Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
EGF (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
EGF EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4); also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Hormone; Membrane protein, integral; Ligand, receptor tyrosine kinase
Cellular Component: extracellular space; membrane; lysosomal membrane; integral to membrane; plasma membrane; intracellular
Molecular Function: protein binding; growth factor activity; calcium ion binding; epidermal growth factor receptor binding
Biological Process: epidermal growth factor receptor signaling pathway; peptidyl-tyrosine phosphorylation; positive regulation of mitosis; activation of MAPKK activity; positive regulation of transcription, DNA-dependent; regulation of protein transport; positive regulation of MAP kinase activity; regulation of protein secretion; positive regulation of epidermal growth factor receptor activity; branching morphogenesis of a tube; positive regulation of cell proliferation; negative regulation of secretion; angiogenesis; regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphorylation; STAT protein nuclear translocation; positive regulation of DNA binding; positive regulation of granule cell precursor proliferation
Reference #:  P01132 (UniProtKB)
Alt. Names/Synonyms: Egf; epidermal growth factor
Gene Symbols: Egf
Molecular weight: 133,072 Da
Basal Isoelectric point: 6.02  Predict pI for various phosphorylation states
CST Pathways:  ErbB/HER Signaling  |  IL6 Signaling
Select Structure to View Below

EGF

Protein Structure Not Found.


STRING  |  Reactome  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 1 S268 FGDRIFYSVLKSKAI
0 1 K284 IANKHTGKDTVRINL
0 1 M302 FVTPGKLMVVHPRAQ
0 1 S354 CAEGYTLSRDRKYCE
0 1 S645-p DRVLIASsNLLEPSG
0 1 Y1184 GNSHLPSYRPVGPEK
  human

 
S262-p FGDRIFYsTWKMKTI
K278-ub IANKHTGkDMVRINL
K296-ub FVPLGELkVVHPLAQ
S348-p CAEGYALsRDRKYCE
S639 GRLVIASSDLIWPSG
Y1170-p RSFHMPSyGTQTLEG
  rat

 
S263 FGDKILYSALKEKAI
K279 IADKHTGKNVVRVNL
R297 SVPPRELRVVHLHAQ
S349 CAEGYTLSRDRKYCE
S641 DRTLIASSNLLEPSG
- gap
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.