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Receptor tyrosine-protein kinase erbB-4 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-4) [Cleaved into: ERBB4 intracellular domain (4ICD) (E4ICD) (s80HER4)]

 ERBB4_MOUSE             Reviewed;        1308 AA.
Q61527; B2KGF5; B2KGF6; O88460; Q3UNS6;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 5.
11-DEC-2019, entry version 180.
RecName: Full=Receptor tyrosine-protein kinase erbB-4;
EC=2.7.10.1;
AltName: Full=Proto-oncogene-like protein c-ErbB-4;
Contains:
RecName: Full=ERBB4 intracellular domain;
Short=4ICD;
Short=E4ICD;
AltName: Full=s80HER4;
Flags: Precursor;
Name=Erbb4; Synonyms=Mer4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1263 (JM-A CYT-2).
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 624-650 (ISOFORMS JM-A CYT-2 AND JM-B CYT-2).
TISSUE=Heart, and Kidney;
PubMed=9334263; DOI=10.1074/jbc.272.42.26761;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1019-1102 (ISOFORM JM-A CYT-1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=7589796; DOI=10.1006/dbio.1995.0012;
Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P., Sanes J.R.;
"Synapse-associated expression of an acetylcholine receptor-inducing
protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in
developing mammalian muscle.";
Dev. Biol. 172:158-169(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1019-1093 (ISOFORM JM-A CYT-1).
STRAIN=CD-1; TISSUE=Uterus;
Lim H., Das S.K., Dey S.K.;
"Potential signaling network by EGF-like growth factors in the mouse uterus
during early pregnancy.";
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=7477376; DOI=10.1038/378390a0;
Gassmann M., Casagranda F., Orioli D., Simon H., Lai C., Klein R.,
Lemke G.;
"Aberrant neural and cardiac development in mice lacking the ErbB4
neuregulin receptor.";
Nature 378:390-394(1995).
[7]
FUNCTION IN MAMMARY GLAND DEVELOPMENT AND ACTIVATION OF STAT5A, AND
INTERACTION WITH STAT5A.
PubMed=10508857; DOI=10.1083/jcb.147.1.77;
Jones F.E., Welte T., Fu X.Y., Stern D.F.;
"ErbB4 signaling in the mammary gland is required for lobuloalveolar
development and Stat5 activation during lactation.";
J. Cell Biol. 147:77-88(1999).
[8]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=10353604; DOI=10.1038/sj.onc.1202612;
Elenius K., Choi C.J., Paul S., Santiestevan E., Nishi E., Klagsbrun M.;
"Characterization of a naturally occurring ErbB4 isoform that does not bind
or activate phosphatidyl inositol 3-kinase.";
Oncogene 18:2607-2615(1999).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10655590; DOI=10.1038/35000058;
Golding J.P., Trainor P., Krumlauf R., Gassmann M.;
"Defects in pathfinding by cranial neural crest cells in mice lacking the
neuregulin receptor ErbB4.";
Nat. Cell Biol. 2:103-109(2000).
[10]
DISRUPTION PHENOTYPE.
PubMed=12954715; DOI=10.1242/dev.00715;
Long W., Wagner K.U., Lloyd K.C., Binart N., Shillingford J.M.,
Hennighausen L., Jones F.E.;
"Impaired differentiation and lactational failure of Erbb4-deficient
mammary glands identify ERBB4 as an obligate mediator of STAT5.";
Development 130:5257-5268(2003).
[11]
DISRUPTION PHENOTYPE.
PubMed=12824469; DOI=10.1073/pnas.1436402100;
Tidcombe H., Jackson-Fisher A., Mathers K., Stern D.F., Gassmann M.,
Golding J.P.;
"Neural and mammary gland defects in ErbB4 knockout mice genetically
rescued from embryonic lethality.";
Proc. Natl. Acad. Sci. U.S.A. 100:8281-8286(2003).
[12]
FUNCTION IN NEUROBLAST MIGRATION.
