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P01127

- PDGFB_HUMAN

UniProt

P01127 - PDGFB_HUMAN

Protein

Platelet-derived growth factor subunit B

Gene

PDGFB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei108 – 1081Involved in receptor binding
    Sitei111 – 1111Involved in receptor binding

    GO - Molecular functioni

    1. chemoattractant activity Source: BHF-UCL
    2. collagen binding Source: MGI
    3. growth factor activity Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. platelet-derived growth factor binding Source: BHF-UCL
    6. platelet-derived growth factor receptor binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein heterodimerization activity Source: BHF-UCL
    9. protein homodimerization activity Source: BHF-UCL
    10. superoxide-generating NADPH oxidase activator activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. activation of protein kinase activity Source: UniProtKB
    3. activation of protein kinase B activity Source: UniProtKB
    4. blood coagulation Source: Reactome
    5. blood vessel morphogenesis Source: Ensembl
    6. branching involved in salivary gland morphogenesis Source: Ensembl
    7. cell chemotaxis Source: UniProtKB
    8. cell growth Source: Ensembl
    9. cell projection assembly Source: Ensembl
    10. cellular response to growth factor stimulus Source: BHF-UCL
    11. cellular response to mycophenolic acid Source: UniProtKB
    12. DNA replication Source: Ensembl
    13. embryonic placenta development Source: UniProtKB
    14. epidermal growth factor receptor signaling pathway Source: Reactome
    15. epithelial cell proliferation involved in salivary gland morphogenesis Source: Ensembl
    16. extracellular matrix organization Source: Reactome
    17. Fc-epsilon receptor signaling pathway Source: Reactome
    18. fibroblast growth factor receptor signaling pathway Source: Reactome
    19. heart development Source: UniProtKB
    20. innate immune response Source: Reactome
    21. metanephric glomerular endothelium development Source: Ensembl
    22. metanephric glomerular mesangial cell development Source: UniProtKB
    23. metanephric glomerular mesangial cell proliferation involved in metanephros development Source: Ensembl
    24. monocyte chemotaxis Source: BHF-UCL
    25. negative regulation of cell migration Source: Ensembl
    26. negative regulation of phosphatidylinositol biosynthetic process Source: BHF-UCL
    27. negative regulation of platelet activation Source: BHF-UCL
    28. negative regulation of transcription, DNA-templated Source: UniProtKB
    29. neurotrophin TRK receptor signaling pathway Source: Reactome
    30. paracrine signaling Source: UniProtKB
    31. peptidyl-serine phosphorylation Source: UniProtKB
    32. peptidyl-tyrosine phosphorylation Source: UniProtKB
    33. phosphatidylinositol-mediated signaling Source: Reactome
    34. platelet activation Source: Reactome
    35. platelet degranulation Source: Reactome
    36. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
    37. positive chemotaxis Source: GOC
    38. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
    39. positive regulation of calcium ion import Source: UniProtKB
    40. positive regulation of cell division Source: UniProtKB-KW
    41. positive regulation of cell migration Source: UniProtKB
    42. positive regulation of cell proliferation Source: BHF-UCL
    43. positive regulation of chemotaxis Source: UniProtKB
    44. positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    45. positive regulation of DNA biosynthetic process Source: UniProtKB
    46. positive regulation of DNA replication Source: BHF-UCL
    47. positive regulation of endothelial cell proliferation Source: BHF-UCL
    48. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    49. positive regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
    50. positive regulation of fibroblast proliferation Source: UniProtKB
    51. positive regulation of glomerular filtration Source: UniProtKB
    52. positive regulation of glomerular mesangial cell proliferation Source: UniProtKB
    53. positive regulation of hyaluronan biosynthetic process Source: UniProtKB
    54. positive regulation of MAPK cascade Source: UniProtKB
    55. positive regulation of MAP kinase activity Source: UniProtKB
    56. positive regulation of metanephric mesenchymal cell migration Source: UniProtKB
    57. positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
    58. positive regulation of mitosis Source: UniProtKB
    59. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    60. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    61. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    62. positive regulation of protein autophosphorylation Source: UniProtKB
    63. positive regulation of protein tyrosine kinase activity Source: UniProtKB
    64. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    65. positive regulation of smooth muscle cell migration Source: UniProtKB
    66. positive regulation of smooth muscle cell proliferation Source: UniProtKB
    67. positive regulation of transcription, DNA-templated Source: UniProtKB
    68. protein phosphorylation Source: UniProtKB
    69. reactive oxygen species metabolic process Source: UniProtKB
    70. response to drug Source: Ensembl
    71. response to estradiol Source: Ensembl
    72. response to hypoxia Source: Ensembl
    73. response to insulin Source: Ensembl
    74. response to wounding Source: UniProtKB
    75. substrate-dependent cell migration Source: Ensembl
    76. transforming growth factor beta receptor signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Growth factor, Mitogen

