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Reviewed, UniProtKB/Swiss-Prot P01127 (PDGFB_HUMAN)

Last modified November 3, 2009. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Platelet-derived growth factor subunit B
      Short name=PDGF subunit B
Alternative name(s):
    Platelet-derived growth factor B chain
    Platelet-derived growth factor beta polypeptide
    PDGF-2
    c-sis
    INN=Becaplermin
Gene names
Name: PDGFB
Synonyms: PDGF2, SIS
OrganismHomo sapiens (Human) [Complete 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

Platelet-derived growth factor is a potent mitogen for cells of mesenchymal origin. Binding of this growth factor to its affinity receptor elicits a variety of cellular responses. It is released by platelets upon wounding and plays an important role in stimulating adjacent cells to grow and thereby heals the wound.

Subunit structure

Antiparallel disulfide-linked dimer of non-identical (A and B) chains. Homodimers of A and B chains are implicated in transformation processes. Interacts with XLKD1 By similarity.

Subcellular location

Secreted.

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.17

Involvement in disease

A chromosomal aberration involving PDGFB is a cause of dermatofibrosarcoma protuberans (DFSP) [MIM:607907]. Translocation t(17;22)(q22;q13) with COLA1. DFSP is an uncommon, locally aggressive, but rarely metastasizing tumor of the deep dermis and subcutaneous tissue. It typically occurs during early or middle adult life and is most frequently located on the trunk and proximal extremities. Ref.19

Pharmaceutical use

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

Miscellaneous

A-A and B-B, as well as A-B, dimers can bind to the PDGF receptor.

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainSignal
   Molecular functionGrowth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Gene Ontology (GO)
   Biological processmonocyte chemotaxis

Inferred from direct assay. Source: UniProtKB

negative regulation of phosphatidylinositol biosynthetic process

Inferred from direct assay. Source: UniProtKB

negative regulation of platelet activation

Inferred from direct assay. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay. Source: UniProtKB

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay. Source: UniProtKB

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of chemotaxis

Inferred from direct assay. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of smooth muscle cell migration

Inferred from direct assay. Source: UniProtKB

response to wounding Ref.15

Non-traceable author statement. Source: UniProtKB

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

extracellular region Ref.15

Non-traceable author statement. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: InterPro

platelet dense granule lumen

Inferred from Experiment. Source: Reactome

   Molecular functioncell surface binding

Inferred from direct assay. Source: UniProtKB

collagen binding

Inferred from direct assay. Source: MGI

growth factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

platelet-derived growth factor binding

Inferred from physical interaction. Source: UniProtKB

platelet-derived growth factor receptor binding Ref.15

Non-traceable author statement. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDGFRBP096191EBI-1554925,EBI-641237

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.16
Disulfide bond124Interchain Ref.16
Disulfide bond130 ↔ 178 Ref.16
Disulfide bond133Interchain Ref.16
Disulfide bond134 ↔ 180 Ref.16

Natural variations

Natural variant881I → V: dbSNP rs17565.
VAR_014578

Experimental info

Sequence conflict1011T → E AA sequence Ref.13
Sequence conflict1051E → C AA sequence Ref.13
Sequence conflict1071S → C AA sequence Ref.13

Secondary structure

............. 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01127-1 [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

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: 6740330] [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: 4033772] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2991848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 3472769] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 3517869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Lung, Pancreas and Testis.
[9]"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: 8988177] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, CHROMOSOMAL TRANSLOCATION WITH COL1A1.
[10]"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: 6327048] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-241.
[11]"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: 3456904] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-241.
[12]"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: 6306471] [Abstract]
Cited for: PROTEIN SEQUENCE OF 82-112.
[13]"Human platelet-derived growth factor (PDGF): amino-terminal amino acid sequence."
Antoniades H.N., Hunkapiller M.W.
Science 220:963-965(1983) [PubMed: 6844921] [Abstract]
Cited for: PROTEIN SEQUENCE OF 82-110.
[14]"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: 6329745] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-200, PARTIAL PROTEIN SEQUENCE.
[15]"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: 1661670] [Abstract]
Cited for: MUTAGENESIS, IMPORTANCE OF ARG-108 AND ILE-111 FOR RECEPTOR BINDING.
[16]"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: 1317862] [Abstract]
Cited for: INTERCHAIN DISULFIDE BONDS.
[17]"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: 11331882] [Abstract]
Cited for: TISSUE SPECIFICITY.
[18]"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: 1396586] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[19]"Dermatofibrosarcoma protuberans of breast."
Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.
Cancer Genet. Cytogenet. 142:56-59(2003) [PubMed: 12660034] [Abstract]
Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH COL1A1.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
BC029822 mRNA. Translation: AAH29822.1.
BC077725 mRNA. Translation: AAH77725.1.
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.
IPIIPI00000044.
PIRPFHUG2. A94276.
RefSeqNP_002599.1.
NP_148937.1.
UniGeneHs.1976

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PDGX-ray3.00A/B/C82-190[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5737N.
IntActP01127. 2 interactions.
STRINGP01127.

Proteomic databases

PRIDEP01127.

Genome annotation databases

EnsemblENST00000331163; ENSP00000330382; ENSG00000100311; Homo sapiens. [Genome view]
ENST00000381551; ENSP00000370963; ENSG00000100311; Homo sapiens. [Genome view]
ENST00000396740; ENSP00000379966; ENSG00000100311; Homo sapiens. [Genome view]
ENST00000423652; ENSP00000408574; ENSG00000100311; Homo sapiens. [Genome view]
ENST00000440375; ENSP00000405780; ENSG00000100311; Homo sapiens. [Genome view]
ENST00000455790; ENSP00000402306; ENSG00000100311; Homo sapiens. [Genome view]
GeneID5155.
KEGGhsa:5155.
UCSCuc003axf.1. human.

Organism-specific databases

CTD5155.
GeneCardsGC22M037944.
H-InvDBHIX0016487.
HGNCHGNC:8800. PDGFB.
HPACAB011604.
CAB018341.
HPA011972.
MIM190040. gene.
607907. phenotype.
Orphanet31112. Dermatofibrosarcoma protuberans.
PharmGKBPA33145.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP01127.
HOVERGENP01127.
OMACKCETVV.

Enzyme and pathway databases

Pathway_Interaction_DBpdgfrapathway. PDGFR-alpha signaling pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.
ReactomeREACT_16888. Signaling by PDGF.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP01127.
BgeeP01127.
CleanExHS_PDGFB.
GenevestigatorP01127.
GermOnlineENSG00000100311. Homo sapiens.

Family and domain databases

InterProIPR000072. PD_growth_factor.
IPR015583. PDGF_B.
IPR006782. PDGF_N.
[Graphical view]
PANTHERPTHR11633:SF2. PDGF_B. 1 hit.
PfamPF00341. PDGF. 1 hit.
PF04692. PDGF_N. 1 hit.
[Graphical view]
ProDomPD001629. PD_growth_factor. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00141. PDGF. 1 hit.
[Graphical view]
PROSITEPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00102. Becaplermin.
NextBio19940.
PMAP-CutDBP01127.
SOURCESearch...

Entry information

Entry namePDGFB_HUMAN
AccessionPrimary (citable) accession number: P01127
Secondary accession number(s): P78431, Q9UF23
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 3, 2009
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents