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P01127 (PDGFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 177. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PDGFB
Synonyms:PDGF2, SIS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.19 Ref.24

Subcellular location

Secreted. Note: Released by platelets upon wounding.

Tissue specificity

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. Ref.20

Involvement in disease

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. Ref.21 Ref.25

A chromosomal aberration involving PDGFB is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGFB. Ref.21

Pharmaceutical use

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

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative promoter usage
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Proto-oncogene
   DomainSignal
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: Ensembl

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase B activity

Inferred from direct assay PubMed 16530387. Source: UniProtKB

activation of protein kinase activity

Inferred from direct assay PubMed 16530387. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

blood vessel morphogenesis

Inferred from electronic annotation. Source: Ensembl

branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell chemotaxis

Inferred from direct assay PubMed 16014047. Source: UniProtKB

cell growth

Inferred from electronic annotation. Source: Ensembl

cell projection assembly

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

cellular response to mycophenolic acid

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic placenta development

Inferred from sequence or structural similarity. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

epithelial cell proliferation involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

metanephric glomerular endothelium development

Inferred from electronic annotation. Source: Ensembl

metanephric glomerular mesangial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric glomerular mesangial cell proliferation involved in metanephros development

Inferred from electronic annotation. Source: Ensembl

monocyte chemotaxis

Inferred from direct assay PubMed 17991872. Source: BHF-UCL

negative regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of phosphatidylinositol biosynthetic process

Inferred from direct assay PubMed 2538439. Source: BHF-UCL

negative regulation of platelet activation

Inferred from direct assay PubMed 2538439. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16530387. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

paracrine signaling

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 16530387. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 10734101PubMed 16530387. Source: UniProtKB

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 21245381PubMed 2439522PubMed 2536956PubMed 2836953. Source: BHF-UCL

positive chemotaxis

Inferred from direct assay PubMed 21245381. Source: GOC

positive regulation of DNA biosynthetic process

Inferred from direct assay PubMed 10644978PubMed 10734101PubMed 11788434PubMed 12070119PubMed 16530387PubMed 17942966PubMed 19019919. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay PubMed 2439522PubMed 2836953. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 11788434PubMed 16530387PubMed 17942966. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 11788434PubMed 16530387PubMed 17942966. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from mutant phenotype PubMed 11788434. Source: UniProtKB

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 9685360. Source: BHF-UCL

positive regulation of calcium ion import

Inferred from direct assay PubMed 19019919. Source: UniProtKB

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell migration

Inferred from direct assay PubMed 11788434. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 2836953PubMed 7073684. Source: BHF-UCL

positive regulation of chemotaxis

Inferred from direct assay PubMed 19019919. Source: UniProtKB

positive regulation of cyclin-dependent protein kinase activity

Inferred from direct assay PubMed 16530387. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from direct assay PubMed 9685360. Source: BHF-UCL

positive regulation of fibroblast growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from direct assay PubMed 10644978PubMed 17324121. Source: UniProtKB

positive regulation of glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glomerular mesangial cell proliferation

Inferred from direct assay PubMed 11788434PubMed 16014047. Source: UniProtKB

positive regulation of hyaluronan biosynthetic process

Inferred from direct assay PubMed 17324121. Source: UniProtKB

positive regulation of metanephric mesenchymal cell migration

Inferred from direct assay PubMed 10734101. Source: UniProtKB

positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway

Inferred from direct assay PubMed 19019919. Source: UniProtKB

positive regulation of mitosis

Inferred from direct assay PubMed 10644978PubMed 10734101PubMed 17942966. Source: UniProtKB

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from direct assay PubMed 16530387. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 10734101PubMed 11788434PubMed 17942966. Source: UniProtKB

positive regulation of protein autophosphorylation

Inferred from direct assay PubMed 12070119PubMed 16530387. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from direct assay PubMed 16530387. Source: UniProtKB

positive regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 19019919. Source: UniProtKB

positive regulation of smooth muscle cell migration

Inferred from direct assay PubMed 12070119. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 12070119. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16530387PubMed 17324121. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 17942966. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 17942966. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to wounding

Non-traceable author statement Ref.18. Source: UniProtKB

substrate-dependent cell migration

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from direct assay PubMed 2538439PubMed 2836953PubMed 291037PubMed 9685360. Source: BHF-UCL

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement Ref.18. Source: UniProtKB

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionchemoattractant activity

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

collagen binding

Inferred from direct assay PubMed 8900172. Source: MGI

growth factor activity

Inferred from direct assay PubMed 12070119. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.23PubMed 7679113. Source: IntAct

platelet-derived growth factor binding

Inferred from physical interaction PubMed 7073684. Source: BHF-UCL

platelet-derived growth factor receptor binding

Non-traceable author statement Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12070119. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 7073684. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 2836953. Source: BHF-UCL

superoxide-generating NADPH oxidase activator activity

Inferred from direct assay PubMed 17942966. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: P01127-1)

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.
Isoform 2 (identifier: P01127-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Propeptide21 – 8161Removed in mature form
PRO_0000023371
Chain82 – 190109Platelet-derived growth factor subunit B
PRO_0000023372
Propeptide191 – 24151Removed in mature form
PRO_0000023373

Sites

Site1081Involved in receptor binding
Site1111Involved in receptor binding

Amino acid modifications

Disulfide bond97 ↔ 141 Ref.19 Ref.24
Disulfide bond124Interchain Ref.19 Ref.24
Disulfide bond130 ↔ 178 Ref.19 Ref.24
Disulfide bond133Interchain Ref.19 Ref.24
Disulfide bond134 ↔ 180 Ref.19 Ref.24

