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Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (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) (PDGFR-1) (CD antigen CD140b)

 PGFRB_MOUSE             Reviewed;        1098 AA.
P05622; E9QPE2;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
03-JUL-2019, sequence version 2.
17-JUN-2020, entry version 214.
RecName: Full=Platelet-derived growth factor receptor beta;
Short=PDGF-R-beta;
Short=PDGFR-beta;
EC=2.7.10.1;
AltName: Full=Beta platelet-derived growth factor receptor;
AltName: Full=Beta-type platelet-derived growth factor receptor;
AltName: Full=CD140 antigen-like family member B;
AltName: Full=Platelet-derived growth factor receptor 1;
Short=PDGFR-1;
AltName: CD_antigen=CD140b;
Flags: Precursor;
Name=Pdgfrb; Synonyms=Pdgfr, Pdgfr1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fibroblast;
PubMed=3020426; DOI=10.1038/323226a0;
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.;
"Structure of the receptor for platelet-derived growth factor helps define
a family of closely related growth factor receptors.";
Nature 323:226-232(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBUNIT, AND AUTOPHOSPHORYLATION.
PubMed=8440729;
Seifert R.A., van Koppen A., Bowen-Pope D.F.;
"PDGF-AB requires PDGF receptor alpha-subunits for high-affinity, but not
for low-affinity, binding and signal transduction.";
J. Biol. Chem. 268:4473-4480(1993).
[4]
DISRUPTION PHENOTYPE.
PubMed=7958864; DOI=10.1101/gad.8.16.1888;
Soriano P.;
"Abnormal kidney development and hematological disorders in PDGF beta-
receptor mutant mice.";
Genes Dev. 8:1888-1896(1994).
[5]
INTERACTION WITH GRB10.
PubMed=10454568; DOI=10.1128/mcb.19.9.6217;
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
Swamy O.R., Leone M.E., Riedel H.;
"Grb10, a positive, stimulatory signaling adapter in platelet-derived
growth factor BB-, insulin-like growth factor I-, and insulin-mediated
mitogenesis.";
Mol. Cell. Biol. 19:6217-6228(1999).
[6]
TISSUE SPECIFICITY.
PubMed=14514732; DOI=10.1097/01.asn.0000089828.73014.c8;
Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V.,
Truong L., Johnson R.J., Alpers C.E.;
"Obstructive uropathy in mice and humans: potential role for PDGF-D in the
progression of tubulointerstitial injury.";
J. Am. Soc. Nephrol. 14:2544-2555(2003).
[7]
FUNCTION, AND MUTAGENESIS OF TYR-578; TYR-715; TYR-739; TYR-750; TYR-770;
TYR-1008 AND TYR-1020.
PubMed=14624252; DOI=10.1371/journal.pbio.0000052;
Tallquist M.D., French W.J., Soriano P.;
"Additive effects of PDGF receptor beta signaling pathways in vascular
smooth muscle cell development.";
PLoS Biol. 1:E52-E52(2003).
[8]
REVIEW ON FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15207813; DOI=10.1016/j.cytogfr.2004.03.005;
Betsholtz C.;
"Insight into the physiological functions of PDGF through genetic studies
in mice.";
Cytokine Growth Factor Rev. 15:215-228(2004).
[9]
MUTAGENESIS OF ASP-849, CATALYTIC ACTIVITY, FUNCTION, AND INTERACTION WITH
PIK3R1.
PubMed=15284236; DOI=10.1074/jbc.m406051200;
Chiara F., Goumans M.J., Forsberg H., Ahgren A., Rasola A., Aspenstrom P.,
Wernstedt C., Hellberg C., Heldin C.H., Heuchel R.;
"A gain of function mutation in the activation loop of platelet-derived
growth factor beta-receptor deregulates its kinase activity.";
J. Biol. Chem. 279:42516-42527(2004).
[10]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
PubMed=14966296; DOI=10.1128/mcb.24.5.2190-2201.2004;
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.;
"Site-selective regulation of platelet-derived growth factor beta receptor
tyrosine phosphorylation by T-cell protein tyrosine phosphatase.";
Mol. Cell. Biol. 24:2190-2201(2004).
[11]
FUNCTION, AND PHOSPHORYLATION AT TYR-685; TYR-933 AND TYR-969.
PubMed=14993293; DOI=10.1128/mcb.24.6.2573-2583.2004;
Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
"Bidirectional signaling links the Abelson kinases to the platelet-derived
growth factor receptor.";
Mol. Cell. Biol. 24:2573-2583(2004).
[12]
INTERACTION WITH CBL, AND UBIQUITINATION.
