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Q05030

- PGFRB_RAT

UniProt

Q05030 - PGFRB_RAT

Protein

Platelet-derived growth factor receptor beta

Gene

Pdgfrb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (25 Jul 2003)
      Previous versions | rss
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    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. 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.By similarity

    Catalytic activityi

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

    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 By similarity.By similarity

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylinositol 3-kinase binding Source: RGD
    3. platelet-derived growth factor-activated receptor activity Source: RGD
    4. platelet-derived growth factor beta-receptor activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: RGD
    7. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. adrenal gland development Source: Ensembl
    2. cardiac myofibril assembly Source: UniProtKB
    3. cell chemotaxis Source: UniProtKB
    4. cell migration Source: UniProtKB
    5. cell migration involved in coronary angiogenesis Source: UniProtKB
    6. cell migration involved in vasculogenesis Source: UniProtKB
    7. cellular response to platelet-derived growth factor stimulus Source: GOC
    8. glycosaminoglycan biosynthetic process Source: RGD
    9. inner ear development Source: RGD
    10. intracellular signal transduction Source: RGD
    11. in utero embryonic development Source: Ensembl
    12. metanephric comma-shaped body morphogenesis Source: UniProtKB
    13. metanephric glomerular capillary formation Source: UniProtKB
    14. metanephric glomerular mesangial cell proliferation involved in metanephros development Source: UniProtKB
    15. metanephric glomerulus morphogenesis Source: UniProtKB
    16. metanephric mesenchymal cell migration Source: UniProtKB
    17. metanephric mesenchyme development Source: UniProtKB
    18. metanephric S-shaped body morphogenesis Source: UniProtKB
    19. negative regulation of apoptotic process Source: RGD
    20. peptidyl-tyrosine phosphorylation Source: UniProtKB
    21. phosphatidylinositol-mediated signaling Source: UniProtKB
    22. phosphatidylinositol metabolic process Source: UniProtKB
    23. positive regulation of calcium ion import Source: UniProtKB
    24. positive regulation of cell migration Source: UniProtKB
    25. positive regulation of cell proliferation Source: RGD
    26. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: Ensembl
    27. positive regulation of chemotaxis Source: UniProtKB
    28. positive regulation of collagen biosynthetic process Source: RGD
    29. positive regulation of DNA biosynthetic process Source: UniProtKB
    30. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    31. positive regulation of MAP kinase activity Source: UniProtKB
    32. positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
    33. positive regulation of mitosis Source: UniProtKB
    34. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    35. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    36. positive regulation of phospholipase C activity Source: UniProtKB
    37. positive regulation of phosphoprotein phosphatase activity Source: Ensembl
    38. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    39. positive regulation of smooth muscle cell migration Source: UniProtKB
    40. positive regulation of smooth muscle cell proliferation Source: UniProtKB
    41. protein autophosphorylation Source: UniProtKB
    42. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    43. response to estradiol Source: RGD
    44. response to estrogen Source: RGD
    45. response to fluid shear stress Source: RGD
    46. response to hydrogen peroxide Source: RGD
    47. response to hyperoxia Source: RGD
    48. response to lipid Source: RGD
    49. response to organic cyclic compound Source: RGD
    50. response to retinoic acid Source: RGD
    51. response to toxic substance Source: RGD
    52. retina vasculature development in camera-type eye Source: UniProtKB
    53. skeletal system morphogenesis Source: Ensembl
    54. smooth muscle tissue development Source: Ensembl
    55. tissue homeostasis Source: Ensembl
    56. wound healing Source: RGD

    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

    ReactomeiREACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_206819. Downstream signal transduction.
    REACT_212371. Signaling by PDGF.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 18

    Organism-specific databases

    RGDi3285. Pdgfrb.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cytoplasmic vesicle By similarity. Lysosome lumen By similarity
    Note: After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. intrinsic component of plasma membrane Source: Ensembl
    6. lysosomal lumen Source: UniProtKB-SubCell
    7. membrane Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 10971066Platelet-derived growth factor receptor betaPRO_0000016759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi53 ↔ 99PROSITE-ProRule annotation
    Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi148 ↔ 189PROSITE-ProRule annotation
    Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi234 ↔ 290PROSITE-ProRule annotation
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi435 ↔ 507PROSITE-ProRule annotation
    Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi467 – 4671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis
    Modified residuei561 – 5611Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei578 – 5781Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei580 – 5801Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei588 – 5881Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei685 – 6851Phosphotyrosine; by ABL1 and ABL2By similarity
    Modified residuei715 – 7151Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei739 – 7391Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei750 – 7501Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei762 – 7621Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei770 – 7701Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei774 – 7741Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei777 – 7771Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei856 – 8561Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei933 – 9331Phosphotyrosine; by ABL1 and ABL2By similarity
    Modified residuei969 – 9691Phosphotyrosine; by ABL1 and ABL2By similarity
    Modified residuei1008 – 10081Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1020 – 10201Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    N-glycosylated.By similarity
    Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation By similarity.By similarity
    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.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ05030.
    PRIDEiQ05030.

    PTM databases

    PhosphoSiteiQ05030.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05030.

    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

    Protein-protein interaction databases

    IntActiQ05030. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05030.
    SMRiQ05030. Positions 558-706, 794-959.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 531500ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini553 – 1097545CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei532 – 55221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 11988Ig-like C2-type 1Add
    BLAST
    Domaini128 – 20982Ig-like C2-type 2Add
    BLAST
    Domaini213 – 30896Ig-like C2-type 3Add
    BLAST
    Domaini415 – 523109Ig-like C2-type 4Add
    BLAST
    Domaini599 – 961363Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108490.
    HOGENOMiHOG000112009.
    HOVERGENiHBG004335.
    InParanoidiQ05030.
    KOiK05089.
    OMAiAPYDNYV.
    OrthoDBiEOG7GXP9Q.
    PhylomeDBiQ05030.

