Q15303 (ERBB4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Receptor tyrosine-protein kinase erbB-4
EC=2.7.10.1

Alternative name(s):
Proto-oncogene-like protein c-ErbB-4
Tyrosine kinase-type cell surface receptor HER4
p180erbB4

Cleaved into the following chain:

1. ERBB4 intracellular domain
   Short name=4ICD
   Short name=E4ICD
   Alternative name(s):
   s80HER4

Gene names

Name:	ERBB4
Synonyms:	HER4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1308 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	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. Ref.1 Ref.2 Ref.7 Ref.9 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.38 Ref.40 Ref.48
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.7 Ref.38 Ref.50 Ref.51
Enzyme regulation	Binding of a cognate ligand leads to dimerization and activation by autophosphorylation on tyrosine residues. In vitro kinase activity is increased by Mg2+. Inhibited by PD153035, lapatinib, gefitinib (iressa, ZD1839), AG1478 and BIBX1382BS. Ref.7 Ref.21 Ref.38 Ref.41 Ref.51
Subunit structure	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 CBFA2T3 By similarity. 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, HNRPU, 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 STAT5A. Interacts (soluble intracellular domain) with BCL2. Interacts (phosphorylated) with STAT1. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.31 Ref.34 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.51
Subcellular location	Cell membrane; Single-pass type I membrane protein. Note: In response to NRG1 treatment, the activated receptor is internalized. Ref.1 Ref.2 Ref.16 Ref.23 Ref.25 Ref.28 Ref.30 Ref.31 Ref.33 Ref.35 Ref.37 Ref.40 ERBB4 intracellular domain: Nucleus. Mitochondrion. 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. Ref.1 Ref.2 Ref.16 Ref.23 Ref.25 Ref.28 Ref.30 Ref.31 Ref.33 Ref.35 Ref.37 Ref.40
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 CYT-1 and isoform JM-B CYT-1 are expressed in cerebellum, but only the isoform JM-B is expressed in the heart. Ref.1 Ref.2 Ref.15 Ref.48
Post-translational modification	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. 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. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.17 Ref.19 Ref.21 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.38 Ref.50 Ref.51 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. Ref.33 Ref.37
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily. Contains 1 protein kinase domain.
Caution	Conflicting reports about the role of ERBB4 in mediating apoptosis, differentiation, or tumor cell proliferation may be explained by the opposite functions of the different isoforms and their intracellular fragments, and by the formation of heterodimers with other EGF receptor family members (Ref.46 and Ref.48). Thus, heterodimer formation of a kinase-dead ERBB4 mutant with ERBB2 is sufficient for the activation of AKT1, MAPK1/ERK2 and MAPK3/ERK1 (Ref.38).

Ontologies

Keywords
Biological process	Apoptosis Lactation Transcription Transcription regulation
Cellular component	Cell membrane Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from mutant phenotype Ref.28. Source: UniProtKB cardiac muscle tissue regeneration Inferred from sequence or structural similarity. Source: UniProtKB cell fate commitment Inferred from electronic annotation. Source: Compara cell proliferation Traceable author statement Ref.1. Source: ProtInc central nervous system morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB embryonic pattern specification Inferred from sequence or structural similarity. Source: UniProtKB epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome heart development Inferred from sequence or structural similarity. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome lactation Inferred from mutant phenotype Ref.25. Source: UniProtKB mammary gland alveolus development Inferred from sequence or structural similarity. Source: UniProtKB mammary gland epithelial cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype Ref.17. Source: UniProtKB negative regulation of cell proliferation Inferred from mutant phenotype Ref.32. Source: UniProtKB neural crest cell migration Inferred from sequence or structural similarity. Source: UniProtKB neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome olfactory bulb interneuron differentiation Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.51. Source: UniProtKB phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome positive regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype Ref.16. Source: UniProtKB positive regulation of STAT protein import into nucleus Inferred from mutant phenotype Ref.25. Source: UniProtKB positive regulation of cardiac muscle cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase activity Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.25. Source: UniProtKB positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from mutant phenotype Ref.31. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.51. Source: UniProtKB regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basolateral plasma membrane Inferred from direct assay PubMed 12646923. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial matrix Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro transcription regulatory region DNA binding Inferred from mutant phenotype Ref.25. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from direct assay Ref.51. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DLG4	P78352	6	EBI-80371,EBI-80389
EGFR	P00533	2	EBI-80371,EBI-297353
ERBB2	P04626	2	EBI-80371,EBI-641062
ERBB3	P21860	4	EBI-80371,EBI-720706
HSP90AB1	P08238	2	EBI-80371,EBI-352572

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform JM-A CYT-1 (identifier: Q15303-1)

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.

Note: Proteolytical processing generates E4ICD1 (s80Cyt1).

Isoform JM-B CYT-1 (identifier: Q15303-2)

The sequence of this isoform differs from the canonical sequence as follows:
     626-648: NGPTSHDCIYYPWTGHSTLPQHA → IGSSIEDCIGLMD

Isoform JM-A CYT-2 (identifier: Q15303-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1046-1061: Missing.

Note: Proteolytical processing generates E4ICD2 (s80Cyt2).

Isoform JM-B CYT-2 (identifier: Q15303-4)

The sequence of this isoform differs from the canonical sequence as follows:
     626-648: NGPTSHDCIYYPWTGHSTLPQHA → IGSSIEDCIGLMD
     1046-1061: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 1308

