Skip Header

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

Platelet-derived growth factor receptor beta

Gene

Pdgfrb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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 (By similarity). 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 similarity9 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Activity 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei633ATPPROSITE-ProRule annotation1
Active sitei825Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi605 – 613ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processChemotaxis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1 3474

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97531 Pdgfrb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 531ExtracellularSequence analysisAdd BLAST500
Transmembranei532 – 552HelicalSequence analysisAdd BLAST21
Topological domaini553 – 1098CytoplasmicSequence analysisAdd BLAST546

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

Pathology & Biotechi

Disruption phenotypei

No apparent phenotype up to 16 dpc. Lethality late during gestation or at birth, due to widespread bleedings. This is due to a severe shortage of vascular smooth muscle cells and pericytes, especially in the central nervous system, skin, lung and heart. Mutants suffer from hemorrhages, anemia, thrombocytopenia, and show defects in the formation of kidney glomeruli, due to a lack of mesangial cells.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi578Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-715; F-739; F-750; F-770; F-1008 and F-1020. 1 Publication1
Mutagenesisi715Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-739; F-750; F-770; F-1008 and F-1020. 1 Publication1
Mutagenesisi739Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-750; F-770; F-1008 and F-1020. 1 Publication1
Mutagenesisi750Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-770; F-1008 and F-1020. 1 Publication1
Mutagenesisi770Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-1008 and F-1020. 1 Publication1
Mutagenesisi849D → N: Increased autophosphorylation in the absence of PDGFB binding. Increased autophosphorylation in response to PDGFB binding. Constitutive interaction with PIK3R1, and constitutive AKT1 activation. 1 Publication1
Mutagenesisi1008Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-770 and F-1020. 1 Publication1
Mutagenesisi1020Y → F: Strongly reduced levels of vascular smooth muscle cells and pericytes in developing blood vessels; when associated with F-578; F-715; F-739; F-750; F-770 and F-1008. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2749
GuidetoPHARMACOLOGYi1804

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000001675832 – 1098Platelet-derived growth factor receptor betaAdd BLAST1067

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi44N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi53 ↔ 99PROSITE-ProRule annotation
Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi102N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi148 ↔ 189PROSITE-ProRule annotation
Glycosylationi214N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi234 ↔ 290PROSITE-ProRule annotation
Glycosylationi291N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi306N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi353N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi370N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 507PROSITE-ProRule annotation
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi467N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi478N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei561Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei578Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei580Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei685Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei715Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei739Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei750Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei762Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei770Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei774Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei777Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei856Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei933Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei969Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei1008Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1020Phosphotyrosine; by autocatalysisBy similarity1

Post-translational modificationi

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 (By similarity). Dephosphorylated by PTPN2 at Tyr-578 and Tyr-1020.By similarity
N-glycosylated.By similarity
Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05622
PaxDbiP05622
PRIDEiP05622

PTM databases

iPTMnetiP05622
PhosphoSitePlusiP05622

Expressioni

Tissue specificityi

Weakly expressed in glomerular mesangial cells and interstitial cells. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, increased expression in interstitial cells at day 4 and expression is markedly elevated at day 7 and is maximal at day 14.1 Publication

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

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202089, 7 interactors
ComplexPortaliCPX-2903 PDGF receptor alpha-beta - PDGF-AB complex
CPX-2904 PDGF receptor beta - PDGF-AB complex
CPX-2907 PDGF receptor alpha-beta - PDGF-BB complex
CPX-2908 PDGF receptor beta - PDGF-BB complex
CPX-2913 PDGF receptor alpha-beta - PDGF-CC complex
CPX-2914 PDGF receptor beta - PDGF-CC complex
CPX-2916 PDGF receptor alpha-beta - PDGF-DD complex
CPX-2917 PDGF receptor beta - PDGF-DD complex
CORUMiP05622
DIPiDIP-39669N
IntActiP05622, 15 interactors
MINTiP05622
STRINGi10090.ENSMUSP00000025522

Chemistry databases

BindingDBiP05622

Structurei

3D structure databases

ProteinModelPortaliP05622
SMRiP05622
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05622

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 119Ig-like C2-type 1Add BLAST87
Domaini128 – 209Ig-like C2-type 2Add BLAST82
Domaini213 – 308Ig-like C2-type 3Add BLAST96
Domaini330 – 402Ig-like C2-type 4Add BLAST73
Domaini415 – 523Ig-like C2-type 5Add BLAST109
Domaini599 – 961Protein kinasePROSITE-ProRule annotationAdd BLAST363

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
HOVERGENiHBG004335
InParanoidiP05622
KOiK05089
PhylomeDBiP05622

