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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_RAT               Reviewed;        1097 AA.
Q05030; Q8R406; Q925F7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
25-JUL-2003, sequence version 2.
02-DEC-2020, entry version 186.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Wang Y., Culty M.;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-533.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=8318539; DOI=10.1016/0167-4781(93)90127-y;
Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.;
"Conservation in sequence and affinity of human and rodent PDGF ligands and
receptors.";
Biochim. Biophys. Acta 1173:294-302(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 528-1090.
STRAIN=Wistar;
PubMed=11346654; DOI=10.1074/jbc.m102995200;
Okuyama H., Shimahara Y., Kawada N., Seki S., Kristensen D.B.,
Yoshizato K., Uyama N., Yamaoka Y.;
"Regulation of cell growth by redox-mediated extracellular proteolysis of
platelet-derived growth factor receptor beta.";
J. Biol. Chem. 276:28274-28280(2001).
-!- 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. 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 similarity).
{ECO:0000250}.
-!- 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};
-!- 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 (By
similarity). {ECO:0000250}.
-!- 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}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}.
Lysosome lumen {ECO:0000250}. Note=After ligand binding, the
autophosphorylated receptor is ubiquitinated and internalized, leading
to its degradation. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
polyubiquitinated, leading to its degradation (By similarity).
{ECO:0000250}.
-!- 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. Dephosphorylated by PTPN2 at Tyr-
578 and Tyr-1020 (By similarity). {ECO:0000250}.
-!- 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; AY090783; AAM09098.1; -; mRNA.
EMBL; Z14119; CAA78489.1; -; mRNA.
EMBL; AF359356; AAK43716.1; -; mRNA.
PIR; S33766; S33766.
RefSeq; NP_113713.1; NM_031525.1.
RefSeq; XP_006254851.1; XM_006254789.3.
SMR; Q05030; -.
BioGRID; 246767; 2.
IntAct; Q05030; 2.
MINT; Q05030; -.
STRING; 10116.ENSRNOP00000060534; -.
BindingDB; Q05030; -.
ChEMBL; CHEMBL4125; -.
GlyGen; Q05030; 11 sites.
iPTMnet; Q05030; -.
PhosphoSitePlus; Q05030; -.
jPOST; Q05030; -.
PaxDb; Q05030; -.
PRIDE; Q05030; -.
Ensembl; ENSRNOT00000068535; ENSRNOP00000060534; ENSRNOG00000018461.
Ensembl; ENSRNOT00000078764; ENSRNOP00000070561; ENSRNOG00000018461.
Ensembl; ENSRNOT00000086033; ENSRNOP00000069485; ENSRNOG00000018461.
GeneID; 24629; -.
KEGG; rno:24629; -.
UCSC; RGD:3285; rat.
CTD; 5159; -.
RGD; 3285; Pdgfrb.
eggNOG; KOG0200; Eukaryota.
GeneTree; ENSGT00940000157138; -.
HOGENOM; CLU_000288_49_0_1; -.
InParanoid; Q05030; -.
OMA; TYVCNVS; -.
OrthoDB; 236292at2759; -.
PhylomeDB; Q05030; -.
Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
Reactome; R-RNO-186763; Downstream signal transduction.
Reactome; R-RNO-186797; Signaling by PDGF.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
PRO; PR:Q05030; -.
Proteomes; UP000002494; Chromosome 18.
Bgee; ENSRNOG00000018461; Expressed in female gonad and 20 other tissues.
Genevisible; Q05030; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:RGD.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0001726; C:ruffle; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
GO; GO:0016301; F:kinase activity; ISO:RGD.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB.
GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:RGD.
GO; GO:0005017; F:platelet-derived growth factor-activated receptor activity; IDA:RGD.
GO; GO:0004672; F:protein kinase activity; TAS:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:RGD.
GO; GO:0030325; P:adrenal gland development; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0035909; P:aorta morphogenesis; ISO:RGD.
GO; GO:0001568; P:blood vessel development; ISO:RGD.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0060981; P:cell migration involved in coronary angiogenesis; ISS:UniProtKB.
GO; GO:0035441; P:cell migration involved in vasculogenesis; ISS:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
GO; GO:0048568; P:embryonic organ development; ISO:RGD.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IMP:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0048839; P:inner ear development; IEP:RGD.
GO; GO:0035556; P:intracellular signal transduction; IMP:RGD.
GO; GO:0001822; P:kidney development; ISO:RGD.
GO; GO:0060437; P:lung growth; IMP:RGD.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEP:UniProtKB.
GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; ISS:UniProtKB.
GO; GO:0072223; P:metanephric glomerular mesangium development; ISO:RGD.
GO; GO:0072275; P:metanephric glomerulus morphogenesis; IEP:UniProtKB.
GO; GO:0035789; P:metanephric mesenchymal cell migration; IDA:UniProtKB.
GO; GO:0072075; P:metanephric mesenchyme development; IEP:UniProtKB.
GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IEP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0006807; P:nitrogen compound metabolic process; ISO:RGD.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISO:RGD.
GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IMP:RGD.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS: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; ISS:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:RGD.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0106096; P:response to ceramide; ISO:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0034405; P:response to fluid shear stress; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0033993; P:response to lipid; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
GO; GO:0097178; P:ruffle assembly; ISO:RGD.
GO; GO:0007165; P:signal transduction; ISO:RGD.
GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
GO; GO:0071670; P:smooth muscle cell chemotaxis; ISO:RGD.
GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0042060; P:wound healing; IEP:RGD.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
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; PF07679; I-set; 1.
Pfam; PF00047; ig; 1.
Pfam; PF07714; PK_Tyr_Ser-Thr; 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.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Chemotaxis; Cytoplasmic vesicle;
Developmental protein; 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
/evidence="ECO:0000255"
CHAIN 32..1097
/note="Platelet-derived growth factor receptor beta"
/id="PRO_0000016759"
TOPO_DOM 32..531
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 532..552
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 553..1097
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 32..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 415..523
/note="Ig-like C2-type 4"
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:0000250|UniProtKB:P05622"
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:0000250|UniProtKB:P05622"
MOD_RES 969
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000250|UniProtKB:P05622"
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:0000255"
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:0000255"
CARBOHYD 478
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
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"
SEQUENCE 1097 AA; 122828 MW; 5E6540FA0C5CF22B CRC64;
MGLPEVMPAS VLRGQLLLFV LLLLGPQISQ GLVITPPGPE FVLNISSTFV LTCSSSAPVM
WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV YNNSLGPELS ERKRIYIFVP
DPTMGFLPMD SEDLFIFVTD VTETTIPCRV TDPQLEVTLH EKKVDIPLHV PYDHQRGFIG
TFEDKTYICK TTIGDREVDS DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND
VVNFQWTYPR MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG
DEKAINVTVI ENGYVRLLET LEDVQIAELH RSRTLQVVFE AYPTPSVLWF KDNRTLGDSS
AGELVLSTRN VSETRYVSEL TLVRVKVSEA GYYTMRAFHA DDQVQLSFKL QVNVPVRVLE
LSESHPANGE QILRCRGRGM PQPNVTWSTC RDLKRCPRKL SPTPLGNSSK EESQLETNVT
FWEEDQEYEV VSTLRLRHVD QPLSVRCMLQ NSMGRDSQEV TVVPHSLPFK VVVISAILAL
VVLTVISLII LIMLWQRKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV
LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH
LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QRHSNKHCPP STELYSNALP
VGLSLPSHLN LTGESDGGYM DMSKDESVDY VPMLDMKGHI KYADIESSSY MAPYDNYVPS
APERTYRATL INDSPVLSYT DLVGFSYQVA NGMEFLASKN CVHRDLAARN VLICEGKLVK
ICDFGLARDI MRDSNYISKG STFLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL
LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR LPGLHSLRSP LDTSSVLYTA VQPNETDNDY
IIPLPDPKPD AADEGLLEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ AEPEAQLEQP
QDSGCPGPLA EAEDSFL


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