1283

Receptor tyrosine-protein kinase erbB-4

PRO_0000016674

Chain

676 – 1308

633

ERBB4 intracellular domain By similarity

PRO_0000396797

Regions

Topological domain

26 – 651

626

Extracellular Potential

Transmembrane

652 – 675

24

Potential

Topological domain

676 – 1308

633

Cytoplasmic Potential

Domain

718 – 985

268

Protein kinase

Nucleotide binding

724 – 732

9

ATP By similarity

Nucleotide binding

797 – 799

3

ATP By similarity

Nucleotide binding

843 – 848

6

ATP By similarity

Motif

676 – 684

9

Nuclear localization signal

Motif

1032 – 1035

4

PPxY motif 1

Motif

1053 – 1056

4

PPxY motif 2

Motif

1298 – 1301

4

PPxY motif 3

Motif

1306 – 1308

3

PDZ-binding

Compositional bias

186 – 334

149

Cys-rich

Compositional bias

496 – 633

138

Cys-rich

Sites

Active site

843

1

Proton acceptor By similarity

Binding site

751

1

ATP By similarity

Amino acid modifications

Modified residue

875

1

Phosphotyrosine; by autocatalysis Ref.36

Modified residue

1035

1

Phosphotyrosine; by autocatalysis Ref.36

Modified residue

1056

1

Phosphotyrosine; by autocatalysis Ref.7 Ref.32 Ref.36

Modified residue

1150

1

Phosphotyrosine; by autocatalysis Ref.36

Modified residue

1162

1

Phosphotyrosine; by autocatalysis Ref.36

Modified residue

1188

1

Phosphotyrosine; by autocatalysis Ref.7 Ref.36

Modified residue

1202

1

Phosphotyrosine; by autocatalysis Ref.36

Modified residue

1242

1

Phosphotyrosine; by autocatalysis Ref.7 Ref.36

Modified residue

1258

1

Phosphotyrosine; by autocatalysis Ref.36

Modified residue

1284

1

Phosphotyrosine; by autocatalysis Ref.36

Glycosylation

138

1

N-linked (GlcNAc...) Ref.49

Glycosylation

174

1

N-linked (GlcNAc...) Ref.49

Glycosylation

181

1

N-linked (GlcNAc...) Potential

Glycosylation

253

1

N-linked (GlcNAc...) Ref.49

Glycosylation

358

1

N-linked (GlcNAc...) Ref.49

Glycosylation

410

1

N-linked (GlcNAc...) Ref.49

Glycosylation

473

1

N-linked (GlcNAc...) Ref.49

Glycosylation

495

1

N-linked (GlcNAc...) Ref.49

Glycosylation

548

1

N-linked (GlcNAc...) Potential

Glycosylation

576

1

N-linked (GlcNAc...) Ref.49

Glycosylation

620

1

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 56

Ref.49

Disulfide bond

156 ↔ 186

Ref.49

Disulfide bond

189 ↔ 197

Ref.49

Disulfide bond

193 ↔ 205

Ref.49

Disulfide bond

213 ↔ 221

Ref.49

Disulfide bond

217 ↔ 229

Ref.49

Disulfide bond

230 ↔ 238

Ref.49

Disulfide bond

234 ↔ 246

Ref.49

Disulfide bond

249 ↔ 258

Ref.49

Disulfide bond

262 ↔ 289

Ref.49

Disulfide bond

293 ↔ 304

Ref.49

Disulfide bond

308 ↔ 323

Ref.49

Disulfide bond

326 ↔ 330

Ref.49

Disulfide bond

503 ↔ 512

Ref.49

Disulfide bond

507 ↔ 520

Ref.49

Disulfide bond

523 ↔ 532

Ref.49

Disulfide bond

536 ↔ 552

Ref.49

Disulfide bond

555 ↔ 569

Ref.49

Disulfide bond

559 ↔ 577

Ref.49

Disulfide bond

580 ↔ 589

Ref.49

Disulfide bond

593 ↔ 614

Ref.49

Disulfide bond

617 ↔ 625

Ref.49

Disulfide bond

621 ↔ 633

Ref.49

Natural variations

Alternative sequence

626 – 648

23

NGPTS…LPQHA → IGSSIEDCIGLMD in isoform JM-B CYT-1 and isoform JM-B CYT-2.

VSP_002895

Alternative sequence

1046 – 1061

16

Missing in isoform JM-A CYT-2 and isoform JM-B CYT-2.

VSP_022148

Natural variant

140

1

T → I in a colorectal adenocarcinoma sample; somatic mutation. Ref.52

VAR_042113

Natural variant

303

1

S → Y in a lung squamous cell carcinoma sample; somatic mutation. Ref.52

VAR_042114

Experimental info

Mutagenesis

646

1

Q → C: Constitutively activated kinase. Ref.32

Mutagenesis

675

1

V → A: Abolishes proteolytic processing and nuclear localization. Ref.27 Ref.33

Mutagenesis

681 – 684

4

KKKR → EIMG: Abolishes nuclear localization of the ERBB4 intracellular domain. Ref.25

Mutagenesis

710

1

L → N: Strongly reduced autophosphorylation. Ref.50

Mutagenesis

721

1

V → I: No effect on kinase activity. Ref.38

Mutagenesis

751

1

K → R: Abolishes kinase activity. Abolishes phosphorylation, proteolytic processing and nuclear localization. Ref.22 Ref.33 Ref.35

Mutagenesis

766

1

M → R: Strongly reduced autophosphorylation. Ref.50

Mutagenesis

773

1

A → S: No effect on kinase activity. Ref.38

Mutagenesis

782

1

R → Q: No effect on kinase activity. Ref.38

Mutagenesis

810

1

E → K: No effect on kinase activity. Ref.38

Mutagenesis

843

1

D → N: Loss of kinase activity. Ref.34

Mutagenesis

854

1

P → Q: No effect on kinase activity. Ref.38

Mutagenesis

861

1

D → Y: Loss of kinase activity. Ref.38

Mutagenesis

864

1

L → R: Strongly reduced autophosphorylation. Ref.50

Mutagenesis

872

1

E → K: No effect on kinase activity. Ref.38

Mutagenesis

926

1

T → M: No effect on kinase activity. Ref.38

Mutagenesis

947

1

I → R: Constitutively autophosphorylated. Ref.50

Mutagenesis

992

1

R → A: Abolishes APC/C-mediated degradation; when associated with A-995 and A-1000. Ref.33

Mutagenesis

995

1

L → A: Abolishes APC/C-mediated degradation; when associated with A-992 and A-1000. Ref.33

Mutagenesis

1000

1

D → A: Abolishes APC/C-mediated degradation; when associated with A-992 and A-995. Ref.33

Mutagenesis

1035

1

Y → A: No effect on interaction with WWOX. Abolishes interaction with WWOX; when associated with A-1301. Ref.26

Mutagenesis

1056

1

Y → A: Abolishes interaction with NEDD4 and impairs ubiquitination. Promotes nuclear translocation of ERBB4 intracellular domain E4ICD1. Ref.39

Mutagenesis

1056

1

Y → F: Abolishes interaction with WWP1; when associated with F-1301. Ref.39

Mutagenesis

1301

1

Y → A: Abolishes interaction with NEDD4 and impairs ubiquitination. Ref.23 Ref.26 Ref.39

Mutagenesis

1301

1

Y → A: No effect on interaction with WWOX. Abolishes interaction with WWOX; when associated with A-1035. Loss of interaction with YAP1 and stimulation of transcription. Ref.23 Ref.26 Ref.39

Mutagenesis

1301

1

Y → F: Abolishes interaction with WWP1; when associated with F-1056. Ref.23 Ref.26 Ref.39

Secondary structure

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1308

Helix Strand Turn

Details...

