P09619 (PGFRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet-derived growth factor receptor beta
Short name=PDGF-R-beta
Short name=PDGFR-beta
EC=2.7.10.1

Alternative name(s):
Beta platelet-derived growth factor receptor
Beta-type platelet-derived growth factor receptor
CD140 antigen-like family member B
Platelet-derived growth factor receptor 1
Short name=PDGFR-1
CD_antigen=CD140b

Gene names

Name:	PDGFRB
Synonyms:	PDGFR, PDGFR1

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	Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol-1,4,5-trisphosphate, mobilization of cytosolic Ca2+ and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20 Ref.28 Ref.29 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.12 Ref.17 Ref.37
Enzyme regulation	Present in an inactive conformation in the absence of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib. Ref.33
Subunit structure	Interacts with homodimeric PDGFB and PDGFD, and with heterodimers formed by PDGFA and PDGFB. May also interact with homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts with SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB. Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated) with SRC and SRC family kinases. Interacts (tyrosine phosphorylated) with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated) with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by SHC1. Interacts (via C-terminus) with SLC9A3R1. Ref.1 Ref.2 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.35 Ref.40 Ref.47 Ref.48
Subcellular location	Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note: After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. Ref.1 Ref.2 Ref.9 Ref.12 Ref.35 Ref.37
Post-translational modification	Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-579, and to a lesser degree, at Tyr-581, is important for interaction with SRC family kinases. Phosphorylation at Tyr-740 and Tyr-751 is important for interaction with PIK3R1. Phosphorylation at Tyr-751 is important for interaction with NCK1. Phosphorylation at Tyr-771 and Tyr-857 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-857 is important for efficient phosphorylation of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased cell proliferation. Phosphorylation at Tyr-1009 is important for interaction with PTPN11. Phosphorylation at Tyr-1009 and Tyr-1021 is important for interaction with PLCG1. Phosphorylation at Tyr-1021 is important for interaction with CBL; PLCG1 and CBL compete for the same binding site. Dephosphorylated by PTPRJ at Tyr-751, Tyr-857, Tyr-1009 and Tyr-1021. Ref.1 Ref.2 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20 Ref.26 Ref.34 Ref.37 Ref.40 N-glycosylated. Ref.2 Ref.48 Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation. Ref.15 Ref.35
Involvement in disease	Note=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). Note=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. Note=A chromosomal aberration involving PDGFRB may be a cause of juvenile myelomonocytic leukemia. Translocation t(5;17)(q33;p11.2) with SPECC1. Defects in PDGFRB are a cause of myeloproliferative disorder chronic with eosinophilia (MPE) [MIM:131440]. A hematologic disorder characterized by malignant eosinophils proliferation. Note=A chromosomal aberration involving PDGFRB is found in many instances of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein. Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1 fusion protein. Note=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
Biological process	Chemotaxis
Cellular component	Cell membrane Cytoplasmic vesicle Lysosome Membrane
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	aorta morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL cardiac myofibril assembly Inferred from sequence or structural similarity. Source: UniProtKB cell migration involved in coronary angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB cell migration involved in vasculogenesis Inferred from sequence or structural similarity. Source: UniProtKB metanephric glomerular capillary formation Inferred from sequence or structural similarity. Source: UniProtKB metanephric glomerular mesangial cell proliferation involved in metanephros development Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.10Ref.2. Source: UniProtKB phosphatidylinositol metabolic process Inferred from mutant phenotype Ref.10. Source: UniProtKB phosphatidylinositol-mediated signaling Inferred from mutant phenotype Ref.9. Source: UniProtKB positive regulation of DNA biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype Ref.41. Source: UniProtKB positive regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of calcium ion import Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of mitosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase activity Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phospholipase C activity Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of phosphoprotein phosphatase activity Inferred from direct assay Ref.19. Source: UniProtKB positive regulation of reactive oxygen species metabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of smooth muscle cell migration Inferred from mutant phenotype Ref.41. Source: UniProtKB positive regulation of smooth muscle cell proliferation Inferred from mutant phenotype Ref.41. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.13Ref.2. Source: UniProtKB regulation of actin cytoskeleton organization Inferred from sequence or structural similarity. Source: BHF-UCL retina vasculature development in camera-type eye Inferred from sequence or structural similarity. Source: UniProtKB smooth muscle cell chemotaxis Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	apical plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from electronic annotation. Source: InterPro lysosomal lumen Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW platelet activating factor receptor activity Traceable author statement. Source: ProtInc platelet-derived growth factor beta-receptor activity Inferred from direct assay Ref.13Ref.2. Source: UniProtKB platelet-derived growth factor binding Inferred from direct assay Ref.9Ref.2. Source: UniProtKB platelet-derived growth factor receptor binding Inferred from physical interaction. Source: BHF-UCL vascular endothelial growth factor-activated receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTPN12	Q05209	2	EBI-641237,EBI-2266035

