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Protein

Platelet-derived growth factor subunit B

Gene

PDGFB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 heterodimerization activity Source: BHF-UCL
  8. protein homodimerization activity Source: BHF-UCL
  9. 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 migration Source: UniProtKB
  41. positive regulation of cell proliferation Source: BHF-UCL
  42. positive regulation of chemotaxis Source: UniProtKB
  43. positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  44. positive regulation of DNA biosynthetic process Source: UniProtKB
  45. positive regulation of DNA replication Source: BHF-UCL
  46. positive regulation of endothelial cell proliferation Source: BHF-UCL
  47. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  48. positive regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
  49. positive regulation of fibroblast proliferation Source: UniProtKB
  50. positive regulation of glomerular filtration Source: UniProtKB
  51. positive regulation of glomerular mesangial cell proliferation Source: UniProtKB
  52. positive regulation of hyaluronan biosynthetic process Source: UniProtKB
  53. positive regulation of MAPK cascade Source: UniProtKB
  54. positive regulation of MAP kinase activity Source: UniProtKB
  55. positive regulation of metanephric mesenchymal cell migration Source: UniProtKB
  56. positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  57. positive regulation of mitotic cell cycle, embryonic Source: Ensembl
  58. positive regulation of mitotic nuclear division 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
Complete GO annotation...

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_318. Platelet degranulation.
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 Componenti: 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: GO_Central
  7. Golgi membrane Source: Reactome
  8. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Basal ganglia calcification, idiopathic, 5 (IBGC5)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:615483
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.

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

BgeeiP01127.
CleanExiHS_PDGFB.
ExpressionAtlasiP01127. baseline and differential.
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. 20 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 – 1059Combined sources
Helixi108 – 1114Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi123 – 1319Combined sources
Beta strandi140 – 15920Combined sources
Beta strandi162 – 18120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00510000046755.
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. AlignAdd to basket

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

        10         20         30         40         50
MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG
60 70 80 90 100
DPGEEDGAEL DLNMTRSHSG GELESLARGR RSLGSLTIAE PAMIAECKTR
110 120 130 140 150
TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP
160 170 180 190 200
VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETVAAARPVT RSPGGSQEQR
210 220 230 240
AKTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG A
Length:241
Mass (Da):27,283
Last modified:July 20, 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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi111181. 20 interactions.
DIPiDIP-5737N.
IntActiP01127. 6 interactions.
STRINGi9606.ENSP00000330382.

Chemistry

BindingDBiP01127.
ChEMBLiCHEMBL3108633.

PTM databases

PhosphoSiteiP01127.

Polymorphism databases

DMDMi129724.

Proteomic databases

PaxDbiP01127.
PRIDEiP01127.

Protocols and materials databases

DNASUi5155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5155.
GeneCardsiGC22M039619.
HGNCiHGNC:8800. PDGFB.
HPAiCAB011604.
CAB018341.
HPA011972.
MIMi190040. gene.
607907. phenotype.
615483. phenotype.
neXtProtiNX_P01127.
Orphaneti1980. Bilateral striopallidodentate calcinosis.
31112. Dermatofibrosarcoma protuberans.
263662. Familial multiple meningioma.
PharmGKBiPA33145.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG72843.
GeneTreeiENSGT00510000046755.
HOGENOMiHOG000286027.
HOVERGENiHBG053546.
InParanoidiP01127.
KOiK17386.
OMAiHGDSVDE.
OrthoDBiEOG78H3VV.
PhylomeDBiP01127.
TreeFamiTF319554.

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_318. Platelet degranulation.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiP01127.

Miscellaneous databases

ChiTaRSiPDGFB. human.
EvolutionaryTraceiP01127.
GeneWikiiPDGFB.
GenomeRNAii5155.
NextBioi19940.
PMAP-CutDBP01127.
PROiP01127.
SOURCEiSearch...

Gene expression databases

BgeeiP01127.
CleanExiHS_PDGFB.
ExpressionAtlasiP01127. baseline and differential.
GenevestigatoriP01127.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1983) [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(1984) [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(1984) [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(1985) [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(1985) [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 (MAY-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(1998) [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(2003) [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(1994) [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(1996) [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(1983) [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(1985) [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(1982) [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(1982) [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(1983) [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(1990) [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(1991) [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(2007) [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(1991) [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(2009) [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 20, 1986
Last sequence update: July 20, 1986
Last modified: March 31, 2015
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.