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P09619

- PGFRB_HUMAN

UniProt

P09619 - PGFRB_HUMAN

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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

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 kinase binding Source: UniProtKB
  8. protein tyrosine kinase activity Source: UniProtKB
  9. receptor binding Source: UniProtKB
  10. 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 532500ExtracellularSequence AnalysisAdd
BLAST
Transmembranei533 – 55321HelicalSequence AnalysisAdd
BLAST
Topological domaini554 – 1106553CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. cell surface Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. cytoplasmic vesicle Source: UniProtKB-KW
  5. extracellular vesicular exosome Source: UniProt
  6. focal adhesion Source: UniProtKB
  7. integral component of membrane Source: UniProtKB-KW
  8. intrinsic component of plasma membrane Source: UniProtKB
  9. lysosome Source: UniProtKB-KW
  10. membrane Source: UniProtKB
  11. nucleus Source: UniProtKB
  12. plasma membrane Source: Reactome
Complete GO annotation...

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...)1 Publication
Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
Disulfide bondi149 ↔ 1901 PublicationPROSITE-ProRule annotation
Glycosylationi215 – 2151N-linked (GlcNAc...)1 Publication
Glycosylationi230 – 2301N-linked (GlcNAc...)1 Publication
Disulfide bondi235 ↔ 2911 PublicationPROSITE-ProRule annotation
Glycosylationi292 – 2921N-linked (GlcNAc...)1 Publication
Glycosylationi307 – 3071N-linked (GlcNAc...)1 Publication
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

BgeeiP09619.
CleanExiHS_PDGFRB.
ExpressionAtlasiP09619. baseline and differential.
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 – 434Combined sources
Beta strandi50 – 589Combined sources
Beta strandi61 – 644Combined sources
Beta strandi70 – 756Combined sources
Beta strandi81 – 877Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 1016Combined sources
Beta strandi114 – 1196Combined sources
Helixi132 – 1354Combined sources
Beta strandi136 – 1416Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi158 – 1647Combined sources
Turni175 – 1773Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi185 – 19410Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi204 – 2085Combined sources
Beta strandi217 – 2215Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi231 – 2399Combined sources
Beta strandi241 – 2488Combined sources
Beta strandi252 – 2554Combined sources
Beta strandi261 – 2655Combined sources
Turni267 – 2704Combined sources
Beta strandi271 – 28010Combined sources
Beta strandi287 – 2959Combined sources
Turni296 – 2994Combined sources
Beta strandi300 – 31112Combined sources
Helixi530 – 55627Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112009.
HOVERGENiHBG004335.
InParanoidiP09619.
KOiK05089.
OMAiAPYDNYV.
OrthoDBiEOG7GXP9Q.
PhylomeDBiP09619.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 3 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

        10         20         30         40         50
MRLPGAMPAL ALKGELLLLS LLLLLEPQIS QGLVVTPPGP ELVLNVSSTF
60 70 80 90 100
VLTCSGSAPV VWERMSQEPP QEMAKAQDGT FSSVLTLTNL TGLDTGEYFC
110 120 130 140 150
THNDSRGLET DERKRLYIFV PDPTVGFLPN DAEELFIFLT EITEITIPCR
160 170 180 190 200
VTDPQLVVTL HEKKGDVALP VPYDHQRGFS GIFEDRSYIC KTTIGDREVD
210 220 230 240 250
SDAYYVYRLQ VSSINVSVNA VQTVVRQGEN ITLMCIVIGN EVVNFEWTYP
260 270 280 290 300
RKESGRLVEP VTDFLLDMPY HIRSILHIPS AELEDSGTYT CNVTESVNDH
310 320 330 340 350
QDEKAINITV VESGYVRLLG EVGTLQFAEL HRSRTLQVVF EAYPPPTVLW
360 370 380 390 400
FKDNRTLGDS SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGHYTMRAFH
410 420 430 440 450
EDAEVQLSFQ LQINVPVRVL ELSESHPDSG EQTVRCRGRG MPQPNIIWSA
460 470 480 490 500
CRDLKRCPRE LPPTLLGNSS EEESQLETNV TYWEEEQEFE VVSTLRLQHV
510 520 530 540 550
DRPLSVRCTL RNAVGQDTQE VIVVPHSLPF KVVVISAILA LVVLTIISLI
560 570 580 590 600
ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL
610 620 630 640 650
VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS
660 670 680 690 700
ELKIMSHLGP HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF
710 720 730 740 750
LQHHSDKRRP PSAELYSNAL PVGLPLPSHV SLTGESDGGY MDMSKDESVD
760 770 780 790 800
YVPMLDMKGD VKYADIESSN YMAPYDNYVP SAPERTCRAT LINESPVLSY
810 820 830 840 850
MDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV KICDFGLARD
860 870 880 890 900
IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG
910 920 930 940 950
GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP
960 970 980 990 1000
FSQLVLLLER LLGEGYKKKY QQVDEEFLRS DHPAILRSQA RLPGFHGLRS
1010 1020 1030 1040 1050
PLDTSSVLYT AVQPNEGDND YIIPLPDPKP EVADEGPLEG SPSLASSTLN
1060 1070 1080 1090 1100
EVNTSSTISC DSPLEPQDEP EPEPQLELQV EPEPELEQLP DSGCPAPRAE

AEDSFL
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:
EMBLi
GenBanki
DDBJi
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. [P09619-1]
PIRiA28206. PFHUGB.
RefSeqiNP_002600.1. NM_002609.3. [P09619-1]
UniGeneiHs.509067.

Genome annotation databases

EnsembliENST00000261799; ENSP00000261799; ENSG00000113721. [P09619-1]
GeneIDi5159.
KEGGihsa:5159.
UCSCiuc003lro.3. human. [P09619-1]

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:
EMBLi
GenBanki
DDBJi
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. [P09619-1 ]
PIRi A28206. PFHUGB.
RefSeqi NP_002600.1. NM_002609.3. [P09619-1 ]
UniGenei Hs.509067.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 CHEMBL2095189.
DrugBanki DB00102. Becaplermin.
DB01254. Dasatinib.
DB00619. Imatinib.
DB06589. Pazopanib.
DB08896. Regorafenib.
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 . [P09619-1 ]
GeneIDi 5159.
KEGGi hsa:5159.
UCSCi uc003lro.3. human. [P09619-1 ]

Organism-specific databases

CTDi 5159.
GeneCardsi GC05M149494.
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.
GeneTreei ENSGT00760000118923.
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

Bgeei P09619.
CleanExi HS_PDGFRB.
ExpressionAtlasi P09619. baseline and differential.
Genevestigatori P09619.

Family and domain databases

Gene3Di 2.60.40.10. 3 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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 187 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