PubMed=15753096; DOI=10.1074/jbc.m410265200;
Takayama Y., May P., Anderson R.G., Herz J.;
"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).";
J. Biol. Chem. 280:18504-18510(2005).
[13]
INTERACTION WITH CBL AND PLCG1, AND FUNCTION.
PubMed=17620338; DOI=10.1074/jbc.m701797200;
Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J.,
Naramura M., Band V., Band H.;
"Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived
growth factor receptor beta provides a dual mechanism of negative
regulation.";
J. Biol. Chem. 282:29336-29347(2007).
[14]
FUNCTION.
PubMed=18948621; DOI=10.1161/circresaha.108.176768;
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.;
"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.";
Circ. Res. 103:1393-1401(2008).
[15]
DISRUPTION PHENOTYPE.
PubMed=18213589; DOI=10.1002/dvdy.21436;
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.;
"PDGF-B signaling is important for murine cardiac development: its role in
developing atrioventricular valves, coronaries, and cardiac innervation.";
Dev. Dyn. 237:494-503(2008).
[16]
FUNCTION.
PubMed=19030102; DOI=10.1371/journal.pone.0003794;
Wu E., Palmer N., Tian Z., Moseman A.P., Galdzicki M., Wang X., Berger B.,
Zhang H., Kohane I.S.;
"Comprehensive dissection of PDGF-PDGFR signaling pathways in PDGFR
genetically defined cells.";
PLoS ONE 3:E3794-E3794(2008).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-306; ASN-467 AND ASN-478.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[18]
FUNCTION, AND INTERACTION WITH PIK3R1.
PubMed=19742316; DOI=10.1371/journal.pone.0006922;
Zhou L., Takayama Y., Boucher P., Tallquist M.D., Herz J.;
"LRP1 regulates architecture of the vascular wall by controlling PDGFRbeta-
dependent phosphatidylinositol 3-kinase activation.";
PLoS ONE 4:E6922-E6922(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[20]
FUNCTION.
PubMed=21664579; DOI=10.1016/j.devcel.2011.04.019;
Olson L.E., Soriano P.;
"PDGFRbeta signaling regulates mural cell plasticity and inhibits fat
development.";
Dev. Cell 20:815-826(2011).
[21]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1005-1015 IN COMPLEX WITH PTPN11,
AND INTERACTION WITH PTPN11.
PubMed=7521735; DOI=10.1016/s0969-2126(00)00044-7;
Lee C.-H., Kominos D., Jacques S., Margolis B., Schlessinger J.,
Shoelson S.E., Kuriyan J.;
"Crystal structures of peptide complexes of the amino-terminal SH2 domain
of the Syp tyrosine phosphatase.";
Structure 2:423-438(1994).
-!- 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 Ca(2+) 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.
{ECO:0000250, ECO:0000269|PubMed:14624252, ECO:0000269|PubMed:14993293,
ECO:0000269|PubMed:15284236, ECO:0000269|PubMed:17620338,
ECO:0000269|PubMed:18948621, ECO:0000269|PubMed:19030102,
ECO:0000269|PubMed:19742316, ECO:0000269|PubMed:21664579,
ECO:0000269|PubMed:8440729}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
ECO:0000269|PubMed:15284236};
-!- ACTIVITY 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: 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).
{ECO:0000250}.
-!- INTERACTION:
P05622; P39688: Fyn; NbExp=3; IntAct=EBI-1554855, EBI-524514;
P05622; Q9JHL1: Slc9a3r2; NbExp=2; IntAct=EBI-1554855, EBI-538451;
P05622; Q91YD9: Wasl; NbExp=2; IntAct=EBI-1554855, EBI-642417;
P05622; C5IAU5: E5; Xeno; NbExp=2; IntAct=EBI-1554855, EBI-15646370;
P05622; P18031: PTPN1; Xeno; NbExp=3; IntAct=EBI-1554855, EBI-968788;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cytoplasmic vesicle {ECO:0000250}. Lysosome lumen
{ECO:0000250}. Note=After ligand binding, the autophosphorylated
receptor is ubiquitinated and internalized, leading to its degradation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P05622-1; Sequence=Displayed;
Name=2;
IsoId=P05622-2; Sequence=VSP_060195;
-!- 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. {ECO:0000269|PubMed:14514732}.
-!- PTM: 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. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
polyubiquitinated, leading to its degradation.
{ECO:0000269|PubMed:15753096}.
-!- 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.
{ECO:0000269|PubMed:15207813, ECO:0000269|PubMed:18213589,
ECO:0000269|PubMed:7958864}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X04367; CAA27882.1; -; mRNA.
EMBL; AC124448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS50300.1; -. [P05622-2]
PIR; A25742; PFMSRB.