Beta strand

28 – 30

3

Beta strand

38 – 41

4

Helix

42 – 53

12

Beta strand

57 – 61

5

Beta strand

63 – 67

5

Helix

75 – 79

5

Beta strand

82 – 85

4

Beta strand

87 – 91

5

Beta strand

95 – 98

4

Turn

112 – 114

3

Beta strand

115 – 120

6

Beta strand

125 – 128

4

Beta strand

133 – 135

3

Beta strand

144 – 150

7

Helix

158 – 160

3

Helix

163 – 165

3

Helix

173 – 175

3

Beta strand

176 – 178

3

Turn

191 – 193

3

Beta strand

197 – 201

5

Helix

202 – 204

3

Beta strand

221 – 225

5

Helix

226 – 228

3

Beta strand

234 – 242

9

Beta strand

245 – 254

10

Beta strand

257 – 261

5

Beta strand

265 – 269

5

Turn

270 – 273

4

Beta strand

274 – 277

4

Beta strand

283 – 285

3

Beta strand

288 – 292

5

Beta strand

298 – 300

3

Beta strand

303 – 307

5

Beta strand

312 – 317

6

Beta strand

320 – 325

6

Beta strand

327 – 329

3

Beta strand

333 – 335

3

Helix

340 – 342

3

Turn

350 – 352

3

Helix

353 – 356

4

Beta strand

360 – 364

5

Beta strand

366 – 368

3

Helix

370 – 374

5

Helix

377 – 379

3

Helix

386 – 394

9

Beta strand

397 – 400

4

Beta strand

402 – 405

4

Helix

415 – 417

3

Beta strand

432 – 438

7

Beta strand

455 – 461

7

Helix

469 – 471

3

Helix

474 – 476

3

Beta strand

479 – 482

4

Beta strand

485 – 487

3

Beta strand

489 – 491

3

Helix

493 – 497

5

Turn

498 – 500

3

Beta strand

512 – 516

5

Beta strand

519 – 528

10

Beta strand

531 – 534

4

Beta strand

537 – 543

7

Beta strand

545 – 548

4

Beta strand

551 – 554

4

Beta strand

568 – 573

6

Beta strand

576 – 585

10

Beta strand

588 – 592

5

Beta strand

595 – 608

14

Beta strand

612 – 616

5

Beta strand

625 – 629

5

Helix

651 – 676

26

Helix

715 – 717

3

Beta strand

718 – 729

12

Beta strand

731 – 737

7

Beta strand

740 – 743

4

Beta strand

746 – 752

7

Helix

762 – 773

12

Beta strand

778 – 780

3

Beta strand

783 – 787

5

Beta strand

789 – 791

3

Beta strand

793 – 797

5

Helix

804 – 810

7

Helix

812 – 814

3

Helix

817 – 836

20

Helix

846 – 848

3

Beta strand

849 – 853

5

Beta strand

856 – 859

4

Helix

864 – 869

6

Helix

884 – 886

3

Helix

889 – 893

5

Helix

899 – 914

16

Turn

920 – 923

4

Turn

926 – 928

3

Helix

929 – 934

6

Helix

947 – 955

9

Helix

961 – 963

3

Helix

967 – 977

11

Helix

981 – 983

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform JM-A CYT-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5E4AE80985D88761	FASTA	1,308	146,808
	10 20 30 40 50 60 MKPATGLWVW VSLLVAAGTV QPSDSQSVCA GTENKLSSLS DLEQQYRALR KYYENCEVVM 70 80 90 100 110 120 GNLEITSIEH NRDLSFLRSV REVTGYVLVA LNQFRYLPLE NLRIIRGTKL YEDRYALAIF 130 140 150 160 170 180 LNYRKDGNFG LQELGLKNLT EILNGGVYVD QNKFLCYADT IHWQDIVRNP WPSNLTLVST 190 200 210 220 230 240 NGSSGCGRCH KSCTGRCWGP TENHCQTLTR TVCAEQCDGR CYGPYVSDCC HRECAGGCSG 250 260 270 280 290 300 PKDTDCFACM NFNDSGACVT QCPQTFVYNP TTFQLEHNFN AKYTYGAFCV KKCPHNFVVD 310 320 330 340 350 360 SSSCVRACPS SKMEVEENGI KMCKPCTDIC PKACDGIGTG SLMSAQTVDS SNIDKFINCT 370 380 390 400 410 420 KINGNLIFLV TGIHGDPYNA IEAIDPEKLN VFRTVREITG FLNIQSWPPN MTDFSVFSNL 430 440 450 460 470 480 VTIGGRVLYS GLSLLILKQQ GITSLQFQSL KEISAGNIYI TDNSNLCYYH TINWTTLFST 490 500 510 520 530 540 INQRIVIRDN RKAENCTAEG MVCNHLCSSD GCWGPGPDQC LSCRRFSRGR ICIESCNLYD 550 560 570 580 590 600 GEFREFENGS ICVECDPQCE KMEDGLLTCH GPGPDNCTKC SHFKDGPNCV EKCPDGLQGA 610 620 630 640 650 660 NSFIFKYADP DRECHPCHPN CTQGCNGPTS HDCIYYPWTG HSTLPQHART PLIAAGVIGG 670 680 690 700 710 720 LFILVIVGLT FAVYVRRKSI KKKRALRRFL ETELVEPLTP SGTAPNQAQL RILKETELKR 730 740 750 760 770 780 VKVLGSGAFG TVYKGIWVPE GETVKIPVAI KILNETTGPK ANVEFMDEAL IMASMDHPHL 790 800 810 820 830 840 VRLLGVCLSP TIQLVTQLMP HGCLLEYVHE HKDNIGSQLL LNWCVQIAKG MMYLEERRLV 850 860 870 880 890 900 HRDLAARNVL VKSPNHVKIT DFGLARLLEG DEKEYNADGG KMPIKWMALE CIHYRKFTHQ 910 920 930 940 950 960 SDVWSYGVTI WELMTFGGKP YDGIPTREIP DLLEKGERLP QPPICTIDVY MVMVKCWMID 970 980 990 1000 1010 1020 ADSRPKFKEL AAEFSRMARD PQRYLVIQGD DRMKLPSPND SKFFQNLLDE EDLEDMMDAE 1030 1040 1050 1060 1070 1080 EYLVPQAFNI PPPIYTSRAR IDSNRSEIGH SPPPAYTPMS GNQFVYRDGG FAAEQGVSVP 1090 1100 1110 1120 1130 1140 YRAPTSTIPE APVAQGATAE IFDDSCCNGT LRKPVAPHVQ EDSSTQRYSA DPTVFAPERS 1150 1160 1170 1180 1190 1200 PRGELDEEGY MTPMRDKPKQ EYLNPVEENP FVSRRKNGDL QALDNPEYHN ASNGPPKAED 1210 1220 1230 1240 1250 1260 EYVNEPLYLN TFANTLGKAE YLKNNILSMP EKAKKAFDNP DYWNHSLPPR STLQHPDYLQ 1270 1280 1290 1300 EYSTKYFYKQ NGRIRPIVAE NPEYLSEFSL KPGTVLPPPP YRHRNTVV
	Isoform JM-B CYT-1 [UniParc]. Checksum: 346C1288AD041961	FASTA	1,298	145,578
	10 20 30 40 50 60 MKPATGLWVW VSLLVAAGTV QPSDSQSVCA GTENKLSSLS DLEQQYRALR KYYENCEVVM 70 80 90 100 110 120 GNLEITSIEH NRDLSFLRSV REVTGYVLVA LNQFRYLPLE NLRIIRGTKL YEDRYALAIF 130 140 150 160 170 180 LNYRKDGNFG LQELGLKNLT EILNGGVYVD QNKFLCYADT IHWQDIVRNP WPSNLTLVST 190 200 210 220 230 240 NGSSGCGRCH KSCTGRCWGP TENHCQTLTR TVCAEQCDGR CYGPYVSDCC HRECAGGCSG 250 260 270 280 290 300 PKDTDCFACM NFNDSGACVT QCPQTFVYNP TTFQLEHNFN AKYTYGAFCV KKCPHNFVVD 310 320 330 340 350 360 SSSCVRACPS SKMEVEENGI KMCKPCTDIC PKACDGIGTG SLMSAQTVDS SNIDKFINCT 370 380 390 400 410 420 KINGNLIFLV TGIHGDPYNA IEAIDPEKLN VFRTVREITG FLNIQSWPPN MTDFSVFSNL 430 440 450 460 470 480 VTIGGRVLYS GLSLLILKQQ GITSLQFQSL KEISAGNIYI TDNSNLCYYH TINWTTLFST 490 500 510 520 530 540 INQRIVIRDN RKAENCTAEG MVCNHLCSSD GCWGPGPDQC LSCRRFSRGR ICIESCNLYD 550 560 570 580 590 600 GEFREFENGS ICVECDPQCE KMEDGLLTCH GPGPDNCTKC SHFKDGPNCV EKCPDGLQGA 610 620 