Primary information |
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ID | 33043 |
Uniprot ID | Q15303 |
Description | Receptor tyrosine-protein kinase erbB-4 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-4) (Tyrosine kinase-type cell surface receptor HER4) (p180erbB4) [Cleaved into- ERBB4 intracellular domain (4I |
Organism | Homo sapiens |
Txonomy | Homo ; Homininae ; Hominidae ; Hominoidea ; Catarrhini ; Simiiformes ; Haplorrhini ; Primates ; Euarchontoglires ; Boreoeutheria ; Eutheria ; Theria ; Mammalia ; Amniota ; Tetrapoda ; Dipnotetrapodomorpha ; Sarcopterygii ; Euteleostomi ; Teleostomi ; Gnathostomata ; Vertebrata ; Craniata ; Chordata ; Deuterostomia ; Bilateria ; Eumetazoa ; Metazoa ; Opisthokonta ; Eukaryota ; cellular organisms |
Subcellular Location | Cell membrane |
Developmental Stage | NA |
Similarity | NA |
Post Translational Modification | Isoform JM-A CYT-1 and isoform JM-A CYT-2 are processed by ADAM17. Proteolytic processing in response to ligand or 12-O-tetradecanoylphorbol-13-acetate stimulation results in the production of 120 kDa soluble receptor forms and intermediate membrane-anchored 80 kDa fragments (m80HER4); which are further processed by a presenilin-dependent gamma-secretase to release a cytoplasmic intracellular domain (E4ICD; E4ICD1/s80Cyt1 or E4ICD2/s80Cyt2; depending on the isoform). Membrane-anchored 80 kDa fra |
Function | Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart; the central nervous system and the mammary gland; gene transcription; cell proliferation; differentiation; migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development; and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system; especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation; induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1; NRG2; NRG3 and NRG4 and the EGF family members BTC; EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alter |
Length | 1308 |
Molecular Weight | 146808 |
Reference | 8383326; 9334263; 15 |
Hormone | NA |
PDB ID | NA
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