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Q05030 (PGFRB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet-derived growth factor receptor beta

Short name=PDGF-R-beta
Short name=PDGFR-beta
EC=2.7.10.1
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 names
Name:Pdgfrb
Synonyms:Pdgfr, Pdgfr1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1097 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 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 activity

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

Enzyme 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.

Subunit structure

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.

Subcellular location

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.

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 4 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell membrane
Cytoplasmic vesicle
Lysosome
Membrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadrenal gland development

Inferred from electronic annotation. Source: Ensembl

cardiac myofibril assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration involved in coronary angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration involved in vasculogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to platelet-derived growth factor stimulus

Inferred from direct assay PubMed 11903042Ref.2. Source: GOC

glycosaminoglycan biosynthetic process

Inferred from mutant phenotype PubMed 11903042. Source: RGD

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

inner ear development

Inferred from expression pattern PubMed 15267171. Source: RGD

intracellular signal transduction

Inferred from mutant phenotype PubMed 18298916. Source: RGD

metanephric S-shaped body morphogenesis

Inferred from expression pattern PubMed 10734101. Source: UniProtKB

metanephric comma-shaped body morphogenesis

Inferred from expression pattern PubMed 10734101. Source: UniProtKB

metanephric glomerular capillary formation

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric glomerular mesangial cell proliferation involved in metanephros development

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric glomerulus morphogenesis

Inferred from expression pattern PubMed 10734101. Source: UniProtKB

metanephric mesenchymal cell migration

Inferred from direct assay PubMed 10734101. Source: UniProtKB

metanephric mesenchyme development

Inferred from expression pattern PubMed 10734101. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 15978205. Source: RGD

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of calcium ion import

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15267171. Source: RGD

positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of collagen biosynthetic process

Inferred from mutant phenotype PubMed 15978205. Source: RGD

positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from expression pattern PubMed 15039427. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 12604637. Source: RGD

response to fluid shear stress

Inferred from expression pattern PubMed 12738619. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 12226102. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 15722379. Source: RGD

response to lipid

Inferred from expression pattern PubMed 15044318. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 16041643. Source: RGD

response to retinoic acid

Inferred from expression pattern PubMed 17303670. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 17654254. Source: RGD

retina vasculature development in camera-type eye

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

smooth muscle tissue development

Inferred from electronic annotation. Source: Ensembl

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from expression pattern PubMed 12533868. Source: RGD

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 10550325. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 10802145PubMed 11788434. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

lysosomal lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11788434. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 10802145PubMed 11788434. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol 3-kinase binding

Inferred from physical interaction PubMed 18421086. Source: RGD

platelet-derived growth factor beta-receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

platelet-derived growth factor-activated receptor activity

Inferred from direct assay PubMed 11903042Ref.2. Source: RGD

protein binding

Inferred from physical interaction PubMed 16530387. Source: UniProtKB

protein kinase activity

Traceable author statement PubMed 11557582. Source: RGD

protein tyrosine kinase activity

Inferred from direct assay PubMed 16530387. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 10971066Platelet-derived growth factor receptor beta
PRO_0000016759

Regions

Topological domain32 – 531500Extracellular Potential
Transmembrane532 – 55221Helical; Potential
Topological domain553 – 1097545Cytoplasmic Potential
Domain32 – 11988Ig-like C2-type 1
Domain128 – 20982Ig-like C2-type 2
Domain213 – 30896Ig-like C2-type 3
Domain415 – 523109Ig-like C2-type 4
Domain599 – 961363Protein kinase
Nucleotide binding605 – 6139ATP By similarity

Sites

Active site8251Proton acceptor By similarity
Binding site6331ATP By similarity

Amino acid modifications

Modified residue5611Phosphotyrosine; by autocatalysis By similarity
Modified residue5781Phosphotyrosine; by autocatalysis By similarity
Modified residue5801Phosphotyrosine; by autocatalysis By similarity
Modified residue5881Phosphotyrosine; by autocatalysis By similarity
Modified residue6851Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residue7151Phosphotyrosine; by autocatalysis By similarity
Modified residue7391Phosphotyrosine; by autocatalysis By similarity
Modified residue7501Phosphotyrosine; by autocatalysis By similarity
Modified residue7621Phosphotyrosine; by autocatalysis By similarity
Modified residue7701Phosphotyrosine; by autocatalysis By similarity
Modified residue7741Phosphotyrosine; by autocatalysis By similarity
Modified residue7771Phosphotyrosine; by autocatalysis By similarity
Modified residue8561Phosphotyrosine; by autocatalysis By similarity
Modified residue9331Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residue9691Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residue10081Phosphotyrosine; by autocatalysis By similarity
Modified residue10201Phosphotyrosine; by autocatalysis By similarity
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation3061N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation4671N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 99 By similarity
Disulfide bond148 ↔ 189 By similarity
Disulfide bond234 ↔ 290 By similarity
Disulfide bond435 ↔ 507 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05030 [UniParc].

