SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q05030

- PGFRB_RAT

UniProt

Q05030 - PGFRB_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Platelet-derived growth factor receptor beta
Gene
Pdgfrb, Pdgfr, Pdgfr1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca2+ and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. 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.

Catalytic activityi

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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei633 – 6331ATP By similarity
Active sitei825 – 8251Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi605 – 6139ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphatidylinositol 3-kinase binding Source: RGD
  3. platelet-derived growth factor beta-receptor activity Source: UniProtKB
  4. platelet-derived growth factor-activated receptor activity Source: RGD
  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. in utero embryonic development Source: Ensembl
  10. inner ear development Source: RGD
  11. intracellular signal transduction Source: RGD
  12. metanephric S-shaped body morphogenesis Source: UniProtKB
  13. metanephric comma-shaped body morphogenesis Source: UniProtKB
  14. metanephric glomerular capillary formation Source: UniProtKB
  15. metanephric glomerular mesangial cell proliferation involved in metanephros development Source: UniProtKB
  16. metanephric glomerulus morphogenesis Source: UniProtKB
  17. metanephric mesenchymal cell migration Source: UniProtKB
  18. metanephric mesenchyme development Source: UniProtKB
  19. negative regulation of apoptotic process Source: RGD
  20. peptidyl-tyrosine phosphorylation Source: UniProtKB
  21. phosphatidylinositol metabolic process Source: UniProtKB
  22. phosphatidylinositol-mediated signaling Source: UniProtKB
  23. positive regulation of DNA biosynthetic process Source: UniProtKB
  24. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  25. positive regulation of MAP kinase activity Source: UniProtKB
  26. positive regulation of calcium ion import Source: UniProtKB
  27. positive regulation of cell migration Source: UniProtKB
  28. positive regulation of cell proliferation Source: RGD
  29. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: Ensembl
  30. positive regulation of chemotaxis Source: UniProtKB
  31. positive regulation of collagen biosynthetic process Source: RGD
  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
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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; 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 531500Extracellular Reviewed prediction
Add
BLAST
Transmembranei532 – 55221Helical; Reviewed prediction
Add
BLAST
Topological domaini553 – 1097545Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 10971066Platelet-derived growth factor receptor beta
PRO_0000016759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi53 ↔ 99 By similarity
Glycosylationi88 – 881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi102 – 1021N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi148 ↔ 189 By similarity
Glycosylationi214 – 2141N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi234 ↔ 290 By similarity
Glycosylationi291 – 2911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi306 – 3061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi353 – 3531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi370 – 3701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi435 ↔ 507 By similarity
Glycosylationi444 – 4441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi467 – 4671N-linked (GlcNAc...) Reviewed prediction
Glycosylationi478 – 4781N-linked (GlcNAc...) Reviewed prediction
Modified residuei561 – 5611Phosphotyrosine; by autocatalysis By similarity
Modified residuei578 – 5781Phosphotyrosine; by autocatalysis By similarity
Modified residuei580 – 5801Phosphotyrosine; by autocatalysis By similarity
Modified residuei588 – 5881Phosphotyrosine; by autocatalysis By similarity
Modified residuei685 – 6851Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residuei715 – 7151Phosphotyrosine; by autocatalysis By similarity
Modified residuei739 – 7391Phosphotyrosine; by autocatalysis By similarity
Modified residuei750 – 7501Phosphotyrosine; by autocatalysis By similarity
Modified residuei762 – 7621Phosphotyrosine; by autocatalysis By similarity
Modified residuei770 – 7701Phosphotyrosine; by autocatalysis By similarity
Modified residuei774 – 7741Phosphotyrosine; by autocatalysis By similarity
Modified residuei777 – 7771Phosphotyrosine; by autocatalysis By similarity
Modified residuei856 – 8561Phosphotyrosine; by autocatalysis By similarity
Modified residuei933 – 9331Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residuei969 – 9691Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residuei1008 – 10081Phosphotyrosine; by autocatalysis By similarity
Modified residuei1020 – 10201Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

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

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.

Protein-protein interaction databases

IntActiQ05030. 2 interactions.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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: September 3, 2014
This is version 139 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

Similar proteinsi