Natural variations

Alternative sequence1 – 2121MNRCW…LVSAE → MFIMGL in isoform 2.
VSP_044913
Natural variant91L → R in IBGC5. Ref.25
VAR_070870
Natural variant881I → V.
Corresponds to variant rs17565 [ dbSNP | Ensembl ].
VAR_014578
Natural variant1191L → P in IBGC5. Ref.25
VAR_070871

Experimental info

Sequence conflict1011T → E AA sequence Ref.16
Sequence conflict1051E → C AA sequence Ref.16
Sequence conflict1071S → C AA sequence Ref.16

Secondary structure

............. 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9F9A3474CE203C0B

FASTA24127,283
        10         20         30         40         50         60 
MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG DPGEEDGAEL 

        70         80         90        100        110        120 
DLNMTRSHSG GELESLARGR RSLGSLTIAE PAMIAECKTR TEVFEISRRL IDRTNANFLV 

       130        140        150        160        170        180 
WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC 

       190        200        210        220        230        240 
ETVAAARPVT RSPGGSQEQR AKTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG 


A 

« Hide

Isoform 2 [UniParc].

Checksum: 523AC7394E29C0D5
Show »

FASTA22625,502

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"PDGF D, a novel protease-activated growth factor."
LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A., Giese N.A., Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C., Burgess C.E., Fernandez E., Deegler L.L., Rittman B., Shimkets J., Shimkets R.A., Rothberg J.M., Lichenstein H.S.
Nat. Cell Biol. 3:517-521(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[21]"Dermatofibrosarcoma protuberans of breast."
Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.
Cancer Genet. Cytogenet. 142:56-59(2003) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in the gene encoding PDGF-B cause brain calcifications in humans and mice."
Keller A., Westenberger A., Sobrido M.J., Garcia-Murias M., Domingo A., Sears R.L., Lemos R.R., Ordonez-Ugalde A., Nicolas G., da Cunha J.E., Rushing E.J., Hugelshofer M., Wurnig M.C., Kaech A., Reimann R., Lohmann K., Dobricic V., Carracedo A. expand/collapse author list , Petrovic I., Miyasaki J.M., Abakumova I., Mae M.A., Raschperger E., Zatz M., Zschiedrich K., Klepper J., Spiteri E., Prieto J.M., Navas I., Preuss M., Dering C., Jankovic M., Paucar M., Svenningsson P., Saliminejad K., Khorshid H.R., Novakovic I., Aguzzi A., Boss A., Le Ber I., Defer G., Hannequin D., Kostic V.S., Campion D., Geschwind D.H., Coppola G., Betsholtz C., Klein C., Oliveira J.R.
Nat. Genet. 45:1077-1082(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBGC5 ARG-9 AND PRO-119.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01401 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS13987.1. [P01127-1]
CCDS33650.1. [P01127-2]
PIRPFHUG2. A94276.
RefSeqNP_002599.1. NM_002608.2. [P01127-1]
NP_148937.1. NM_033016.2. [P01127-2]
UniGeneHs.1976.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PDGX-ray3.00A/B/C82-190[»]
3MJGX-ray2.30A/B21-185[»]
4HQUX-ray2.20A82-190[»]
4HQXX-ray2.30A82-183[»]
ProteinModelPortalP01127.
SMRP01127. Positions 25-182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111181. 19 interactions.
DIPDIP-5737N.
IntActP01127. 6 interactions.
STRING9606.ENSP00000330382.

Chemistry

BindingDBP01127.
DrugBankDB00102. Becaplermin.

PTM databases

PhosphoSiteP01127.

Polymorphism databases

DMDM129724.

Proteomic databases

PaxDbP01127.
PRIDEP01127.

Protocols and materials databases

DNASU5155.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331163; ENSP00000330382; ENSG00000100311. [P01127-1]
ENST00000381551; ENSP00000370963; ENSG00000100311. [P01127-2]
GeneID5155.
KEGGhsa:5155.
UCSCuc003axe.3. human.
uc003axf.3. human. [P01127-1]

Organism-specific databases

CTD5155.
GeneCardsGC22M039619.
HGNCHGNC:8800. PDGFB.
HPACAB011604.
CAB018341.
HPA011972.
MIM190040. gene.
607907. phenotype.
615483. phenotype.
neXtProtNX_P01127.
Orphanet1980. Bilateral striopallidodentate calcinosis.
31112. Dermatofibrosarcoma protuberans.
263662. Familial multiple meningioma.
PharmGKBPA33145.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72843.
HOGENOMHOG000286027.
HOVERGENHBG053546.
InParanoidP01127.
KOK17386.
OMAHGDSVDE.
OrthoDBEOG78H3VV.
PhylomeDBP01127.
TreeFamTF319554.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP01127.

Gene expression databases

ArrayExpressP01127.
BgeeP01127.
CleanExHS_PDGFB.
GenevestigatorP01127.

Family and domain databases

Gene3D2.10.90.10. 1 hit.
InterProIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR006782. PDGF_N.
[Graphical view]
PfamPF00341. PDGF. 1 hit.
PF04692. PDGF_N. 1 hit.
[Graphical view]
SMARTSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMSSF57501. SSF57501. 1 hit.
PROSITEPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDGFB. human.
EvolutionaryTraceP01127.
GeneWikiPDGFB.
GenomeRNAi5155.
NextBio19940.
PMAP-CutDBP01127.
PROP01127.
SOURCESearch...

Entry information

Entry namePDGFB_HUMAN
AccessionPrimary (citable) accession number: P01127
Secondary accession number(s): G3XAG8 expand/collapse secondary AC list , P78431, Q15354, Q6FHE7, Q9UF23
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 177 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM