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receptor tyrosine-protein kinase erbB-3; c-erbB3; tyrosine kinase-type cell surface receptor HER3 (ERBB3, HER3)
Function:
- binds & is activated by neuregulins & NTAK
- heterodimer with each of the other ERBB receptors (putative)
- interacts with CSPG5, PA2G4 & MUC1
- ligand-binding increases phosphorylation on Tyr & promotes its association with the p85 subunit of phosphatidylinositol 3-kinase (putative)
Structure:
- cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins
- belongs to the protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily
- contains 1 protein kinase domain
Compartment:
- isoform 1: cell membrane
- isoform 2: secreted
Alternative splicing: named isoforms=2
Expression: epithelial tissues & brain
Pathology:
- overexpressed in a subset of human mammary tumors
- defects in ERBB3 are the cause of lethal congenital contracture syndrome type 2
Related
erb-B3 proto-oncogene
HER3/ERB-B3 Ag in tissue
General
EGF receptor family protein or erbB proto-oncogene protein
Properties
SIZE: entity length = 1342 aa
MW = 148 kD
COMPARTMENT: plasma membrane
STATE: active state
MOTIF: signal sequence {1-19}
cysteine residue {C29}
MODIFICATION: cysteine residue {C56}
cysteine residue {C56}
MODIFICATION: cysteine residue {C29}
N-glycosylation site {N126}
cysteine residue {C156}
MODIFICATION: cysteine residue {C183}
cysteine residue {C183}
MODIFICATION: cysteine residue {C156}
cysteine residue {C186}
MODIFICATION: cysteine residue {C194}
cysteine residue {C190}
MODIFICATION: cysteine residue {C202}
cysteine residue {C194}
MODIFICATION: cysteine residue {C186}
cysteine residue {C202}
MODIFICATION: cysteine residue {C190}
cysteine residue {C210}
MODIFICATION: cysteine residue {C218}
cysteine residue {C214}
MODIFICATION: cysteine residue {C226}
cysteine residue {C218}
MODIFICATION: cysteine residue {C210}
cysteine residue {C226}
MODIFICATION: cysteine residue {C214}
cysteine residue {C227}
MODIFICATION: cysteine residue {C235}
cysteine residue {C231}
MODIFICATION: cysteine residue {C243}
cysteine residue {C235}
MODIFICATION: cysteine residue {C227}
cysteine residue {C243}
MODIFICATION: cysteine residue {C231}
cysteine residue {C246}
MODIFICATION: cysteine residue {C255}
N-glycosylation site {N250}
cysteine residue {C255}
MODIFICATION: cysteine residue {C246}
cysteine residue {C259}
MODIFICATION: cysteine residue {C286}
cysteine residue {C286}
MODIFICATION: cysteine residue {C259}
cysteine residue {C290}
MODIFICATION: cysteine residue {C301}
cysteine residue {C301}
MODIFICATION: cysteine residue {C290}
cysteine residue {C305}
MODIFICATION: cysteine residue {C320}
cysteine residue {C320}
MODIFICATION: cysteine residue {C305}
cysteine residue {C323}
MODIFICATION: cysteine residue {C327}
cysteine residue {C327}
MODIFICATION: cysteine residue {C323}
N-glycosylation site {N353}
N-glycosylation site {N408}
N-glycosylation site {N414}
N-glycosylation site {N437}
N-glycosylation site {N469}
cysteine residue {C500}
MODIFICATION: cysteine residue {C509}
cysteine residue {C504}
MODIFICATION: cysteine residue {C517}
cysteine residue {C509}
MODIFICATION: cysteine residue {C500}
cysteine residue {C517}
MODIFICATION: cysteine residue {C504}
cysteine residue {C520}
MODIFICATION: cysteine residue {C529}
N-glycosylation site {N522}
cysteine residue {C529}
MODIFICATION: cysteine residue {C520}
cysteine residue {C533}
MODIFICATION: cysteine residue {C549}
cysteine residue {C549}
MODIFICATION: cysteine residue {C533}
cysteine residue {C552}
MODIFICATION: cysteine residue {C565}
cysteine residue {C556}
MODIFICATION: cysteine residue {C573}
cysteine residue {C565}
MODIFICATION: cysteine residue {C552}
N-glycosylation site {N566}
cysteine residue {C573}
MODIFICATION: cysteine residue {C556}
cysteine residue {C576}
MODIFICATION: cysteine residue {C585}
cysteine residue {C585}
MODIFICATION: cysteine residue {C576}
cysteine residue {C589}
MODIFICATION: cysteine residue {C610}
cysteine residue {C610}
MODIFICATION: cysteine residue {C589}
cysteine residue {C613}
MODIFICATION: cysteine residue {C621}
N-glycosylation site {N616}
cysteine residue {C617}
MODIFICATION: cysteine residue {C629}
cysteine residue {C621}
MODIFICATION: cysteine residue {C613}
cysteine residue {C629}
MODIFICATION: cysteine residue {C617}
transmembrane domain {644-664}
kinase domain
SITE: 709-966
MOTIF: ATP-binding site
NAME: ATP-binding site
SITE: 715-723
ATP-binding site
NAME: ATP-binding site
SITE: 742-742
asparagine residue {N834}
Tyr phosphorylation site {Y1328}
Database Correlations
OMIM correlations
UniProt P21860
PFAM correlations
Entrez Gene 2065
Kegg hsa:2065
ENZYME 2.7.10.1
References
UniProt :accession P21860