    Family and domain databases

    Gene3Di2.60.40.10. 5 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    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. 1 hit.
    PfamiPF07679. I-set. 1 hit.
    PF00047. ig. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500948. Beta-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTiSM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. 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.

    Q05030-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLPEVMPAS VLRGQLLLFV LLLLGPQISQ GLVITPPGPE FVLNISSTFV     50
    LTCSSSAPVM WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV 100
    YNNSLGPELS ERKRIYIFVP DPTMGFLPMD SEDLFIFVTD VTETTIPCRV 150
    TDPQLEVTLH EKKVDIPLHV PYDHQRGFIG TFEDKTYICK TTIGDREVDS 200
    DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND VVNFQWTYPR 250
    MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG 300
    DEKAINVTVI ENGYVRLLET LEDVQIAELH RSRTLQVVFE AYPTPSVLWF 350
    KDNRTLGDSS AGELVLSTRN VSETRYVSEL TLVRVKVSEA GYYTMRAFHA 400
    DDQVQLSFKL QVNVPVRVLE LSESHPANGE QILRCRGRGM PQPNVTWSTC 450
    RDLKRCPRKL SPTPLGNSSK EESQLETNVT FWEEDQEYEV VSTLRLRHVD 500
    QPLSVRCMLQ NSMGRDSQEV TVVPHSLPFK VVVISAILAL VVLTVISLII 550
    LIMLWQRKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV 600
    LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE 650
    LKIMSHLGPH LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL 700
    QRHSNKHCPP STELYSNALP VGLSLPSHLN LTGESDGGYM DMSKDESVDY 750
    VPMLDMKGHI KYADIESSSY MAPYDNYVPS APERTYRATL INDSPVLSYT 800
    DLVGFSYQVA NGMEFLASKN CVHRDLAARN VLICEGKLVK ICDFGLARDI 850
    MRDSNYISKG STFLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG 900
    TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF 950
    SQLVLLLERL LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR LPGLHSLRSP 1000
    LDTSSVLYTA VQPNETDNDY IIPLPDPKPD AADEGLLEGS PSLASSTLNE 1050
    VNTSSTISCD SPLELQEEPQ AEPEAQLEQP QDSGCPGPLA EAEDSFL 1097
    Length:1,097
    Mass (Da):122,828
    Last modified:July 25, 2003 - v2
    Checksum:i5E6540FA0C5CF22B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090783 mRNA. Translation: AAM09098.1.
    Z14119 mRNA. Translation: CAA78489.1.
    AF359356 mRNA. Translation: AAK43716.1.
    PIRiS33766.
    RefSeqiNP_113713.1. NM_031525.1.
    XP_006254851.1. XM_006254789.1.
    UniGeneiRn.98311.

    Genome annotation databases

    EnsembliENSRNOT00000068535; ENSRNOP00000060534; ENSRNOG00000018461.
    GeneIDi24629.
    KEGGirno:24629.
    UCSCiRGD:3285. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090783 mRNA. Translation: AAM09098.1 .
    Z14119 mRNA. Translation: CAA78489.1 .
    AF359356 mRNA. Translation: AAK43716.1 .
    PIRi S33766.
    RefSeqi NP_113713.1. NM_031525.1.
    XP_006254851.1. XM_006254789.1.
    UniGenei Rn.98311.

    3D structure databases

    ProteinModelPortali Q05030.
    SMRi Q05030. Positions 558-706, 794-959.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q05030. 2 interactions.

    Chemistry

    BindingDBi Q05030.
    ChEMBLi CHEMBL4125.

    PTM databases

    PhosphoSitei Q05030.

    Proteomic databases

    PaxDbi Q05030.
    PRIDEi Q05030.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000068535 ; ENSRNOP00000060534 ; ENSRNOG00000018461 .
    GeneIDi 24629.
    KEGGi rno:24629.
    UCSCi RGD:3285. rat.

    Organism-specific databases

    CTDi 5159.
    RGDi 3285. Pdgfrb.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108490.
    HOGENOMi HOG000112009.
    HOVERGENi HBG004335.
    InParanoidi Q05030.
    KOi K05089.
    OMAi APYDNYV.
    OrthoDBi EOG7GXP9Q.
    PhylomeDBi Q05030.

    Enzyme and pathway databases

    Reactomei REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_206819. Downstream signal transduction.
    REACT_212371. Signaling by PDGF.

    Miscellaneous databases

    NextBioi 603908.
    PROi Q05030.

    Gene expression databases

    Genevestigatori Q05030.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    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 ]
    PANTHERi PTHR24416:SF53. PTHR24416:SF53. 1 hit.
    Pfami PF07679. I-set. 1 hit.
    PF00047. ig. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500948. Beta-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTi SM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50835. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. Wang Y., Culty M.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
    2. "Conservation in sequence and affinity of human and rodent PDGF ligands and receptors."
      Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.
      Biochim. Biophys. Acta 1173:294-302(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-533.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    3. "Regulation of cell growth by redox-mediated extracellular proteolysis of platelet-derived growth factor receptor beta."
      Okuyama H., Shimahara Y., Kawada N., Seki S., Kristensen D.B., Yoshizato K., Uyama N., Yamaoka Y.
      J. Biol. Chem. 276:28274-28280(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 528-1090.
      Strain: Wistar.

    Entry informationi

    Entry nameiPGFRB_RAT
    AccessioniPrimary (citable) accession number: Q05030
    Secondary accession number(s): Q8R406, Q925F7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 25, 2003
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3