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Entry version 193 (08 May 2019)
Sequence version 3 (26 Feb 2008)
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Protein

Platelet-derived growth factor receptor alpha

Gene

Pdgfra

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 a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -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 PIK3R1, PLCG1, and PTPN11. 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. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. 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.4 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 PDGFA and/or PDGFB leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib, nilotinib and sorafenib (By similarity).By similarity

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 sitei627ATPPROSITE-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 sitei818Proton 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 bindingi599 – 607ATPPROSITE-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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-186763 Downstream signal transduction
R-MMU-186797 Signaling by PDGF
R-MMU-5673001 RAF/MAP kinase cascade
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling

<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 alpha (EC:2.7.10.1)
Short name:
PDGF-R-alpha
Short name:
PDGFR-alpha
Alternative name(s):
Alpha platelet-derived growth factor receptor
Alpha-type platelet-derived growth factor receptor
CD140 antigen-like family member A
Platelet-derived growth factor alpha receptor
CD_antigen: CD140a
<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:Pdgfra
<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: Chromosome 5

Organism-specific databases

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

More...
MGIi
MGI:97530 Pdgfra

<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 & Seán O’Donoghue; 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 domaini25 – 528ExtracellularSequence analysisAdd BLAST504
<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>Transmembranei529 – 549HelicalSequence analysisAdd BLAST21
Topological domaini550 – 1089CytoplasmicSequence analysisAdd BLAST540

Keywords - Cellular componenti

Cell membrane, Cell projection, Golgi apparatus, 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

Embryonically lethal. Most embryos survive up to 13 dpc, but display important defects in skeleton development, including spina bifida, fusions of cervical vertebrae and ribs, and incomplete fusion of the skull parietal bone. Embryos display also abnormal mucosa lining the gastrointestinal tract, including fewer and misshapen villi and loss of pericryptal mesenchyme. At about 16 dpc, embryos display extensive hemorrhaging.3 Publications

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2096980

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1803

<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 – 24Sequence analysisAdd BLAST24
<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_000001676125 – 1089Platelet-derived growth factor receptor alphaAdd BLAST1065

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>Glycosylationi42N-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 bondi49 ↔ 100PROSITE-ProRule annotation
Glycosylationi76N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi89N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi103N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi150 ↔ 189PROSITE-ProRule annotation
Glycosylationi179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi235 ↔ 290PROSITE-ProRule annotation
Glycosylationi353N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi359N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 501PROSITE-ProRule annotation
Glycosylationi458N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi506N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei572Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei574Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei720Phosphotyrosine; by autocatalysisBy similarityCurated1
Modified residuei731Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei742Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei754Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei762Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei768Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei849Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei988Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1018Phosphotyrosine; 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

Ubiquitinated, leading to its internalization and degradation.1 Publication
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-731 and Tyr-742 is important for interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for interaction with PTPN11. Phosphorylation at Tyr-762 is important for interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction with PLCG1 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P26618

MaxQB - The MaxQuant DataBase

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MaxQBi
P26618

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

More...
PaxDbi
P26618

PeptideAtlas

More...
PeptideAtlasi
P26618

PRoteomics IDEntifications database

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PRIDEi
P26618

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P26618

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

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PhosphoSitePlusi
P26618

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P26618

<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

Focally expressed in cortical interstitial cells and highly expressed in the interstitium of the papillary region. Also expressed by adventitial cells in arterial vessels. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, expression in cortical interstitial cells becomes prominent at day 4 which increases progressively until day 14.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by growth arrest.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000029231 Expressed in 384 organ(s), highest expression level in epididymis

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P26618 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P26618 MM

<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 PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB (via SH2 domain). Interacts (tyrosine phosphorylated) with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
202088, 4 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-2899 PDGF receptor alpha - PDGF-AA complex
CPX-2901 PDGF receptor alpha - PDGF-AB complex
CPX-2903 PDGF receptor alpha-beta - PDGF-AB complex
CPX-2906 PDGF receptor alpha - PDGF-BB complex
CPX-2907 PDGF receptor alpha-beta - PDGF-BB complex
CPX-2912 PDGF receptor alpha - PDGF-CC complex
CPX-2913 PDGF receptor alpha-beta - PDGF-CC complex
CPX-2916 PDGF receptor alpha-beta - PDGF-DD complex

Protein interaction database and analysis system

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IntActi
P26618, 3 interactors

Molecular INTeraction database

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MINTi
P26618

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000127173

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P26618

<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

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

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SMRi
P26618

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...

<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>Domaini25 – 113Ig-like C2-type 1Add BLAST89
Domaini117 – 201Ig-like C2-type 2Add BLAST85
Domaini202 – 306Ig-like C2-type 3Add BLAST105
Domaini319 – 410Ig-like C2-type 4Add BLAST92
Domaini414 – 517Ig-like C2-type 5Add BLAST104
Domaini593 – 954Protein kinasePROSITE-ProRule annotationAdd BLAST362

<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

Ensembl GeneTree

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GeneTreei
ENSGT00940000156021

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000112009

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P26618

KEGG Orthology (KO)

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KOi
K04363

Identification of Orthologs from Complete Genome Data

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OMAi
CKDIKKC

Database of Orthologous Groups

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OrthoDBi
236292at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P26618

TreeFam database of animal gene trees

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TreeFami
TF325768

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
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR027290 PDGFRA
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
PF07679 I-set, 2 hits
PF07714 Pkinase_Tyr, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF500950 Alpha-PDGF_receptor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00409 IG, 4 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

More...
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>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P26618-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGTSHQVFLV LSCLLTGPGL ISCQLLLPSI LPNENEKIVQ LNSSFSLRCV
60 70 80 90 100
GESEVSWQHP MSEEDDPNVE IRSEENNSGL FVTVLEVVNA SAAHTGWYTC
110 120 130 140 150
YYNHTQTDES EIEGRHIYIY VPDPDMAFVP LGMTDSLVIV EEDDSAIIPC
160 170 180 190 200
RTTDPETQVT LHNNGRLVPA SYDSRQGFNG TFSVGPYICE ATVKGRTFKT
210 220 230 240 250
SEFNVYALKA TSELNLEMDA RQTVYKAGET IVVTCAVFNN EVVDLQWTYP
260 270 280 290 300
GEVRNKGITM LEEIKLPSIK LVYTLTVPKA TVKDSGEYEC AARQATKEVK
310 320 330 340 350
EMKRVTISVH EKGFVEIEPT FGQLEAVNLH EVREFVVEVQ AYPTPRISWL
360 370 380 390 400
KDNLTLIENL TEITTDVQKS QETRYQSKLK LIRAKEEDSG HYTIIVQNED
410 420 430 440 450
DVKSYTFELS TLVPASILDL VDDHHGSGGG QTVRCTAEGT PLPEIDWMIC
460 470 480 490 500
KHIKKCNNDT SWTVLASNVS NIITELPRRG RSTVEGRVSF AKVEETIAVR
510 520 530 540 550
CLAKNNLSVV ARELKLVAPT LRSELTVAAA VLVLLVIVIV SLIVLVVIWK
560 570 580 590 600
QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG
610 620 630 640 650
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH
660 670 680 690 700
LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFMSQHPEK
710 720 730 740 750
PKKDLDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE
760 770 780 790 800
VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDDSEGL TLLDLLSFTY
810 820 830 840 850
QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV
860 870 880 890 900
SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
910 920 930 940 950
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV QCWNSEPEKR PSFYHLSEIV
960 970 980 990 1000
ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL
1010 1020 1030 1040 1050
KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI
1060 1070 1080
ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL
Length:1,089
Mass (Da):122,683
Last modified:February 26, 2008 - v3
<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:i07AAFD2BAA12533A
GO
Isoform 2 (identifier: P26618-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     775-790: DSEVKNLLSDDDSEGL → GKSAHAHSGKYDLSVV
     791-1089: Missing.

Note: No experimental confirmation available.
Show »
Length:790
Mass (Da):88,629
Checksum:iFE13756876B68B95
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0J9YV87A0A0J9YV87_MOUSE
Platelet-derived growth factor rece...
Pdgfra
481Annotation score:

Annotation score:1 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>
A0A0J9YUD9A0A0J9YUD9_MOUSE
Platelet-derived growth factor rece...
Pdgfra
139Annotation score:

Annotation score:1 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>
A0A0J9YVF3A0A0J9YVF3_MOUSE
Platelet-derived growth factor rece...
Pdgfra
243Annotation score:

Annotation score:1 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>
A0A0J9YV49A0A0J9YV49_MOUSE
Platelet-derived growth factor rece...
Pdgfra
88Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti65D → E in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti65D → E in AAA39904 (PubMed:1321404).Curated1
Sequence conflicti192T → A in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti202E → A in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti252E → G in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti271L → V in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti322G → S in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti326A → P in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti439 – 440GT → EG in AAA39733 (PubMed:2174116).Curated2
Sequence conflicti472I → V in BAE37548 (PubMed:16141072).Curated1
Sequence conflicti529A → E in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti737A → D in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti849Y → D in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti936E → D in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti950V → L in AAA39733 (PubMed:2174116).Curated1
Sequence conflicti1005G → S in AAA39904 (PubMed:1321404).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_031877775 – 790DSEVK…DSEGL → GKSAHAHSGKYDLSVV in isoform 2. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_031878791 – 1089Missing in isoform 2. 1 PublicationAdd BLAST299