630 640 650 660 NSFIFKYADP DRECHPCHPN CTQGCIGSSI EDCIGLMDRT PLIAAGVIGG LFILVIVGLT 670 680 690 700 710 720 FAVYVRRKSI KKKRALRRFL ETELVEPLTP SGTAPNQAQL RILKETELKR VKVLGSGAFG 730 740 750 760 770 780 TVYKGIWVPE GETVKIPVAI KILNETTGPK ANVEFMDEAL IMASMDHPHL VRLLGVCLSP 790 800 810 820 830 840 TIQLVTQLMP HGCLLEYVHE HKDNIGSQLL LNWCVQIAKG MMYLEERRLV HRDLAARNVL 850 860 870 880 890 900 VKSPNHVKIT DFGLARLLEG DEKEYNADGG KMPIKWMALE CIHYRKFTHQ SDVWSYGVTI 910 920 930 940 950 960 WELMTFGGKP YDGIPTREIP DLLEKGERLP QPPICTIDVY MVMVKCWMID ADSRPKFKEL 970 980 990 1000 1010 1020 AAEFSRMARD PQRYLVIQGD DRMKLPSPND SKFFQNLLDE EDLEDMMDAE EYLVPQAFNI 1030 1040 1050 1060 1070 1080 PPPIYTSRAR IDSNRSEIGH SPPPAYTPMS GNQFVYRDGG FAAEQGVSVP YRAPTSTIPE 1090 1100 1110 1120 1130 1140 APVAQGATAE IFDDSCCNGT LRKPVAPHVQ EDSSTQRYSA DPTVFAPERS PRGELDEEGY 1150 1160 1170 1180 1190 1200 MTPMRDKPKQ EYLNPVEENP FVSRRKNGDL QALDNPEYHN ASNGPPKAED EYVNEPLYLN 1210 1220 1230 1240 1250 1260 TFANTLGKAE YLKNNILSMP EKAKKAFDNP DYWNHSLPPR STLQHPDYLQ EYSTKYFYKQ 1270 1280 1290 NGRIRPIVAE NPEYLSEFSL KPGTVLPPPP YRHRNTVV
	Isoform JM-A CYT-2 [UniParc]. Checksum: 60C0DFD446C7FA89	FASTA	1,292	145,198
	10 20 30 40 50 60 MKPATGLWVW VSLLVAAGTV QPSDSQSVCA GTENKLSSLS DLEQQYRALR KYYENCEVVM 70 80 90 100 110 120 GNLEITSIEH NRDLSFLRSV REVTGYVLVA LNQFRYLPLE NLRIIRGTKL YEDRYALAIF 130 140 150 160 170 180 LNYRKDGNFG LQELGLKNLT EILNGGVYVD QNKFLCYADT IHWQDIVRNP WPSNLTLVST 190 200 210 220 230 240 NGSSGCGRCH KSCTGRCWGP TENHCQTLTR TVCAEQCDGR CYGPYVSDCC HRECAGGCSG 250 260 270 280 290 300 PKDTDCFACM NFNDSGACVT QCPQTFVYNP TTFQLEHNFN AKYTYGAFCV KKCPHNFVVD 310 320 330 340 350 360 SSSCVRACPS SKMEVEENGI KMCKPCTDIC PKACDGIGTG SLMSAQTVDS SNIDKFINCT 370 380 390 400 410 420 KINGNLIFLV TGIHGDPYNA IEAIDPEKLN VFRTVREITG FLNIQSWPPN MTDFSVFSNL 430 440 450 460 470 480 VTIGGRVLYS GLSLLILKQQ GITSLQFQSL KEISAGNIYI TDNSNLCYYH TINWTTLFST 490 500 510 520 530 540 INQRIVIRDN RKAENCTAEG MVCNHLCSSD GCWGPGPDQC LSCRRFSRGR ICIESCNLYD 550 560 570 580 590 600 GEFREFENGS ICVECDPQCE KMEDGLLTCH GPGPDNCTKC SHFKDGPNCV EKCPDGLQGA 610 620 630 640 650 660 NSFIFKYADP DRECHPCHPN CTQGCNGPTS HDCIYYPWTG HSTLPQHART PLIAAGVIGG 670 680 690 700 710 720 LFILVIVGLT FAVYVRRKSI KKKRALRRFL ETELVEPLTP SGTAPNQAQL RILKETELKR 730 740 750 760 770 780 VKVLGSGAFG TVYKGIWVPE GETVKIPVAI KILNETTGPK ANVEFMDEAL IMASMDHPHL 790 800 810 820 830 840 VRLLGVCLSP TIQLVTQLMP HGCLLEYVHE HKDNIGSQLL LNWCVQIAKG MMYLEERRLV 850 860 870 880 890 900 HRDLAARNVL VKSPNHVKIT DFGLARLLEG DEKEYNADGG KMPIKWMALE CIHYRKFTHQ 910 920 930 940 950 960 SDVWSYGVTI WELMTFGGKP YDGIPTREIP DLLEKGERLP QPPICTIDVY MVMVKCWMID 970 980 990 1000 1010 1020 ADSRPKFKEL AAEFSRMARD PQRYLVIQGD DRMKLPSPND SKFFQNLLDE EDLEDMMDAE 1030 1040 1050 1060 1070 1080 EYLVPQAFNI PPPIYTSRAR IDSNRNQFVY RDGGFAAEQG VSVPYRAPTS TIPEAPVAQG 1090 1100 1110 1120 1130 1140 ATAEIFDDSC CNGTLRKPVA PHVQEDSSTQ RYSADPTVFA PERSPRGELD EEGYMTPMRD 1150 1160 1170 1180 1190 1200 KPKQEYLNPV EENPFVSRRK NGDLQALDNP EYHNASNGPP KAEDEYVNEP LYLNTFANTL 1210 1220 1230 1240 1250 1260 GKAEYLKNNI LSMPEKAKKA FDNPDYWNHS LPPRSTLQHP DYLQEYSTKY FYKQNGRIRP 1270 1280 1290 IVAENPEYLS EFSLKPGTVL PPPPYRHRNT VV
	Isoform JM-B CYT-2 [UniParc]. Checksum: 68F27777BC9E2F74	FASTA	1,282	143,968
	10 20 30 40 50 60 MKPATGLWVW VSLLVAAGTV QPSDSQSVCA GTENKLSSLS DLEQQYRALR KYYENCEVVM 70 80 90 100 110 120 GNLEITSIEH NRDLSFLRSV REVTGYVLVA LNQFRYLPLE NLRIIRGTKL YEDRYALAIF 130 140 150 160 170 180 LNYRKDGNFG LQELGLKNLT EILNGGVYVD QNKFLCYADT IHWQDIVRNP WPSNLTLVST 190 200 210 220 230 240 NGSSGCGRCH KSCTGRCWGP TENHCQTLTR TVCAEQCDGR CYGPYVSDCC HRECAGGCSG 250 260 270 280 290 300 PKDTDCFACM NFNDSGACVT QCPQTFVYNP TTFQLEHNFN AKYTYGAFCV KKCPHNFVVD 310 320 330 340 350 360 SSSCVRACPS SKMEVEENGI KMCKPCTDIC PKACDGIGTG SLMSAQTVDS SNIDKFINCT 370 380 390 400 410 420 KINGNLIFLV TGIHGDPYNA IEAIDPEKLN VFRTVREITG FLNIQSWPPN MTDFSVFSNL 430 440 450 460 470 480 VTIGGRVLYS GLSLLILKQQ GITSLQFQSL KEISAGNIYI TDNSNLCYYH TINWTTLFST 490 500 510 520 530 540 INQRIVIRDN RKAENCTAEG MVCNHLCSSD GCWGPGPDQC LSCRRFSRGR ICIESCNLYD 550 560 570 580 590 600 GEFREFENGS ICVECDPQCE KMEDGLLTCH GPGPDNCTKC SHFKDGPNCV EKCPDGLQGA 610 620 630 640 650 660 NSFIFKYADP DRECHPCHPN CTQGCIGSSI EDCIGLMDRT PLIAAGVIGG LFILVIVGLT 670 680 690 700 710 720 FAVYVRRKSI KKKRALRRFL ETELVEPLTP SGTAPNQAQL RILKETELKR VKVLGSGAFG 730 740 750 760 770 780 TVYKGIWVPE GETVKIPVAI KILNETTGPK ANVEFMDEAL IMASMDHPHL VRLLGVCLSP 790 800 810 820 830 840 TIQLVTQLMP HGCLLEYVHE HKDNIGSQLL LNWCVQIAKG MMYLEERRLV HRDLAARNVL 850 860 870 880 890 900 VKSPNHVKIT DFGLARLLEG DEKEYNADGG KMPIKWMALE CIHYRKFTHQ SDVWSYGVTI 910 920 930 940 950 960 WELMTFGGKP YDGIPTREIP DLLEKGERLP QPPICTIDVY MVMVKCWMID ADSRPKFKEL 970 980 990 1000 1010 1020 AAEFSRMARD PQRYLVIQGD DRMKLPSPND SKFFQNLLDE EDLEDMMDAE EYLVPQAFNI 1030 1040 1050 1060 1070 1080 PPPIYTSRAR IDSNRNQFVY RDGGFAAEQG VSVPYRAPTS TIPEAPVAQG ATAEIFDDSC 1090 1100 1110 1120 1130 1140 CNGTLRKPVA PHVQEDSSTQ RYSADPTVFA PERSPRGELD EEGYMTPMRD KPKQEYLNPV 1150 1160 1170 1180 1190 1200 EENPFVSRRK NGDLQALDNP EYHNASNGPP KAEDEYVNEP LYLNTFANTL GKAEYLKNNI 1210 1220 1230 1240 1250 1260 LSMPEKAKKA FDNPDYWNHS LPPRSTLQHP DYLQEYSTKY FYKQNGRIRP IVAENPEYLS 1270 1280 EFSLKPGTVL PPPPYRHRNT VV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ligand-specific activation of HER4/p180erbB4, a fourth member of the epidermal growth factor receptor family." Plowman G.D., Culouscou J.-M., Whitney G.S., Green J.M., Carlton G.W., Foy L., Neubauer M.G., Shoyab M. Proc. Natl. Acad. Sci. U.S.A. 90:1746-1750(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JM-A CYT-1), FUNCTION AS CELL SURFACE RECEPTOR, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Mammary carcinoma.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS JM-A CYT-1 AND JM-B CYT-1), TISSUE SPECIFICITY, FUNCTION AS CELL SURFACE RECEPTOR FOR NRG1 AND BTC, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PROTEOLYTIC PROCESSING. Tissue: Fetal brain.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS JM-A CYT-1; JM-B CYT-1; JM-A CYT-2 AND JM-B CYT-2). Tissue: Brain.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 401-1308 (ISOFORM JM-A CYT-2). Tissue: Brain.
[5]	"Characterization of a breast cancer cell differentiation factor that specifically activates the HER4/p180erbB4 receptor." Culouscou J.-M., Plowman G.D., Carlton G.W., Green J.M., Shoyab M. J. Biol. Chem. 268:18407-18410(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NRG1, AUTOPHOSPHORYLATION.
[6]	"Heregulin induces tyrosine phosphorylation of HER4/p180erbB4." Plowman G.D., Green J.M., Culouscou J.M., Carlton G.W., Rothwell V.M., Buckley S. Nature 366:473-475(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NRG1, AUTOPHOSPHORYLATION.
[7]	"HER4-mediated biological and biochemical properties in NIH 3T3 cells. Evidence for HER1-HER4 heterodimers." Cohen B.D., Green J.M., Foy L., Fell H.P. J. Biol. Chem. 271:4813-4818(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NRG1 RECEPTOR IN REGULATION OF CELL PROLIFERATION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-1056; TYR-1188 AND TYR-1242, INTERACTION WITH EGFR; SHC1 AND PIK3R1.
[8]	"Betacellulin activates the epidermal growth factor receptor and erbB-4, and induces cellular response patterns distinct from those stimulated by epidermal growth factor or neuregulin-beta." Riese D.J. II, Bermingham Y., van Raaij T.M., Buckley S., Plowman G.D., Stern D.F. Oncogene 12:345-353(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BTC, AUTOPHOSPHORYLATION.
[9]	"Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation." Elenius K., Paul S., Allison G., Sun J., Klagsbrun M. EMBO J. 16:1268-1278(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS HBEGF RECEPTOR; IN CELL MIGRATION; CELL PROLIFERATION AND IN ACTIVATION OF PIK3R1, INTERACTION WITH HBEGF AND PIK3R1, AUTOPHOSPHORYLATION.
[10]	"Neuregulin-2, a new ligand of ErbB3/ErbB4-receptor tyrosine kinases." Carraway K.L. III, Weber J.L., Unger M.J., Ledesma J., Yu N., Gassmann M., Lai C. Nature 387:512-516(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NRG2, FUNCTION AS NRG2 RECEPTOR, PHOSPHORYLATION.
[11]	"Epiregulin binds to epidermal growth factor receptor and ErbB-4 and induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-2, ErbB-3 and ErbB-4." Komurasaki T., Toyoda H., Uchida D., Morimoto S. Oncogene 15:2841-2848(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EREG, AUTOPHOSPHORYLATION.
[12]	"Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that binds and activates ErbB4." Zhang D., Sliwkowski M.X., Mark M., Frantz G., Akita R., Sun Y., Hillan K., Crowley C., Brush J., Godowski P.J. Proc. Natl. Acad. Sci. U.S.A. 94:9562-9567(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NRG3, AUTOPHOSPHORYLATION.
[13]	"Analysis of Grb7 recruitment by heregulin-activated erbB receptors reveals a novel target selectivity for erbB3." Fiddes R.J., Campbell D.H., Janes P.W., Sivertsen S.P., Sasaki H., Wallasch C., Daly R.J. J. Biol. Chem. 273:7717-7724(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB7.
[14]	"ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases." Olayioye M.A., Beuvink I., Horsch K., Daly J.M., Hynes N.E. J. Biol. Chem. 274:17209-17218(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERBB2, FUNCTION IN ACTIVATION OF STAT5A.
[15]	"Characterization of a naturally occurring ErbB4 isoform that does not bind or activate phosphatidyl inositol 3-kinase." Elenius K., Choi C.J., Paul S., Santiestevan E., Nishi E., Klagsbrun M. Oncogene 18:2607-2615(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF PIK3R1, INTERACTION WITH NRG1 AND PIKR3R1, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[16]	"Neuregulin-4: a novel growth factor that acts through the ErbB-4 receptor tyrosine kinase." Harari D., Tzahar E., Romano J., Shelly M., Pierce J.H., Andrews G.C., Yarden Y. Oncogene 18:2681-2689(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NRG4 RECEPTOR IN ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1 AND IN CELL PROLIFERATION, INTERACTION WITH NRG4, SUBCELLULAR LOCATION.
[17]	"A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis." Kainulainen V., Sundvall M., Maatta J.A., Santiestevan E., Klagsbrun M., Elenius K. J. Biol. Chem. 275:8641-8649(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NRG1 RECEPTOR IN CELL PROLIFERATION; MIGRATION; SURVIVAL AND IN PHOSPHORYLATION OF SHC1; ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1, ALTERNATIVE SPLICING.
[18]	"Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4." Rio C., Buxbaum J.D., Peschon J.J., Corfas G. J. Biol. Chem. 275:10379-10387(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[19]	"Ligand discrimination in signaling through an ErbB4 receptor homodimer." Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C., Carraway K.L. III J. Biol. Chem. 275:19803-19807(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF AKT1; MAPK1/ERK2 AND MAPK3/ERK1, INTERACTION WITH PIK3R1; GRB2; SHC1; BTC; NRG1; NRG2 AND NRG3, LIGAND-SPECIFIC AUTOPHOSPHORYLATION.
