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; OMA:PDGFB - orthologs
Gene location (Human)
Chr.	Chromosome 22 (human)
End	39,244,982 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	80,014,977 bp
RNA expression pattern
	Top expressed in
	olfactory bulb; ; apex of heart; ; 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;
	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]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100311 – Ensembl, May 2017
^ ^a ^b ^c 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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100311 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000000489 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2991848-5] 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.

[pmid1661670-6] 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.

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