Reviewed,
UniProtKB/Swiss-Prot Q61527 (ERBB4_MOUSE)
Last modified
October 13, 2009.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Receptor tyrosine-protein kinase erbB-4 EC=2.7.10.1 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1292 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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 By similarity. |
| Catalytic activity | ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. |
| Subunit structure | Homodimer or heterodimer with each of the other ERBB receptors. Interacts with PDZ domains of DLG2, DLG3, DLG4 and the syntrophin SNTB2. Interacts with WWOX and MUC1 By similarity. Interacts with CBFA2T3. |
| Subcellular location | |
| Post-translational modification | Ligand-binding increases phosphorylation on tyrosine residues. |
| Sequence similarities | Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily. Contains 1 protein kinase domain. |
Ontologies
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] Note: The 2 isoforms differ functionally in their response to phorbol ester: isoform JM-A is processed but not isoform JM-B. So, they respectively represent cleavable and non-cleavable forms of the receptor. Both isoforms are expressed in cerebellum, cerebral cortex, spinal cord, medulla oblongata and eye, but the kidney expresses solely isoform JM-A and the heart solely isoform JM-B. | ||||||
| Isoform JM-A (identifier: Q61527-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform JM-B (identifier: Q61527-2) The sequence of this isoform differs from the canonical sequence as follows: 626-648: NGPTSHDCIYYPWTGHSTLPQHA → IGSSIEDCIGLTD | ||||||
| Isoform 3 (identifier: Q61527-3) The sequence of this isoform differs from the canonical sequence as follows: 1045-1045: R → RSEIGHSPPPAYTPMWG | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||||
| Chain | 26 – 1292 | 1267 | Receptor tyrosine-protein kinase erbB-4 | PRO_0000270146 | |||||||
Regions | |||||||||||
| Topological domain | 26 – 652 | 627 | Extracellular Potential | ||||||||
| Transmembrane | 653 – 673 | 21 | Potential | ||||||||
| Topological domain | 674 – 1292 | 619 | Cytoplasmic Potential | ||||||||
| Domain | 718 – 985 | 268 | Protein kinase | ||||||||
| Nucleotide binding | 724 – 732 | 9 | ATP By similarity | ||||||||
| Motif | 1032 – 1035 | 4 | WW-binding 1 By similarity | ||||||||
| Motif | 1282 – 1285 | 4 | WW-binding 2 By similarity | ||||||||
| Motif | 1290 – 1292 | 3 | PDZ-binding By similarity | ||||||||
| Compositional bias | 186 – 262 | 77 | Cys-rich | ||||||||
| Compositional bias | 496 – 593 | 98 | Cys-rich | ||||||||
| Compositional bias | 1281 – 1284 | 4 | Poly-Pro | ||||||||
Sites | |||||||||||
| Active site | 843 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 751 | 1 | ATP By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 733 | 1 | Phosphotyrosine By similarity | ||||||||
| Modified residue | 1146 | 1 | Phosphotyrosine; by autocatalysis By similarity | ||||||||
| Modified residue | 1172 | 1 | Phosphotyrosine; by autocatalysis By similarity | ||||||||
| Modified residue | 1242 | 1 | Phosphotyrosine; by autocatalysis By similarity | ||||||||
| Modified residue | 1268 | 1 | Phosphotyrosine; by autocatalysis By similarity | ||||||||
| Glycosylation | 138 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 174 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 181 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 253 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 410 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 473 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 495 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 548 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 576 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 620 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 29 ↔ 56 | By similarity | |||||||||
| Disulfide bond | 156 ↔ 186 | By similarity | |||||||||
| Disulfide bond | 189 ↔ 197 | By similarity | |||||||||
| Disulfide bond | 193 ↔ 205 | By similarity | |||||||||
| Disulfide bond | 213 ↔ 221 | By similarity | |||||||||
| Disulfide bond | 217 ↔ 229 | By similarity | |||||||||
| Disulfide bond | 230 ↔ 238 | By similarity | |||||||||
| Disulfide bond | 234 ↔ 246 | By similarity | |||||||||
| Disulfide bond | 249 ↔ 258 | By similarity | |||||||||
| Disulfide bond | 262 ↔ 289 | By similarity | |||||||||
| Disulfide bond | 293 ↔ 304 | By similarity | |||||||||
| Disulfide bond | 308 ↔ 323 | By similarity | |||||||||
| Disulfide bond | 326 ↔ 330 | By similarity | |||||||||
| Disulfide bond | 503 ↔ 512 | By similarity | |||||||||
| Disulfide bond | 507 ↔ 520 | By similarity | |||||||||
| Disulfide bond | 523 ↔ 532 | By similarity | |||||||||
| Disulfide bond | 536 ↔ 552 | By similarity | |||||||||
| Disulfide bond | 555 ↔ 569 | By similarity | |||||||||
| Disulfide bond | 559 ↔ 577 | By similarity | |||||||||
| Disulfide bond | 580 ↔ 589 | By similarity | |||||||||
| Disulfide bond | 593 ↔ 614 | By similarity | |||||||||
| Disulfide bond | 617 ↔ 625 | By similarity | |||||||||
| Disulfide bond | 621 ↔ 633 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 626 – 648 | 23 | NGPTS…LPQHA → IGSSIEDCIGLTD in isoform JM-B. | VSP_002896 | |||||||
| Alternative sequence | 1045 | 1 | R → RSEIGHSPPPAYTPMWG in isoform 3. | VSP_022149 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 1019 | 1 | A → V in AAC28334. Ref.5 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "The transcriptional landscape of the mammalian genome." 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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1247. Strain: C57BL/6J. Tissue: Kidney. |
| [3] | "A novel juxtamembrane domain isoform of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester." Elenius K., Corfas G., Paul S., Choi C.J., Rio C., Plowman G.D., Klagsbrun M. J. Biol. Chem. 272:26761-26768(1997) [PubMed: 9334263] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 624-650 (ISOFORMS JM-A AND JM-B). Tissue: Heart and Kidney. |
| [4] | "Synapse-associated expression of an acetylcholine receptor-inducing protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in developing mammalian muscle." Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P., Sanes J.R. Dev. Biol. 172:158-169(1995) [PubMed: 7589796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1019-1086. Strain: C57BL/6. Tissue: Brain. |
| [5] | "Potential signaling network by EGF-like growth factors in the mouse uterus during early pregnancy." Lim H., Das S.K., Dey S.K. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1019-1077 (ISOFORM 3). Strain: CD-1. Tissue: Uterus. |
| [6] | "ErbB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional repression." Linggi B., Carpenter G. J. Biol. Chem. 281:25373-25380(2006) [PubMed: 16815842] [Abstract] Cited for: INTERACTION WITH CBFA2T3. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AC099604 Genomic DNA. No translation available. AC107673 Genomic DNA. No translation available. AC138110 Genomic DNA. No translation available. AC138285 Genomic DNA. No translation available. AC139369 Genomic DNA. No translation available. CAAA01019932 Genomic DNA. No translation available. CAAA01109085 Genomic DNA. No translation available. AK144050 mRNA. Translation: BAE25671.1. L47241 mRNA. Translation: AAA93534.1. AF059177 mRNA. Translation: AAC28334.1. | |
| IPI | IPI00122341. IPI00357770. IPI00896073. |
| RefSeq | NP_034284.1. |
| UniGene | Mm.442420 |
3D structure databases | |
| SMR | Q61527. Positions 26-641. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q61527. |
Proteomic databases | |
| PRIDE | Q61527. |
Genome annotation databases | |
| Ensembl | ENSMUST00000082184; ENSMUSP00000080821; ENSMUSG00000062209; Mus musculus. [Genome view] ENSMUST00000097703; ENSMUSP00000095310; ENSMUSG00000062209; Mus musculus. [Genome view] ENSMUST00000119142; ENSMUSP00000112713; ENSMUSG00000062209; Mus musculus. [Genome view] ENSMUST00000121473; ENSMUSP00000114123; ENSMUSG00000062209; Mus musculus. [Genome view] |
| GeneID | 13869. |
| KEGG | mmu:13869. |
| UCSC | uc007bjb.1. mouse. |
Organism-specific databases | |
| CTD | 13869. |
| MGI | MGI:104771. Erbb4. |
Phylogenomic databases | |
| HOVERGEN | Q61527. |
Enzyme and pathway databases | |
| BRENDA | 2.7.10.1. 244. |
Gene expression databases | |
| ArrayExpress | Q61527. |
| Bgee | Q61527. |
| Genevestigator | Q61527. |
| GermOnline | ENSMUSG00000062209. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000494. EGF_rcpt_L. IPR006211. Furin-like. IPR006212. Furin_repeat. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR016245. Tyr_kinase_rcpt_EGF/ERB/XmrK. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. IPR004019. YLP_motif. [Graphical view] |
| Pfam | PF00757. Furin-like. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF01030. Recep_L_domain. 2 hits. PF02757. YLP. 2 hits. [Graphical view] |
| PIRSF | PIRSF000619. TyrPK_EGF-R. 1 hit. |
| PRINTS | PR00109. TYRKINASE. |
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00261. FU. 5 hits. SM00219. TyrKc. 1 hit. [Graphical view] |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 284772. |
| SOURCE | Search... |
Entry information
| Entry name | ERBB4_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q61527 Secondary accession number(s): O88460, Q3UNS6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| SIMILARITY comments Index of protein domains and families |

Clusters with