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Ref.7

Chain

33 – 1106

1074

Platelet-derived growth factor receptor beta

PRO_0000016757

Regions

Topological domain

33 – 532

500

Extracellular Potential

Transmembrane

533 – 553

21

Helical; Potential

Topological domain

554 – 1106

553

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 Probable

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

562

1

Phosphotyrosine; by autocatalysis Ref.26

Modified residue

579

1

Phosphotyrosine; by autocatalysis Ref.17 Ref.34

Modified residue

581

1

Phosphotyrosine; by autocatalysis Ref.17 Ref.34

Modified residue

589

1

Phosphotyrosine; by autocatalysis

Modified residue

686

1

Phosphotyrosine; by ABL1 and ABL2 By similarity

Modified residue

716

1

Phosphotyrosine; by autocatalysis Ref.34

Modified residue

740

1

Phosphotyrosine; by autocatalysis Ref.13 Ref.34

Modified residue

751

1

Phosphotyrosine; by autocatalysis Ref.8 Ref.11 Ref.13 Ref.26

Modified residue

763

1

Phosphotyrosine; by autocatalysis Ref.26

Modified residue

771

1

Phosphotyrosine; by autocatalysis Ref.13 Ref.26 Ref.34

Modified residue

775

1

Phosphotyrosine; by autocatalysis Ref.26

Modified residue

778

1

Phosphotyrosine; by autocatalysis Ref.26

Modified residue

857

1

Phosphotyrosine; by autocatalysis Ref.8 Ref.11 Ref.13 Ref.26 Ref.34

Modified residue

934

1

Phosphotyrosine; by ABL1 and ABL2 By similarity

Modified residue

970

1

Phosphotyrosine; by ABL1 and ABL2 By similarity

Modified residue

1009

1

Phosphotyrosine; by autocatalysis Ref.14 Ref.26 Ref.34

Modified residue

1021

1

Phosphotyrosine; by autocatalysis Ref.14 Ref.26 Ref.34

Glycosylation

45

1

N-linked (GlcNAc...) Potential

Glycosylation

89

1

N-linked (GlcNAc...) Ref.48

Glycosylation

103

1

N-linked (GlcNAc...) Ref.48

Glycosylation

215

1

N-linked (GlcNAc...) Ref.48

Glycosylation

230

1

N-linked (GlcNAc...) Ref.48

Glycosylation

292

1

N-linked (GlcNAc...) Ref.48

Glycosylation

307

1

N-linked (GlcNAc...) Ref.48

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

Ref.48

Disulfide bond

149 ↔ 190

Ref.48

Disulfide bond

235 ↔ 291

Ref.48

Disulfide bond

436 ↔ 508

By similarity

Natural variations

Natural variant

29

1

I → F. Ref.49
Corresponds to variant rs17110944 [ dbSNP | Ensembl ].

VAR_034377

Natural variant

180

1

S → F. Ref.4
Corresponds to variant rs17853027 [ dbSNP | Ensembl ].

VAR_035125

Natural variant

282

1

E → K. Ref.49
Corresponds to variant rs34586048 [ dbSNP | Ensembl ].

VAR_042027

Natural variant

345

1

P → S.
Corresponds to variant rs2229558 [ dbSNP | Ensembl ].