    Enzyme and pathway databases

    ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_16888. Signaling by PDGF.
    REACT_17025. Downstream signal transduction.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiP01127.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-derived growth factor subunit B
    Short name:
    PDGF subunit B
    Alternative name(s):
    PDGF-2
    Platelet-derived growth factor B chain
    Platelet-derived growth factor beta polypeptide
    Proto-oncogene c-Sis
    INN: Becaplermin
    Gene namesi
    Name:PDGFB
    Synonyms:PDGF2, SIS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:8800. PDGFB.

    Subcellular locationi

    Secreted
    Note: Released by platelets upon wounding.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB
    2. cell surface Source: BHF-UCL
    3. cytoplasm Source: UniProtKB
    4. endoplasmic reticulum lumen Source: Reactome
    5. extracellular region Source: UniProtKB
    6. extracellular space Source: RefGenome
    7. Golgi membrane Source: Reactome
    8. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Basal ganglia calcification, idiopathic, 5 (IBGC5) [MIM:615483]: 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 varianti9 – 91L → R in IBGC5. 1 Publication
    VAR_070870
    Natural varianti119 – 1191L → P in IBGC5. 1 Publication
    VAR_070871
    A chromosomal aberration involving PDGFB is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGFB.1 Publication

    Pharmaceutical usei

    Available under the name Regranex (Ortho-McNeil). Used to promote healing in diabetic neuropathic foot ulcers.

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi607907. phenotype.
    615483. phenotype.
    Orphaneti1980. Bilateral striopallidodentate calcinosis.
    31112. Dermatofibrosarcoma protuberans.
    263662. Familial multiple meningioma.
    PharmGKBiPA33145.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Propeptidei21 – 8161Removed in mature formPRO_0000023371Add
    BLAST
    Chaini82 – 190109Platelet-derived growth factor subunit BPRO_0000023372Add
    BLAST
    Propeptidei191 – 24151Removed in mature formPRO_0000023373Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi97 ↔ 1411 Publication
    Disulfide bondi124 – 124Interchain1 Publication
    Disulfide bondi130 ↔ 1781 Publication
    Disulfide bondi133 – 133Interchain1 Publication
    Disulfide bondi134 ↔ 1801 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PaxDbiP01127.
    PRIDEiP01127.

    PTM databases

    PhosphoSiteiP01127.

    Miscellaneous databases

    PMAP-CutDBP01127.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the heart, brain (sustantia nigra), placenta and fetal kidney. Expressed at moderate levels in the brain (hippocampus), skeletal muscle, kidney and lung.1 Publication

    Gene expression databases

    ArrayExpressiP01127.
    BgeeiP01127.
    CleanExiHS_PDGFB.
    GenevestigatoriP01127.

    Organism-specific databases

    HPAiCAB011604.
    CAB018341.
    HPA011972.

    Interactioni

    Subunit structurei

    Homodimer; antiparallel disulfide-linked dimer. Heterodimer with PDGFA; antiparallel disulfide-linked dimer. The PDGFB homodimer interacts with PDGFRA and PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB interacts with PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts with XLKD1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1554925,EBI-1554925
    PDGFRAP1623411EBI-1554925,EBI-2861522
    PDGFRBP0961913EBI-1554925,EBI-641237

    Protein-protein interaction databases

    BioGridi111181. 19 interactions.
    DIPiDIP-5737N.
    IntActiP01127. 6 interactions.
    STRINGi9606.ENSP00000330382.

    Structurei

    Secondary structure

    1
    241
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi97 – 1059
    Helixi108 – 1114
    Beta strandi118 – 1214
    Beta strandi123 – 1319
    Beta strandi140 – 15920
    Beta strandi162 – 18120

