P05622 (PGFRB_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1098 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 By similarity. 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.2 Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.8
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.
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 By similarity. Ref.2 Ref.4 Ref.8 Ref.10 Ref.11 Ref.16 Ref.18
Subcellular location	Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle By similarity. Lysosome lumen By similarity. Note: After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
Tissue specificity	Weakly expressed in glomerular mesangial cells and interstitial cells. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, increased expression in interstitial cells at day 4 and expression is markedly elevated at day 7 and is maximal at day 14. Ref.5
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-578, and to a lesser degree, Tyr-580 is important for interaction with SRC. Phosphorylation at Tyr-715 is important for interaction with GRB2. Phosphorylation at Tyr-739 and Tyr-750 is important for interaction with PIK3R1. Phosphorylation at Tyr-750 is important for interaction with NCK1. Phosphorylation at Tyr-770 and Tyr-856 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-856 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-1008 is important for interaction with PTPN11. Phosphorylation at Tyr-1008 and Tyr-1020 is important for interaction with PLCG1. Dephosphorylated by PTPRJ at Tyr-750, Tyr-856, Tyr-1008 and Tyr-1020 By similarity. Ref.2 Ref.9 N-glycosylated By similarity. Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation. Ref.10
Disruption phenotype	No apparent phenotype up to 16 dpc. Lethality late during gestation or at birth, due to widespread bleedings. This is due to a severe shortage of vascular smooth muscle cells and pericytes, especially in the central nervous system, skin, lung and heart. Mutants suffer from hemorrhages, anemia, thrombocytopenia, and show defects in the formation of kidney glomeruli, due to a lack of mesangial cells. Ref.3 Ref.7 Ref.13
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
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	adrenal gland development Inferred from genetic interaction PubMed 19056881. Source: MGI aorta morphogenesis Inferred from genetic interaction Ref.16. Source: BHF-UCL cardiac myofibril assembly Inferred from genetic interaction PubMed 11239463. Source: UniProtKB cardiac vascular smooth muscle cell differentiation Traceable author statement PubMed 20299672. Source: DFLAT cell migration involved in coronary angiogenesis Inferred from mutant phenotype Ref.6. Source: UniProtKB cell migration involved in vasculogenesis Inferred from mutant phenotype Ref.6. Source: UniProtKB embryonic organ development Inferred from expression pattern PubMed 10375497. Source: UniProtKB in utero embryonic development Inferred from mutant phenotype PubMed 17143286. Source: MGI metanephric glomerular capillary formation Inferred from genetic interaction PubMed 11239463. Source: UniProtKB metanephric glomerular mesangial cell proliferation involved in metanephros development Inferred from mutant phenotype PubMed 9693135. Source: UniProtKB nitrogen compound metabolic process Inferred from mutant phenotype PubMed 17143286. Source: MGI peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.6. Source: UniProtKB positive regulation of DNA biosynthetic process Inferred from mutant phenotype PubMed 19019919. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from direct assay PubMed 17942966. Source: UniProtKB positive regulation of MAP kinase activity Inferred from direct assay PubMed 17942966. Source: UniProtKB positive regulation of calcium ion import Inferred from mutant phenotype PubMed 19019919. Source: UniProtKB positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of chemotaxis Inferred from direct assay PubMed 19019919. Source: UniProtKB positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Inferred from mutant phenotype PubMed 19019919. Source: UniProtKB positive regulation of mitosis Inferred from direct assay PubMed 17942966. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Inferred from direct assay PubMed 17942966. Source: UniProtKB positive regulation of reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 19019919. Source: UniProtKB positive regulation of smooth muscle cell migration Inferred from mutant phenotype PubMed 10375497. Source: UniProtKB positive regulation of smooth muscle cell proliferation Inferred from mutant phenotype PubMed 10375497. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.6. Source: UniProtKB regulation of actin cytoskeleton organization Inferred from genetic interaction Ref.16. Source: BHF-UCL regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype PubMed 11940581. Source: MGI retina vasculature development in camera-type eye Inferred from mutant phenotype Ref.6. Source: UniProtKB skeletal system morphogenesis Inferred from mutant phenotype PubMed 17143286. Source: MGI smooth muscle cell chemotaxis Inferred from genetic interaction Ref.16. Source: BHF-UCL smooth muscle tissue development Inferred from mutant phenotype PubMed 17143286. Source: MGI tissue homeostasis Inferred from mutant phenotype PubMed 17143286. Source: MGI vascular endothelial growth factor receptor signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	apical plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm 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-derived growth factor beta-receptor activity Inferred from sequence or structural similarity. Source: UniProtKB platelet-derived growth factor binding Traceable author statement PubMed 20299672. Source: DFLAT vascular endothelial growth factor-activated receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31