[20]	"The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses." Garcia R.A., Vasudevan K., Buonanno A. Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DLG2; DLG3; DLG4 AND SNTB2.
[21]	"BIBX1382BS, but not AG1478 or PD153035, inhibits the ErbB kinases at different concentrations in intact cells." Egeblad M., Mortensen O.H., van Kempen L.C., Jaattela M. Biochem. Biophys. Res. Commun. 281:25-31(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NRG1 RECEPTOR AND IN ACTIVATION OF MAP KINASES, AUTOPHOSPHORYLATION, ENZYME REGULATION.
[22]	"Her4 mediates ligand-dependent antiproliferative and differentiation responses in human breast cancer cells." Sartor C.I., Zhou H., Kozlowska E., Guttridge K., Kawata E., Caskey L., Harrelson J., Hynes N., Ethier S., Calvo B., Earp H.S. III Mol. Cell. Biol. 21:4265-4275(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-751, FUNCTION IN PROMOTING CELL DIFFERENTIATION AND INHIBITING CELL PROLIFERATION.
[23]	"WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus." Komuro A., Nagai M., Navin N.E., Sudol M. J. Biol. Chem. 278:33334-33341(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, INTERACTION WITH YAP1, MUTAGENESIS OF TYR-1301.
[24]	"Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein." Li Y., Yu W.-H., Ren J., Chen W., Huang L., Kharbanda S., Loda M., Kufe D. Mol. Cancer Res. 1:765-775(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MUC1.
[25]	"The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone." Williams C.C., Allison J.G., Vidal G.A., Burow M.E., Beckman B.S., Marrero L., Jones F.E. J. Cell Biol. 167:469-478(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STAT5A, SUBCELLULAR LOCATION, FUNCTION IN NUCLEAR LOCALIZATION OF STAT5A; DNA-BINDING AND TRANSCRIPTION ACTIVATION OF GENES FOR MILK PROTEINS, MUTAGENESIS OF 681-LYS--ARG-684.
[26]	"WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function." Aqeilan R.I., Donati V., Palamarchuk A., Trapasso F., Kaou M., Pekarsky Y., Sudol M., Croce C.M. Cancer Res. 65:6764-6772(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWOX, DOMAIN, MUTAGENESIS OF TYR-1035 AND TYR-1301.
[27]	"Presenilin-dependent gamma-secretase processing regulates multiple ERBB4/HER4 activities." Vidal G.A., Naresh A., Marrero L., Jones F.E. J. Biol. Chem. 280:19777-19783(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF VAL-675.
[28]	"The ERBB4/HER4 intracellular domain 4ICD is a BH3-only protein promoting apoptosis of breast cancer cells." Naresh A., Long W., Vidal G.A., Wimley W.C., Marrero L., Sartor C.I., Tovey S., Cooke T.G., Bartlett J.M., Jones F.E. Cancer Res. 66:6412-6420(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PROMOTING APOPTOSIS, SUBCELLULAR LOCATION, INTERACTION WITH BCL2.
[29]	"ErbB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional repression." Linggi B., Carpenter G. J. Biol. Chem. 281:25373-25380(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
[30]	"Proteolytic cleavage and phosphorylation of a tumor-associated ErbB4 isoform promote ligand-independent survival and cancer cell growth." Maatta J.A., Sundvall M., Junttila T.T., Peri L., Laine V.J., Isola J., Egeblad M., Elenius K. Mol. Biol. Cell 17:67-79(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[31]	"The intracellular domain of ErbB4 induces differentiation of mammary epithelial cells." Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L., Feng S.M., Elenius K., Earp H.S. III Mol. Biol. Cell 17:4118-4129(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DIFFERENTIATION OF MAMMARY EPITHELIUM; STAT5A PHOSPHORYLATION AND TRANSCRIPTION ACTIVATION OF GENES FOR MILK PROTEINS, PROTEOLYTIC PROCESSSING, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH STAT5A.
[32]	"Phosphorylation of ErbB4 on tyrosine 1056 is critical for ErbB4 coupling to inhibition of colony formation by human mammary cell lines." Pitfield S.E., Bryant I., Penington D.J., Park G., Riese D.J. II Oncol. Res. 16:179-193(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TUMOR SUPPRESSOR, MUTAGENESIS OF GLN-646, PHOSPHORYLATION AT TYR-1056.
[33]	"HER4 D-box sequences regulate mitotic progression and degradation of the nuclear HER4 cleavage product s80HER4." Strunk K.E., Husted C., Miraglia L.C., Sandahl M., Rearick W.A., Hunter D.M., Earp H.S. III, Muraoka-Cook R.S. Cancer Res. 67:6582-6590(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF ERBB4 INTRACELLULAR DOMAIN, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, UBIQUITINATION OF ERBB4 INTRACELLULAR DOMAIN, MUTAGENESIS OF VAL-675; LYS-751; ARG-992; LEU-995 AND ASP-1000.
[34]	"Neuregulin-1 only induces trans-phosphorylation between ErbB receptor heterodimer partners." Li Z., Mei Y., Liu X., Zhou M. Cell. Signal. 19:466-471(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERBB2, MUTAGENESIS OF ASP-843, AUTOPHOSPHORYLATION IN TRANS.
[35]	"Differential nuclear localization and kinase activity of alternative ErbB4 intracellular domains." Sundvall M., Peri L., Maatta J.A., Tvorogov D., Paatero I., Savisalo M., Silvennoinen O., Yarden Y., Elenius K. Oncogene 26:6905-6914(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF E4ICD, PHOSPHORYLATION, SUBCELLULAR LOCATION OF E4ICD, MUTAGENESIS OF LYS-751.
[36]	"System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties." Kaushansky A., Gordus A., Budnik B.A., Lane W.S., Rush J., MacBeath G. Chem. Biol. 15:808-817(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-875; TYR-1035; TYR-1056; TYR-1150; TYR-1162; TYR-1188; TYR-1202; TYR-1242; TYR-1258 AND TYR-1284, INTERACTION WITH PIK3R1 AND STAT1, MASS SPECTROMETRY.