Last modified July 25, 2003. Version 2.
Checksum: 5E6540FA0C5CF22B

FASTA1,097122,828
        10         20         30         40         50         60 
MGLPEVMPAS VLRGQLLLFV LLLLGPQISQ GLVITPPGPE FVLNISSTFV LTCSSSAPVM 

        70         80         90        100        110        120 
WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV YNNSLGPELS ERKRIYIFVP 

       130        140        150        160        170        180 
DPTMGFLPMD SEDLFIFVTD VTETTIPCRV TDPQLEVTLH EKKVDIPLHV PYDHQRGFIG 

       190        200        210        220        230        240 
TFEDKTYICK TTIGDREVDS DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND 

       250        260        270        280        290        300 
VVNFQWTYPR MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG 

       310        320        330        340        350        360 
DEKAINVTVI ENGYVRLLET LEDVQIAELH RSRTLQVVFE AYPTPSVLWF KDNRTLGDSS 

       370        380        390        400        410        420 
AGELVLSTRN VSETRYVSEL TLVRVKVSEA GYYTMRAFHA DDQVQLSFKL QVNVPVRVLE 

       430        440        450        460        470        480 
LSESHPANGE QILRCRGRGM PQPNVTWSTC RDLKRCPRKL SPTPLGNSSK EESQLETNVT 

       490        500        510        520        530        540 
FWEEDQEYEV VSTLRLRHVD QPLSVRCMLQ NSMGRDSQEV TVVPHSLPFK VVVISAILAL 

       550        560        570        580        590        600 
VVLTVISLII LIMLWQRKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV 

       610        620        630        640        650        660 
LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH 

       670        680        690        700        710        720 
LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QRHSNKHCPP STELYSNALP 

       730        740        750        760        770        780 
VGLSLPSHLN LTGESDGGYM DMSKDESVDY VPMLDMKGHI KYADIESSSY MAPYDNYVPS 

       790        800        810        820        830        840 
APERTYRATL INDSPVLSYT DLVGFSYQVA NGMEFLASKN CVHRDLAARN VLICEGKLVK 

       850        860        870        880        890        900 
ICDFGLARDI MRDSNYISKG STFLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG 

       910        920        930        940        950        960 
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL 

       970        980        990       1000       1010       1020 
LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR LPGLHSLRSP LDTSSVLYTA VQPNETDNDY 

      1030       1040       1050       1060       1070       1080 
IIPLPDPKPD AADEGLLEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ AEPEAQLEQP 

      1090 
QDSGCPGPLA EAEDSFL 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY090783 mRNA. Translation: AAM09098.1.
Z14119 mRNA. Translation: CAA78489.1.
AF359356 mRNA. Translation: AAK43716.1.
PIRS33766.
RefSeqNP_113713.1. NM_031525.1.
XP_006254851.1. XM_006254789.1.
UniGeneRn.98311.

3D structure databases

ProteinModelPortalQ05030.
SMRQ05030. Positions 558-706, 794-959.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ05030. 2 interactions.

Chemistry

BindingDBQ05030.
ChEMBLCHEMBL4125.

PTM databases

PhosphoSiteQ05030.

Proteomic databases

PaxDbQ05030.
PRIDEQ05030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000068535; ENSRNOP00000060534; ENSRNOG00000018461.
GeneID24629.
KEGGrno:24629.
UCSCRGD:3285. rat.

Organism-specific databases

CTD5159.
RGD3285. Pdgfrb.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108490.
HOGENOMHOG000112009.
HOVERGENHBG004335.
InParanoidQ05030.
KOK05089.
OMAAPYDNYV.
OrthoDBEOG7GXP9Q.
PhylomeDBQ05030.

Gene expression databases

GenevestigatorQ05030.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR007110. 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]
PANTHERPTHR24416:SF53. PTHR24416:SF53. 1 hit.
PfamPF07679. I-set. 1 hit.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500948. Beta-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. 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]
ProtoNetSearch...

Other

NextBio603908.
PROQ05030.

Entry information

Entry namePGFRB_RAT
AccessionPrimary (citable) accession number: Q05030
Secondary accession number(s): Q8R406, Q925F7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 25, 2003
Last modified: June 11, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families