Family and domain databases

Gene3Di2.60.40.10, 5 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
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
IPR001824 Tyr_kinase_rcpt_3_CS
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF500948 Beta-PDGF_receptor, 1 hit
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 4 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P05622-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLPGVIPAL VLRGQLLLSV LWLLGPQTSR GLVITPPGPE FVLNISSTFV
60 70 80 90 100
LTCSGSAPVM WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV
110 120 130 140 150
YNNSLGPELS ERKRIYIFVP DPTMGFLPMD SEDLFIFVTD VTETTIPCRV
160 170 180 190 200
TDPQLEVTLH EKKVDIPLHV PYDHQRGFTG TFEDKTYICK TTIGDREVDS
210 220 230 240 250
DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND VVNFQWTYPR
260 270 280 290 300
MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG
310 320 330 340 350
DEKAINISVI ENGYVRLLET LGDVEIAELH RSRTLRVVFE AYPMPSVLWL
360 370 380 390 400
KDNRTLGDSG AGELVLSTRN MSETRYVSEL ILVRVKVSEA GYYTMRAFHE
410 420 430 440 450
DDEVQLSFKL QVNVPVRVLE LSESHPANGE QTIRCRGRGM PQPNVTWSTC
460 470 480 490 500
RDLKRCPRKL SPTPLGNSSK EESQLETNVT FWEEDQEYEV VSTLRLRHVD
510 520 530 540 550
QPLSVRCMLQ NSMGGDSQEV TVVPHSLPFK VVVISAILAL VVLTVISLII
560 570 580 590 600
LIMLWQKKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV
610 620 630 640 650
LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE
660 670 680 690 700
LKIMSHLGPH LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL
710 720 730 740 750
QRHSNKHCPP SAELYSNALP VGFSLPSHLN LTGESDGGYM DMSKDESIDY
760 770 780 790 800
VPMLDMKGDI KYADIESPSY MAPYDNYVPS APERTYRATL INDSPVLSYT
810 820 830 840 850
DLVGFSYQVA NGMDFLASKN CVHRDLAARN VLICEGKLVK ICDFGLARDI
860 870 880 890 900
MRDSNYISKG STYLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG
910 920 930 940 950
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF
960 970 980 990 1000
SQLVLLLERL LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR FPGIHSLRSP
1010 1020 1030 1040 1050
LDTSSVLYTA VQPNESDNDY IIPLPDPKPD VADEGLPEGS PSLASSTLNE
1060 1070 1080 1090
VNTSSTISCD SPLELQEEPQ QAEPEAQLEQ PQDSGCPGPL AEAEDSFL
Length:1,098
Mass (Da):122,806
Last modified:November 1, 1988 - v1
Checksum:i8D391CAFAC3FC31D
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9QPE2E9QPE2_MOUSE
Platelet-derived growth factor rece...
Pdgfrb
1,099Annotation score:
E9QN12E9QN12_MOUSE
Platelet-derived growth factor rece...
Pdgfrb
1,103Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04367 mRNA Translation: CAA27882.1
PIRiA25742 PFMSRB
RefSeqiNP_001139740.1, NM_001146268.1
NP_032835.2, NM_008809.2
UniGeneiMm.4146

Genome annotation databases

GeneIDi18596
KEGGimmu:18596
UCSCiuc008fbk.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04367 mRNA Translation: CAA27882.1
PIRiA25742 PFMSRB
RefSeqiNP_001139740.1, NM_001146268.1
NP_032835.2, NM_008809.2
UniGeneiMm.4146

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYAX-ray2.05P/Q1005-1015[»]
1AYCX-ray2.30P736-744[»]
ProteinModelPortaliP05622
SMRiP05622
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202089, 7 interactors
ComplexPortaliCPX-2903 PDGF receptor alpha-beta - PDGF-AB complex
CPX-2904 PDGF receptor beta - PDGF-AB complex
CPX-2907 PDGF receptor alpha-beta - PDGF-BB complex
CPX-2908 PDGF receptor beta - PDGF-BB complex
CPX-2913 PDGF receptor alpha-beta - PDGF-CC complex
CPX-2914 PDGF receptor beta - PDGF-CC complex
CPX-2916 PDGF receptor alpha-beta - PDGF-DD complex
CPX-2917 PDGF receptor beta - PDGF-DD complex
CORUMiP05622
DIPiDIP-39669N
IntActiP05622, 15 interactors
MINTiP05622
STRINGi10090.ENSMUSP00000025522

Chemistry databases

BindingDBiP05622
ChEMBLiCHEMBL2749
GuidetoPHARMACOLOGYi1804

PTM databases

iPTMnetiP05622
PhosphoSitePlusiP05622

Proteomic databases

MaxQBiP05622
PaxDbiP05622
PRIDEiP05622

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18596
KEGGimmu:18596
UCSCiuc008fbk.2 mouse

Organism-specific databases

CTDi5159
MGIiMGI:97531 Pdgfrb

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
HOVERGENiHBG004335
InParanoidiP05622
KOiK05089
PhylomeDBiP05622

Enzyme and pathway databases

BRENDAi2.7.10.1 3474

Miscellaneous databases

EvolutionaryTraceiP05622
PROiPR:P05622
SOURCEiSearch...

Family and domain databases

Gene3Di2.60.40.10, 5 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
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
IPR001824 Tyr_kinase_rcpt_3_CS
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF500948 Beta-PDGF_receptor, 1 hit
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 4 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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
ProtoNetiSearch...

Entry informationi

Entry nameiPGFRB_MOUSE
AccessioniPrimary (citable) accession number: P05622
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 7, 2018
This is version 201 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again