SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P01127

- PDGFB_HUMAN

UniProt

P01127 - PDGFB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Platelet-derived growth factor subunit B
Gene
PDGFB, PDGF2, SIS
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

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
Complete GO annotation...

GO - Biological processi

  1. DNA replication Source: Ensembl
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. actin cytoskeleton organization Source: Ensembl
  4. activation of protein kinase B activity Source: UniProtKB
  5. activation of protein kinase activity Source: UniProtKB
  6. blood coagulation Source: Reactome
  7. blood vessel morphogenesis Source: Ensembl
  8. branching involved in salivary gland morphogenesis Source: Ensembl
  9. cell chemotaxis Source: UniProtKB
  10. cell growth Source: Ensembl
  11. cell projection assembly Source: Ensembl
  12. cellular response to growth factor stimulus Source: BHF-UCL
  13. cellular response to mycophenolic acid Source: UniProtKB
  14. embryonic placenta development Source: UniProtKB
  15. epidermal growth factor receptor signaling pathway Source: Reactome
  16. epithelial cell proliferation involved in salivary gland morphogenesis Source: Ensembl
  17. extracellular matrix organization 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 DNA biosynthetic process Source: UniProtKB
  39. positive regulation of DNA replication Source: BHF-UCL
  40. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  41. positive regulation of MAP kinase activity Source: UniProtKB
  42. positive regulation of MAPK cascade Source: UniProtKB
  43. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  44. positive regulation of calcium ion import Source: UniProtKB
  45. positive regulation of cell division Source: UniProtKB-KW
  46. positive regulation of cell migration Source: UniProtKB
  47. positive regulation of cell proliferation Source: BHF-UCL
  48. positive regulation of chemotaxis Source: UniProtKB
  49. positive regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  50. positive regulation of endothelial cell proliferation Source: BHF-UCL
  51. positive regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
  52. positive regulation of fibroblast proliferation Source: UniProtKB
  53. positive regulation of glomerular filtration Source: UniProtKB
  54. positive regulation of glomerular mesangial cell proliferation Source: UniProtKB
  55. positive regulation of hyaluronan biosynthetic process 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
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_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. Golgi membrane Source: Reactome
  2. basolateral plasma membrane Source: UniProtKB
  3. cell surface Source: BHF-UCL
  4. cytoplasm Source: UniProtKB
  5. endoplasmic reticulum lumen Source: Reactome
  6. extracellular region Source: UniProtKB
  7. extracellular space Source: RefGenome
  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) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 – 2020
Add
BLAST
Propeptidei21 – 8161Removed in mature form
PRO_0000023371Add
BLAST
Chaini82 – 190109Platelet-derived growth factor subunit B
PRO_0000023372Add
BLAST
Propeptidei191 – 24151Removed in mature form
PRO_0000023373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi97 ↔ 1412 Publications
Disulfide bondi124 – 124Interchain2 Publications
Disulfide bondi130 ↔ 1782 Publications
Disulfide bondi133 – 133Interchain2 Publications
Disulfide bondi134 ↔ 1802 Publications

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.2 Publications

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

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.

Miscellaneous databases

EvolutionaryTraceiP01127.

Family & Domainsi

Sequence similaritiesi

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

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.
VSP_044913Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011T → E AA sequence 1 Publication
Sequence conflicti105 – 1051E → C AA sequence 1 Publication
Sequence conflicti107 – 1071S → C AA sequence 1 Publication

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...

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

« 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(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: September 3, 2014
This is version 178 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