PubMed=15543145; DOI=10.1038/nn1345;
Anton E.S., Ghashghaei H.T., Weber J.L., McCann C., Fischer T.M.,
Cheung I.D., Gassmann M., Messing A., Klein R., Schwab M.H., Lloyd K.C.,
Lai C.;
"Receptor tyrosine kinase ErbB4 modulates neuroblast migration and
placement in the adult forebrain.";
Nat. Neurosci. 7:1319-1328(2004).
[13]
FUNCTION.
PubMed=15863494; DOI=10.1074/jbc.m414044200;
Clark D.E., Williams C.C., Duplessis T.T., Moring K.L., Notwick A.R.,
Long W., Lane W.S., Beuvink I., Hynes N.E., Jones F.E.;
"ERBB4/HER4 potentiates STAT5A transcriptional activity by regulating novel
STAT5A serine phosphorylation events.";
J. Biol. Chem. 280:24175-24180(2005).
[14]
INTERACTION WITH CBFA2T3.
PubMed=16815842; DOI=10.1074/jbc.m603998200;
Linggi B., Carpenter G.;
"ErbB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional
repression.";
J. Biol. Chem. 281:25373-25380(2006).
[15]
FUNCTION, PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
PubMed=16837552; DOI=10.1091/mbc.e06-02-0101;
Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L.,
Feng S.M., Elenius K., Earp H.S. III;
"The intracellular domain of ErbB4 induces differentiation of mammary
epithelial cells.";
Mol. Biol. Cell 17:4118-4129(2006).
[16]
FUNCTION OF E4ICD.
PubMed=19596786; DOI=10.1128/mcb.01705-08;
Muraoka-Cook R.S., Sandahl M.A., Strunk K.E., Miraglia L.C., Husted C.,
Hunter D.M., Elenius K., Chodosh L.A., Earp H.S. III;
"ErbB4 splice variants Cyt1 and Cyt2 differ by 16 amino acids and exert
opposing effects on the mammary epithelium in vivo.";
Mol. Cell. Biol. 29:4935-4948(2009).
[17]
FUNCTION AS NRG1 RECEPTOR IN POSTNATAL CARDIOMYOCYTE PROLIFERATION.
PubMed=19632177; DOI=10.1016/j.cell.2009.04.060;
Bersell K., Arab S., Haring B., Kuhn B.;
"Neuregulin1/ErbB4 signaling induces cardiomyocyte proliferation and repair
of heart injury.";
Cell 138:257-270(2009).
[18]
REVIEW.
PubMed=14504474;
Jones F.E., Golding J.P., Gassmann M.;
"ErbB4 signaling during breast and neural development: novel genetic models
reveal unique ErbB4 activities.";
Cell Cycle 2:555-559(2003).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[20]
REVIEW ON ROLE AS NEUREGULIN RECEPTOR.
PubMed=21295966; DOI=10.1016/j.gde.2010.12.010;
Rico B., Marin O.;
"Neuregulin signaling, cortical circuitry development and schizophrenia.";
Curr. Opin. Genet. Dev. 21:262-270(2011).
-!- 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 alternative
splicing, proteolytic processing, and by the formation of heterodimers
with other ERBB family members, thereby creating multiple combinations
of intracellular phosphotyrosines that trigger ligand- and context-
specific cellular responses. Mediates phosphorylation of SHC1 and
activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A
CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the
activation of phosphatidylinositol 3-kinase and AKT1 and protect cells
against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate
reorganization of the actin cytoskeleton and promote cell migration in
response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the
phosphotyrosine that mediates interaction with PIK3R1, and hence do not
phosphorylate PIK3R1, do not protect cells against apoptosis, and do
not promote reorganization of the actin cytoskeleton and cell
migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-
A CYT-2 gives rise to the corresponding soluble intracellular domains
(4ICD) that translocate to the nucleus, promote nuclear import of
STAT5A, activation of STAT5A, mammary epithelium differentiation, cell
proliferation and activation of gene expression. The ERBB4 soluble
intracellular domains (4ICD) colocalize with STAT5A at the CSN2
promoter to regulate transcription of milk proteins during lactation.
