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V-erb-b2 erythroblastic leukemia viral oncogene homolog 3 (avian)

PDB rendering based on 1m6b.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols ERBB3 ; ErbB-3; HER3; LCCS2; MDA-BF-1; c-erbB-3; c-erbB3; erbB3-S; p180-ErbB3; p45-sErbB3; p85-sErbB3
External IDs OMIM190151 MGI95411 HomoloGene20457 ChEMBL: 5838 GeneCards: ERBB3 Gene
EC number
RNA expression pattern
PBB GE ERBB3 202454 s at tn.png
More reference expression data
Species Human Mouse
Entrez 2065 13867
Ensembl ENSG00000065361 ENSMUSG00000018166
UniProt P21860 Q61526
RefSeq (mRNA) NM_001005915 NM_010153
RefSeq (protein) NP_001005915 NP_034283
Location (UCSC) Chr 12:
56.47 – 56.5 Mb
Chr 10:
128.57 – 128.59 Mb
PubMed search [1] [2]

Receptor tyrosine-protein kinase erbB-3 is an enzyme that in humans is encoded by the ERBB3 gene.

This gene encodes a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound protein has a neuregulin binding domain but not an active kinase domain. It therefore can bind this ligand but not convey the signal into the cell through protein phosphorylation. However, it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers, including prostate, bladder, and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. One isoform lacks the intramembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported, but they have not been thoroughly characterized.[1]

It is thought that ERBB3, when activated, becomes a substrate for dimerization and subsequent phosphorylation by ERBB1, ERBB2 and ERBB4.

Like many of the receptor tyrosine-kinases, ERBB3 is activated by extracellular ligand. Ligands known to bind to ERBB3 include heregulin.


ERBB3 has been shown to interact with Neuregulin 1,[2][3][4] PA2G4,[5][6] PIK3R1[7][8] and RGS4.[9]

See also[edit]


  1. ^ "Entrez Gene: ERBB3 v-erb-b2 erythroblastic leukemia viral oncogene homolog 3 (avian)". 
  2. ^ Singer, E; Landgraf R, Horan T, Slamon D, Eisenberg D (November 2001). "Identification of a heregulin binding site in HER3 extracellular domain". J. Biol. Chem. (United States) 276 (47): 44266–74. doi:10.1074/jbc.M105428200. ISSN 0021-9258. PMID 11555649. 
  3. ^ Horan, T; Wen J, Arakawa T, Liu N, Brankow D, Hu S, Ratzkin B, Philo J S (October 1995). "Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3". J. Biol. Chem. (UNITED STATES) 270 (41): 24604–8. doi:10.1074/jbc.270.41.24604. ISSN 0021-9258. PMID 7592681. 
  4. ^ Carraway, K L; Weber J L, Unger M J, Ledesma J, Yu N, Gassmann M, Lai C (May 1997). "Neuregulin-2, a new ligand of ErbB3/ErbB4-receptor tyrosine kinases". Nature (ENGLAND) 387 (6632): 512–6. doi:10.1038/387512a0. ISSN 0028-0836. PMID 9168115. 
  5. ^ Lessor, T J; Hamburger A W (April 2001). "Regulation of the ErbB3 binding protein Ebp1 by protein kinase C". Mol. Cell. Endocrinol. (Ireland) 175 (1–2): 185–91. doi:10.1016/S0303-7207(01)00387-2. ISSN 0303-7207. PMID 11325528. 
  6. ^ Yoo, J Y; Wang X W, Rishi A K, Lessor T, Xia X M, Gustafson T A, Hamburger A W (February 2000). "Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin". Br. J. Cancer (SCOTLAND) 82 (3): 683–90. doi:10.1054/bjoc.1999.0981. ISSN 0007-0920. PMC 2363329. PMID 10682683. 
  7. ^ Hellyer, N J; Kim M S, Koland J G (November 2001). "Heregulin-dependent activation of phosphoinositide 3-kinase and Akt via the ErbB2/ErbB3 co-receptor". J. Biol. Chem. (United States) 276 (45): 42153–61. doi:10.1074/jbc.M102079200. ISSN 0021-9258. PMID 11546794. 
  8. ^ Lin, J; Adam R M, Santiestevan E, Freeman M R (June 1999). "The phosphatidylinositol 3'-kinase pathway is a dominant growth factor-activated cell survival pathway in LNCaP human prostate carcinoma cells". Cancer Res. (UNITED STATES) 59 (12): 2891–7. ISSN 0008-5472. PMID 10383151. 
  9. ^ Thaminy, Safia; Auerbach Daniel, Arnoldo Anthony, Stagljar Igor (July 2003). "Identification of novel ErbB3-interacting factors using the split-ubiquitin membrane yeast two-hybrid system". Genome Res. (United States) 13 (7): 1744–53. doi:10.1101/gr.1276503. ISSN 1088-9051. PMC 403748. PMID 12840049. 

Further reading[edit]