1	EBI-641237,EBI-1265766
PTPRC	P08575	1	EBI-641237,EBI-1341
PTPRE	P23469	1	EBI-641237,EBI-2258070
PTPRG	P23470	1	EBI-641237,EBI-2258115
PTPRJ	Q12913	1	EBI-641237,EBI-2264500
PTPRK	Q15262	1	EBI-641237,EBI-474052
PTPRO	Q16827	1	EBI-641237,EBI-723739
PTPRR	Q15256	1	EBI-641237,EBI-2265659

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Ref.6

Chain

33 – 1106

1074

Beta-type platelet-derived growth factor receptor

PRO_0000016757

Regions

Topological domain

33 – 531

499

Extracellular Potential

Transmembrane

532 – 556

25

Potential

Topological domain

557 – 1106

550

Cytoplasmic Potential

Domain

33 – 120

88

Ig-like C2-type 1

Domain

129 – 210

82

Ig-like C2-type 2

Domain

214 – 309

96

Ig-like C2-type 3

Domain

331 – 403

73

Ig-like C2-type 4

Domain

416 – 524

109

Ig-like C2-type 5

Domain

600 – 962

363

Protein kinase

Nucleotide binding

606 – 614

9

ATP By similarity

Sites

Active site

826

1

Proton acceptor By similarity

Binding site

634

1

ATP By similarity

Site

527 – 528

2

Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein

Site

527 – 528

2

Breakpoint for translocation to form TRIP11-PDGFRB

Amino acid modifications

Modified residue

751

1

Phosphotyrosine; by autocatalysis Ref.7

Modified residue

857

1

Phosphotyrosine; by autocatalysis Ref.7

Glycosylation

45

1

N-linked (GlcNAc...) Potential

Glycosylation

89

1

N-linked (GlcNAc...) Potential

Glycosylation

103

1

N-linked (GlcNAc...) Potential

Glycosylation

215

1

N-linked (GlcNAc...) Potential

Glycosylation

230

1

N-linked (GlcNAc...) Potential

Glycosylation

292

1

N-linked (GlcNAc...) Potential

Glycosylation

307

1

N-linked (GlcNAc...) Potential

Glycosylation

354

1

N-linked (GlcNAc...) Potential

Glycosylation

371

1

N-linked (GlcNAc...) Potential

Glycosylation

468

1

N-linked (GlcNAc...) Potential

Glycosylation

479

1

N-linked (GlcNAc...) Potential

Disulfide bond

54 ↔ 100

Potential

Disulfide bond

149 ↔ 190

Potential

Disulfide bond

235 ↔ 291

Potential

Disulfide bond

436 ↔ 508

Potential

Natural variations

Natural variant

29

1

I → F: dbSNP rs17110944. Ref.18

VAR_034377

Natural variant

180

1

S → F: dbSNP rs17853027. Ref.3

VAR_035125

Natural variant

282

1

E → K: dbSNP rs34586048. Ref.18

VAR_042027

Natural variant

345

1

P → S: dbSNP rs2229558.

VAR_049717

Natural variant

485

1

E → K Ref.18

VAR_042028

Natural variant

589

1

Y → H in a gastric adenocarcinoma sample; somatic mutation. Ref.18

VAR_042029

Natural variant

718

1

N → Y Ref.18

VAR_042030

Natural variant

882

1

T → I in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.18

VAR_042031

Experimental info

Sequence conflict

241

1

E → D in AAA36427. Ref.2

Secondary structure

1

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1106

Helix Strand Turn

Details...