[37]	"Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells." Zeng F., Xu J., Harris R.C. FASEB J. 23:1935-1945(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEDD4, SUBCELLULAR LOCATION, UBIQUITINATION OF E4ICD1.
[38]	"Somatic mutations of ErbB4: selective loss-of-function phenotype affecting signal transduction pathways in cancer." Tvorogov D., Sundvall M., Kurppa K., Hollmen M., Repo S., Johnson M.S., Elenius K. J. Biol. Chem. 284:5582-5591(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TUMOR SUPPRESSOR AND IN ACTIVATION OF SIGNALING PATHWAYS, INTERACTION WITH ERBB2, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, PHOSPHORYLATION BY ERBB2, ENZYME REGULATION, MUTAGENESIS OF VAL-721; ALA-773; ARG-782; GLU-810; PRO-854; ASP-861; GLU-872 AND THR-926.
[39]	"WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer." Li Y., Zhou Z., Alimandi M., Chen C. Oncogene 28:2948-2958(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWP1, MUTAGENESIS OF TYR-1056 AND TYR-1301.
[40]	"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways." Gilmore-Hebert M., Ramabhadran R., Stern D.F. Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TXNL4A; DDX23; MATR3; RBM15; ILF3; TRIM28; U5S1; U2SURP; ITCH; HNRPU; AP2A1; NULC; LEO1; WWP2; MDM2; HXK1 AND ARS2, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[41]	"Small tyrosine kinase inhibitors interrupt EGFR signaling by interacting with erbB3 and erbB4 in glioblastoma cell lines." Carrasco-Garcia E., Saceda M., Grasso S., Rocamora-Reverte L., Conde M., Gomez-Martinez A., Garcia-Morales P., Ferragut J.A., Martinez-Lacaci I. Exp. Cell Res. 317:1476-1489(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[42]	"ErbB4 signaling during breast and neural development: novel genetic models reveal unique ErbB4 activities." Jones F.E., Golding J.P., Gassmann M. Cell Cycle 2:555-559(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN BREAST AND NEURAL DEVELOPMENT.
[43]	"The diverse signaling network of EGFR, HER2, HER3 and HER4 tyrosine kinase receptors and the consequences for therapeutic approaches." Zaczek A., Brandt B., Bielawski K.P. Histol. Histopathol. 20:1005-1015(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[44]	"ErbB4/HER4: role in mammary gland development, differentiation and growth inhibition." Muraoka-Cook R.S., Feng S.M., Strunk K.E., Earp H.S. III J. Mammary Gland Biol. Neoplasia 13:235-246(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN MAMMARY GLAND DEVELOPMENT.
[45]	"HER4 intracellular domain (4ICD) activity in the developing mammary gland and breast cancer." Jones F.E. J. Mammary Gland Biol. Neoplasia 13:247-258(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE OF THE ERBB4 INTRACELLULAR DOMAIN.
[46]	"Role of ErbB4 in breast cancer." Sundvall M., Iljin K., Kilpinen S., Sara H., Kallioniemi O.P., Elenius K. J. Mammary Gland Biol. Neoplasia 13:259-268(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON LIGAND SPECIFICITY AND SIGNALING.
[47]	"Neuregulin-1/ErbB signaling and chronic heart failure." Xu Y., Li X., Liu X., Zhou M. Adv. Pharmacol. 59:31-51(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN NRG1 SIGNALING AND CARDIOVASCULAR HEALTH.
[48]	"Function of ERBB4 is determined by alternative splicing." Veikkolainen V., Vaparanta K., Halkilahti K., Iljin K., Sundvall M., Elenius K. Cell Cycle 10:2647-2657(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ALTERNATIVE SPLICNG AND PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY, SIGNALING, ROLE IN DISEASE.
[49]	"The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand." Bouyain S., Longo P.A., Li S., Ferguson K.M., Leahy D.J. Proc. Natl. Acad. Sci. U.S.A. 102:15024-15029(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-641, DISULFIDE BONDS, GLYCOSYLATION AT ASN-138; ASN-174; ASN-253; ASN-358; ASN-410; ASN-473; ASN-495 AND ASN-576.
[50]	"6-Ethynylthieno[3,2-d]- and 6-ethynylthieno[2,3-d]pyrimidin-4-anilines as tunable covalent modifiers of ErbB kinases." Wood E.R., Shewchuk L.M., Ellis B., Brignola P., Brashear R.L., Caferro T.R., Dickerson S.H., Dickson H.D., Donaldson K.H., Gaul M., Griffin R.J., Hassell A.M., Keith B., Mullin R., Petrov K.G., Reno M.J., Rusnak D.W., Tadepalli S.M. , Ulrich J.C., Wagner C.D., Vanderwall D.E., Waterson A.G., Williams J.D., White W.L., Uehling D.E. Proc. Natl. Acad. Sci. U.S.A. 105:2773-2778(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 690-999 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LEU-710; MET-766; LEU-864 AND ILE-947.
[51]	"Mechanism of activation and inhibition of the HER4/ErbB4 kinase." Qiu C., Tarrant M.K., Choi S.H., Sathyamurthy A., Bose R., Banjade S., Pal A., Bornmann W.G., Lemmon M.A., Cole P.A., Leahy D.J. Structure 16:460-467(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 702-1029 OF APOPROTEIN AND IN COMPLEX WITH LAPATINIB, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, SUBUNIT.
[52]	"Patterns of somatic mutation in human cancer genomes." 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. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-140 AND TYR-303.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07868 mRNA. Translation: AAB59446.1.
BC112199 mRNA. Translation: AAI12200.1.
BC143741 mRNA. Translation: AAI43742.1.
BC143747 mRNA. Translation: AAI43748.1.
BC143749 mRNA. Translation: AAI43750.1.
AB209697 mRNA. Translation: BAD92934.1.

