Pdgfrb
entrez
24629
canonical
uniprot
Q05030
canonical
ensembl
ENSRNOG00000018461
resolver
ensp
ENSRNOP00000069485
resolver
genesymbol
Pdgfrb
resolver
genesymbol_syn
Pdgfr
resolver
genesymbol_syn
Pdgfr1
resolver
uniprot
Q8R406
resolver
uniprot
Q925F7
resolver
uniprot_entry
PGFRB_RAT
resolver
uniprot_sec
Q8R406
resolver
uniprot_sec
Q925F7
resolver
activity_regulation
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}.
uniprot
proteins
amino_acid_sequence
MGLPEVMPASVLRGQLLLFVLLLLGPQISQGLVITPPGPEFVLNISSTFVLTCSSSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFIGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINVTVIENGYVRLLETLEDVQIAELHRSRTLQVVFEAYPTPSVLWFKDNRTLGDSSAGELVLSTRNVSETRYVSELTLVRVKVSEAGYYTMRAFHADDQVQLSFKLQVNVPVRVLELSESHPANGEQILRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGRDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQRKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSTELYSNALPVGLSLPSHLNLTGESDGGYMDMSKDESVDYVPMLDMKGHIKYADIESSSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGLHSLRSPLDTSSVLYTAVQPNETDNDYIIPLPDPKPDAADEGLLEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQAEPEAQLEQPQDSGCPGPLAEAEDSFL
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a 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}.
uniprot
proteins
mass_dalton
122828
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
CSF-1/PDGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
11346654
uniprot
proteins
pubmed
8318539
uniprot
proteins
sequence_length
1097
uniprot
proteins
subcellular_location
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}.
uniprot
proteins
transmembrane_region
TRANSMEM 532..552; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins