human ERBB4 Adenovirus

ALS19; avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4; ERBB4 transcript variant I12DEL; ERBB4 transcript variant I20DEL; HER4; human epidermal growth factor receptor 4; p180erbB4; proto-oncogene-like protein c-ErbB-4; receptor tyrosine-protein kinase erbB-4; tyrosine kinase-type cell surface receptor HER4; v-erb-a erythroblastic leukemia viral oncogene homolog 4; v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4

ErbB4 is a member of the receptor tyrosine kinase family of proteins. The four members of this family are ErbB1 (Epidermal growth factor receptor; EGFR/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4). The ErbB receptor members are single-pass transmembrane proteins with an extracellular ligand-binding domain and a cytoplasmic tyrosine-kinase domain. The epidermal growth factor (EGF) and its related proteins serve as the ligands for the ErbB receptors. Upon binding, the receptors homo- or heterodimerize, autophosphorylate and make contact with adapter molecules to transmit cellular signals involved in cell proliferation, survival, and differentiation. The ligands preferred by ErbB4 include neuregulins (NRG-2 and NRG-3), heparin-binding EGF-like growth factor, and betacellulin, and epiregulin. ErbB4 appears to be important to mammary gland development and lactation; however its role in breast cancer has not been unequivocally determined.

ERBB4 is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.

2066

erb-b2 receptor tyrosine kinase 4

erb-b2 receptor tyrosine kinase 4

ERBB4

HGNC:3432

9606.0

3897

3897 bp

Receptor tyrosine-protein kinase erbB-4

NM_005235

NM_005235, NM_001042599, BC143749, BC143747, BC143741, BC112199,

Amyotrophic Lateral Sclerosis (ALS),Apoptosis,B-cell Receptor Signaling,Breast Cancer,Cancer,Cardiac Development,Cardiology,Cardiovascular,EGFR Signaling,EGFR Signaling in Cancer,Fc Receptor Signaling,FGF Signaling,Immunology,Innate Immunity,JAK-STAT Signaling,Kinase/Phosphatase,Metabolism/Metabolic Process,Mitochondrion,Neurobiology,Neurodegeneration,Neurodevelopment,NGF Signaling,PDGF Signaling,PI3K/Akt Signaling,PI3K-AKT Signaling in Cancer,Prolactin Signaling,SCF-KIT Signaling,Signal Transduction,Transcription Factor/Regulator,Tumor Suppressors/Oncoproteins

cancer,cardiovascular,cell_biology,developmental_biology,immunology,metabolism,neurobiology,signal_transduction,stem_cell_biology,transcription_translation

human

ErbB4 is a member of the receptor tyrosine kinase family of proteins. The four members of this family are ErbB1 (Epidermal growth factor receptor; EGFR/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4). The ErbB receptor members are single-pass transmembrane proteins with an extracellular ligand-binding domain and a cytoplasmic tyrosine-kinase domain. The epidermal growth factor (EGF) and its related proteins serve as the ligands for the ErbB receptors. Upon binding, the receptors homo- or heterodimerize, autophosphorylate and make contact with adapter molecules to transmit cellular signals involved in cell proliferation, survival, and differentiation. The ligands preferred by ErbB4 include neuregulins (NRG-2 and NRG-3), heparin-binding EGF-like growth factor, and betacellulin, and epiregulin. ErbB4 appears to be important to mammary gland development and lactation; however its role in breast cancer has not been unequivocally determined.

Hs.390729

Q15303