Epidermal growth factor information

EGF
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1IVO, 1JL9, 1NQL, 1P9J, 2KV4, 3NJP
Identifiers
Aliases	EGF, HOMG4, URG, epidermal growth factor, epithelial growth factor
External IDs	OMIM: 131530 MGI: 95290 HomoloGene: 1483 GeneCards: EGF
Gene location (Human)
Chr.	Chromosome 4 (human)
End	110,013,766 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	129,548,965 bp
RNA expression pattern
	Top expressed in
	renal medulla; ; body of pancreas; ; kidney; ; kidney tubule; ; gastrocnemius muscle; ; biceps brachii; ; deltoid muscle; ; vastus lateralis muscle; ; secondary oocyte; ; metanephric glomerulus;
	Top expressed in
	submandibular gland; ; kidney; ; parotid gland; ; prostate; ; extensor digitorum longus muscle; ; plantaris muscle; ; vastus lateralis muscle; ; lacrimal gland; ; triceps brachii muscle; ; digastric muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	calcium ion binding; transmembrane receptor protein tyrosine kinase activator activity; epidermal growth factor receptor binding; Wnt-protein binding; protein binding; growth factor activity; Wnt-activated receptor activity; protein tyrosine kinase activity; phosphatidylinositol-4,5-bisphosphate 3-kinase activity;
Cellular component	integral component of membrane; membrane; receptor complex; extracellular region; lysosomal membrane; extracellular exosome; platelet alpha granule lumen; extracellular space; clathrin-coated vesicle membrane; plasma membrane;
Biological process	negative regulation of epidermal growth factor receptor signaling pathway; positive regulation of MAP kinase activity; epidermal growth factor receptor signaling pathway; regulation of protein localization to cell surface; ERK1 and ERK2 cascade; platelet degranulation; regulation of calcium ion import; mammary gland alveolus development; MAPK cascade; DNA replication; positive regulation of transcription, DNA-templated; negative regulation of secretion; positive regulation of hyaluronan biosynthetic process; positive regulation of peptidyl-threonine phosphorylation; positive regulation of ubiquitin-dependent protein catabolic process; angiogenesis; Wnt signaling pathway involved in dorsal/ventral axis specification; positive regulation of cell population proliferation; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of cerebellar granule cell precursor proliferation; canonical Wnt signaling pathway; negative regulation of cholesterol efflux; peptidyl-tyrosine phosphorylation; positive regulation of DNA binding; positive regulation of phosphorylation; positive regulation of mitotic nuclear division; branching morphogenesis of an epithelial tube; signal transduction; regulation of peptidyl-tyrosine phosphorylation; ERBB2 signaling pathway; phosphatidylinositol phosphate biosynthetic process; positive regulation of protein tyrosine kinase activity; activation of transmembrane receptor protein tyrosine kinase activity; regulation of cell motility; positive regulation of receptor internalization; positive regulation of epidermal growth factor-activated receptor activity; membrane organization; negative regulation of ERBB signaling pathway; embryonic retina morphogenesis in camera-type eye; positive regulation of gene expression; positive regulation of cell migration; positive regulation of protein kinase B signaling; negative regulation of Notch signaling pathway; regulation of receptor signaling pathway via JAK-STAT; positive regulation of canonical Wnt signaling pathway; positive regulation of protein localization to early endosome;
	Sources:Amigo / QuickGO
Orthologs
	1950
	13645
	ENSG00000138798
	ENSMUSG00000028017
	P01133
	P01132
	NM_001178130; NM_001178131; NM_001963; NM_001357021
	NM_010113; NM_001310737; NM_001329594
	NP_001171601; NP_001171602; NP_001954; NP_001343950
	NP_001297666; NP_001316523; NP_034243
	Wikidata
View/Edit Human	View/Edit Mouse

Epidermal growth factor (EGF) is a protein that stimulates cell growth and differentiation by binding to its receptor, EGFR. Human EGF is 6-kDa^[5] and has 53 amino acid residues and three intramolecular disulfide bonds.^[6]

EGF was originally described as a secreted peptide found in the submaxillary glands of mice and in human urine. EGF has since been found in many human tissues, including platelets,^[7] submandibular gland (submaxillary gland),^[8] and parotid gland.^[8] Initially, human EGF was known as urogastrone.^[9]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138798 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028017 – 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.
^ Harris RC, Chung E, Coffey RJ (March 2003). "EGF receptor ligands". Experimental Cell Research. 284 (1): 2–13. doi:10.1016/S0014-4827(02)00105-2. PMID 12648462.
^ Carpenter G, Cohen S (May 1990). "Epidermal growth factor". The Journal of Biological Chemistry. 265 (14): 7709–12. doi:10.1016/S0021-9258(19)38983-5. PMID 2186024.
^ Custo, S; Baron, B; Felice, A; Seria, E (5 July 2022). "A comparative profile of total protein and six angiogenically-active growth factors in three platelet products". GMS Interdisciplinary Plastic and Reconstructive Surgery DGPW. 11 (Doc06): Doc06. doi:10.3205/iprs000167. PMC 9284722. PMID 35909816.
^ ^a ^b Cite error: The named reference Venturi2009 was invoked but never defined (see the help page).
^ Hollenberg MD, Gregory H (May 1980). "Epidermal growth factor-urogastrone: biological activity and receptor binding of derivatives". Molecular Pharmacology. 17 (3): 314–20. PMID 6248761.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000138798 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028017 – 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.

[pmid12648462-5] Harris RC, Chung E, Coffey RJ (March 2003). "EGF receptor ligands". Experimental Cell Research. 284 (1): 2–13. doi:10.1016/S0014-4827(02)00105-2. PMID 12648462.

[pmid2186024-6] Carpenter G, Cohen S (May 1990). "Epidermal growth factor". The Journal of Biological Chemistry. 265 (14): 7709–12. doi:10.1016/S0021-9258(19)38983-5. PMID 2186024.

[Custo-7] Custo, S; Baron, B; Felice, A; Seria, E (5 July 2022). "A comparative profile of total protein and six angiogenically-active growth factors in three platelet products". GMS Interdisciplinary Plastic and Reconstructive Surgery DGPW. 11 (Doc06): Doc06. doi:10.3205/iprs000167. PMC 9284722. PMID 35909816.

[Venturi2009-8] Cite error: The named reference Venturi2009 was invoked but never defined (see the help page).

[:0-9] Hollenberg MD, Gregory H (May 1980). "Epidermal growth factor-urogastrone: biological activity and receptor binding of derivatives". Molecular Pharmacology. 17 (3): 314–20. PMID 6248761.

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