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PDGX-ray3.00A/B/C82-190[»]
    3MJGX-ray2.30A/B21-185[»]
    4HQUX-ray2.20A82-190[»]
    4HQXX-ray2.30A82-183[»]
    ProteinModelPortaliP01127.
    SMRiP01127. Positions 25-182.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01127.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PDGF/VEGF growth factor family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG72843.
    HOGENOMiHOG000286027.
    HOVERGENiHBG053546.
    InParanoidiP01127.
    KOiK17386.
    OMAiHGDSVDE.
    OrthoDBiEOG78H3VV.
    PhylomeDBiP01127.
    TreeFamiTF319554.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    InterProiIPR029034. Cystine-knot_cytokine.
    IPR023581. PD_growth_factor_CS.
    IPR000072. PDGF/VEGF_dom.
    IPR006782. PDGF_N.
    [Graphical view]
    PfamiPF00341. PDGF. 1 hit.
    PF04692. PDGF_N. 1 hit.
    [Graphical view]
    SMARTiSM00141. PDGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    PROSITEiPS00249. PDGF_1. 1 hit.
    PS50278. PDGF_2. 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 promoter usage. Align

    Isoform 1 (identifier: P01127-1) [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

    MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG    50
    DPGEEDGAEL DLNMTRSHSG GELESLARGR RSLGSLTIAE PAMIAECKTR 100
    TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP 150
    VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETVAAARPVT RSPGGSQEQR 200
    AKTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG A 241
    Length:241
    Mass (Da):27,283
    Last modified:July 21, 1986 - v1
    Checksum:i9F9A3474CE203C0B
    GO
    Isoform 2 (identifier: P01127-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MNRCWALFLSLCCYLRLVSAE → MFIMGL

    Show »
    Length:226
    Mass (Da):25,502
    Checksum:i523AC7394E29C0D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011T → E AA sequence (PubMed:6844921)Curated
    Sequence conflicti105 – 1051E → C AA sequence (PubMed:6844921)Curated
    Sequence conflicti107 – 1071S → C AA sequence (PubMed:6844921)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91L → R in IBGC5. 1 Publication
    VAR_070870
    Natural varianti88 – 881I → V.
    Corresponds to variant rs17565 [ dbSNP | Ensembl ].
    VAR_014578
    Natural varianti119 – 1191L → P in IBGC5. 1 Publication
    VAR_070871

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121MNRCW…LVSAE → MFIMGL in isoform 2. 1 PublicationVSP_044913Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01401
    , K01918, J00121, K01398, K01399, K01400 Genomic DNA. Translation: AAA60552.1.
    X02811 mRNA. Translation: CAA26579.1.
    X02744 mRNA. Translation: CAA26524.1.
    M12783 mRNA. Translation: AAA60553.1.
    CR456538 mRNA. Translation: CAG30424.1.
    Z81010 Genomic DNA. Translation: CAB02635.1.
    Z81010 Genomic DNA. Translation: CAP58849.1.
    CR541807 mRNA. Translation: CAG46606.1.
    CH471095 Genomic DNA. Translation: EAW60306.1.
    CH471095 Genomic DNA. Translation: EAW60307.1.
    BC029822 mRNA. Translation: AAH29822.1.
    BC077725 mRNA. Translation: AAH77725.1.
    X83705 mRNA. Translation: CAA58679.1.
    X98706 Genomic DNA. Translation: CAA67262.1.
    K01917
    , K01913, K01914, K01915, K01916 Genomic DNA. Translation: AAA98793.1.
    X03702 mRNA. Translation: CAA27333.1.
    X00561 Genomic DNA. Translation: CAA25228.1.
    X00561 Genomic DNA. Translation: CAA25229.1.
    CCDSiCCDS13987.1. [P01127-1]
    CCDS33650.1. [P01127-2]
    PIRiA94276. PFHUG2.
    RefSeqiNP_002599.1. NM_002608.2. [P01127-1]
    NP_148937.1. NM_033016.2. [P01127-2]
    UniGeneiHs.1976.

    Genome annotation databases

    EnsembliENST00000331163; ENSP00000330382; ENSG00000100311. [P01127-1]
    ENST00000381551; ENSP00000370963; ENSG00000100311. [P01127-2]
    GeneIDi5155.
    KEGGihsa:5155.
    UCSCiuc003axe.3. human.
    uc003axf.3. human. [P01127-1]

    Polymorphism databases

    DMDMi129724.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    R&D Systems' cytokine source book: PDGF
    Regranex