	Chain	32 – 1098	1067	Platelet-derived growth factor receptor beta		PRO_0000016758
Regions
	Topological domain	32 – 531	500	Extracellular Potential
	Transmembrane	532 – 552	21	Helical; Potential
	Topological domain	553 – 1098	546	Cytoplasmic Potential
	Domain	33 – 119	87	Ig-like C2-type 1
	Domain	128 – 209	82	Ig-like C2-type 2
	Domain	213 – 308	96	Ig-like C2-type 3
	Domain	330 – 402	73	Ig-like C2-type 4
	Domain	415 – 523	109	Ig-like C2-type 5
	Domain	599 – 961	363	Protein kinase
	Nucleotide binding	605 – 613	9	ATP By similarity
Sites
	Active site	825	1	Proton acceptor By similarity
	Binding site	633	1	ATP By similarity
Amino acid modifications
	Modified residue	561	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	578	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	580	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	588	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	685	1	Phosphotyrosine; by ABL1 and ABL2 Ref.9
	Modified residue	715	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	739	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	750	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	762	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	770	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	774	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	777	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	856	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	933	1	Phosphotyrosine; by ABL1 and ABL2 Ref.9
	Modified residue	969	1	Phosphotyrosine; by ABL1 and ABL2 Ref.9
	Modified residue	1008	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1020	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	102	1	N-linked (GlcNAc...) Potential
	Glycosylation	214	1	N-linked (GlcNAc...) Potential
	Glycosylation	291	1	N-linked (GlcNAc...) Potential
	Glycosylation	306	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	312	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	353	1	N-linked (GlcNAc...) Potential
	Glycosylation	370	1	N-linked (GlcNAc...) Potential
	Glycosylation	444	1	N-linked (GlcNAc...) Potential
	Glycosylation	467	1	N-linked (GlcNAc...) Ref.15
	Glycosylation	478	1	N-linked (GlcNAc...) Ref.15
	Disulfide bond	53 ↔ 99		By similarity
	Disulfide bond	148 ↔ 189		By similarity
	Disulfide bond	234 ↔ 290		By similarity
	Disulfide bond	435 ↔ 507		By similarity
Experimental info
	Mutagenesis	578	1	Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-715; F-739; F-750; F-770; F-1008 and F-1020. Ref.6
	Mutagenesis	715	1	Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-739; F-750; F-770; F-1008 and F-1020. Ref.6
	Mutagenesis	739	1	Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-750; F-770; F-1008 and F-1020. Ref.6
	Mutagenesis	750	1	Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-770; F-1008 and F-1020. Ref.6
	Mutagenesis	770	1	Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-1008 and F-1020. Ref.6
	Mutagenesis	849	1	D → N: Increased autophosphorylation in the absence of PDGFB binding. Increased autophosphorylation in response to PDGFB binding. Constitutive interaction with PIK3R1, and constitutive AKT1 activation. Ref.8
	Mutagenesis	1008	1	Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-770 and F-1020. Ref.6
	Mutagenesis	1020	1	Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-770 and F-1008. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P05622 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 8D391CAFAC3FC31D	FASTA	1,098	122,806
	10 20 30 40 50 60 MGLPGVIPAL VLRGQLLLSV LWLLGPQTSR GLVITPPGPE FVLNISSTFV LTCSGSAPVM 70 80 90 100 110 120 WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV YNNSLGPELS ERKRIYIFVP 130 140 150 160 170 180 DPTMGFLPMD SEDLFIFVTD VTETTIPCRV TDPQLEVTLH EKKVDIPLHV PYDHQRGFTG 190 200 210 220 230 240 TFEDKTYICK TTIGDREVDS DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND 250 260 270 280 290 300 VVNFQWTYPR MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG 310 320 330 340 350 360 DEKAINISVI ENGYVRLLET LGDVEIAELH RSRTLRVVFE AYPMPSVLWL KDNRTLGDSG 370 380 390 400 410 420 AGELVLSTRN MSETRYVSEL ILVRVKVSEA GYYTMRAFHE DDEVQLSFKL QVNVPVRVLE 430 440 450 460 470 480 LSESHPANGE QTIRCRGRGM PQPNVTWSTC RDLKRCPRKL SPTPLGNSSK EESQLETNVT 490 500 510 520 530 540 FWEEDQEYEV VSTLRLRHVD QPLSVRCMLQ NSMGGDSQEV TVVPHSLPFK VVVISAILAL 550 560 570 580 590 600 VVLTVISLII LIMLWQKKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV 610 620 630 640 650 660 LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH 670 680 690 