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
M57683 mRNA Translation: AAA39733.1
M84607 mRNA Translation: AAA39904.1
AK081664 mRNA Translation: BAC38283.1
AK136490 mRNA Translation: BAE23004.1
AK147267 mRNA Translation: BAE27808.1
AK163952 mRNA Translation: BAE37548.1
BC053036 mRNA Translation: AAH53036.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS19351.1 [P26618-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
I57511 S33727

NCBI Reference Sequences

More...
RefSeqi
NP_001076785.1, NM_001083316.2 [P26618-1]
NP_001334647.1, NM_001347718.1 [P26618-2]
NP_001334648.1, NM_001347719.1 [P26618-2]
NP_035188.2, NM_011058.3 [P26618-1]
XP_006504324.1, XM_006504261.3 [P26618-1]
XP_006504325.1, XM_006504262.3 [P26618-1]
XP_006504326.1, XM_006504263.3 [P26618-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231 [P26618-1]
ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231 [P26618-1]
ENSMUST00000201711; ENSMUSP00000143891; ENSMUSG00000029231 [P26618-2]
ENSMUST00000202681; ENSMUSP00000143906; ENSMUSG00000029231 [P26618-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
18595

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:18595

UCSC genome browser

More...
UCSCi
uc008xub.1 mouse [P26618-2]
uc008xuc.1 mouse [P26618-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
M57683 mRNA Translation: AAA39733.1
M84607 mRNA Translation: AAA39904.1
AK081664 mRNA Translation: BAC38283.1
AK136490 mRNA Translation: BAE23004.1
AK147267 mRNA Translation: BAE27808.1
AK163952 mRNA Translation: BAE37548.1
BC053036 mRNA Translation: AAH53036.1
CCDSiCCDS19351.1 [P26618-1]
PIRiI57511 S33727
RefSeqiNP_001076785.1, NM_001083316.2 [P26618-1]
NP_001334647.1, NM_001347718.1 [P26618-2]
NP_001334648.1, NM_001347719.1 [P26618-2]
NP_035188.2, NM_011058.3 [P26618-1]
XP_006504324.1, XM_006504261.3 [P26618-1]
XP_006504325.1, XM_006504262.3 [P26618-1]
XP_006504326.1, XM_006504263.3 [P26618-1]

3D structure databases

SMRiP26618
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202088, 4 interactors
ComplexPortaliCPX-2899 PDGF receptor alpha - PDGF-AA complex
CPX-2901 PDGF receptor alpha - PDGF-AB complex
CPX-2903 PDGF receptor alpha-beta - PDGF-AB complex
CPX-2906 PDGF receptor alpha - PDGF-BB complex
CPX-2907 PDGF receptor alpha-beta - PDGF-BB complex
CPX-2912 PDGF receptor alpha - PDGF-CC complex
CPX-2913 PDGF receptor alpha-beta - PDGF-CC complex
CPX-2916 PDGF receptor alpha-beta - PDGF-DD complex
IntActiP26618, 3 interactors
MINTiP26618
STRINGi10090.ENSMUSP00000127173

Chemistry databases

BindingDBiP26618
ChEMBLiCHEMBL2096980
GuidetoPHARMACOLOGYi1803

PTM databases

iPTMnetiP26618
PhosphoSitePlusiP26618
SwissPalmiP26618

Proteomic databases

jPOSTiP26618
MaxQBiP26618
PaxDbiP26618
PeptideAtlasiP26618
PRIDEiP26618

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231 [P26618-1]
ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231 [P26618-1]
ENSMUST00000201711; ENSMUSP00000143891; ENSMUSG00000029231 [P26618-2]
ENSMUST00000202681; ENSMUSP00000143906; ENSMUSG00000029231 [P26618-2]
GeneIDi18595
KEGGimmu:18595
UCSCiuc008xub.1 mouse [P26618-2]
uc008xuc.1 mouse [P26618-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5156
MGIiMGI:97530 Pdgfra

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000156021
HOGENOMiHOG000112009
InParanoidiP26618
KOiK04363
OMAiCKDIKKC
OrthoDBi236292at2759
PhylomeDBiP26618
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 3474
ReactomeiR-MMU-1257604 PIP3 activates AKT signaling
R-MMU-186763 Downstream signal transduction
R-MMU-186797 Signaling by PDGF
R-MMU-5673001 RAF/MAP kinase cascade
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Pdgfra mouse

Protein Ontology

More...
PROi
PR:P26618

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000029231 Expressed in 384 organ(s), highest expression level in epididymis
ExpressionAtlasiP26618 baseline and differential
GenevisibleiP26618 MM

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
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR027290 PDGFRA
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
PF07679 I-set, 2 hits
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF500950 Alpha-PDGF_receptor, 1 hit
SMARTiView protein in SMART
SM00409 IG, 4 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 nameiPGFRA_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: P26618
Secondary accession number(s): Q3TQ37
, Q62046, Q7TSJ3, Q8C4N3
<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: August 1, 1992
Last sequence update: February 26, 2008
Last modified: May 8, 2019
This is version 193 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

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