The ERBB4 soluble intracellular domains can also translocate to
mitochondria and promote apoptosis. {ECO:0000269|PubMed:10508857,
ECO:0000269|PubMed:10655590, ECO:0000269|PubMed:15543145,
ECO:0000269|PubMed:15863494, ECO:0000269|PubMed:16837552,
ECO:0000269|PubMed:19596786, ECO:0000269|PubMed:19632177,
ECO:0000269|PubMed:7477376}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- ACTIVITY REGULATION: Binding of a cognate ligand leads to dimerization
and activation by autophosphorylation on tyrosine residues. In vitro
kinase activity is increased by Mg(2+) (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer in the absence of bound ligand. Homodimer or
heterodimer with another ERBB family member upon ligand binding, thus
forming heterotetramers. Interacts with EGFR and ERBB2. Interacts with
DLG2 (via its PDZ domain), DLG3 (via its PDZ domain), DLG4 (via its PDZ
domain) and SNTB2 (via its PDZ domain). Interacts with MUC1. Interacts
(via its PPxy motifs) with WWOX. Interacts (via the PPxY motif 3 of
isoform JM-A CYT-2) with YAP1 (via the WW domain 1 of isoform 1).
Interacts (isoform JM-A CYT-1 and isoform JM-B CYT-1) with WWP1.
Interacts (via its intracellular domain) with TRIM28. Interacts (via
the intracellular domains of both CYT-1 and CYT-2 isoforms) with KAP1;
the interaction does not phosphorylate KAP1 but represses ERBB4-
mediated transcriptional activity. Interacts with PRPU, DDX23, MATR3,
RBM15, ILF3, KAP1, U5S1, U2SURP, ITCH, HNRNPU, AP2A1, NULC, LEO1, WWP2,
IGHG1, HXK1, GRB7 AND ARS2. Interacts (phosphorylated isoform JM-A CYT-
1 and isoform JM-B CYT-1) with PIK3R1. Interacts with SHC1. Interacts
with GRB2. Interacts (soluble intracellular domain) with BCL2.
Interacts (phosphorylated) with STAT1 (By similarity). Interacts with
CBFA2T3. Interacts (soluble intracellular domain) with STAT5A.
{ECO:0000250, ECO:0000269|PubMed:10508857,
ECO:0000269|PubMed:16815842}.
-!- INTERACTION:
Q9NZC7:WWOX (xeno); NbExp=3; IntAct=EBI-4398741, EBI-4320739;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16837552};
Single-pass type I membrane protein {ECO:0000269|PubMed:16837552}.
Note=In response to NRG1 treatment, the activated receptor is
internalized.
-!- SUBCELLULAR LOCATION: [ERBB4 intracellular domain]: Nucleus.
Mitochondrion {ECO:0000250}. Note=Following proteolytical processing
E4ICD (E4ICD1 or E4ICD2 generated from the respective isoforms) is
translocated to the nucleus. Significantly more E4ICD2 than E4ICD1 is
found in the nucleus. E4ICD2 colocalizes with YAP1 in the nucleus (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=JM-A CYT-1;
IsoId=Q61527-1; Sequence=Displayed;
Name=JM-B CYT-2;
IsoId=Q61527-2; Sequence=VSP_002896;
Name=JM-A CYT-2;
IsoId=Q61527-3; Sequence=VSP_042131;
-!- TISSUE SPECIFICITY: Isoform JM-A CYT-2 and isoform JM-B CYT-2 are
expressed in cerebellum, cerebral cortex, spinal cord, medulla
oblongata and eye, but the kidney expresses solely isoform JM-A CYT-2
and the heart solely isoform JM-B CYT-2. {ECO:0000269|PubMed:10353604}.
-!- PTM: 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 fragments of the processed isoform JM-A CYT-1
are more readily degraded by the proteasome than fragments of isoform
JM-A CYT-2, suggesting a prevalence of E4ICD2 over E4ICD1. Isoform JM-B
CYT-1 and isoform JM-B CYT-2 lack the ADAM17 cleavage site and are not
processed by ADAM17, precluding further processing by gamma-secretase
(By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues in response to ligand
binding. Autophosphorylation occurs in trans, i.e. one subunit of the
dimeric receptor phosphorylates tyrosine residues on the other subunit.
Ligands trigger phosphorylation at specific tyrosine residues, thereby
creating binding sites for scaffold proteins and effectors.
Constitutively phosphorylated at a basal level when overexpressed in
heterologous systems; ligand binding leads to increased
phosphorylation. Phosphorylation at Tyr-1035 is important for
interaction with STAT1. Phosphorylation at Tyr-1056 is important for
interaction with PIK3R1. Phosphorylation at Tyr-1242 is important for
interaction with SHC1. Phosphorylation at Tyr-1188 may also contribute
to the interaction with SHC1. Isoform JM-A CYT-2 is constitutively
phosphorylated on tyrosine residues in a ligand-independent manner.
E4ICD2 but not E4ICD1 is phosphorylated on tyrosine residues (By
similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. During mitosis, the ERBB4 intracellular domain is
ubiquitinated by the APC/C complex and targeted to proteasomal
degradation. Isoform JM-A CYT-1 and isoform JM-B CYT-1 are
ubiquitinated by WWP1. The ERBB4 intracellular domain (E4ICD1) is
ubiquitinated, and this involves NEDD4 (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonically lethal. Embryos die at about 10
dpc, due to defects in the development of myocardial trabeculae in the
heart ventricle that lead to severely reduced embryonic blood flow.
Mice also display aberrant innervation from and to the hindbrain,
especially concerning the trigeminal, facial and acoustic ganglia. This
is due to aberrant migration of a subpopulation of cranial neural crest
cells. {ECO:0000269|PubMed:10655590, ECO:0000269|PubMed:12824469,
ECO:0000269|PubMed:12954715, ECO:0000269|PubMed:7477376}.
-!- MISCELLANEOUS: [Isoform JM-A CYT-1]: Proteolytical processing generates
E4ICD1 (s80Cyt1).
-!- MISCELLANEOUS: [Isoform JM-A CYT-2]: Proteolytical processing generates
E4ICD2 (s80Cyt2). {ECO:0000305}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; CU368746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU372923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU392849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU405881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU407006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU459008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU459207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK144050; BAE25671.1; -; mRNA.
EMBL; L47241; AAA93534.1; -; mRNA.
EMBL; AF059177; AAC28334.1; -; mRNA.
CCDS; CCDS48285.1; -. [Q61527-3]
RefSeq; NP_034284.1; NM_010154.2. [Q61527-3]
RefSeq; XP_006495755.1; XM_006495692.3. [Q61527-1]
RefSeq; XP_006495756.1; XM_006495693.3. [Q61527-2]
SMR; Q61527; -.
BioGrid; 199498; 5.
DIP; DIP-29887N; -.
IntAct; Q61527; 3.
STRING; 10090.ENSMUSP00000114123; -.
GlyConnect; 2677; -.
iPTMnet; Q61527; -.
PhosphoSitePlus; Q61527; -.
jPOST; Q61527; -.
PaxDb; Q61527; -.
PeptideAtlas; Q61527; -.
PRIDE; Q61527; -.
DNASU; 13869; -.
Ensembl; ENSMUST00000119142; ENSMUSP00000112713; ENSMUSG00000062209. [Q61527-1]
Ensembl; ENSMUST00000121473; ENSMUSP00000114123; ENSMUSG00000062209. [Q61527-3]
GeneID; 13869; -.
KEGG; mmu:13869; -.
UCSC; uc007bjb.1; mouse. [Q61527-3]
CTD; 2066; -.
MGI; MGI:104771; Erbb4.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
GeneTree; ENSGT00940000154695; -.
HOGENOM; HOG000230982; -.
InParanoid; Q61527; -.
KO; K05085; -.
OMA; PASHDCI; -.
OrthoDB; 81952at2759; -.
PhylomeDB; Q61527; -.
TreeFam; TF106002; -.
Reactome; R-MMU-1227986; Signaling by ERBB2.
Reactome; R-MMU-1236394; Signaling by ERBB4.
Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-MMU-1250342; PI3K events in ERBB4 signaling.
Reactome; R-MMU-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-MMU-1251985; Nuclear signaling by ERBB4.
Reactome; R-MMU-1253288; Downregulation of ERBB4 signaling.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8847993; ERBB2 Activates PTK6 Signaling.
Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
ChiTaRS; Erbb4; mouse.
PRO; PR:Q61527; -.
Proteomes; UP000000589; Chromosome 1.
RNAct; Q61527; protein.
Bgee; ENSMUSG00000062209; Expressed in 238 organ(s), highest expression level in rest of cerebellum marginal layer (mouse).
ExpressionAtlas; Q61527; baseline and differential.
Genevisible; Q61527; MM.
GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
GO; GO:0038132; F:neuregulin binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0061026; P:cardiac muscle tissue regeneration; IMP:UniProtKB.
GO; GO:0045165; P:cell fate commitment; IDA:MGI.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:MGI.
GO; GO:0021551; P:central nervous system morphogenesis; IMP:UniProtKB.
GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0007595; P:lactation; IMP:UniProtKB.
GO; GO:0060749; P:mammary gland alveolus development; IMP:UniProtKB.
GO; GO:0060644; P:mammary gland epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISO:MGI.
GO; GO:2001223; P:negative regulation of neuron migration; IMP:MGI.
GO; GO:0007399; P:nervous system development; IMP:MGI.
GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
GO; GO:0021889; P:olfactory bulb interneuron differentiation; IMP:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IGI:MGI.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IGI:MGI.
GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IMP:UniProtKB.
GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0043129; P:surfactant homeostasis; ISO:MGI.
GO; GO:0007416; P:synapse assembly; IDA:SynGO.
GO; GO:0060074; P:synapse maturation; ISO:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:UniProtKB.
CDD; cd00064; FU; 3.
Gene3D; 3.80.20.20; -; 2.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
Pfam; PF00757; Furin-like; 1.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00261; FU; 5.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
Developmental protein; Disulfide bond; Glycoprotein; Kinase; Lactation;
Membrane; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Receptor; Reference proteome; Repeat; Signal; Transcription;
Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1..25
/evidence="ECO:0000255"
CHAIN 26..1308
/note="Receptor tyrosine-protein kinase erbB-4"
/id="PRO_0000270146"
CHAIN 676..1308
/note="ERBB4 intracellular domain"
/id="PRO_0000396798"
TOPO_DOM 26..652
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 653..673
/evidence="ECO:0000255"
TOPO_DOM 674..1308
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 718..985
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 724..732
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 797..799
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 843..848
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOTIF 676..684
/note="Nuclear localization signal"
/evidence="ECO:0000250"
MOTIF 1032..1035
/note="PPxy motif 1"
/evidence="ECO:0000250"
MOTIF 1282..1285
/note="PPxY motif 2"
/evidence="ECO:0000250"
MOTIF 1290..1292
/note="PDZ-binding"
/evidence="ECO:0000250"
COMPBIAS 186..262
/note="Cys-rich"
COMPBIAS 496..593
/note="Cys-rich"
COMPBIAS 1281..1284
/note="Poly-Pro"
ACT_SITE 843
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 751
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 875
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1035
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1056
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1150
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1162
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1188
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1202
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1242
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1258
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
MOD_RES 1284
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q15303"
CARBOHYD 138
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 174
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 181
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 253
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 410
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 473
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 495
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 548
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 576
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 620
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 29..56
/evidence="ECO:0000250"
DISULFID 156..186
/evidence="ECO:0000250"
DISULFID 189..197
/evidence="ECO:0000250"
DISULFID 193..205
/evidence="ECO:0000250"
DISULFID 213..221
/evidence="ECO:0000250"
DISULFID 217..229
/evidence="ECO:0000250"
DISULFID 230..238
/evidence="ECO:0000250"
DISULFID 234..246
/evidence="ECO:0000250"
DISULFID 249..258
/evidence="ECO:0000250"
DISULFID 262..289
/evidence="ECO:0000250"
DISULFID 293..304
/evidence="ECO:0000250"
DISULFID 308..323
/evidence="ECO:0000250"
DISULFID 326..330
/evidence="ECO:0000250"
DISULFID 503..512
/evidence="ECO:0000250"
DISULFID 507..520
/evidence="ECO:0000250"
DISULFID 523..532
/evidence="ECO:0000250"
DISULFID 536..552
/evidence="ECO:0000250"
DISULFID 555..569
/evidence="ECO:0000250"
DISULFID 559..577
/evidence="ECO:0000250"
DISULFID 580..589
/evidence="ECO:0000250"
DISULFID 593..614
/evidence="ECO:0000250"
DISULFID 617..625
/evidence="ECO:0000250"
DISULFID 621..633
/evidence="ECO:0000250"
VAR_SEQ 626..648
/note="NGPTSHDCIYYPWTGHSTLPQHA -> IGSSIEDCIGLTD (in isoform
JM-B CYT-2)"
/evidence="ECO:0000303|PubMed:9334263"
/id="VSP_002896"
VAR_SEQ 1046..1061
/note="Missing (in isoform JM-A CYT-2)"
/evidence="ECO:0000303|PubMed:9334263"
/id="VSP_042131"
CONFLICT 1019
/note="A -> V (in Ref. 5; AAC28334)"
/evidence="ECO:0000305"
SEQUENCE 1308 AA; 146855 MW; 65943278A7E7F2F6 CRC64;
MKLATGLWVW GSLLMAAGTV QPSASQSVCA GTENKLSSLS DLEQQYRALR KYYENCEVVM
GNLEITSIEH NRDLSFLRSI REVTGYVLVA LNQFRYLPLE NLRIIRGTKL YEDRYALAIF
LNYRKDGNFG LQELGLKNLT EILNGGVYVD QNKFLCYADT IHWQDIVRNP WPSNMTLVST
NGSSGCGRCH KSCTGRCWGP TENHCQTLTR TVCAEQCDGR CYGPYVSDCC HRECAGGCSG
PKDTDCFACM NFNDSGACVT QCPQTFVYNP TTFQLEHNFN AKYTYGAFCV KKCPHNFVVD
SSSCVRACPS SKMEVEENGI KMCKPCTDIC PKACDGIGTG SLMSAQTVDS SNIDKFINCT
KINGNLIFLV TGIHGDPYNA IDAIDPEKLN VFRTVREITG FLNIQSWPPN MTDFSVFSNL
VTIGGRVLYS GLSLLILKQQ GITSLQFQSL KEISAGNIYI TDNSNLCYYH TINWTTLFST
INQRIVIRDN RRAENCTAEG MVCNHLCSND GCWGPGPDQC LSCRRFSRGK ICIESCNLYD
GEFREFENGS ICVECDSQCE KMEDGLLTCH GPGPDNCTKC SHFKDGPNCV EKCPDGLQGA
NSFIFKYADQ DRECHPCHPN CTQGCNGPTS HDCIYYPWTG HSTLPQHART PLIAAGVIGG
LFILVIMALT FAVYVRRKSI KKKRALRRFL ETELVEPLTP SGTAPNQAQL RILKETELKR
VKVLGSGAFG TVYKGIWVPE GETVKIPVAI KILNETTGPK ANVEFMDEAL IMASMDHPHL
VRLLGVCLSP TIQLVTQLMP HGCLLDYVHE HKDNIGSQLL LNWCVQIAKG MMYLEERRLV
HRDLAARNVL VKSPNHVKIT DFGLARLLEG DEKEYNADGG KMPIKWMALE CIHYRKFTHQ
SDVWSYGVTI WELMTFGGKP YDGIPTREIP DLLEKGERLP QPPICTIDVY MVMVKCWMID
ADSRPKFKEL AAEFSRMARD PQRYLVIQGD DRMKLPSPND SKFFQNLLDE EDLEDMMDAE
EYLVPQAFNI PPPIYTSRTR IDSNRSEIGH SPPPAYTPMS GNQFVYQDGG FATQQGMPMP
YRATTSTIPE APVAQGATAE MFDDSCCNGT LRKPVAPHVQ EDSSTQRYSA DPTVFAPERN
PRGELDEEGY MTPMHDKPKQ EYLNPVEENP FVSRRKNGDL QALDNPEYHS ASSGPPKAED
EYVNEPLYLN TFANALGSAE YMKNSVLSVP EKAKKAFDNP DYWNHSLPPR STLQHPDYLQ
EYSTKYFYKQ NGRIRPIVAE NPEYLSEFSL KPGTMLPPPP YRHRNTVV


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