700 710 720 LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QRHSNKHCPP SAELYSNALP 730 740 750 760 770 780 VGFSLPSHLN LTGESDGGYM DMSKDESIDY VPMLDMKGDI KYADIESPSY MAPYDNYVPS 790 800 810 820 830 840 APERTYRATL INDSPVLSYT DLVGFSYQVA NGMDFLASKN CVHRDLAARN VLICEGKLVK 850 860 870 880 890 900 ICDFGLARDI MRDSNYISKG STYLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG 910 920 930 940 950 960 TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL 970 980 990 1000 1010 1020 LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR FPGIHSLRSP LDTSSVLYTA VQPNESDNDY 1030 1040 1050 1060 1070 1080 IIPLPDPKPD VADEGLPEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ QAEPEAQLEQ 1090 PQDSGCPGPL AEAEDSFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors." Yarden Y., Escobedo J.A., Kuang W.-J., Yang-Feng T.L., Daniel T.O., Tremble P.M., Chen E.Y., Ando M.E., Harkins R.N., Francke U., Fried V.A., Ullrich A., Williams L.T. Nature 323:226-232(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Fibroblast.
[2]	"PDGF-AB requires PDGF receptor alpha-subunits for high-affinity, but not for low-affinity, binding and signal transduction." Seifert R.A., van Koppen A., Bowen-Pope D.F. J. Biol. Chem. 268:4473-4480(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBUNIT, AUTOPHOSPHORYLATION.
[3]	"Abnormal kidney development and hematological disorders in PDGF beta-receptor mutant mice." Soriano P. Genes Dev. 8:1888-1896(1994) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[4]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB10.
[5]	"Obstructive uropathy in mice and humans: potential role for PDGF-D in the progression of tubulointerstitial injury." Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V., Truong L., Johnson R.J., Alpers C.E. J. Am. Soc. Nephrol. 14:2544-2555(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Additive effects of PDGF receptor beta signaling pathways in vascular smooth muscle cell development." Tallquist M.D., French W.J., Soriano P. PLoS Biol. 1:E52-E52(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-578; TYR-715; TYR-739; TYR-750; TYR-770; TYR-1008 AND TYR-1020.
[7]	"Insight into the physiological functions of PDGF through genetic studies in mice." Betsholtz C. Cytokine Growth Factor Rev. 15:215-228(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION, DISRUPTION PHENOTYPE.
[8]	"A gain of function mutation in the activation loop of platelet-derived growth factor beta-receptor deregulates its kinase activity." Chiara F., Goumans M.J., Forsberg H., Ahgren A., Rasola A., Aspenstrom P., Wernstedt C., Hellberg C., Heldin C.H., Heuchel R. J. Biol. Chem. 279:42516-42527(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-849, CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH PIK3R1.
[9]	"Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor." Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M. Mol. Cell. Biol. 24:2573-2583(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT TYR-685; TYR-933 AND TYR-969.
[10]	"Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor beta (PDGFR beta)." Takayama Y., May P., Anderson R.G., Herz J. J. Biol. Chem. 280:18504-18510(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBL, UBIQUITINATION.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBL AND PLCG1, FUNCTION.
[12]	"Platelet-derived growth factor receptor beta signaling is required for efficient epicardial cell migration and development of two distinct coronary vascular smooth muscle cell populations." Mellgren A.M., Smith C.L., Olsen G.S., Eskiocak B., Zhou B., Kazi M.N., Ruiz F.R., Pu W.T., Tallquist M.D. Circ. Res. 103:1393-1401(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"PDGF-B signaling is important for murine cardiac development: its role in developing atrioventricular valves, coronaries, and cardiac innervation." Van den Akker N.M., Winkel L.C., Nisancioglu M.H., Maas S., Wisse L.J., Armulik A., Poelmann R.E., Lie-Venema H., Betsholtz C., Gittenberger-de Groot A.C. Dev. Dyn. 237:494-503(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[14]	"Comprehensive dissection of PDGF-PDGFR signaling pathways in PDGFR genetically defined cells." Wu E., Palmer N., Tian Z., Moseman A.P., Galdzicki M., Wang X., Berger B., Zhang H., Kohane I.S. PLoS ONE 3:E3794-E3794(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-306; ASN-312; ASN-467 AND ASN-478, MASS SPECTROMETRY. Tissue: Myoblast.
[16]	"LRP1 regulates architecture of the vascular wall by controlling PDGFRbeta-dependent phosphatidylinositol 3-kinase activation." Zhou L., Takayama Y., Boucher P., Tallquist M.D., Herz J. PLoS ONE 4:E6922-E6922(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PIK3R1.
[17]	"PDGFRbeta signaling regulates mural cell plasticity and inhibits fat development." Olson L.E., Soriano P. Dev. Cell 20:815-826(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase." Lee C.-H., Kominos D., Jacques S., Margolis B., Schlessinger J., Shoelson S.E., Kuriyan J. Structure 2:423-438(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1005-1015 IN COMPLEX WITH PTPN11, INTERACTION WITH PTPN11.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04367 mRNA. Translation: CAA27882.1.