    Clinical information on Regranex

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01401
    , K01918 , J00121 , K01398 , K01399 , K01400 Genomic DNA. Translation: AAA60552.1 .
    X02811 mRNA. Translation: CAA26579.1 .
    X02744 mRNA. Translation: CAA26524.1 .
    M12783 mRNA. Translation: AAA60553.1 .
    CR456538 mRNA. Translation: CAG30424.1 .
    Z81010 Genomic DNA. Translation: CAB02635.1 .
    Z81010 Genomic DNA. Translation: CAP58849.1 .
    CR541807 mRNA. Translation: CAG46606.1 .
    CH471095 Genomic DNA. Translation: EAW60306.1 .
    CH471095 Genomic DNA. Translation: EAW60307.1 .
    BC029822 mRNA. Translation: AAH29822.1 .
    BC077725 mRNA. Translation: AAH77725.1 .
    X83705 mRNA. Translation: CAA58679.1 .
    X98706 Genomic DNA. Translation: CAA67262.1 .
    K01917
    , K01913 , K01914 , K01915 , K01916 Genomic DNA. Translation: AAA98793.1 .
    X03702 mRNA. Translation: CAA27333.1 .
    X00561 Genomic DNA. Translation: CAA25228.1 .
    X00561 Genomic DNA. Translation: CAA25229.1 .
    CCDSi CCDS13987.1. [P01127-1 ]
    CCDS33650.1. [P01127-2 ]
    PIRi A94276. PFHUG2.
    RefSeqi NP_002599.1. NM_002608.2. [P01127-1 ]
    NP_148937.1. NM_033016.2. [P01127-2 ]
    UniGenei Hs.1976.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PDG X-ray 3.00 A/B/C 82-190 [» ]
    3MJG X-ray 2.30 A/B 21-185 [» ]
    4HQU X-ray 2.20 A 82-190 [» ]
    4HQX X-ray 2.30 A 82-183 [» ]
    ProteinModelPortali P01127.
    SMRi P01127. Positions 25-182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111181. 19 interactions.
    DIPi DIP-5737N.
    IntActi P01127. 6 interactions.
    STRINGi 9606.ENSP00000330382.

    Chemistry

    BindingDBi P01127.
    DrugBanki DB00102. Becaplermin.

    PTM databases

    PhosphoSitei P01127.

    Polymorphism databases

    DMDMi 129724.

    Proteomic databases

    PaxDbi P01127.
    PRIDEi P01127.

    Protocols and materials databases

    DNASUi 5155.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331163 ; ENSP00000330382 ; ENSG00000100311 . [P01127-1 ]
    ENST00000381551 ; ENSP00000370963 ; ENSG00000100311 . [P01127-2 ]
    GeneIDi 5155.
    KEGGi hsa:5155.
    UCSCi uc003axe.3. human.
    uc003axf.3. human. [P01127-1 ]

    Organism-specific databases

    CTDi 5155.
    GeneCardsi GC22M039619.
    HGNCi HGNC:8800. PDGFB.
    HPAi CAB011604.
    CAB018341.
    HPA011972.
    MIMi 190040. gene.
    607907. phenotype.
    615483. phenotype.
    neXtProti NX_P01127.
    Orphaneti 1980. Bilateral striopallidodentate calcinosis.
    31112. Dermatofibrosarcoma protuberans.
    263662. Familial multiple meningioma.
    PharmGKBi PA33145.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72843.
    HOGENOMi HOG000286027.
    HOVERGENi HBG053546.
    InParanoidi P01127.
    KOi K17386.
    OMAi HGDSVDE.
    OrthoDBi EOG78H3VV.
    PhylomeDBi P01127.
    TreeFami TF319554.

    Enzyme and pathway databases

    Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_16888. Signaling by PDGF.
    REACT_17025. Downstream signal transduction.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki P01127.