IPI

IPI00016371.
IPI00215722.
IPI00816395.
IPI00969544.

PIR

A47253.

RefSeq

NP_001036064.1. NM_001042599.1.
NP_005226.1. NM_005235.2.

UniGene

Hs.390729.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AHX	X-ray	2.40	A/B	26-641	[»]
2L2T	NMR	-	A/B	642-685	[»]
2LCX	NMR	-	A/B	642-685	[»]
2R4B	X-ray	2.40	A/B	690-999	[»]
3BBT	X-ray	2.80	B/D	702-1029	[»]
3BBW	X-ray	4.00	A/B	702-1029	[»]
3BCE	X-ray	2.50	A/B/C	702-1029	[»]
3U2P	X-ray	2.57	A	26-522	[»]
3U7U	X-ray	3.03	A/B/C/D/E/F	26-640	[»]
3U9U	X-ray	3.42	E/F	26-650	[»]

ProteinModelPortal

Q15303.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29650N.
DIP-29850N.
DIP-6094N.

IntAct

Q15303. 13 interactions.

MINT

MINT-125091.

STRING

9606.ENSP00000342235.

PTM databases

PhosphoSite

Q15303.

Polymorphism databases

DMDM

3913590.

Proteomic databases

PaxDb

Q15303.

PRIDE

Q15303.

Protocols and materials databases

DNASU

2066.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342788; ENSP00000342235; ENSG00000178568.
ENST00000402597; ENSP00000385565; ENSG00000178568.
ENST00000436443; ENSP00000403204; ENSG00000178568.

GeneID

2066.

KEGG

hsa:2066.

UCSC

uc002veg.1. human.
uc002veh.1. human.
uc010zji.1. human.
uc010zjj.1. human.

Organism-specific databases

CTD

2066.

GeneCards

GC02M212210.

HGNC

HGNC:3432. ERBB4.

HPA

CAB000276.
CAB025522.
HPA012016.

MIM

600543. gene.

neXtProt

NX_Q15303.

PharmGKB

PA27847.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000230982.

HOVERGEN

HBG000490.

InParanoid

Q15303.

KO

K05085.

OMA

CNGPTSH.

OrthoDB

EOG4T4CTM.

PhylomeDB

Q15303.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

SignaLink

Q15303.

Gene expression databases

ArrayExpress

Q15303.

Bgee

Q15303.

CleanEx

HS_ERBB4.

Genevestigator

Q15303.

GermOnline

ENSG00000178568. Homo sapiens.

Family and domain databases

Gene3D

3.80.20.20. 2 hits.

InterPro

IPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]

Pfam

PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]

PIRSF

PIRSF000619. TyrPK_EGF-R. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00261. FU. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF57184. Grow_fac_recept. 2 hits.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q15303.

ChEMBL

CHEMBL3009.

ChiTaRS

ERBB4. human.

EvolutionaryTrace

Q15303.

GenomeRNAi

2066.

NextBio

8397.

PMAP-CutDB

Q15303.

SOURCE

Search...

Entry information

Entry name

ERBB4_HUMAN

Accession

Primary (citable) accession number: Q15303
Secondary accession number(s): B7ZLD7 , B7ZLE2, B7ZLE3, Q2M1W1, Q59EW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 153 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.