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Protein

Platelet-derived growth factor receptor beta

Gene

Pdgfrb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity9 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei633 – 6331ATPPROSITE-ProRule annotation
Active sitei825 – 8251Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi605 – 6139ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: MGI
  • platelet-derived growth factor beta-receptor activity Source: UniProtKB
  • platelet-derived growth factor binding Source: DFLAT
  • platelet-derived growth factor receptor binding Source: MGI
  • protein kinase binding Source: MGI
  • protein tyrosine kinase activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • signal transducer activity Source: MGI
  • vascular endothelial growth factor binding Source: MGI

GO - Biological processi

  • adrenal gland development Source: MGI
  • aorta morphogenesis Source: BHF-UCL
  • blood vessel development Source: UniProtKB
  • cardiac myofibril assembly Source: UniProtKB
  • cardiac vascular smooth muscle cell differentiation Source: DFLAT
  • cell chemotaxis Source: UniProtKB
  • cell migration Source: MGI
  • cell migration involved in coronary angiogenesis Source: UniProtKB
  • cell migration involved in vasculogenesis Source: UniProtKB
  • embryonic organ development Source: UniProtKB
  • in utero embryonic development Source: MGI
  • kidney development Source: MGI
  • metanephric glomerular capillary formation Source: UniProtKB
  • metanephric glomerular mesangial cell proliferation involved in metanephros development Source: UniProtKB
  • metanephric glomerular mesangium development Source: UniProtKB
  • nitrogen compound metabolic process Source: MGI
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: MGI
  • phosphatidylinositol metabolic process Source: MGI
  • platelet-derived growth factor receptor-beta signaling pathway Source: MGI
  • platelet-derived growth factor receptor signaling pathway Source: MGI
  • positive regulation of calcium ion import Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of chemotaxis Source: UniProtKB
  • positive regulation of DNA biosynthetic process Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of phospholipase C activity Source: MGI
  • positive regulation of phosphoprotein phosphatase activity Source: MGI
  • positive regulation of reactive oxygen species metabolic process Source: UniProtKB
  • positive regulation of smooth muscle cell migration Source: UniProtKB
  • positive regulation of smooth muscle cell proliferation Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of actin cytoskeleton organization Source: BHF-UCL
  • regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • retina vasculature development in camera-type eye Source: UniProtKB
  • signal transduction Source: MGI
  • skeletal system morphogenesis Source: MGI
  • smooth muscle cell chemotaxis Source: BHF-UCL
  • smooth muscle tissue development Source: MGI
  • tissue homeostasis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-derived growth factor receptor beta (EC:2.7.10.1)
Short name:
PDGF-R-beta
Short name:
PDGFR-beta
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 namesi
Name:Pdgfrb
Synonyms:Pdgfr, Pdgfr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97531. Pdgfrb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 531500ExtracellularSequence analysisAdd
BLAST
Transmembranei532 – 55221HelicalSequence analysisAdd
BLAST
Topological domaini553 – 1098546CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi578 – 5781Y → 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. 1 Publication
Mutagenesisi715 – 7151Y → 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. 1 Publication
Mutagenesisi739 – 7391Y → 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. 1 Publication
Mutagenesisi750 – 7501Y → 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. 1 Publication
Mutagenesisi770 – 7701Y → 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. 1 Publication
Mutagenesisi849 – 8491D → N: Increased autophosphorylation in the absence of PDGFB binding. Increased autophosphorylation in response to PDGFB binding. Constitutive interaction with PIK3R1, and constitutive AKT1 activation. 1 Publication
Mutagenesisi1008 – 10081Y → 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. 1 Publication
Mutagenesisi1020 – 10201Y → 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. 1 Publication

Chemistry

ChEMBLiCHEMBL2096980.
GuidetoPHARMACOLOGYi1804.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Add
BLAST
Chaini32 – 10981067Platelet-derived growth factor receptor betaPRO_0000016758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi53 ↔ 99PROSITE-ProRule annotation
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence analysis
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi148 ↔ 189PROSITE-ProRule annotation
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence analysis
Disulfide bondi234 ↔ 290PROSITE-ProRule annotation
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)1 Publication
Glycosylationi312 – 3121N-linked (GlcNAc...); atypical1 Publication
Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi435 ↔ 507PROSITE-ProRule annotation
Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence analysis
Glycosylationi467 – 4671N-linked (GlcNAc...)1 Publication
Glycosylationi478 – 4781N-linked (GlcNAc...)1 Publication
Modified residuei561 – 5611Phosphotyrosine; by autocatalysisBy similarity
Modified residuei578 – 5781Phosphotyrosine; by autocatalysisBy similarity
Modified residuei580 – 5801Phosphotyrosine; by autocatalysisBy similarity
Modified residuei685 – 6851Phosphotyrosine; by ABL1 and ABL21 Publication
Modified residuei715 – 7151Phosphotyrosine; by autocatalysisBy similarity
Modified residuei739 – 7391Phosphotyrosine; by autocatalysisBy similarity
Modified residuei750 – 7501Phosphotyrosine; by autocatalysisBy similarity
Modified residuei762 – 7621Phosphotyrosine; by autocatalysisBy similarity
Modified residuei770 – 7701Phosphotyrosine; by autocatalysisBy similarity
Modified residuei774 – 7741Phosphotyrosine; by autocatalysisBy similarity
Modified residuei777 – 7771Phosphotyrosine; by autocatalysisBy similarity
Modified residuei856 – 8561Phosphotyrosine; by autocatalysisBy similarity
Modified residuei933 – 9331Phosphotyrosine; by ABL1 and ABL21 Publication
Modified residuei969 – 9691Phosphotyrosine; by ABL1 and ABL21 Publication
Modified residuei1008 – 10081Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1020 – 10201Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

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). Dephosphorylated by PTPN2 at Tyr-578 and Tyr-1020.By similarity
N-glycosylated.By similarity
Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05622.
PaxDbiP05622.
PRIDEiP05622.

PTM databases

iPTMnetiP05622.
PhosphoSiteiP05622.

Expressioni

Tissue specificityi

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 14.1 Publication

Interactioni

Subunit structurei

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 and RASA1. 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FynP396883EBI-1554855,EBI-524514
PTPN1P180313EBI-1554855,EBI-968788From a different organism.
Slc9a3r2Q9JHL12EBI-1554855,EBI-538451
WaslQ91YD92EBI-1554855,EBI-642417

GO - Molecular functioni

  • platelet-derived growth factor binding Source: DFLAT
  • platelet-derived growth factor receptor binding Source: MGI
  • protein kinase binding Source: MGI
  • receptor binding Source: UniProtKB
  • vascular endothelial growth factor binding Source: MGI

Protein-protein interaction databases

BioGridi202089. 5 interactions.
DIPiDIP-39669N.
IntActiP05622. 13 interactions.
MINTiMINT-2832882.
STRINGi10090.ENSMUSP00000025522.

Chemistry

BindingDBiP05622.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYAX-ray2.05P/Q1005-1015[»]
1AYCX-ray2.30P736-744[»]
ProteinModelPortaliP05622.
SMRiP05622. Positions 32-311, 525-562, 575-694, 797-958.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05622.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 11987Ig-like C2-type 1Add
BLAST
Domaini128 – 20982Ig-like C2-type 2Add
BLAST
Domaini213 – 30896Ig-like C2-type 3Add
BLAST
Domaini330 – 40273Ig-like C2-type 4Add
BLAST
Domaini415 – 523109Ig-like C2-type 5Add
BLAST
Domaini599 – 961363Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOVERGENiHBG004335.
InParanoidiP05622.
KOiK05089.
PhylomeDBiP05622.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR027288. PGFRB.
IPR000719. Prot_kinase_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.
[Graphical view]
PANTHERiPTHR24416:SF53. PTHR24416:SF53. 3 hits.
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500948. Beta-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLPGVIPAL VLRGQLLLSV LWLLGPQTSR GLVITPPGPE FVLNISSTFV
60 70 80 90 100
LTCSGSAPVM WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV
110 120 130 140 150
YNNSLGPELS ERKRIYIFVP DPTMGFLPMD SEDLFIFVTD VTETTIPCRV
160 170 180 190 200
TDPQLEVTLH EKKVDIPLHV PYDHQRGFTG TFEDKTYICK TTIGDREVDS
210 220 230 240 250
DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND VVNFQWTYPR
260 270 280 290 300
MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG
310 320 330 340 350
DEKAINISVI ENGYVRLLET LGDVEIAELH RSRTLRVVFE AYPMPSVLWL
360 370 380 390 400
KDNRTLGDSG AGELVLSTRN MSETRYVSEL ILVRVKVSEA GYYTMRAFHE
410 420 430 440 450
DDEVQLSFKL QVNVPVRVLE LSESHPANGE QTIRCRGRGM PQPNVTWSTC
460 470 480 490 500
RDLKRCPRKL SPTPLGNSSK EESQLETNVT FWEEDQEYEV VSTLRLRHVD
510 520 530 540 550
QPLSVRCMLQ NSMGGDSQEV TVVPHSLPFK VVVISAILAL VVLTVISLII
560 570 580 590 600
LIMLWQKKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV
610 620 630 640 650
LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE
660 670 680 690 700
LKIMSHLGPH LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL
710 720 730 740 750
QRHSNKHCPP SAELYSNALP VGFSLPSHLN LTGESDGGYM DMSKDESIDY
760 770 780 790 800
VPMLDMKGDI KYADIESPSY MAPYDNYVPS APERTYRATL INDSPVLSYT
810 820 830 840 850
DLVGFSYQVA NGMDFLASKN CVHRDLAARN VLICEGKLVK ICDFGLARDI
860 870 880 890 900
MRDSNYISKG STYLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG
910 920 930 940 950
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF
960 970 980 990 1000
SQLVLLLERL LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR FPGIHSLRSP
1010 1020 1030 1040 1050
LDTSSVLYTA VQPNESDNDY IIPLPDPKPD VADEGLPEGS PSLASSTLNE
1060 1070 1080 1090
VNTSSTISCD SPLELQEEPQ QAEPEAQLEQ PQDSGCPGPL AEAEDSFL
Length:1,098
Mass (Da):122,806
Last modified:November 1, 1988 - v1
Checksum:i8D391CAFAC3FC31D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04367 mRNA. Translation: CAA27882.1.
PIRiA25742. PFMSRB.
RefSeqiNP_001139740.1. NM_001146268.1.
NP_032835.2. NM_008809.2.
UniGeneiMm.4146.

Genome annotation databases

GeneIDi18596.
KEGGimmu:18596.
UCSCiuc008fbk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04367 mRNA. Translation: CAA27882.1.
PIRiA25742. PFMSRB.
RefSeqiNP_001139740.1. NM_001146268.1.
NP_032835.2. NM_008809.2.
UniGeneiMm.4146.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYAX-ray2.05P/Q1005-1015[»]
1AYCX-ray2.30P736-744[»]
ProteinModelPortaliP05622.
SMRiP05622. Positions 32-311, 525-562, 575-694, 797-958.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202089. 5 interactions.
DIPiDIP-39669N.
IntActiP05622. 13 interactions.
MINTiMINT-2832882.
STRINGi10090.ENSMUSP00000025522.

Chemistry

BindingDBiP05622.
ChEMBLiCHEMBL2096980.
GuidetoPHARMACOLOGYi1804.

PTM databases

iPTMnetiP05622.
PhosphoSiteiP05622.

Proteomic databases

MaxQBiP05622.
PaxDbiP05622.
PRIDEiP05622.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18596.
KEGGimmu:18596.
UCSCiuc008fbk.2. mouse.

Organism-specific databases

CTDi5159.
MGIiMGI:97531. Pdgfrb.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOVERGENiHBG004335.
InParanoidiP05622.
KOiK05089.
PhylomeDBiP05622.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Miscellaneous databases

EvolutionaryTraceiP05622.
PROiP05622.
SOURCEiSearch...

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR027288. PGFRB.
IPR000719. Prot_kinase_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.
[Graphical view]
PANTHERiPTHR24416:SF53. PTHR24416:SF53. 3 hits.
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500948. Beta-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Site-selective regulation of platelet-derived growth factor beta receptor tyrosine phosphorylation by T-cell protein tyrosine phosphatase."
    Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B., Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L., Ostman A., Hellberg C.
    Mol. Cell. Biol. 24:2190-2201(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
    Tissue: Myoblast.
  17. "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.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung and Spleen.
  19. "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.
  20. "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.

Entry informationi

Entry nameiPGFRB_MOUSE
AccessioniPrimary (citable) accession number: P05622
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 8, 2016
This is version 182 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.