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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)DescriptionActionsGraphical viewLength
Binding sitei633ATPPROSITE-ProRule annotation1
Active sitei825Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi605 – 613ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: MGI
  • 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)DescriptionActionsGraphical viewLength
Topological domaini32 – 531ExtracellularSequence analysisAdd BLAST500
Transmembranei532 – 552HelicalSequence analysisAdd BLAST21
Topological domaini553 – 1098CytoplasmicSequence analysisAdd BLAST546

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)DescriptionActionsGraphical viewLength
Mutagenesisi578Y → 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 Publication1
Mutagenesisi715Y → 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 Publication1
Mutagenesisi739Y → 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 Publication1
Mutagenesisi750Y → 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 Publication1
Mutagenesisi770Y → 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 Publication1
Mutagenesisi849D → 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 Publication1
Mutagenesisi1008Y → 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 Publication1
Mutagenesisi1020Y → 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 Publication1

Chemistry databases

ChEMBLiCHEMBL2749.
GuidetoPHARMACOLOGYi1804.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000001675832 – 1098Platelet-derived growth factor receptor betaAdd BLAST1067

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi44N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi53 ↔ 99PROSITE-ProRule annotation
Glycosylationi88N-linked (GlcNAc...)Sequence analysis1
Glycosylationi102N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi148 ↔ 189PROSITE-ProRule annotation
Glycosylationi214N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi234 ↔ 290PROSITE-ProRule annotation
Glycosylationi291N-linked (GlcNAc...)Sequence analysis1
Glycosylationi306N-linked (GlcNAc...)1 Publication1
Glycosylationi312N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi353N-linked (GlcNAc...)Sequence analysis1
Glycosylationi370N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi435 ↔ 507PROSITE-ProRule annotation
Glycosylationi444N-linked (GlcNAc...)Sequence analysis1
Glycosylationi467N-linked (GlcNAc...)1 Publication1
Glycosylationi478N-linked (GlcNAc...)1 Publication1
Modified residuei561Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei578Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei580Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei685Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei715Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei739Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei750Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei762Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei770Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei774Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei777Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei856Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei933Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei969Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei1008Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1020Phosphotyrosine; by autocatalysisBy similarity1

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.
PhosphoSitePlusiP05622.

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

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP05622.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYAX-ray2.05P/Q1005-1015[»]
1AYCX-ray2.30P736-744[»]
ProteinModelPortaliP05622.
SMRiP05622.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05622.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 119Ig-like C2-type 1Add BLAST87
Domaini128 – 209Ig-like C2-type 2Add BLAST82
Domaini213 – 308Ig-like C2-type 3Add BLAST96
Domaini330 – 402Ig-like C2-type 4Add BLAST73
Domaini415 – 523Ig-like C2-type 5Add BLAST109
Domaini599 – 961Protein kinasePROSITE-ProRule annotationAdd BLAST363

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYAX-ray2.05P/Q1005-1015[»]
1AYCX-ray2.30P736-744[»]
ProteinModelPortaliP05622.
SMRiP05622.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP05622.
ChEMBLiCHEMBL2749.
GuidetoPHARMACOLOGYi1804.

PTM databases

iPTMnetiP05622.
PhosphoSitePlusiP05622.

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...

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: November 30, 2016
This is version 185 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.