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P09619

- PGFRB_HUMAN

UniProt

P09619 - PGFRB_HUMAN

Protein

Platelet-derived growth factor receptor beta

Gene

PDGFRB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 185 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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. 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.19 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.3 PublicationsPROSITE-ProRule annotation

    Enzyme 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. Inhibited by imatinib.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei527 – 5282Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein
    Sitei527 – 5282Breakpoint for translocation to form TRIP11-PDGFRB
    Sitei558 – 5592Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein
    Binding sitei634 – 6341ATPCurated
    Active sitei826 – 8261Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi606 – 6149ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. platelet activating factor receptor activity Source: ProtInc
    3. platelet-derived growth factor-activated receptor activity Source: ProtInc
    4. platelet-derived growth factor beta-receptor activity Source: UniProtKB
    5. platelet-derived growth factor binding Source: UniProtKB
    6. platelet-derived growth factor receptor binding Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. protein kinase binding Source: UniProtKB
    9. protein tyrosine kinase activity Source: UniProtKB
    10. receptor binding Source: UniProtKB
    11. vascular endothelial growth factor binding Source: BHF-UCL

    GO - Biological processi

    1. adrenal gland development Source: Ensembl
    2. aorta morphogenesis Source: BHF-UCL
    3. cardiac myofibril assembly Source: UniProtKB
    4. cell chemotaxis Source: UniProtKB
    5. cell migration Source: UniProtKB
    6. cell migration involved in coronary angiogenesis Source: UniProtKB
    7. cell migration involved in vasculogenesis Source: UniProtKB
    8. cellular response to platelet-derived growth factor stimulus Source: GOC
    9. epidermal growth factor receptor signaling pathway Source: Reactome
    10. Fc-epsilon receptor signaling pathway Source: Reactome
    11. fibroblast growth factor receptor signaling pathway Source: Reactome
    12. glycosaminoglycan biosynthetic process Source: Ensembl
    13. G-protein coupled receptor signaling pathway Source: GOC
    14. innate immune response Source: Reactome
    15. inner ear development Source: Ensembl
    16. in utero embryonic development Source: Ensembl
    17. metanephric comma-shaped body morphogenesis Source: Ensembl
    18. metanephric glomerular capillary formation Source: UniProtKB
    19. metanephric glomerular mesangial cell proliferation involved in metanephros development Source: UniProtKB
    20. metanephric mesenchymal cell migration Source: Ensembl
    21. metanephric mesenchyme development Source: Ensembl
    22. metanephric S-shaped body morphogenesis Source: Ensembl
    23. negative regulation of apoptotic process Source: Ensembl
    24. neurotrophin TRK receptor signaling pathway Source: Reactome
    25. peptidyl-tyrosine phosphorylation Source: UniProtKB
    26. phosphatidylinositol-mediated signaling Source: UniProtKB
    27. phosphatidylinositol metabolic process Source: UniProtKB
    28. platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
    29. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    30. positive regulation of calcium ion import Source: UniProtKB
    31. positive regulation of cell migration Source: BHF-UCL
    32. positive regulation of cell proliferation Source: UniProtKB
    33. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
    34. positive regulation of chemotaxis Source: UniProtKB
    35. positive regulation of collagen biosynthetic process Source: Ensembl
    36. positive regulation of DNA biosynthetic process Source: UniProtKB
    37. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    38. positive regulation of MAP kinase activity Source: UniProtKB
    39. positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
    40. positive regulation of mitosis Source: UniProtKB
    41. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    42. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    43. positive regulation of phospholipase C activity Source: UniProtKB
    44. positive regulation of phosphoprotein phosphatase activity Source: UniProtKB
    45. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    46. positive regulation of smooth muscle cell migration Source: UniProtKB
    47. positive regulation of smooth muscle cell proliferation Source: UniProtKB
    48. protein autophosphorylation Source: UniProtKB
    49. regulation of actin cytoskeleton organization Source: BHF-UCL
    50. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    51. response to estradiol Source: Ensembl
    52. response to fluid shear stress Source: Ensembl
    53. response to hydrogen peroxide Source: Ensembl
    54. response to hyperoxia Source: Ensembl
    55. response to retinoic acid Source: Ensembl
    56. response to toxic substance Source: Ensembl
    57. retina vasculature development in camera-type eye Source: UniProtKB
    58. signal transduction Source: UniProtKB
    59. skeletal system morphogenesis Source: Ensembl
    60. smooth muscle cell chemotaxis Source: BHF-UCL
    61. smooth muscle tissue development Source: Ensembl
    62. tissue homeostasis Source: Ensembl
    63. transforming growth factor beta receptor signaling pathway Source: Ensembl
    64. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Chemotaxis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_16888. Signaling by PDGF.
    REACT_17025. Downstream signal transduction.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiP09619.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-derived growth factor receptor beta (EC:2.7.10.1)
    Short name:
    PDGF-R-beta
    Short name:
    PDGFR-beta
    Alternative name(s):
    Beta platelet-derived growth factor receptor
    Beta-type platelet-derived growth factor receptor
    CD140 antigen-like family member B
    Platelet-derived growth factor receptor 1
    Short name:
    PDGFR-1
    CD_antigen: CD140b
    Gene namesi
    Name:PDGFRB
    Synonyms:PDGFR, PDGFR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:8804. PDGFRB.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen
    Note: After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of membrane Source: UniProtKB-KW
    6. intrinsic component of plasma membrane Source: UniProtKB
    7. lysosomal lumen Source: UniProtKB-SubCell
    8. membrane Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving PDGFRB is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;12)(q33;p13) with EVT6/TEL. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML).
    Myeloproliferative disorder chronic with eosinophilia (MPE) [MIM:131440]: A hematologic disorder characterized by malignant eosinophils proliferation.
    Note: The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving PDGFRB have been found in many instances of chronic myeloproliferative disorder with eosinophilia. Translocation t(5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein (PubMed:12181402). Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1 fusion protein (PubMed:15492236). Translocation t(1;5)(q23;q33) that forms a PDE4DIP-PDGFRB fusion protein (PubMed:12907457). Translocation t(5;6)(q33-34;q23) with CEP85L that fuses the 5'-end of CEP85L (isoform 4) to the 3'-end of PDGFRB (PubMed:21938754).4 Publications
    Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
    Note: The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with AML. Translocation t(5;14)(q33;q32) with TRIP11 (PubMed:9373237).1 Publication
    Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages.
    Note: The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with JMML. Translocation t(5;17)(q33;p11.2) with SPECC1 (PubMed:15087372).1 Publication
    Basal ganglia calcification, idiopathic, 4 (IBGC4) [MIM:615007]: A form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti658 – 6581L → P in IBGC4. 1 Publication
    VAR_069320
    Natural varianti987 – 9871R → W in IBGC4. 1 Publication
    VAR_069321
    Myofibromatosis, infantile 1 (IMF1) [MIM:228550]: A rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti561 – 5611R → C in IMF1. 1 Publication
    VAR_069925
    Natural varianti660 – 6601P → T in IMF1. 1 Publication
    Corresponds to variant rs144050370 [ dbSNP | Ensembl ].
    VAR_069926

