PDGFB

PDGFB
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1PDG, 3MJG, 4HQU, 4HQX, 4QCI
Identifiers
Aliases	PDGFB, IBGC5, PDGF-2, PDGF2, SIS, SSV, c-sis, platelet derived growth factor subunit B
External IDs	OMIM: 190040 MGI: 97528 HomoloGene: 74303 GeneCards: PDGFB
Gene location (Human)
Chr.	Chromosome 22 (human)[1]
End	39,244,982 bp[1]
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)[2]
End	80,014,977 bp[2]
RNA expression pattern
	Top expressed in
	olfactory bulb; ; pancreatic ductal cell; ; right lung; ; vena cava; ; subcutaneous adipose tissue; ; triceps brachii muscle; ; left ventricle; ; upper lobe of left lung; ; right lobe of thyroid gland; ; parotid gland;
	Top expressed in
	triceps brachii muscle; ; left lung; ; right lung; ; digastric muscle; ; left lung lobe; ; vastus lateralis muscle; ; sternocleidomastoid muscle; ; ankle; ; temporal muscle; ; right ventricle;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	protein homodimerization activity; protein heterodimerization activity; chemoattractant activity; platelet-derived growth factor receptor binding; platelet-derived growth factor binding; superoxide-generating NADPH oxidase activator activity; growth factor activity; identical protein binding; collagen binding; protein binding; phosphatidylinositol-4,5-bisphosphate 3-kinase activity;
Cellular component	platelet alpha granule lumen; cytoplasm; extracellular region; Golgi membrane; basolateral plasma membrane; cell surface; endoplasmic reticulum lumen; membrane; extracellular matrix; extracellular space; Golgi lumen; collagen-containing extracellular matrix;
Biological process	activation of protein kinase B activity; positive regulation of DNA biosynthetic process; positive regulation of chemotaxis; cellular response to growth factor stimulus; positive regulation of protein tyrosine kinase activity; peptidyl-tyrosine phosphorylation; positive regulation of cell division; heart development; positive regulation of glomerular filtration; positive regulation of mitotic nuclear division; positive regulation of MAP kinase activity; positive regulation of metanephric mesenchymal cell migration; positive regulation of hyaluronan biosynthetic process; MAPK cascade; protein phosphorylation; positive regulation of glomerular mesangial cell proliferation; cellular response to mycophenolic acid; positive regulation of fibroblast proliferation; activation of protein kinase activity; multicellular organism development; positive regulation of protein autophosphorylation; positive regulation of reactive oxygen species metabolic process; reactive oxygen species metabolic process; negative regulation of transcription, DNA-templated; protein kinase C signaling; metanephric glomerular mesangial cell development; negative regulation of phosphatidylinositol biosynthetic process; response to wounding; positive regulation of phosphatidylinositol 3-kinase activity; cell chemotaxis; positive regulation of ERK1 and ERK2 cascade; platelet degranulation; positive regulation of cell population proliferation; positive regulation of DNA replication; positive regulation of gene expression; embryonic placenta development; paracrine signaling; monocyte chemotaxis; positive regulation of endothelial cell proliferation; positive regulation of phosphatidylinositol 3-kinase signaling; positive regulation of calcium ion import; positive regulation of transcription, DNA-templated; peptidyl-serine phosphorylation; positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; positive regulation of blood vessel endothelial cell migration; hemopoiesis; positive regulation of cell migration; positive regulation of peptidyl-tyrosine phosphorylation; extracellular matrix organization; negative regulation of protein binding; positive regulation of MAPK cascade; positive regulation of cyclin-dependent protein serine/threonine kinase activity; negative regulation of platelet activation; phosphatidylinositol phosphate biosynthetic process; positive regulation of vascular associated smooth muscle cell migration; positive chemotaxis; negative regulation of vascular associated smooth muscle cell differentiation; interleukin-18-mediated signaling pathway; positive regulation of pri-miRNA transcription by RNA polymerase II; negative regulation of pri-miRNA transcription by RNA polymerase II; negative regulation of gene expression; positive regulation of smooth muscle cell migration; positive regulation of smooth muscle cell proliferation; positive regulation of vascular associated smooth muscle cell dedifferentiation; platelet-derived growth factor receptor signaling pathway; positive regulation of vascular associated smooth muscle cell proliferation; negative regulation of platelet-derived growth factor receptor-beta signaling pathway; regulation of signaling receptor activity; positive regulation of protein kinase B signaling;
	Sources:Amigo / QuickGO
Orthologs
	5155
	18591
	ENSG00000100311
	ENSMUSG00000000489
	P01127
	P31240
	NM_033016; NM_002608
	NM_011057
	NP_002599; NP_148937
	NP_035187
	Wikidata
View/Edit Human	View/Edit Mouse

Platelet-derived growth factor subunit B is a protein that in humans is encoded by the PDGFB gene.[5][6]

Function

The protein encoded by this gene is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha (PDGFA) polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds.

Clinical significance

Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 17, at sites where the PDGFB and COL1A1 genes are respectively located or, alternatively, an abnormal small supernumerary ring chromosome merge these two genes to form a COL1A-PDGFB fusion gene. This fusion gene greatly overproduces PDGFB and is considered responsible for causing the development and/or progression of three closely related fibroblastic and myofibroblastic tumors of the skin: giant cell fibroblastoma, dermatofibrosarcoma protuberans, and dermatofibrosarcoma protuberans, sarcomatous.[7]

Two splice variants have been identified for the PDGFB gene.[8]

References

GRCh38: Ensembl release 89: ENSG00000100311 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000000489 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Ratner L, Josephs SF, Jarrett R, Reitz MS, Wong-Staal F (Sep 1985). "Nucleotide sequence of transforming human c-sis cDNA clones with homology to platelet-derived growth factor". Nucleic Acids Res. 13 (14): 5007–18. doi:10.1093/nar/13.14.5007. PMC 321845. PMID 2991848.
Clements JM, Bawden LJ, Bloxidge RE, Catlin G, Cook AL, Craig S, Drummond AH, Edwards RM, Fallon A, Green DR (Jan 1992). "Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor binding and activation". EMBO J. 10 (13): 4113–20. doi:10.1002/j.1460-2075.1991.tb04988.x. PMC 453161. PMID 1661670.
Baranov E, Hornick JL (March 2020). "Soft Tissue Special Issue: Fibroblastic and Myofibroblastic Neoplasms of the Head and Neck". Head and Neck Pathology. 14 (1): 43–58. doi:10.1007/s12105-019-01104-3. PMC 7021862. PMID 31950474.
"Entrez Gene: PDGFB platelet-derived growth factor beta polypeptide (simian sarcoma viral (v-sis) oncogene homolog)".

PDGFB

Function

Clinical significance

See also

References

Further reading