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Protein

Platelet-derived growth factor receptor beta

Gene

Pdgfrb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei633ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei825Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi605 – 613ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 3474

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Pdgfrb
Synonyms:Pdgfr, Pdgfr1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:97531 Pdgfrb

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini32 – 531ExtracellularSequence analysisAdd BLAST500
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei532 – 552HelicalSequence analysisAdd BLAST21
Topological domaini553 – 1098CytoplasmicSequence analysisAdd BLAST546

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2749

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1804

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 31Add BLAST31
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001675832 – 1098Platelet-derived growth factor receptor betaAdd BLAST1067

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi44N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P05622

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P05622

PRoteomics IDEntifications database

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PRIDEi
P05622

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P05622

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P05622

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
202089, 7 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-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

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P05622

Database of interacting proteins

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DIPi
DIP-39669N

Protein interaction database and analysis system

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IntActi
P05622, 15 interactors

Molecular INTeraction database

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MINTi
P05622

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000025522

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P05622

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P05622

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P05622

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P05622

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004335

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P05622

KEGG Orthology (KO)

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KOi
K05089

Database for complete collections of gene phylogenies

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PhylomeDBi
P05622

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 5 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

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Pfami
View protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF500948 Beta-PDGF_receptor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48726 SSF48726, 4 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8D391CAFAC3FC31D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9QN12E9QN12_MOUSE
Platelet-derived growth factor rece...
Pdgfrb
1,103Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X04367 mRNA Translation: CAA27882.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A25742 PFMSRB

NCBI Reference Sequences

More...
RefSeqi
NP_001139740.1, NM_001146268.1
NP_032835.2, NM_008809.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.4146

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
18596

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:18596

UCSC genome browser

More...
UCSCi
uc008fbk.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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

Comparative Toxicogenomics Database

More...
CTDi
5159
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

Protein Ontology

More...
PROi
PR:P05622

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPGFRB_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P05622
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: December 5, 2018
This is version 202 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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