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi579 – 5791Y → F: Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10. 2 Publications
    Mutagenesisi581 – 5811Y → F: Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10. 2 Publications
    Mutagenesisi634 – 6341K → A or R: Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 3 Publications
    Mutagenesisi716 – 7161Y → F: No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity. 2 Publications
    Mutagenesisi740 – 7401Y → F: Strongly reduces up-regulation of cell proliferation; when associated with F-751. Strongly decreases phosphatidylinositol 3-kinase activity. No effect on interaction with GRB10 and RASA1. 4 Publications
    Mutagenesisi751 – 7511Y → F: Strongly reduces up-regulation of cell proliferation; when associated with F-740. Abolishes phosphatidylinositol 3-kinase activity and interaction wit NCK1, and slightly reduces interaction with RASA1. No effect on interaction with GRB10. 6 Publications
    Mutagenesisi763 – 7631Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. 1 Publication
    Mutagenesisi771 – 7711Y → F: Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 3 Publications
    Mutagenesisi775 – 7751Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. 1 Publication
    Mutagenesisi778 – 7781Y → F: Strongly reduces expression levels. 1 Publication
    Mutagenesisi857 – 8571Y → F: Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 4 Publications
    Mutagenesisi1009 – 10091Y → F: No effect on interaction with GRB10. Abolishes interaction with PLCG1; when associated with F-1021. 3 Publications
    Mutagenesisi1021 – 10211Y → F: Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on interaction with GRB10. 4 Publications

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi131440. phenotype.
    228550. phenotype.
    601626. phenotype.
    607785. phenotype.
    615007. phenotype.
    Orphaneti1980. Bilateral striopallidodentate calcinosis.
    98823. Chronic myelomonocytic leukemia.
    3260. Idiopathic hypereosinophilic syndrome.
    2591. Infantile myofibromatosis.
    168950. Myeloid neoplasm associated with PDGFRB rearrangement.
    86830. Unclassified chronic myeloproliferative disease.
    PharmGKBiPA33148.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 32321 PublicationAdd
    BLAST
    Chaini33 – 11061074Platelet-derived growth factor receptor betaPRO_0000016757Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi54 ↔ 1001 PublicationPROSITE-ProRule annotation
    Glycosylationi89 – 891N-linked (GlcNAc...)2 Publications
    Glycosylationi103 – 1031N-linked (GlcNAc...)2 Publications
    Disulfide bondi149 ↔ 1901 PublicationPROSITE-ProRule annotation
    Glycosylationi215 – 2151N-linked (GlcNAc...)2 Publications
    Glycosylationi230 – 2301N-linked (GlcNAc...)2 Publications
    Disulfide bondi235 ↔ 2911 PublicationPROSITE-ProRule annotation
    Glycosylationi292 – 2921N-linked (GlcNAc...)2 Publications
    Glycosylationi307 – 3071N-linked (GlcNAc...)2 Publications
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi436 ↔ 508PROSITE-ProRule annotation
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
    Modified residuei562 – 5621Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei579 – 5791Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei581 – 5811Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei589 – 5891Phosphotyrosine; by autocatalysis
    Modified residuei686 – 6861Phosphotyrosine; by ABL1 and ABL2By similarity
    Modified residuei716 – 7161Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei740 – 7401Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei751 – 7511Phosphotyrosine; by autocatalysis5 Publications
    Modified residuei763 – 7631Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei771 – 7711Phosphotyrosine; by autocatalysis4 Publications
    Modified residuei775 – 7751Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei778 – 7781Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei857 – 8571Phosphotyrosine; by autocatalysis5 Publications
    Modified residuei934 – 9341Phosphotyrosine; by ABL1 and ABL2By similarity
    Modified residuei970 – 9701Phosphotyrosine; by ABL1 and ABL2By similarity
    Modified residuei1009 – 10091Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei1021 – 10211Phosphotyrosine; by autocatalysis4 Publications

