UniProtKB - P26618 (PGFRA_MOUSE)
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Protein
Platelet-derived growth factor receptor alpha
Gene
Pdgfra
Organism
Mus musculus (Mouse)
Status
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
Catalytic activityi
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation
Enzyme 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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Binding sitei | 627 | ATPPROSITE-ProRule annotation | 1 | |
| Active sitei | 818 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Nucleotide bindingi | 599 – 607 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- platelet-derived growth factor alpha-receptor activity Source: UniProtKB
- platelet-derived growth factor binding Source: UniProtKB
- platelet-derived growth factor receptor binding Source: MGI
- protein complex binding Source: MGI
- protein homodimerization activity Source: UniProtKB
- protein kinase activity Source: MGI
- transmembrane receptor protein tyrosine kinase activity Source: MGI
- vascular endothelial growth factor-activated receptor activity Source: UniProtKB
- vascular endothelial growth factor binding Source: MGI
GO - Biological processi
- adrenal gland development Source: MGI
- anatomical structure morphogenesis Source: MGI
- animal organ morphogenesis Source: MGI
- cardiac myofibril assembly Source: UniProtKB
- cell chemotaxis Source: UniProtKB
- cell migration Source: UniProtKB
- cellular response to amino acid stimulus Source: MGI
- cellular response to reactive oxygen species Source: MGI
- embryonic cranial skeleton morphogenesis Source: UniProtKB
- embryonic digestive tract morphogenesis Source: UniProtKB
- estrogen metabolic process Source: MGI
- extracellular matrix organization Source: MGI
- face morphogenesis Source: MGI
- female gonad development Source: MGI
- hematopoietic progenitor cell differentiation Source: MGI
- in utero embryonic development Source: MGI
- Leydig cell differentiation Source: MGI
- lung development Source: MGI
- luteinization Source: MGI
- male genitalia development Source: MGI
- metanephric glomerular capillary formation Source: UniProtKB
- negative regulation of platelet activation Source: UniProtKB
- odontogenesis of dentin-containing tooth Source: MGI
- palate development Source: MGI
- peptidyl-tyrosine phosphorylation Source: UniProtKB
- phosphatidylinositol-mediated signaling Source: UniProtKB
- platelet aggregation Source: UniProtKB
- platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
- platelet-derived growth factor receptor signaling pathway Source: MGI
- positive regulation of cell migration Source: UniProtKB
- positive regulation of cell proliferation Source: UniProtKB
- positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
- positive regulation of cytosolic calcium ion concentration Source: UniProtKB
- positive regulation of DNA replication Source: UniProtKB
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
- positive regulation of fibroblast proliferation Source: UniProtKB
- positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
- positive regulation of phospholipase C activity Source: MGI
- protein autophosphorylation Source: UniProtKB
- regulation of chemotaxis Source: MGI
- regulation of mesenchymal stem cell differentiation Source: UniProtKB
- retina vasculature development in camera-type eye Source: UniProtKB
- signal transduction involved in regulation of gene expression Source: MGI
- skeletal system morphogenesis Source: MGI
- wound healing Source: UniProtKB
Keywordsi
| Molecular function | Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase |
| Biological process | Chemotaxis |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
| BRENDAi | 2.7.10.1. 3474. |
| 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. |
Names & Taxonomyi
| 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 |
| Gene namesi | Name:Pdgfra |
| Organismi | Mus musculus (Mouse) |
| Taxonomic identifieri | 10090 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
| Proteomesi |
|
Organism-specific databases
| MGIi | MGI:97530. Pdgfra. |
Subcellular locationi
- Cell membrane; Single-pass type I membrane protein
Note: The activated receptor is rapidly internalized and degraded.By similarity
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Topological domaini | 25 – 528 | ExtracellularSequence analysisAdd BLAST | 504 | |
| Transmembranei | 529 – 549 | HelicalSequence analysisAdd BLAST | 21 | |
| Topological domaini | 550 – 1089 | CytoplasmicSequence analysisAdd BLAST | 540 |
GO - Cellular componenti
- cell junction Source: MGI
- cell surface Source: BHF-UCL
- cytoplasm Source: MGI
- external side of plasma membrane Source: MGI
- integral component of plasma membrane Source: UniProtKB
- intrinsic component of plasma membrane Source: MGI
- membrane Source: MGI
- microvillus Source: MGI
- nucleus Source: MGI
- plasma membrane Source: MGI
- protein complex Source: MGI
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
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-oncogeneChemistry databases
| ChEMBLi | CHEMBL2096980. |
| GuidetoPHARMACOLOGYi | 1803. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Signal peptidei | 1 – 24 | Sequence analysisAdd BLAST | 24 | |
| ChainiPRO_0000016761 | 25 – 1089 | Platelet-derived growth factor receptor alphaAdd BLAST | 1065 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Glycosylationi | 42 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 49 ↔ 100 | PROSITE-ProRule annotation | ||
| Glycosylationi | 76 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 89 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 103 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 150 ↔ 189 | PROSITE-ProRule annotation | ||
| Glycosylationi | 179 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 235 ↔ 290 | PROSITE-ProRule annotation | ||
| Glycosylationi | 353 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 359 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 435 ↔ 501 | PROSITE-ProRule annotation | ||