Beta strand

601 – 603

3

Beta strand

606 – 613

8

Beta strand

615 – 617

3

Beta strand

620 – 624

5

Helix

628 – 631

4

Beta strand

632 – 634

3

Helix

641 – 649

9

Beta strand

671 – 673

3

Beta strand

675 – 678

4

Beta strand

681 – 685

5

Helix

686 – 695

10

Beta strand

700 – 702

3

Beta strand

713 – 716

4

Beta strand

726 – 735

10

Beta strand

740 – 746

7

Turn

747 – 749

3

Beta strand

750 – 757

8

Helix

761 – 766

6

Beta strand

775 – 779

5

Beta strand

781 – 783

3

Beta strand

785 – 788

4

Helix

800 – 820

21

Helix

829 – 831

3

Beta strand

832 – 834

3

Helix

836 – 838

3

Beta strand

840 – 842

3

Helix

847 – 850

4

Helix

855 – 858

4

Beta strand

862 – 865

4

Turn

867 – 869

3

Helix

872 – 877

6

Helix

882 – 897

16

Turn

898 – 900

3

Beta strand

903 – 907

5

Helix

910 – 919

10

Helix

931 – 940

10

Turn

945 – 947

3

Helix

951 – 959

9

Sequences

	Sequence		Length	Mass (Da)
	P09619-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 038C15E531D6E89D	FASTA	1,106	123,968
	10 20 30 40 50 60 MRLPGAMPAL ALKGELLLLS LLLLLEPQIS QGLVVTPPGP ELVLNVSSTF VLTCSGSAPV 70 80 90 100 110 120 VWERMSQEPP QEMAKAQDGT FSSVLTLTNL TGLDTGEYFC THNDSRGLET DERKRLYIFV 130 140 150 160 170 180 PDPTVGFLPN DAEELFIFLT EITEITIPCR VTDPQLVVTL HEKKGDVALP VPYDHQRGFS 190 200 210 220 230 240 GIFEDRSYIC KTTIGDREVD SDAYYVYRLQ VSSINVSVNA VQTVVRQGEN ITLMCIVIGN 250 260 270 280 290 300 EVVNFEWTYP RKESGRLVEP VTDFLLDMPY HIRSILHIPS AELEDSGTYT CNVTESVNDH 310 320 330 340 350 360 QDEKAINITV VESGYVRLLG EVGTLQFAEL HRSRTLQVVF EAYPPPTVLW FKDNRTLGDS 370 380 390 400 410 420 SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGHYTMRAFH EDAEVQLSFQ LQINVPVRVL 430 440 450 460 470 480 ELSESHPDSG EQTVRCRGRG MPQPNIIWSA CRDLKRCPRE LPPTLLGNSS EEESQLETNV 490 500 510 520 530 540 TYWEEEQEFE VVSTLRLQHV DRPLSVRCTL RNAVGQDTQE VIVVPHSLPF KVVVISAILA 550 560 570 580 590 600 LVVLTIISLI ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL 610 620 630 640 650 660 VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS ELKIMSHLGP 670 680 690 700 710 720 HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF LQHHSDKRRP PSAELYSNAL 730 740 750 760 770 780 PVGLPLPSHV SLTGESDGGY MDMSKDESVD YVPMLDMKGD VKYADIESSN YMAPYDNYVP 790 800 810 820 830 840 SAPERTCRAT LINESPVLSY MDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV 850 860 870 880 890 900 KICDFGLARD IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG 910 920 930 940 950 960 GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP FSQLVLLLER 970 980 990 1000 1010 1020 LLGEGYKKKY QQVDEEFLRS DHPAILRSQA RLPGFHGLRS PLDTSSVLYT AVQPNEGDND 1030 1040 1050 1060 1070 1080 YIIPLPDPKP EVADEGPLEG SPSLASSTLN EVNTSSTISC DSPLEPQDEP EPEPQLELQV 1090 1100 EPEPELEQLP DSGCPAPRAE AEDSFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a cDNA coding for the human platelet-derived growth factor receptor: evidence for more than one receptor class." Gronwald R.G.K., Grant F.J., Haldeman B.A., Hart C.E., O'Hara P.J., Hagen F.S., Ross R., Bowen-Pope D.F., Murray M.J. Proc. Natl. Acad. Sci. U.S.A. 85:3435-3439(1988) [PubMed: 2835772] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"cDNA cloning and expression of a human platelet-derived growth factor (PDGF) receptor specific for B-chain-containing PDGF molecules." Claesson-Welsh L., Eriksson A., Moren A., Severinsson L., Ek B., Oestman A., Betsholtz C., Heldin C.-H. Mol. Cell. Biol. 8:3476-3486(1988) [PubMed: 2850496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-180. Tissue: Brain.
[4]	"Integration of proviral DNA into the PDGF beta-receptor gene in HTLV-I-infected T-cells results in a novel tyrosine kinase product with transforming activity." Chi K.D., McPhee R.A., Wagner A.S., Dietz J.J., Pantazis P., Goustin A.S. Oncogene 15:1051-1057(1997) [PubMed: 9285559] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-569.
[5]	"Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes." Roberts W.M., Look A.T., Roussel M.F., Sherr C.J. Cell 55:655-661(1988) [PubMed: 2846185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1046-1106.
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-47.
[7]	"Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins." Kazlauskas A., Cooper J.A. Cell 58:1121-1133(1989) [PubMed: 2550144] [Abstract] Cited for: PHOSPHORYLATION AT TYR-751 AND TYR-857.
[8]	"Shb is a ubiquitously expressed Src homology 2 protein." Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L. Oncogene 9:19-27(1994) [PubMed: 8302579] [Abstract] Cited for: INTERACTION WITH SHB.
[9]	"Fusion of the platelet-derived growth factor receptor beta to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution." Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H. Blood 90:4271-4277(1997) [PubMed: 9373237] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH TRIP11.
[10]	"APS, an adaptor protein containing PH and SH2 domains, is associated with the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis." Yokouchi M., Wakioka T., Sakamoto H., Yasukawa H., Ohtsuka S., Sasaki A., Ohtsubo M., Valius M., Inoue A., Komiya S., Yoshimura A. Oncogene 18:759-767(1999) [PubMed: 9989826] [Abstract] Cited for: INTERACTION WITH APS.
[11]	"Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors." Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J. Mol. Cell. Biol. 20:3817-3830(2000) [PubMed: 10805725] [Abstract] Cited for: INTERACTION WITH PIK3C2B.
[12]	"PDGF-D is a specific, protease-activated ligand for the PDGF beta-receptor." Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H., Alitalo K., Eriksson U. Nat. Cell Biol. 3:512-516(2001) [PubMed: 11331881] [Abstract] Cited for: FUNCTION AS A RECEPTOR FOR PDGFD.
[13]	"Response to imatinib mesylate in patients with chronic myeloproliferative diseases with rearrangements of the platelet-derived growth factor receptor beta." Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J., Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E., Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E., Silberman S., Schultheis B., Cross N.C.P., Goldman J.M. N. Engl. J. Med. 347:481-487(2002) [PubMed: 12181402] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ETV6.
[14]	"Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder associated with eosinophilia: involvement of PDGFRB and response to imatinib." Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C., Shipp M.A., Aguiar R.C.T. Blood 102:4187-4190(2003) [PubMed: 12907457] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH PDE4DIP.
[15]	"HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with t(5;17)(q33;p11.2)." Morerio C., Acquila M., Rosanda C., Rapella A., Dufour C., Locatelli F., Maserati E., Pasquali F., Panarello C. Cancer Res. 64:2649-2651(2004) [PubMed: 15087372] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH SPECC1.
[16]	"NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha C-terminal SH2-peptide complex." Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A., Rowsell S., Murshudov G.N. Acta Crystallogr. D 57:1397-1404(2001) [PubMed: 11567151] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 751-755 IN COMPLEX WITH PIK3R1, COMPARISON WITH NMR ANALYSIS.
[17]	"Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors." Karthikeyan S., Leung T., Ladias J.A.A. J. Biol. Chem. 277:18973-18978(2002) [PubMed: 11882663] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1102-1106 IN COMPLEX WITH SLC9A3R1 AND PDGFRA.
[18]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-29; LYS-282; LYS-485; HIS-589; TYR-718 AND ILE-882.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

J03278 mRNA. Translation: AAA60049.1.
M21616 mRNA. Translation: AAA36427.1.
BC032224 mRNA. Translation: AAH32224.1.
U33172 Genomic DNA. Translation: AAC51675.1.

IPI

IPI00015902.

PIR

PFHUGB. A28206.

RefSeq

NP_002600.1.

UniGene

Hs.509067

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQ5	X-ray	2.20	A	1102-1106	[»]
1H9O	X-ray	1.79	B	751-755	[»]
1LWP	model	-	A	600-962	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:558N.

IntAct

P09619. 15 interactions.

PTM databases

PhosphoSite

P09619.

Proteomic databases

PRIDE

P09619.

Genome annotation databases

Ensembl

ENSG00000113721. Homo sapiens. [Contig view]

GeneID

5159.

KEGG

hsa:5159.

Organism-specific databases

GeneCards

GC05M149473.

H-InvDB

HIX0024847.

HGNC

HGNC:8804. PDGFRB.

HPA

CAB003842.
CAB018144.

MIM

131440. phenotype.
173410. gene.

Orphanet

86832. Adult myelodysplastic/myeloproliferative disease.
98274. Chronic myeloproliferative disease.
86830. Chronic myeloproliferative disease, unclassified.
3260. Idiopathic hypereosinophilic syndrome.
98823. Leukemia, myelomonocytic, chronic.

PharmGKB

PA33148.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09619.

HOVERGEN

P09619.

OMA

P09619. GACTKGG.

Enzyme and pathway databases

BRENDA

2.7.10.1. 247.

Pathway_Interaction_DB

pdgfrbpathway. PDGFR-beta signaling pathway.
s1p_s1p1_pathway. S1P1 pathway.
s1p_s1p3_pathway. S1P3 pathway.
ptp1bpathway. Signaling events mediated by PTP1B.

Gene expression databases

ArrayExpress

P09619.

Bgee

P09619.

CleanEx

HS_PDGFRB.

GermOnline

ENSG00000113721. Homo sapiens.

Family and domain databases

InterPro

IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001824. Recept_tyr_kinase-III_CS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016243. TyrPK_CSF1-R.
IPR009134. VEGFR_N.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 3 hits.

Pfam

PF00047. ig. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000615. TyrPK_CSF1-R. 1 hit.

PRINTS

PR01832. VEGFRECEPTOR.

ProDom

PD000001. Prot_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00102. Becaplermin.
DB01254. Dasatinib.
DB00619. Imatinib.
DB00398. Sorafenib.
DB01268. Sunitinib.

NextBio

19958.

SOURCE

Search...

Entry information

Entry name

PGFRB_HUMAN

Accession

Primary (citable) accession number: P09619
Secondary accession number(s): Q8N5L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)