HBEGF

HBEGF (Heparin Binding EGF Like Growth Factor) is a Protein Coding gene. Diseases associated with HBEGF include Diphtheria and Bladder Disease. Among its related pathways are RET signaling and Apoptotic Pathways in Synovial Fibroblasts. Gene Ontology (GO) annotations related to this gene include growth factor activity and epidermal growth factor receptor binding. An important paralog of this gene is AREG.

heparin-binding EGF-like growth factor

Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.

Cell chemotaxis Source: UniProtKB
Epidermal growth factor receptor signaling pathway Source: BHF-UCL
Muscle organ development Source: ProtInc
Negative regulation of elastin biosynthetic process Source: Ensembl
Positive regulation of cell growth Source: Ensembl
Positive regulation of cell migration Source: BHF-UCL
Positive regulation of cell population proliferation Source: GO_Central
Positive regulation of epidermal growth factor-activated receptor activity Source: GO_Central
Positive regulation of keratinocyte migration Source: Ensembl
Positive regulation of protein kinase B signaling Source: BHF-UCL
Positive regulation of smooth muscle cell proliferation Source: Ensembl
Positive regulation of wound healing Source: BHF-UCL
Regulation of heart contraction Source: Ensembl
Signal transduction Source: ProtInc
Wound healing, spreading of epidermal cells Source: Ensembl

Heparin-binding EGF-like growth factor: Extracellular space. Mature HB-EGF is released into the extracellular space and probably binds to a receptor.
Proheparin-binding EGF-like growth factor: Cell membrane

Extracellular: 20-160
Helical: 161-184
Cytoplasmic: 185-208

Several N-termini have been identified by direct sequencing. The forms with N-termini 63, 73 and 74 have been tested and found to be biologically active.
O-glycosylated with core 1 or possibly core 8 glycans. Thr-47 is a minor glycosylation site compared to Thr-44.