    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-579, and to a lesser degree, at Tyr-581, is important for interaction with SRC family kinases. Phosphorylation at Tyr-740 and Tyr-751 is important for interaction with PIK3R1. Phosphorylation at Tyr-751 is important for interaction with NCK1. Phosphorylation at Tyr-771 and Tyr-857 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-857 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-1009 is important for interaction with PTPN11. Phosphorylation at Tyr-1009 and Tyr-1021 is important for interaction with PLCG1. Phosphorylation at Tyr-1021 is important for interaction with CBL; PLCG1 and CBL compete for the same binding site. Dephosphorylated by PTPRJ at Tyr-751, Tyr-857, Tyr-1009 and Tyr-1021. Dephosphorylated by PTPN2 at Tyr-579 and Tyr-1021.8 Publications
    N-glycosylated.2 Publications
    Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP09619.
    PaxDbiP09619.
    PRIDEiP09619.

    PTM databases

    PhosphoSiteiP09619.

    Expressioni

    Gene expression databases

    ArrayExpressiP09619.
    BgeeiP09619.
    CleanExiHS_PDGFRB.
    GenevestigatoriP09619.

    Organism-specific databases

    HPAiCAB003842.
    CAB018144.
    HPA028499.

    Interactioni

    Subunit structurei

    Interacts with homodimeric PDGFB and PDGFD, and with heterodimers formed by PDGFA and PDGFB. May also interact with homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts with SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB. Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated) with SRC and SRC family kinases. Interacts (tyrosine phosphorylated) with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated) with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by SHC1. Interacts (via C-terminus) with SLC9A3R1.20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E5P0CK452EBI-641237,EBI-7015490From a different organism.
    FYNP062413EBI-641237,EBI-515315
    GRB7Q144514EBI-641237,EBI-970191
    PDGFBP0112713EBI-641237,EBI-1554925
    PIK3R1P237276EBI-641237,EBI-520244From a different organism.
    PIK3R1P2798619EBI-641237,EBI-79464
    PLCG1P084873EBI-641237,EBI-8013886From a different organism.
    PLCG1P191745EBI-641237,EBI-79387
    PTENP604843EBI-641237,EBI-696162
    PTPN1P180313EBI-641237,EBI-968788
    PTPN11Q061248EBI-641237,EBI-297779
    PTPN12Q052093EBI-641237,EBI-2266035
    PTPRJQ129134EBI-641237,EBI-2264500
    RAF1P040492EBI-641237,EBI-365996
    RASA1P209363EBI-641237,EBI-1026476
    SLAQ132394EBI-641237,EBI-726214
    SLC9A3R1O147455EBI-641237,EBI-349787
    V-SRCP250204EBI-641237,EBI-8636140From a different organism.

    Protein-protein interaction databases

    BioGridi111185. 43 interactions.
    DIPiDIP-558N.
    IntActiP09619. 56 interactions.
    MINTiMINT-148093.
    STRINGi9606.ENSP00000261799.

    Structurei

    Secondary structure

    1
    1106
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 434
    Beta strandi50 – 589
    Beta strandi61 – 644
    Beta strandi70 – 756
    Beta strandi81 – 877
    Helixi92 – 943
    Beta strandi96 – 1016
    Beta strandi114 – 1196
    Helixi132 – 1354
    Beta strandi136 – 1416
    Beta strandi145 – 1473
    Beta strandi158 – 1647
    Turni175 – 1773
    Beta strandi178 – 1814
    Beta strandi185 – 19410
    Beta strandi197 – 2004
    Beta strandi204 – 2085
    Beta strandi217 – 2215
    Beta strandi223 – 2264
    Beta strandi231 – 2399
    Beta strandi241 – 2488
    Beta strandi252 – 2554
    Beta strandi261 – 2655
    Turni267 – 2704
    Beta strandi271 – 28010
    Beta strandi287 – 2959
    Turni296 – 2994
    Beta strandi300 – 31112
    Helixi530 – 55627

