[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JM-A).
TISSUE=Mammary carcinoma;
DOI=10.1073/pnas.90.5.1746; PubMed=8383326 [NCBI, ExPASy, EBI, Israel, Japan]
Plowman G.D.,
Culouscou J.-M.,
Whitney G.S.,
Green J.M.,
Carlton G.W.,
Foy L.,
Neubauer M.G.,
Shoyab M.;
"Ligand-specific activation of HER4/p180erbB4, a fourth member of the epidermal growth factor receptor family.";
Proc. Natl. Acad. Sci. U.S.A. 90:1746-1750(1993).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS JM-A AND JM-B), AND PROTEOLYTIC PROCESSING.
TISSUE=Fetal brain;
DOI=10.1074/jbc.272.42.26761; PubMed=9334263 [NCBI, ExPASy, EBI, Israel, Japan]
Elenius K.,
Corfas G.,
Paul S.,
Choi C.J.,
Rio C.,
Plowman G.D.,
Klagsbrun M.;
"A novel juxtamembrane domain isoform of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester.";
J. Biol. Chem. 272:26761-26768(1997).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM JM-A).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 401-1308 (ISOFORM 3).
TISSUE=Brain;
Totoki Y.,
Toyoda A.,
Takeda T.,
Sakaki Y.,
Tanaka A.,
Yokoyama S.,
Ohara O.,
Nagase T.,
Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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[5]
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INTERACTION WITH DLG2; DLG3; DLG4 AND SNTB2.
DOI=10.1073/pnas.070042497; PubMed=10725395 [NCBI, ExPASy, EBI, Israel, Japan]
Garcia R.A.,
Vasudevan K.,
Buonanno A.;
"The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses.";
Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000).
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[6]
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INTERACTION WITH MUC1.
PubMed=12939402 [NCBI, ExPASy, EBI, Israel, Japan]
Li Y.,
Yu W.-H.,
Ren J.,
Chen W.,
Huang L.,
Kharbanda S.,
Loda M.,
Kufe D.;
"Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein.";
Mol. Cancer Res. 1:765-775(2003).
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[7]
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INTERACTION WITH WWOX, DOMAIN, AND MUTAGENESIS OF TYR-1035 AND TYR-1301.
DOI=10.1158/0008-5472.CAN-05-1150; PubMed=16061658 [NCBI, ExPASy, EBI, Israel, Japan]
Aqeilan R.I.,
Donati V.,
Palamarchuk A.,
Trapasso F.,
Kaou M.,
Pekarsky Y.,
Sudol M.,
Croce C.M.;
"WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function.";
Cancer Res. 65:6764-6772(2005).
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[8]
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INTERACTION WITH CBFA2T3.
DOI=10.1074/jbc.M603998200; PubMed=16815842 [NCBI, ExPASy, EBI, Israel, Japan]
Linggi B.,
Carpenter G.;
"ErbB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional repression.";
J. Biol. Chem. 281:25373-25380(2006).
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[9]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-733, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K.,
Guo A.,
Zeng Q.,
Possemato A.,
Yu J.,
Haack H.,
Nardone J.,
Lee K.,
Reeves C.,
Li Y.,
Hu Y.,
Tan Z.,
Stokes M.,
Sullivan L.,
Mitchell J.,
Wetzel R.,
Macneill J.,
Ren J.M.,
Yuan J., ![]()
Bakalarski C.E.,
Villen J.,
Kornhauser J.M.,
Smith B.,
Li D.,
Zhou X.,
Gygi S.P.,
Gu T.-L.,
Polakiewicz R.D.,
Rush J.,
Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-641, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-138; ASN-174; ASN-253; ASN-358; ASN-410; ASN-473; ASN-495 AND ASN-576.
DOI=10.1073/pnas.0507591102; PubMed=16203964 [NCBI, ExPASy, EBI, Israel, Japan]
Bouyain S.,
Longo P.A.,
Li S.,
Ferguson K.M.,
Leahy D.J.;
"The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.";
Proc. Natl. Acad. Sci. U.S.A. 102:15024-15029(2005).
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[11]
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VARIANTS [LARGE SCALE ANALYSIS] ILE-140 AND TYR-303.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C.,
Stephens P.,
Smith R.,
Dalgliesh G.L.,
Hunter C.,
Bignell G.,
Davies H.,
Teague J.,
Butler A.,
Stevens C.,
Edkins S.,
O'Meara S.,
Vastrik I.,
Schmidt E.E.,
Avis T.,
Barthorpe S.,
Bhamra G.,
Buck G.,
Choudhury B., ![]()
Clements J.,
Cole J.,
Dicks E.,
Forbes S.,
Gray K.,
Halliday K.,
Harrison R.,
Hills K.,
Hinton J.,
Jenkinson A.,
Jones D.,
Menzies A.,
Mironenko T.,
Perry J.,
Raine K.,
Richardson D.,
Shepherd R.,
Small A.,
Tofts C.,
Varian J.,
Webb T.,
West S.,
Widaa S.,
Yates A.,
Cahill D.P.,
Louis D.N.,
Goldstraw P.,
Nicholson A.G.,
Brasseur F.,
Looijenga L.,
Weber B.L.,
Chiew Y.-E.,
DeFazio A.,
Greaves M.F.,
Green A.R.,
Campbell P.,
Birney E.,
Easton D.F.,
Chenevix-Trench G.,
Tan M.-H.,
Khoo S.K.,
Teh B.T.,
Yuen S.T.,
Leung S.Y.,
Wooster R.,
Futreal P.A.,
Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
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- FUNCTION: Specifically binds and is activated by neuregulins, NRG-2, NRG-3, heparin-binding EGF-like growth factor, betacellulin and NTAK. Interaction with these factors induces cell differentiation. Not activated by EGF, TGF-A, and amphiregulin.
- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
- SUBUNIT: Homodimer or heterodimer with each of the other ERBB receptors (Potential). Interacts with PDZ domains of DLG2, DLG3, DLG4 and the syntrophin SNTB2. Interacts with CBFA2T3, MUC1 and WWOX.
- INTERACTION:
P78352:DLG4; NbExp=3; IntAct=EBI-80371, EBI-80389;
P00533:EGFR; NbExp=2; IntAct=EBI-80371, EBI-297353;
P04626:ERBB2; NbExp=2; IntAct=EBI-80371, EBI-641062;
P21860:ERBB3; NbExp=2; IntAct=EBI-80371, EBI-720706;
Q05586:GRIN1; NbExp=1; IntAct=EBI-80371, EBI-998542;
- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
- ALTERNATIVE PRODUCTS:
3 named isoforms [FASTA] produced by alternative splicing.
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| Name | JM-B |
| Isoform ID | Q15303-2 |
| Features which should be applied to build the isoform sequence: VSP_002895. |
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| Name | 3 |
| Isoform ID | Q15303-3 |
| Features which should be applied to build the isoform sequence: VSP_022148. |
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- TISSUE SPECIFICITY: Expressed at highest levels in brain, heart, kidney, in addition to skeletal muscle, parathyroid, cerebellum, pituitary, spleen, testis and breast. Lower levels in thymus, lung, salivary gland, and pancreas. Isoform JM-A and isoform JM-B are expressed in cerebellum, but only the isoform JM-B is expressed in the heart.
- DOMAIN: The WW-binding motifs mediate interaction with WWOX.
- PTM: Isoform JM-A is processed but not isoform JM-B. So, they respectively represent cleavable and non-cleavable forms of the receptor.
- PTM: Ligand-binding increases phosphorylation on tyrosine residues.
- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.
- SIMILARITY: Contains 1 protein kinase domain.
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