receptor tyrosine-protein kinase erbB-4; p180erbB4; tyrosine kinase-type cell surface receptor HER4 (ERBB4, HER4)

Function: - specifically binds & is activated by neuregulins, NRG-2, NRG-3, heparin-binding EGF-like growth factor, betacellulin & NTAK - interaction with ligand induces cell differentiation - ligand-binding increases Tyr phosphorylation - not activated by EGF, TGF-A, & amphiregulin - isoform JM-A is cleaved but not isoform JM-B is not - interacts with PDZ domains of DLG2, DLG3, DLG4 & the syntrophin SNTB2 - interacts with CBFA2T3, MUC1 & WWOX Structure: - homodimer or heterodimer with each of the other ERBB receptors (putative). - WW-binding motifs mediate interaction with WWOX - belongs to the protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily - contains 1 protein kinase domain Compartment: membrane Alternative splicing: named isoforms=3; JM-A, JM-B Expression: - expressed in brain, heart, kidney, skeletal muscle, parathyroid, cerebellum, pituitary, spleen, testis & breast > thymus, lung, salivary gland, & pancreas - isoform JM-A & isoform JM-B are expressed in cerebellum - only the isoform JM-B is expressed in the heart

Related

HER4/ERB-B4 Ag in tissue her4/erb-B4 proto-oncogene

Properties

SIZE: entity length = 1308 aa MW = 147 kD COMPARTMENT: cellular membrane STATE: active state MOTIF: signal sequence {1-25} cysteine residue {C29} MODIFICATION: cysteine residue {C56} cysteine residue {C56} MODIFICATION: cysteine residue {C29} N-glycosylation site {N138} cysteine residue {C156} MODIFICATION: cysteine residue {C186} N-glycosylation site {N174} N-glycosylation site {N181} cysteine-rich region {186-334} MOTIF: cysteine residue {C186} MODIFICATION: cysteine residue {C156} cysteine residue {C189} MODIFICATION: cysteine residue {C197} cysteine residue {C193} MODIFICATION: cysteine residue {C205} cysteine residue {C197} MODIFICATION: cysteine residue {C189} cysteine residue {C205} MODIFICATION: cysteine residue {C193} cysteine residue {C213} MODIFICATION: cysteine residue {C221} cysteine residue {C217} MODIFICATION: cysteine residue {C229} cysteine residue {C221} MODIFICATION: cysteine residue {C213} cysteine residue {C229} MODIFICATION: cysteine residue {C217} cysteine residue {C230} MODIFICATION: cysteine residue {C238} cysteine residue {C234} MODIFICATION: cysteine residue {C246} cysteine residue {C238} MODIFICATION: cysteine residue {C230} cysteine residue {C246} MODIFICATION: cysteine residue {C234} cysteine residue {C249} MODIFICATION: cysteine residue {C258} N-glycosylation site {N253} cysteine residue {C258} MODIFICATION: cysteine residue {C249} cysteine residue {C262} MODIFICATION: cysteine residue {C289} cysteine residue {C289} MODIFICATION: cysteine residue {C262} cysteine residue {C293} MODIFICATION: cysteine residue {C304} cysteine residue {C304} MODIFICATION: cysteine residue {C293} cysteine residue {C308} MODIFICATION: cysteine residue {C323} cysteine residue {C323} MODIFICATION: cysteine residue {C308} cysteine residue {C326} MODIFICATION: cysteine residue {C330} cysteine residue {C330} MODIFICATION: cysteine residue {C326} N-glycosylation site {N358} N-glycosylation site {N410} N-glycosylation site {N473} N-glycosylation site {N495} cysteine-rich region {496-633} MOTIF: cysteine residue {C503} MODIFICATION: cysteine residue {C512} cysteine residue {C507} MODIFICATION: cysteine residue {C520} cysteine residue {C512} MODIFICATION: cysteine residue {C503} cysteine residue {C520} MODIFICATION: cysteine residue {C507} cysteine residue {C523} MODIFICATION: cysteine residue {C532} cysteine residue {C532} MODIFICATION: cysteine residue {C523} cysteine residue {C536} MODIFICATION: cysteine residue {C552} N-glycosylation site {N548} cysteine residue {C552} MODIFICATION: cysteine residue {C536} cysteine residue {C555} MODIFICATION: cysteine residue {C569} cysteine residue {C559} MODIFICATION: cysteine residue {C577} cysteine residue {C569} MODIFICATION: cysteine residue {C555} N-glycosylation site {N576} cysteine residue {C577} MODIFICATION: cysteine residue {C559} cysteine residue {C580} MODIFICATION: cysteine residue {C589} cysteine residue {C589} MODIFICATION: cysteine residue {C580} cysteine residue {C593} MODIFICATION: cysteine residue {C614} cysteine residue {C614} MODIFICATION: cysteine residue {C593} cysteine residue {C617} MODIFICATION: cysteine residue {C625} N-glycosylation site {N620} cysteine residue {C621} MODIFICATION: cysteine residue {C633} cysteine residue {C625} MODIFICATION: cysteine residue {C617} cysteine residue {C633} MODIFICATION: cysteine residue {C621} transmembrane domain {652-675} kinase domain SITE: 718-985 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 724-732 Tyr phosphorylation site {Y733} ATP-binding site NAME: ATP-binding site SITE: 751-751 aspartate residue {D843} WW-binding 1 {1032-1035} Tyr phosphorylation site {Y1162} Tyr phosphorylation site {Y1188} Tyr phosphorylation site {Y1258} Tyr phosphorylation site {Y1284} WW-binding 2 {1298-1301} PDZ recognition motif NAME: PDZ recognition motif SITE: 1306-1308 FOR-BINDING-VIA: PDZ domain

Database Correlations

OMIM 600543 UniProt Q15303 PFAM correlations Entrez Gene 2066 Kegg hsa:2066

References

UniProt :accession Q15303