RefSeq; NP_001139740.1; NM_001146268.1. [P05622-2]
RefSeq; NP_032835.2; NM_008809.2. [P05622-1]
PDB; 1AYA; X-ray; 2.05 A; P/Q=1005-1015.
PDB; 1AYC; X-ray; 2.30 A; P=736-744.
PDBsum; 1AYA; -.
PDBsum; 1AYC; -.
SMR; P05622; -.
BioGRID; 202089; 11.
ComplexPortal; CPX-2903; PDGF receptor alpha-beta - PDGF-AB complex.
ComplexPortal; CPX-2904; PDGF receptor beta - PDGF-AB complex.
ComplexPortal; CPX-2907; PDGF receptor alpha-beta - PDGF-BB complex.
ComplexPortal; CPX-2908; PDGF receptor beta - PDGF-BB complex.
ComplexPortal; CPX-2913; PDGF receptor alpha-beta - PDGF-CC complex.
ComplexPortal; CPX-2914; PDGF receptor beta - PDGF-CC complex.
ComplexPortal; CPX-2916; PDGF receptor alpha-beta - PDGF-DD complex.
ComplexPortal; CPX-2917; PDGF receptor beta - PDGF-DD complex.
CORUM; P05622; -.
DIP; DIP-39669N; -.
IntAct; P05622; 15.
MINT; P05622; -.
STRING; 10090.ENSMUSP00000025522; -.
ChEMBL; CHEMBL2749; -.
DrugCentral; P05622; -.
GuidetoPHARMACOLOGY; 1804; -.
iPTMnet; P05622; -.
PhosphoSitePlus; P05622; -.
MaxQB; P05622; -.
PaxDb; P05622; -.
PRIDE; P05622; -.
Antibodypedia; 3424; 2035 antibodies.
Ensembl; ENSMUST00000025522; ENSMUSP00000025522; ENSMUSG00000024620. [P05622-2]
GeneID; 18596; -.
KEGG; mmu:18596; -.
UCSC; uc008fbk.2; mouse. [P05622-1]
CTD; 5159; -.
MGI; MGI:97531; Pdgfrb.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000157138; -.
HOGENOM; CLU_000288_49_0_1; -.
InParanoid; P05622; -.
KO; K05089; -.
OMA; TYVCNVS; -.
OrthoDB; 236292at2759; -.
PhylomeDB; P05622; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-186797; Signaling by PDGF.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
BioGRID-ORCS; 18596; 0 hits in 13 CRISPR screens.
EvolutionaryTrace; P05622; -.
PRO; PR:P05622; -.
Proteomes; UP000000589; Chromosome 18.
RNAct; P05622; protein.
Bgee; ENSMUSG00000024620; Expressed in external carotid artery and 315 other tissues.
ExpressionAtlas; P05622; baseline and differential.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0001726; C:ruffle; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
GO; GO:0016301; F:kinase activity; IMP:MGI.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB.
GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
GO; GO:0005017; F:platelet-derived growth factor-activated receptor activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:MGI.
GO; GO:0030325; P:adrenal gland development; IGI:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0035909; P:aorta morphogenesis; IGI:BHF-UCL.
GO; GO:0001568; P:blood vessel development; IEP:UniProtKB.
GO; GO:0055003; P:cardiac myofibril assembly; IGI:UniProtKB.
GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0060981; P:cell migration involved in coronary angiogenesis; IMP:UniProtKB.
GO; GO:0035441; P:cell migration involved in vasculogenesis; IMP:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:MGI.
GO; GO:0048568; P:embryonic organ development; IEP:UniProtKB.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISO:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0060437; P:lung growth; ISO:MGI.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEA:Ensembl.
GO; GO:0072277; P:metanephric glomerular capillary formation; IGI:UniProtKB.
GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; IMP:UniProtKB.
GO; GO:0072223; P:metanephric glomerular mesangium development; IEP:UniProtKB.
GO; GO:0035789; P:metanephric mesenchymal cell migration; ISO:MGI.
GO; GO:0072075; P:metanephric mesenchyme development; IEA:Ensembl.
GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:MGI.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0090280; P:positive regulation of calcium ion import; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:BHF-UCL.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0106096; P:response to ceramide; IMP:MGI.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:UniProtKB.
GO; GO:0097178; P:ruffle assembly; IDA:MGI.
GO; GO:0007165; P:signal transduction; IDA:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0071670; P:smooth muscle cell chemotaxis; IGI:BHF-UCL.
GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027288; PGFRB.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Chemotaxis;
Cytoplasmic vesicle; Developmental protein; Direct protein sequencing;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Lysosome;
Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1..31
CHAIN 32..1098
/note="Platelet-derived growth factor receptor beta"
/id="PRO_0000016758"
TOPO_DOM 32..531
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 532..552
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 553..1098
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 33..119
/note="Ig-like C2-type 1"
DOMAIN 128..209
/note="Ig-like C2-type 2"
DOMAIN 213..308
/note="Ig-like C2-type 3"
DOMAIN 330..402
/note="Ig-like C2-type 4"
DOMAIN 415..523
/note="Ig-like C2-type 5"
DOMAIN 599..961
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 605..613
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 825
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 633
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 561
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 578
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 580
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 685
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000269|PubMed:14993293"
MOD_RES 715
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 739
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 750
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 762
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 770
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 774
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 777
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 856
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 933
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000269|PubMed:14993293"
MOD_RES 969
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000269|PubMed:14993293"
MOD_RES 1008
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 1020
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
CARBOHYD 44
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 88
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 102
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 214
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 291
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 306
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19656770"
CARBOHYD 353
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 370
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 444
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 467
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19656770"
CARBOHYD 478
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19656770"
DISULFID 53..99
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 148..189
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 234..290
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 435..507
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 454
/note="K -> KS (in isoform 2)"
/id="VSP_060195"
MUTAGEN 578
/note="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."
/evidence="ECO:0000269|PubMed:14624252"
MUTAGEN 715
/note="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."
/evidence="ECO:0000269|PubMed:14624252"
MUTAGEN 739
/note="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."
/evidence="ECO:0000269|PubMed:14624252"
MUTAGEN 750
/note="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."
/evidence="ECO:0000269|PubMed:14624252"
MUTAGEN 770
/note="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."
/evidence="ECO:0000269|PubMed:14624252"
MUTAGEN 849
/note="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."
/evidence="ECO:0000269|PubMed:15284236"
MUTAGEN 1008
/note="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."
/evidence="ECO:0000269|PubMed:14624252"
MUTAGEN 1020
/note="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."
/evidence="ECO:0000269|PubMed:14624252"
CONFLICT 863
/note="F -> Y (in Ref. 1; CAA27882)"
/evidence="ECO:0000305"
SEQUENCE 1098 AA; 122790 MW; D08FC7C42B77B794 CRC64;
MGLPGVIPAL VLRGQLLLSV LWLLGPQTSR GLVITPPGPE FVLNISSTFV LTCSGSAPVM
WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV YNNSLGPELS ERKRIYIFVP
DPTMGFLPMD SEDLFIFVTD VTETTIPCRV TDPQLEVTLH EKKVDIPLHV PYDHQRGFTG
TFEDKTYICK TTIGDREVDS DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND
VVNFQWTYPR MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG
DEKAINISVI ENGYVRLLET LGDVEIAELH RSRTLRVVFE AYPMPSVLWL KDNRTLGDSG
AGELVLSTRN MSETRYVSEL ILVRVKVSEA GYYTMRAFHE DDEVQLSFKL QVNVPVRVLE
LSESHPANGE QTIRCRGRGM PQPNVTWSTC RDLKRCPRKL SPTPLGNSSK EESQLETNVT
FWEEDQEYEV VSTLRLRHVD QPLSVRCMLQ NSMGGDSQEV TVVPHSLPFK VVVISAILAL
VVLTVISLII LIMLWQKKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV
LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH
LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QRHSNKHCPP SAELYSNALP
VGFSLPSHLN LTGESDGGYM DMSKDESIDY VPMLDMKGDI KYADIESPSY MAPYDNYVPS
APERTYRATL INDSPVLSYT DLVGFSYQVA NGMDFLASKN CVHRDLAARN VLICEGKLVK
ICDFGLARDI MRDSNYISKG STFLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL
LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR FPGIHSLRSP LDTSSVLYTA VQPNESDNDY
IIPLPDPKPD VADEGLPEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ QAEPEAQLEQ
PQDSGCPGPL AEAEDSFL


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Pathways :
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1367: TGF-beta Receptor Signaling Pathway
WP809: TGF-beta Receptor Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP566: canonical wnt - zebrafish
WP1161: TGF-beta Receptor Signaling Pathway
WP2148: Brain derived neurotrophic factor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP474: Endochondral Ossification
WP2256: Integrated Pancreatic Cancer Pathway
WP2328: Allograft rejection
WP2377: Integrated Pancreatic Cancer Pathway

Related Genes :
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (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) (PDGFR-1) (CD antigen CD140b)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (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) (PDGFR-1) (CD antigen CD140b)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (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) (PDGFR-1) (CD antigen CD140b)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (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) (PDGFR-1) (CD antigen CD140b)
[PDGFRA PDGFR2 RHEPDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a)
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[pdgfrb] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor)
[I79_024441] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA GW7_00400] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[Pdgfra rCG_57147] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)

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