    Miscellaneous databases

    ChiTaRSi PDGFB. human.
    EvolutionaryTracei P01127.
    GeneWikii PDGFB.
    GenomeRNAii 5155.
    NextBioi 19940.
    PMAP-CutDB P01127.
    PROi P01127.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01127.
    Bgeei P01127.
    CleanExi HS_PDGFB.
    Genevestigatori P01127.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR023581. PD_growth_factor_CS.
    IPR000072. PDGF/VEGF_dom.
    IPR006782. PDGF_N.
    [Graphical view ]
    Pfami PF00341. PDGF. 1 hit.
    PF04692. PDGF_N. 1 hit.
    [Graphical view ]
    SMARTi SM00141. PDGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00249. PDGF_1. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transforming potential of human c-sis nucleotide sequences encoding platelet-derived growth factor."
      Josephs S.F., Ratner L., Clarke M.F., Westin E.H., Reitz M.S., Wong-Staal F.
      Science 225:636-639(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cultured human endothelial cells express platelet-derived growth factor B chain: cDNA cloning and structural analysis."
      Collins T., Ginsburg D., Boss J.M., Orkin S.H., Pober J.S.
      Nature 316:748-750(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Nucleotide sequence of transforming human c-sis cDNA clones with homology to platelet-derived growth factor."
      Ratner L., Josephs S.F., Jarrett R., Reitz M.S., Wong-Staal F.
      Nucleic Acids Res. 13:5007-5018(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Oncogenic potential of the human platelet-derived growth factor transcriptional unit."
      Rao C.D., Igarashi H., Pech M.W., Robbins K.C., Aaronson S.A.
      Cold Spring Harb. Symp. Quant. Biol. 51:959-966(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Structure and sequence of the human c-sis/platelet-derived growth factor 2 (SIS/PDGF2) transcriptional unit."
      Rao C.D., Igarashi H., Chiu I.-M., Robbins K.C., Aaronson S.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:2392-2396(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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).
      Tissue: Brain, Lung, Pancreas and Testis.
    11. "A novel human c-sis mRNA species is transcribed from a promoter in c-sis intron 1 and contains the code for an alternative PDGF B-like protein."
      Dirks R.P.H., Onnekink C., Jansen H.J., de Jong A., Bloemers H.P.J.
      Nucleic Acids Res. 23:2815-2822(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-185 (ISOFORM 2).
      Tissue: Choriocarcinoma.
    12. "Deregulation of the platelet-derived growth factor B-chain gene via fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell fibroblastoma."
      Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F., Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N., Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C., Dumanski J.P.
      Nat. Genet. 15:95-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, CHROMOSOMAL TRANSLOCATION WITH COL1A1.
    13. "Nucleotide sequence analysis identifies the human c-sis proto-oncogene as a structural gene for platelet-derived growth factor."
      Chiu I.-M., Reddy E.P., Givol D., Robbins K.C., Tronick S.R., Aaronson S.A.
      Cell 37:123-129(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-241.
    14. "The human osteosarcoma cell line U-2 OS expresses a 3.8 kilobase mRNA which codes for the sequence of the PDGF-B chain."
      Weich H.A., Sebald W., Schairer H.U., Hoppe J.
      FEBS Lett. 198:344-348(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-241 (ISOFORM 1).
    15. "Platelet-derived growth factor is structurally related to the putative transforming protein p28sis of simian sarcoma virus."
      Waterfield M.D., Scrace G.T., Whittle N., Stroobant P., Johnsson A., Wasteson A., Westermark B., Heldin C.H., Huang J.S., Deuel T.F.
      Nature 304:35-39(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 82-112.
    16. "Human platelet-derived growth factor (PDGF): amino-terminal amino acid sequence."
      Antoniades H.N., Hunkapiller M.W.
      Science 220:963-965(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 82-110.
    17. "The c-sis gene encodes a precursor of the B chain of platelet-derived growth factor."
      Johnsson A., Heldin C.H., Wasteson A., Westermark B., Deuel T.F., Huang J.S., Seeburg P.H., Gray A., Ullrich A., Scrace G., Stroobant P., Waterfield M.D.
      EMBO J. 3:921-928(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-200, PARTIAL PROTEIN SEQUENCE.
    18. "Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation."
      Clements J.M., Bawden L.J., Bloxidge R.E., Catlin G., Cook A.L., Craig S., Drummond A.H., Edwards R.M., Fallon A., Green D.R., Hellewell P.G., Kirwin P.M., Nayee P.D., Richardson S.J., Brown D., Chahwala S.B., Snarey M., Winslow D.
      EMBO J. 10:4113-4120(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS, IMPORTANCE OF ARG-108 AND ILE-111 FOR RECEPTOR BINDING.
    19. "Assignment of interchain disulfide bonds in platelet-derived growth factor (PDGF) and evidence for agonist activity of monomeric PDGF."
      Andersson M., Oestman A., Baeckstroem G., Hellman U., George-Nascimento C., Westermark B., Heldin C.-H.
      J. Biol. Chem. 267:11260-11266(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERCHAIN DISULFIDE BONDS.
    20. Cited for: TISSUE SPECIFICITY.
    21. Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH COL1A1.
    22. "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 IN DEVELOPMENT AND DISEASE.
    23. "Crystal structure of human platelet-derived growth factor BB."
      Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M.
      EMBO J. 11:3921-3926(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    24. "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 21-185 IN COMPLEX WITH PDGFRB, SUBUNIT, DISULFIDE BONDS.
    25. Cited for: VARIANTS IBGC5 ARG-9 AND PRO-119.

    Entry informationi

    Entry nameiPDGFB_HUMAN
    AccessioniPrimary (citable) accession number: P01127
    Secondary accession number(s): G3XAG8
    , P78431, Q15354, Q6FHE7, Q9UF23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 179 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, Pharmaceutical, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3