| Glycosylationi | 458 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 468 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 506 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Modified residuei | 572 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 574 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 720 | Phosphotyrosine; by autocatalysisCurated | 1 | |
| Modified residuei | 731 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 742 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 754 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 762 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 768 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 849 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 988 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 1018 | Phosphotyrosine; by autocatalysisBy similarity | 1 |
Post-translational modificationi
Ubiquitinated, leading to its degradation.By similarity
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-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 conjugationProteomic databases
| MaxQBi | P26618. |
| PaxDbi | P26618. |
| PeptideAtlasi | P26618. |
| PRIDEi | P26618. |
PTM databases
| iPTMneti | P26618. |
| PhosphoSitePlusi | P26618. |
| SwissPalmi | P26618. |
Expressioni
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
Gene expression databases
| Bgeei | ENSMUSG00000029231. |
| ExpressionAtlasi | P26618. baseline and differential. |
| Genevisiblei | P26618. MM. |
Interactioni
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
- platelet-derived growth factor binding Source: UniProtKB
- platelet-derived growth factor receptor binding Source: MGI
- protein complex binding Source: MGI
- protein homodimerization activity Source: UniProtKB
- vascular endothelial growth factor binding Source: MGI
Protein-protein interaction databases
| BioGridi | 202088. 1 interactor. |
| IntActi | P26618. 3 interactors. |
| MINTi | MINT-4107325. |
| STRINGi | 10090.ENSMUSP00000000476. |
Chemistry databases
| BindingDBi | P26618. |
Structurei
3D structure databases
| ProteinModelPortali | P26618. |
| SMRi | P26618. |
| ModBasei | Search... |
| MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 25 – 113 | Ig-like C2-type 1Add BLAST | 89 | |
| Domaini | 117 – 201 | Ig-like C2-type 2Add BLAST | 85 | |
| Domaini | 202 – 306 | Ig-like C2-type 3Add BLAST | 105 | |
| Domaini | 319 – 410 | Ig-like C2-type 4Add BLAST | 92 | |
| Domaini | 414 – 517 | Ig-like C2-type 5Add BLAST | 104 | |
| Domaini | 593 – 954 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 362 |
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 helixPhylogenomic databases
| eggNOGi | KOG0200. Eukaryota. COG0515. LUCA. |
| GeneTreei | ENSGT00760000118923. |
| HOGENOMi | HOG000112009. |
| HOVERGENi | HBG004335. |
| InParanoidi | P26618. |
| KOi | K04363. |
| OMAi | CKDIKKC. |
| OrthoDBi | EOG091G01TL. |
| PhylomeDBi | P26618. |
| TreeFami | TF325768. |
Family and domain databases
| Gene3Di | 2.60.40.10. 5 hits. |
| InterProi | View protein in InterPro IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003599. Ig_sub. IPR003598. Ig_sub2. IPR011009. Kinase-like_dom. 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. |
| Pfami | View protein in Pfam PF07679. I-set. 2 hits. PF07714. Pkinase_Tyr. 1 hit. |
| PIRSFi | PIRSF500950. Alpha-PDGF_receptor. 1 hit. |
| SMARTi | View protein in SMART SM00409. IG. 4 hits. SM00408. IGc2. 3 hits. SM00219. TyrKc. 1 hit. |
| SUPFAMi | SSF48726. SSF48726. 4 hits. SSF56112. SSF56112. 2 hits. |
| 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. |
Sequences (2)i
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket
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.
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
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 65 | D → E in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 65 | D → E in AAA39904 (PubMed:1321404).Curated | 1 | |
| Sequence conflicti | 192 | T → A in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 202 | E → A in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 252 | E → G in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 271 | L → V in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 322 | G → S in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 326 | A → P in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 439 – 440 | GT → EG in AAA39733 (PubMed:2174116).Curated | 2 | |
| Sequence conflicti | 472 | I → V in BAE37548 (PubMed:16141072).Curated | 1 | |
| Sequence conflicti | 529 | A → E in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 737 | A → D in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 849 | Y → D in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 936 | E → D in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 950 | V → L in AAA39733 (PubMed:2174116).Curated | 1 | |
| Sequence conflicti | 1005 | G → S in AAA39904 (PubMed:1321404).Curated | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_031877 | 775 – 790 | DSEVK…DSEGL → GKSAHAHSGKYDLSVV in isoform 2. 1 PublicationAdd BLAST | 16 | |
| Alternative sequenceiVSP_031878 | 791 – 1089 | Missing in isoform 2. 1 PublicationAdd BLAST | 299 |
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. |
| CCDSi | CCDS19351.1. [P26618-1] |
| PIRi | I57511. S33727. |
| 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] |
| UniGenei | Mm.221403. |
Genome annotation databases
| Ensembli | ENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231. [P26618-1] ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231. [P26618-1] ENSMUST00000201711; ENSMUSP00000143891; ENSMUSG00000029231. [P26618-2] ENSMUST00000202681; ENSMUSP00000143906; ENSMUSG00000029231. [P26618-2] |
| GeneIDi | 18595. |
| KEGGi | mmu:18595. |
| UCSCi | uc008xub.1. mouse. [P26618-2] uc008xuc.1. mouse. [P26618-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | PGFRA_MOUSE | |
| Accessioni | P26618Primary (citable) accession number: P26618 Secondary accession number(s): Q3TQ37 Q8C4N3 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
| Last sequence update: | February 26, 2008 | |
| Last modified: | June 7, 2017 | |
| This is version 178 of the entry and version 3 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