VAR_049717

Natural variant

485

1

E → K. Ref.49
Corresponds to variant rs41287110 [ dbSNP | Ensembl ].

VAR_042028

Natural variant

589

1

Y → H in a gastric adenocarcinoma sample; somatic mutation. Ref.49

VAR_042029

Natural variant

718

1

N → Y. Ref.49
Corresponds to variant rs35322465 [ dbSNP | Ensembl ].

VAR_042030

Natural variant

882

1

T → I in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.49

VAR_042031

Experimental info

Mutagenesis

579

1

Y → F: Loss of kinase activity; when associated with F-581. Strongly reduced interaction with SRC family kinases. No effect on GRB10-binding. Ref.17 Ref.24

Mutagenesis

581

1

Y → F: Loss of kinase activity; when associated with F-579. No effect on GRB10-binding. Ref.17 Ref.24

Mutagenesis

634

1

K → A or R: Loss of kinase activity. Ref.12 Ref.37

Mutagenesis

635

1

M → R: Loss of kinase activity. Ref.13

Mutagenesis

716

1

Y → F: No effect on GRB10-binding. Ref.24

Mutagenesis

740

1

Y → F: Strongly reduced up-regulation of cell proliferation; when associated with F-751. Strongly decreased PIK3R1 binding. No effect on GRB10-binding. Ref.13 Ref.16 Ref.24 Ref.41

Mutagenesis

751

1

Y → F: Strongly reduced up-regulation of cell proliferation; when associated with F-740. Abolishes interaction with PIK3R1 and NCK1, and slightly reduces interaction with RASA1/GAP. No effect on GRB10-binding. Ref.10 Ref.13 Ref.16 Ref.20 Ref.24 Ref.41

Mutagenesis

771

1

Y → F: Loss of GRB10-binding. Abolishes interaction with RASA1/GAP. Ref.13 Ref.16 Ref.24

Mutagenesis

778

1

Y → F: Strongly reduced expression levels. Ref.13

Mutagenesis

857

1

Y → F: Reduced kinase activity. No effect on GRB10-binding. Abolishes interaction with RASA1/GAP. Reduced. Ref.10 Ref.13 Ref.24 Ref.37

Mutagenesis

1009

1

Y → F: No effect on GRB10-binding. Abolishes interaction with PLCG1; when associated with F-1021. Ref.14 Ref.19 Ref.24

Mutagenesis

1021

1

Y → F: Strongly reduced up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on GRB10-binding. Ref.14 Ref.24 Ref.35 Ref.41

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 [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], FUNCTION AS PDGFB RECEPTOR, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH PDGFB.
[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], FUNCTION AS PDGFB RECEPTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, AUTOPHOSPHORYLATION, INTERACTION WITH PDGFA AND PDGFB.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"Independent expression of human alpha or beta platelet-derived growth factor receptor cDNAs in a naive hematopoietic cell leads to functional coupling with mitogenic and chemotactic signaling pathways." Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S., LaRochelle W.J., Ruggiero M., Aaronson S.A. Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989) [PubMed: 2554309] [Abstract] Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, SUBCELLULAR LOCATION.
[10]	"Functions of the major tyrosine phosphorylation site of the PDGF receptor beta subunit." Kazlauskas A., Durden D.L., Cooper J.A. Cell Regul. 2:413-425(1991) [PubMed: 1653029] [Abstract] Cited for: FUNCTION IN CELL PROLIFERATION; ACTIVATION OF PLCG1 AND IN PHOSPHORYLATION OF PLCG1 AND RASA1/GAP, MUTAGENESIS OF TYR-751 AND TYR-857.
[11]	"Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit dimerization and intersubunit trans-phosphorylation." Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A., Bowen-Pope D.F., Cooper J.A., Kazlauskas A. J. Biol. Chem. 266:8987-8992(1991) [PubMed: 1709159] [Abstract] Cited for: INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, PHOSPHORYLATION AT TYR-857 AND TYR-751.
[12]	"Effect of receptor kinase inactivation on the rate of internalization and degradation of PDGF and the PDGF beta-receptor." Sorkin A., Westermark B., Heldin C.H., Claesson-Welsh L. J. Cell Biol. 112:469-478(1991) [PubMed: 1846866] [Abstract] Cited for: FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-634.
[13]	"Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo." Kashishian A., Kazlauskas A., Cooper J.A. EMBO J. 11:1373-1382(1992) [PubMed: 1314164] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PIK3R1 AND RASA1/GAP AND IN ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE, INTERACTION WITH PIK3R1 AND RASA1/GAP, PHOSPHORYLATION AT TYR-740; TYR-751; TYR-771 AND TYR-857, MUTAGENESIS OF MET-635; TYR-740; TYR-751; TYR-771; TYR-778 AND TYR-857.
[14]	"Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma." Ronnstrand L., Mori S., Arridsson A.K., Eriksson A., Wernstedt C., Hellman U., Claesson-Welsh L., Heldin C.H. EMBO J. 11:3911-3919(1992) [PubMed: 1396585] [Abstract] Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND PHOSPHORYLATION OF PLCG1, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-1009 AND TYR-1021, MUTAGENESIS OF TYR-1009 AND TYR-1021.
[15]	"Ligand-induced polyubiquitination of the platelet-derived growth factor beta-receptor." Mori S., Heldin C.H., Claesson-Welsh L. J. Biol. Chem. 267:6429-6434(1992) [PubMed: 1313434] [Abstract] Cited for: UBIQUITINATION AND DEGRADATION.
[16]	"GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit." Kazlauskas A., Kashishian A., Cooper J.A., Valius M. Mol. Cell. Biol. 12:2534-2544(1992) [PubMed: 1375321] [Abstract] Cited for: INTERACTION WITH PIK3R1 AND RASA1/GAP, MUTAGENESIS OF TYR-740; TYR-751 AND TYR-771.
[17]	"Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases." Mori S., Ronnstrand L., Yokote K., Engstrom A., Courtneidge S.A., Claesson-Welsh L., Heldin C.H. EMBO J. 12:2257-2264(1993) [PubMed: 7685273] [Abstract] Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION, PHOSPHORYLATION AT TYR-579 AND TYR-581; INTERACTION WITH SRC, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-579 AND TYR-581.
[18]	"Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor." Fretto L.J., Snape A.J., Tomlinson J.E., Seroogy J.J., Wolf D.L., LaRochelle W.J., Giese N.A. J. Biol. Chem. 268:3625-3631(1993) [PubMed: 7679113] [Abstract] Cited for: INTERACTION WITH DGFA AND PDGFB.
[19]	"Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor." Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G. J. Biol. Chem. 268:21478-21481(1993) [PubMed: 7691811] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF PTPN11, INTERACTION WITH PTPN11; PIK3R1; PLCG1 AND RASA1/GAP, MUTAGENESIS OF TYR-1009.
[20]	"Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor." Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J. Mol. Cell. Biol. 13:6889-6896(1993) [PubMed: 7692233] [Abstract] Cited for: INTERACTION WITH NCK1 AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF NCK1, MUTAGENESIS OF TYR-751.
[21]	"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.
[22]	"Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors." Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L. J. Biol. Chem. 271:30942-30949(1996) [PubMed: 8940081] [Abstract] Cited for: INTERACTION WITH GRB7.
[23]	"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.
[24]	"Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis." Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H. Mol. Cell. Biol. 19:6217-6228(1999) [PubMed: 10454568] [Abstract] Cited for: INTERACTION WITH GRB10, MUTAGENESIS OF TYR-579; TYR-581; TYR-716; TYR-740; TYR-751; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
[25]	"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 SH2B2/APS.
[26]	"Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1." Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E., Vilella R., Bohmer F., Ostman A. J. Biol. Chem. 275:16219-16226(2000) [PubMed: 10821867] [Abstract] Cited for: AUTOPHOSPHORYLATION AT TYR-562; TYR-751; TYR-763; TYR-771; TYR-775; TYR-778; TYR-857; TYR-1009 AND TYR-1021, DEPHOSPHORYLATION BY PTPRJ AT TYR-751; TYR-857; TYR-1009 AND TYR-1021.
[27]	"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.
[28]	"Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor." Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E. J. Biol. Chem. 276:27406-27414(2001) [PubMed: 11297552] [Abstract] Cited for: FUNCTION AS A RECEPTOR FOR PDGFC, INTERACTION WITH PDGFC.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"p53-Binding protein 1 is fused to the platelet-derived growth factor receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib-responsive eosinophilic myeloproliferative disorder." Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G., Thaler J., Chase A.J., Cross N.C. Cancer Res. 64:7216-7219(2004) [PubMed: 15492236] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH TP53BP1, ENZYME REGULATION.
[34]	"Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II." Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., Park H.S., Kim K.Y., Lee J.S., Choi C., Bae Y.S., Lee B.I., Rhee S.G., Kang S.W. Nature 435:347-353(2005) [PubMed: 15902258] [Abstract] Cited for: AUTOPHOSPHORYLATION AT TYR-579; TYR-581; TYR-716; TYR-740; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
[35]	"Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation." Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H. J. Biol. Chem. 282:29336-29347(2007) [PubMed: 17620338] [Abstract] Cited for: INTERACTION WITH CBL, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1021, UBIQUITINATION.
[36]	"A novel signaling axis of matriptase/PDGF-D/ss-PDGFR in human prostate cancer." Ustach C.V., Huang W., Conley-LaComb M.K., Lin C.Y., Che M., Abrams J., Kim H.R. Cancer Res. 70:9631-9640(2010) [PubMed: 21098708] [Abstract] Cited for: FUNCTION AS PDGFD RECEPTOR.
[37]	"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration." Wardega P., Heldin C.H., Lennartsson J. Cell. Signal. 22:1363-1368(2010) [PubMed: 20494825] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CBL; STAM; PDCD6IP/ALIX; PLCG1 AND PTPN11, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-634 AND TYR-857.
[38]	"Stimulation of platelet-derived growth factor receptor beta (PDGFRbeta) activates ADAM17 and promotes metalloproteinase-dependent cross-talk between the PDGFRbeta and epidermal growth factor receptor (EGFR) signaling pathways." Mendelson K., Swendeman S., Saftig P., Blobel C.P. J. Biol. Chem. 285:25024-25032(2010) [PubMed: 20529858] [Abstract] Cited for: FUNCTION.
[39]	"Glyceollins inhibit platelet-derived growth factor-mediated human arterial smooth muscle cell proliferation and migration." Kim H.J., Cha B.Y., Choi B., Lim J.S., Woo J.T., Kim J.S. Br. J. Nutr. 0:0-0(2011) [PubMed: 21733313] [Abstract] Cited for: FUNCTION IN SMOOTH MUSCLE CELL PROLIFERATION AND MIGRATION.
[40]	"Direct interaction between Shc and the platelet-derived growth factor beta-receptor." Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H., Claesson-Welsh L. J. Biol. Chem. 269:15337-15343(1994) [PubMed: 8195171] [Abstract] Cited for: INTERACTION WITH SHC1 AND GRB2, FUNCTION IN PHOSPHORYLATION OF SHC1.
[41]	"Disruption of platelet-derived growth factor-dependent phosphatidylinositol 3-kinase and phospholipase Cgamma 1 activity abolishes vascular smooth muscle cell proliferation and migration and attenuates neointima formation in vivo." Caglayan E., Vantler M., Leppanen O., Gerhardt F., Mustafov L., Ten Freyhaus H., Kappert K., Odenthal M., Zimmermann W.H., Tallquist M.D., Rosenkranz S. J. Am. Coll. Cardiol. 57:2527-2538(2011) [PubMed: 21679854] [Abstract] Cited for: FUNCTION IN SMOOTH MUSCLE CELL MIGRATION AND NEOINTIMA FORMATION AFTER BLOOD VESSEL INJURY, MUTAGENESIS OF TYR-740; TYR-751 AND TYR-1021.
[42]	"Signal transduction via platelet-derived growth factor receptors." Heldin C.H., Ostman A., Ronnstrand L. Biochim. Biophys. Acta 1378:F79-113(1998) [PubMed: 9739761] [Abstract] Cited for: REVIEW ON SIGNALING AND AUTOPHOSPHORYLATION.
[43]	"PDGF receptors-mediators of autocrine tumor growth and regulators of tumor vasculature and stroma." Ostman A. Cytokine Growth Factor Rev. 15:275-286(2004) [PubMed: 15207817] [Abstract] Cited for: REVIEW.
[44]	"PDGF receptors as targets in tumor treatment." Ostman A., Heldin C.H. Adv. Cancer Res. 97:247-274(2007) [PubMed: 17419949] [Abstract] Cited for: REVIEW.
[45]	"Role of platelet-derived growth factors in physiology and medicine." Andrae J., Gallini R., Betsholtz C. Genes Dev. 22:1276-1312(2008) [PubMed: 18483217] [Abstract] Cited for: REVIEW ON FUNCTION; LIGANDS; ROLE IN DEVELOPMENT AND DISEASE AND ACTIVATION OF SIGNALING PATHWAYS.
[46]	"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.
[47]	"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, INTERACTION WITH SLC9A3R1.
[48]	"Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex." Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X. Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010) [PubMed: 20534510] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-314 IN COMPLEX WITH PDGFB, SUBUNIT, GLYCOSYLATION AT ASN-45; ASN-89; ASN-103; ASN-215; ASN-230; ASN-292 AND ASN-307, DISULFIDE BONDS.
[49]	"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

EMBL
GenBank
DDBJ

J03278 mRNA. Translation: AAA60049.1.
M21616 mRNA. Translation: AAA36427.1.
AC005895 Genomic DNA. No translation available.
AC011382 Genomic DNA. No translation available.
BC032224 mRNA. Translation: AAH32224.1.
U33172 Genomic DNA. Translation: AAC51675.1.

IPI

IPI00015902.

PIR

PFHUGB. A28206.

RefSeq

NP_002600.1. NM_002609.3.

UniGene

Hs.509067.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3MJG	X-ray	2.30	X/Y	33-314	[»]

ProteinModelPortal

P09619.

SMR

P09619. Positions 33-312, 379-529, 559-964.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-558N.

IntAct

P09619. 16 interactions.

MINT

MINT-148093.

STRING

P09619.

PTM databases

PhosphoSite

P09619.

Polymorphism databases

DMDM

129890.

Proteomic databases

PRIDE

P09619.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261799; ENSP00000261799; ENSG00000113721.

GeneID

5159.

KEGG

hsa:5159.

UCSC

uc003lro.1. human.

Organism-specific databases

CTD

5159.

GeneCards

GC05M149473.

H-InvDB

HIX0024847.

HGNC

HGNC:8804. PDGFRB.

HPA

CAB003842.
CAB018144.
HPA028499.

MIM

131440. phenotype.
173410. gene.

neXtProt

NX_P09619.

Orphanet

98823. Chronic myelomonocytic leukemia.
3260. Idiopathic hypereosinophilic syndrome.
168950. Myeloid neoplasm associated with PDGFRB rearrangement.
86830. Unclassified chronic myeloproliferative disease.

PharmGKB

PA33148.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17402.

HOGENOM

HBG445154.

HOVERGEN

HBG004335.

InParanoid

P09619.

OMA

GACTKGG.

OrthoDB

EOG4JT04Q.

PhylomeDB

P09619.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

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

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P09619.

Bgee

P09619.

CleanEx

HS_PDGFRB.

Genevestigator

P09619.

GermOnline

ENSG00000113721. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009134. Tyr_kinase_VEGFR_rcpt_N.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 4 hits.

KO

K05089.

Pfam

PF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000615. TyrPK_CSF1-R. 1 hit.

PRINTS

PR01832. VEGFRECEPTOR.

SMART

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

SUPFAM

SSF56112. Kinase_like. 1 hit.

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

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:	January 25, 2012
This is version 155 of the entry and version 1 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.