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GQ5X-ray2.20A1102-1106[»]
    1H9OX-ray1.79B751-755[»]
    1LWPmodel-A600-962[»]
    1SHAX-ray1.50B751-755[»]
    2L6WNMR-A/B526-563[»]
    2PLDNMR-B1018-1029[»]
    2PLENMR-B1018-1029[»]
    3MJGX-ray2.30X/Y33-314[»]
    ProteinModelPortaliP09619.
    SMRiP09619. Positions 33-463, 526-563, 576-1006.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09619.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 532500ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini554 – 1106553CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei533 – 55321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 12088Ig-like C2-type 1Add
    BLAST
    Domaini129 – 21082Ig-like C2-type 2Add
    BLAST
    Domaini214 – 30996Ig-like C2-type 3Add
    BLAST
    Domaini331 – 40373Ig-like C2-type 4Add
    BLAST
    Domaini416 – 524109Ig-like C2-type 5Add
    BLAST
    Domaini600 – 962363Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000112009.
    HOVERGENiHBG004335.
    InParanoidiP09619.
    KOiK05089.
    OMAiAPYDNYV.
    OrthoDBiEOG7GXP9Q.
    PhylomeDBiP09619.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013151. Immunoglobulin.
    IPR011009. Kinase-like_dom.
    IPR027288. PGFRB.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    [Graphical view]
    PANTHERiPTHR24416:SF53. PTHR24416:SF53. 1 hit.
    PfamiPF07679. I-set. 1 hit.
    PF00047. ig. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500948. Beta-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTiSM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view]

    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. Align

    Isoform 1 (identifier: P09619-1) [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

    MRLPGAMPAL ALKGELLLLS LLLLLEPQIS QGLVVTPPGP ELVLNVSSTF     50
    VLTCSGSAPV VWERMSQEPP QEMAKAQDGT FSSVLTLTNL TGLDTGEYFC 100
    THNDSRGLET DERKRLYIFV PDPTVGFLPN DAEELFIFLT EITEITIPCR 150
    VTDPQLVVTL HEKKGDVALP VPYDHQRGFS GIFEDRSYIC KTTIGDREVD 200
    SDAYYVYRLQ VSSINVSVNA VQTVVRQGEN ITLMCIVIGN EVVNFEWTYP 250
    RKESGRLVEP VTDFLLDMPY HIRSILHIPS AELEDSGTYT CNVTESVNDH 300
    QDEKAINITV VESGYVRLLG EVGTLQFAEL HRSRTLQVVF EAYPPPTVLW 350
    FKDNRTLGDS SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGHYTMRAFH 400
    EDAEVQLSFQ LQINVPVRVL ELSESHPDSG EQTVRCRGRG MPQPNIIWSA 450
    CRDLKRCPRE LPPTLLGNSS EEESQLETNV TYWEEEQEFE VVSTLRLQHV 500
    DRPLSVRCTL RNAVGQDTQE VIVVPHSLPF KVVVISAILA LVVLTIISLI 550
    ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL 600
    VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS 650
    ELKIMSHLGP HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF 700
    LQHHSDKRRP PSAELYSNAL PVGLPLPSHV SLTGESDGGY MDMSKDESVD 750
    YVPMLDMKGD VKYADIESSN YMAPYDNYVP SAPERTCRAT LINESPVLSY 800
    MDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV KICDFGLARD 850
    IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG 900
    GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP 950
    FSQLVLLLER LLGEGYKKKY QQVDEEFLRS DHPAILRSQA RLPGFHGLRS 1000
    PLDTSSVLYT AVQPNEGDND YIIPLPDPKP EVADEGPLEG SPSLASSTLN 1050
    EVNTSSTISC DSPLEPQDEP EPEPQLELQV EPEPELEQLP DSGCPAPRAE 1100
    AEDSFL 1106
    Length:1,106
    Mass (Da):123,968
    Last modified:July 1, 1989 - v1
    Checksum:i038C15E531D6E89D
    GO
    Isoform 2 (identifier: P09619-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         311-336: VESGYVRLLGEVGTLQFAELHRSRTL → RAATCGSWERWAHYNLLSCIGAGHCR
         337-1106: Missing.

    Show »
    Length:336
    Mass (Da):37,412
    Checksum:i5BEDAFC416865068
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti241 – 2411E → D in AAA36427. (PubMed:2850496)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291I → F.1 Publication
    Corresponds to variant rs17110944 [ dbSNP | Ensembl ].
    VAR_034377
    Natural varianti180 – 1801S → F.1 Publication
    Corresponds to variant rs17853027 [ dbSNP | Ensembl ].
    VAR_035125
    Natural varianti282 – 2821E → K.1 Publication
    Corresponds to variant rs34586048 [ dbSNP | Ensembl ].
    VAR_042027
    Natural varianti345 – 3451P → S.
    Corresponds to variant rs2229558 [ dbSNP | Ensembl ].
    VAR_049717
    Natural varianti485 – 4851E → K.1 Publication
    Corresponds to variant rs41287110 [ dbSNP | Ensembl ].
    VAR_042028
    Natural varianti561 – 5611R → C in IMF1. 1 Publication
    VAR_069925
    Natural varianti589 – 5891Y → H in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042029
    Natural varianti658 – 6581L → P in IBGC4. 1 Publication
    VAR_069320
    Natural varianti660 – 6601P → T in IMF1. 1 Publication
    Corresponds to variant rs144050370 [ dbSNP | Ensembl ].
    VAR_069926
    Natural varianti718 – 7181N → Y.1 Publication
    Corresponds to variant rs35322465 [ dbSNP | Ensembl ].
    VAR_042030
    Natural varianti882 – 8821T → I in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_042031
    Natural varianti987 – 9871R → W in IBGC4. 1 Publication
    VAR_069321

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei311 – 33626VESGY…RSRTL → RAATCGSWERWAHYNLLSCI GAGHCR in isoform 2. 1 PublicationVSP_056008Add
    BLAST
    Alternative sequencei337 – 1106770Missing in isoform 2. 1 PublicationVSP_056009Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03278 mRNA. Translation: AAA60049.1.
    M21616 mRNA. Translation: AAA36427.1.
    EU826595 mRNA. Translation: ACF47631.1.
    AC005895 Genomic DNA. No translation available.
    AC011382 Genomic DNA. No translation available.
    BC032224 mRNA. Translation: AAH32224.1.
    U33172 Genomic DNA. Translation: AAC51675.1.
    CCDSiCCDS4303.1.
    PIRiA28206. PFHUGB.
    RefSeqiNP_002600.1. NM_002609.3.
    UniGeneiHs.509067.

    Genome annotation databases

    EnsembliENST00000261799; ENSP00000261799; ENSG00000113721.
    GeneIDi5159.
    KEGGihsa:5159.
    UCSCiuc003lro.3. human.

    Polymorphism databases

    DMDMi129890.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03278 mRNA. Translation: AAA60049.1 .
    M21616 mRNA. Translation: AAA36427.1 .
    EU826595 mRNA. Translation: ACF47631.1 .
    AC005895 Genomic DNA. No translation available.
    AC011382 Genomic DNA. No translation available.
    BC032224 mRNA. Translation: AAH32224.1 .
    U33172 Genomic DNA. Translation: AAC51675.1 .
    CCDSi CCDS4303.1.
    PIRi A28206. PFHUGB.
    RefSeqi NP_002600.1. NM_002609.3.
    UniGenei Hs.509067.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GQ5 X-ray 2.20 A 1102-1106 [» ]
    1H9O X-ray 1.79 B 751-755 [» ]
    1LWP model - A 600-962 [» ]
    1SHA X-ray 1.50 B 751-755 [» ]
    2L6W NMR - A/B 526-563 [» ]
    2PLD NMR - B 1018-1029 [» ]
    2PLE NMR - B 1018-1029 [» ]
    3MJG X-ray 2.30 X/Y 33-314 [» ]
    ProteinModelPortali P09619.
    SMRi P09619. Positions 33-463, 526-563, 576-1006.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111185. 43 interactions.
    DIPi DIP-558N.
    IntActi P09619. 56 interactions.
    MINTi MINT-148093.
    STRINGi 9606.ENSP00000261799.

    Chemistry

    BindingDBi P09619.
    ChEMBLi CHEMBL1913.
    DrugBanki DB00102. Becaplermin.
    DB01254. Dasatinib.
    DB00619. Imatinib.
    DB00398. Sorafenib.
    DB01268. Sunitinib.
    GuidetoPHARMACOLOGYi 1804.

    PTM databases

    PhosphoSitei P09619.

    Polymorphism databases

    DMDMi 129890.

    Proteomic databases

    MaxQBi P09619.
    PaxDbi P09619.
    PRIDEi P09619.

    Protocols and materials databases

    DNASUi 5159.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261799 ; ENSP00000261799 ; ENSG00000113721 .
    GeneIDi 5159.
    KEGGi hsa:5159.
    UCSCi uc003lro.3. human.

    Organism-specific databases

    CTDi 5159.
    GeneCardsi GC05M149473.
    GeneReviewsi PDGFRB.
    HGNCi HGNC:8804. PDGFRB.
    HPAi CAB003842.
    CAB018144.
    HPA028499.
    MIMi 131440. phenotype.
    173410. gene.
    228550. phenotype.
    601626. phenotype.
    607785. phenotype.
    615007. phenotype.
    neXtProti NX_P09619.
    Orphaneti 1980. Bilateral striopallidodentate calcinosis.
    98823. Chronic myelomonocytic leukemia.
    3260. Idiopathic hypereosinophilic syndrome.
    2591. Infantile myofibromatosis.
    168950. Myeloid neoplasm associated with PDGFRB rearrangement.
    86830. Unclassified chronic myeloproliferative disease.
    PharmGKBi PA33148.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000112009.
    HOVERGENi HBG004335.
    InParanoidi P09619.
    KOi K05089.
    OMAi APYDNYV.
    OrthoDBi EOG7GXP9Q.
    PhylomeDBi P09619.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_16888. Signaling by PDGF.
    REACT_17025. Downstream signal transduction.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki P09619.

