human ERBB2 Adenovirus

CD antigen CD340; CD340; c-erb B2/neu protein; HER2; HER-2; HER-2/neu; herstatin; human epidermal growth factor receptor 2; metastatic lymph node gene 19 protein; MLN 19; NEU; neuro/glioblastoma derived oncogene homolog; neuroblastoma/glioblastoma derived oncogene homolog; NGL; p185erbB2; proto-oncogene c-ErbB-2; proto-oncogene Neu; receptor tyrosine-protein kinase erbB-2; TKR1; tyrosine kinase-type cell surface receptor HER2; v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 2; v-erb-b2 avian erythroblastic leukemia viral oncoprotein 2; v-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog

ErbB2 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 heterodimerize, autophosphorylate and make contact with adapter molecules to transmit cellular signals involved in cell proliferation, survival, and differentiation. The ErbB2 receptor is the only member that does not interact with a ligand, but instead functions as a heterodimeric partner to coordinate signals from other ligand bound ErbB receptors. Amplification and/or overexpression of ErbB2 have been reported in many cancers.

ERBB2 encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized.

2064

erb-b2 receptor tyrosine kinase 2

erb-b2 receptor tyrosine kinase 2

ERBB2

HGNC:3430

9606.0

3768

3768 bp

Receptor tyrosine-protein kinase erbB-2

NM_004448

NM_004448, NM_001289938, NM_001289937, NM_001289936, NM_001005862, BC167147, BC156755,

Angiogenesis,Apoptosis,Axon Guidance,B-cell Receptor Signaling,Bladder Cancer,Breast Cancer,Cancer,Cardiac Development,Cardiology,Cardiovascular,DNA Damage/Repair,EGFR Signaling,EGFR Signaling in Cancer,Fc Receptor Signaling,FGF Signaling,Glioma,HIF-1 Signaling,Immunology,Innate Immunity,Interleukin Signaling,Kinase/Phosphatase,Leptin Signaling,Lung Cancer,MAPK Signaling,MicroRNAs in Cancer,Neurobiology,Neurodevelopment,NGF Signaling,PDGF Signaling,PI3K/Akt Signaling,PI3K-AKT Signaling in Cancer,Prolactin Signaling,Prostate Cancer,RNA Binding,SCF-KIT Signaling,Signal Transduction,Transcription Factor/Regulator,Translational Control,Transport,Tumor Suppressors/Oncoproteins

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

human

ErbB2 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 heterodimerize, autophosphorylate and make contact with adapter molecules to transmit cellular signals involved in cell proliferation, survival, and differentiation. The ErbB2 receptor is the only member that does not interact with a ligand, but instead functions as a heterodimeric partner to coordinate signals from other ligand bound ErbB receptors. Amplification and/or overexpression of ErbB2 have been reported in many cancers.

Hs.446352

P04626