IPI

IPI00751332.

PIR

PFMSRB. A25742.

RefSeq

NP_001139740.1. NM_001146268.1.
NP_032835.2. NM_008809.2.

UniGene

Mm.4146.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AYA	X-ray	2.05	P/Q	1005-1015	[»]
1AYC	X-ray	2.30	P	736-744	[»]

ProteinModelPortal

P05622.

SMR

P05622. Positions 32-450, 525-562, 575-1007.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39669N.

IntAct

P05622. 2 interactions.

MINT

MINT-2832882.

PTM databases

PhosphoSite

P05622.

Proteomic databases

PaxDb

P05622.

PRIDE

P05622.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

18596.

KEGG

mmu:18596.

UCSC

uc008fbk.2. mouse.

Organism-specific databases

CTD

5159.

MGI

MGI:97531. Pdgfrb.

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG004335.

InParanoid

P05622.

KO

K05089.

OrthoDB

EOG4JT04Q.

Enzyme and pathway databases

BRENDA

2.7.10.1. 3474.

Gene expression databases

Genevestigator

P05622.

GermOnline

ENSMUSG00000024620. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 5 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR027288. PGFRB.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
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]

Pfam

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

PIRSF

PIRSF500948. Beta-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.

PRINTS

PR01832. VEGFRECEPTOR.

SMART

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

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50835. IG_LIKE. 3 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

BindingDB

P05622.

ChEMBL

CHEMBL2749.

EvolutionaryTrace

P05622.

NextBio

294486.

SOURCE

Search...

Entry information

Entry name

PGFRB_MOUSE

Accession

Primary (citable) accession number: P05622

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 1, 2013
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