    Miscellaneous databases

    ChiTaRSi PDGFRB. human.
    EvolutionaryTracei P09619.
    GeneWikii PDGFRB.
    GenomeRNAii 5159.
    NextBioi 19958.
    PROi P09619.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09619.
    Bgeei P09619.
    CleanExi HS_PDGFRB.
    Genevestigatori P09619.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013151. Immunoglobulin.
    IPR011009. Kinase-like_dom.
    IPR027288. PGFRB.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    [Graphical view ]
    PANTHERi PTHR24416:SF53. PTHR24416:SF53. 1 hit.
    Pfami PF07679. I-set. 1 hit.
    PF00047. ig. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500948. Beta-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTi SM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a cDNA coding for the human platelet-derived growth factor receptor: evidence for more than one receptor class."
      Gronwald R.G.K., Grant F.J., Haldeman B.A., Hart C.E., O'Hara P.J., Hagen F.S., Ross R., Bowen-Pope D.F., Murray M.J.
      Proc. Natl. Acad. Sci. U.S.A. 85:3435-3439(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS PDGFB RECEPTOR, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH PDGFB.
    2. "cDNA cloning and expression of a human platelet-derived growth factor (PDGF) receptor specific for B-chain-containing PDGF molecules."
      Claesson-Welsh L., Eriksson A., Moren A., Severinsson L., Ek B., Oestman A., Betsholtz C., Heldin C.-H.
      Mol. Cell. Biol. 8:3476-3486(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS PDGFB RECEPTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, AUTOPHOSPHORYLATION, INTERACTION WITH PDGFA AND PDGFB.
    3. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
      Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
      Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PHE-180.
      Tissue: Brain.
    6. "Integration of proviral DNA into the PDGF beta-receptor gene in HTLV-I-infected T-cells results in a novel tyrosine kinase product with transforming activity."
      Chi K.D., McPhee R.A., Wagner A.S., Dietz J.J., Pantazis P., Goustin A.S.
      Oncogene 15:1051-1057(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-569.
    7. "Systematic screen for tyrosine kinase rearrangements identifies a novel C6orf204-PDGFRB fusion in a patient with recurrent T-ALL and an associated myeloproliferative neoplasm."
      Chmielecki J., Peifer M., Viale A., Hutchinson K., Giltnane J., Socci N.D., Hollis C.J., Dean R.S., Yenamandra A., Jagasia M., Kim A.S., Dave U.P., Thomas R.K., Pao W.
      Genes Chromosomes Cancer 51:54-65(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 559-1106 (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH CEP85L.
    8. "Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes."
      Roberts W.M., Look A.T., Roussel M.F., Sherr C.J.
      Cell 55:655-661(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1046-1106.
    9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 33-47.
    10. "Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins."
      Kazlauskas A., Cooper J.A.
      Cell 58:1121-1133(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-751 AND TYR-857.
    11. "Independent expression of human alpha or beta platelet-derived growth factor receptor cDNAs in a naive hematopoietic cell leads to functional coupling with mitogenic and chemotactic signaling pathways."
      Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S., LaRochelle W.J., Ruggiero M., Aaronson S.A.
      Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, SUBCELLULAR LOCATION.
    12. "Functions of the major tyrosine phosphorylation site of the PDGF receptor beta subunit."
      Kazlauskas A., Durden D.L., Cooper J.A.
      Cell Regul. 2:413-425(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION; ACTIVATION OF PLCG1 AND IN PHOSPHORYLATION OF PLCG1 AND RASA1/GAP, MUTAGENESIS OF TYR-751 AND TYR-857.
    13. "Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit dimerization and intersubunit trans-phosphorylation."
      Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A., Bowen-Pope D.F., Cooper J.A., Kazlauskas A.
      J. Biol. Chem. 266:8987-8992(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, PHOSPHORYLATION AT TYR-857 AND TYR-751.
    14. "Effect of receptor kinase inactivation on the rate of internalization and degradation of PDGF and the PDGF beta-receptor."
      Sorkin A., Westermark B., Heldin C.H., Claesson-Welsh L.
      J. Cell Biol. 112:469-478(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-634.
    15. "Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo."
      Kashishian A., Kazlauskas A., Cooper J.A.
      EMBO J. 11:1373-1382(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY, INTERACTION WITH PIK3R1 AND RASA1, PHOSPHORYLATION AT TYR-740; TYR-751; TYR-771 AND TYR-857, MUTAGENESIS OF LYS-634; TYR-716; TYR-740; TYR-751; TYR-763; TYR-771; TYR-775; TYR-778 AND TYR-857.
    16. "Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma."
      Ronnstrand L., Mori S., Arridsson A.K., Eriksson A., Wernstedt C., Hellman U., Claesson-Welsh L., Heldin C.H.
      EMBO J. 11:3911-3919(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND PHOSPHORYLATION OF PLCG1, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-1009 AND TYR-1021, MUTAGENESIS OF TYR-1009 AND TYR-1021.
    17. "Ligand-induced polyubiquitination of the platelet-derived growth factor beta-receptor."
      Mori S., Heldin C.H., Claesson-Welsh L.
      J. Biol. Chem. 267:6429-6434(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEGRADATION.
    18. "GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit."
      Kazlauskas A., Kashishian A., Cooper J.A., Valius M.
      Mol. Cell. Biol. 12:2534-2544(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3R1 AND RASA1, MUTAGENESIS OF TYR-740; TYR-751 AND TYR-771.
    19. "Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases."
      Mori S., Ronnstrand L., Yokote K., Engstrom A., Courtneidge S.A., Claesson-Welsh L., Heldin C.H.
      EMBO J. 12:2257-2264(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION, PHOSPHORYLATION AT TYR-579 AND TYR-581; INTERACTION WITH SRC, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-579 AND TYR-581.
    20. "Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor."
      Fretto L.J., Snape A.J., Tomlinson J.E., Seroogy J.J., Wolf D.L., LaRochelle W.J., Giese N.A.
      J. Biol. Chem. 268:3625-3631(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DGFA AND PDGFB.
    21. "Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor."
      Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G.
      J. Biol. Chem. 268:21478-21481(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF PTPN11, INTERACTION WITH PTPN11; PIK3R1; PLCG1 AND RASA1, MUTAGENESIS OF TYR-1009.
    22. "Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor."
      Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J.
      Mol. Cell. Biol. 13:6889-6896(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCK1 AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF NCK1, MUTAGENESIS OF TYR-751.
    23. "Shb is a ubiquitously expressed Src homology 2 protein."
      Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L.
      Oncogene 9:19-27(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    24. "Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors."
      Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.
      J. Biol. Chem. 271:30942-30949(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB7.
    25. "Fusion of the platelet-derived growth factor receptor beta to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution."
      Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H.
      Blood 90:4271-4277(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH TRIP11.
    26. "Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis."
      Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H.
      Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB10, MUTAGENESIS OF TYR-579; TYR-581; TYR-716; TYR-740; TYR-751; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
    27. "APS, an adaptor protein containing PH and SH2 domains, is associated with the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis."
      Yokouchi M., Wakioka T., Sakamoto H., Yasukawa H., Ohtsuka S., Sasaki A., Ohtsubo M., Valius M., Inoue A., Komiya S., Yoshimura A.
      Oncogene 18:759-767(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH2B2/APS.
    28. "Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1."
      Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E., Vilella R., Bohmer F., Ostman A.
      J. Biol. Chem. 275:16219-16226(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-562; TYR-751; TYR-763; TYR-771; TYR-775; TYR-778; TYR-857; TYR-1009 AND TYR-1021, DEPHOSPHORYLATION AT TYR-751; TYR-857; TYR-1009 AND TYR-1021 BY PTPRJ.
    29. "Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors."
      Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.
      Mol. Cell. Biol. 20:3817-3830(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3C2B.
    30. "Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor."
      Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.
      J. Biol. Chem. 276:27406-27414(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A RECEPTOR FOR PDGFC, INTERACTION WITH PDGFC.
    31. "PDGF-D is a specific, protease-activated ligand for the PDGF beta-receptor."
      Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H., Alitalo K., Eriksson U.
      Nat. Cell Biol. 3:512-516(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A RECEPTOR FOR PDGFD.
    32. "Response to imatinib mesylate in patients with chronic myeloproliferative diseases with rearrangements of the platelet-derived growth factor receptor beta."
      Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J., Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E., Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E., Silberman S., Schultheis B., Cross N.C.P., Goldman J.M.
      N. Engl. J. Med. 347:481-487(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH ETV6.
    33. "Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder associated with eosinophilia: involvement of PDGFRB and response to imatinib."
      Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C., Shipp M.A., Aguiar R.C.T.
      Blood 102:4187-4190(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PDE4DIP.
    34. "HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with t(5;17)(q33;p11.2)."
      Morerio C., Acquila M., Rosanda C., Rapella A., Dufour C., Locatelli F., Maserati E., Pasquali F., Panarello C.
      Cancer Res. 64:2649-2651(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH SPECC1.
    35. "p53-Binding protein 1 is fused to the platelet-derived growth factor receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib-responsive eosinophilic myeloproliferative disorder."
      Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G., Thaler J., Chase A.J., Cross N.C.
      Cancer Res. 64:7216-7219(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH TP53BP1, ENZYME REGULATION.
    36. "Site-selective regulation of platelet-derived growth factor beta receptor tyrosine phosphorylation by T-cell protein tyrosine phosphatase."
      Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B., Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L., Ostman A., Hellberg C.
      Mol. Cell. Biol. 24:2190-2201(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-579; TYR-751; TYR-771 AND TYR-1021, DEPHOSPHORYLATION AT TYR-579 AND TYR-1021 BY PTPN2.
    37. "Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II."
      Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., Park H.S., Kim K.Y., Lee J.S., Choi C., Bae Y.S., Lee B.I., Rhee S.G., Kang S.W.
      Nature 435:347-353(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-579; TYR-581; TYR-716; TYR-740; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
    38. "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation."
      Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H.
      J. Biol. Chem. 282:29336-29347(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBL, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1021, UBIQUITINATION.
    39. "A novel signaling axis of matriptase/PDGF-D/ss-PDGFR in human prostate cancer."
      Ustach C.V., Huang W., Conley-LaComb M.K., Lin C.Y., Che M., Abrams J., Kim H.R.
      Cancer Res. 70:9631-9640(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PDGFD RECEPTOR.
    40. "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
      Wardega P., Heldin C.H., Lennartsson J.
      Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CBL; STAM; PDCD6IP/ALIX; PLCG1 AND PTPN11, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-634 AND TYR-857.
    41. "Stimulation of platelet-derived growth factor receptor beta (PDGFRbeta) activates ADAM17 and promotes metalloproteinase-dependent cross-talk between the PDGFRbeta and epidermal growth factor receptor (EGFR) signaling pathways."
      Mendelson K., Swendeman S., Saftig P., Blobel C.P.
      J. Biol. Chem. 285:25024-25032(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    42. "Glyceollins inhibit platelet-derived growth factor-mediated human arterial smooth muscle cell proliferation and migration."
      Kim H.J., Cha B.Y., Choi B., Lim J.S., Woo J.T., Kim J.S.
      Br. J. Nutr. 107:24-35(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SMOOTH MUSCLE CELL PROLIFERATION AND MIGRATION.
    43. "Direct interaction between Shc and the platelet-derived growth factor beta-receptor."
      Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H., Claesson-Welsh L.
      J. Biol. Chem. 269:15337-15343(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHC1 AND GRB2, FUNCTION IN PHOSPHORYLATION OF SHC1.
    44. "Disruption of platelet-derived growth factor-dependent phosphatidylinositol 3-kinase and phospholipase Cgamma 1 activity abolishes vascular smooth muscle cell proliferation and migration and attenuates neointima formation in vivo."
      Caglayan E., Vantler M., Leppanen O., Gerhardt F., Mustafov L., Ten Freyhaus H., Kappert K., Odenthal M., Zimmermann W.H., Tallquist M.D., Rosenkranz S.
      J. Am. Coll. Cardiol. 57:2527-2538(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SMOOTH MUSCLE CELL MIGRATION AND NEOINTIMA FORMATION AFTER BLOOD VESSEL INJURY, MUTAGENESIS OF TYR-740; TYR-751 AND TYR-1021.
    45. "Signal transduction via platelet-derived growth factor receptors."
      Heldin C.H., Ostman A., Ronnstrand L.
      Biochim. Biophys. Acta 1378:F79-113(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON SIGNALING AND AUTOPHOSPHORYLATION.
    46. "PDGF receptors-mediators of autocrine tumor growth and regulators of tumor vasculature and stroma."
      Ostman A.
      Cytokine Growth Factor Rev. 15:275-286(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    47. "PDGF receptors as targets in tumor treatment."
      Ostman A., Heldin C.H.
      Adv. Cancer Res. 97:247-274(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    48. "Role of platelet-derived growth factors in physiology and medicine."
      Andrae J., Gallini R., Betsholtz C.
      Genes Dev. 22:1276-1312(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION; LIGANDS; ROLE IN DEVELOPMENT AND DISEASE AND ACTIVATION OF SIGNALING PATHWAYS.
    49. "NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha C-terminal SH2-peptide complex."
      Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A., Rowsell S., Murshudov G.N.
      Acta Crystallogr. D 57:1397-1404(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 751-755 IN COMPLEX WITH PIK3R1, COMPARISON WITH NMR ANALYSIS.
    50. "Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors."
      Karthikeyan S., Leung T., Ladias J.A.A.
      J. Biol. Chem. 277:18973-18978(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1102-1106 IN COMPLEX WITH SLC9A3R1, INTERACTION WITH SLC9A3R1.
    51. "Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex."
      Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.
      Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-314 IN COMPLEX WITH PDGFB, SUBUNIT, GLYCOSYLATION AT ASN-45; ASN-89; ASN-103; ASN-215; ASN-230; ASN-292 AND ASN-307, DISULFIDE BONDS.
    52. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-29; LYS-282; LYS-485; HIS-589; TYR-718 AND ILE-882.
    53. Cited for: VARIANT IMF1 THR-660.
    54. Cited for: VARIANT IMF1 CYS-561.
    55. Cited for: VARIANTS IBGC4 PRO-658 AND TRP-987.

    Entry informationi

    Entry nameiPGFRB_HUMAN
    AccessioniPrimary (citable) accession number: P09619
    Secondary accession number(s): B5A957, Q8N5L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 185 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3