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Q02297

- NRG1_HUMAN

UniProt

Q02297 - NRG1_HUMAN

Protein

Pro-neuregulin-1, membrane-bound isoform

Gene

NRG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei34 – 341Breakpoint for translocation to form gamma-heregulin

    GO - Molecular functioni

    1. cytokine activity Source: BHF-UCL
    2. ErbB-3 class receptor binding Source: BHF-UCL
    3. growth factor activity Source: BHF-UCL
    4. protein binding Source: IntAct
    5. protein tyrosine kinase activator activity Source: BHF-UCL
    6. receptor binding Source: BHF-UCL
    7. receptor tyrosine kinase binding Source: UniProtKB
    8. transcription cofactor activity Source: MGI
    9. transmembrane receptor protein tyrosine kinase activator activity Source: BHF-UCL

    GO - Biological processi

    1. activation of transmembrane receptor protein tyrosine kinase activity Source: BHF-UCL
    2. cardiac conduction system development Source: Ensembl
    3. cardiac muscle cell differentiation Source: BHF-UCL
    4. cardiac muscle cell myoblast differentiation Source: BHF-UCL
    5. cell communication Source: BHF-UCL
    6. cell migration Source: Ensembl
    7. cell morphogenesis Source: Ensembl
    8. cell proliferation Source: BHF-UCL
    9. cellular protein complex disassembly Source: MGI
    10. embryo development Source: InterPro
    11. endocardial cell differentiation Source: BHF-UCL
    12. epidermal growth factor receptor signaling pathway Source: Reactome
    13. ERBB signaling pathway Source: BHF-UCL
    14. Fc-epsilon receptor signaling pathway Source: Reactome
    15. fibroblast growth factor receptor signaling pathway Source: Reactome
    16. glial cell fate commitment Source: Ensembl
    17. innate immune response Source: Reactome
    18. locomotory behavior Source: Ensembl
    19. mammary gland development Source: BHF-UCL
    20. MAPK cascade Source: Ensembl
    21. negative regulation of cardiac muscle cell apoptotic process Source: BHF-UCL
    22. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    23. negative regulation of protein catabolic process Source: Ensembl
    24. negative regulation of secretion Source: BHF-UCL
    25. negative regulation of transcription, DNA-templated Source: MGI
    26. nervous system development Source: BHF-UCL
    27. neural crest cell development Source: BHF-UCL
    28. neuron fate commitment Source: Ensembl
    29. neurotransmitter receptor metabolic process Source: Ensembl
    30. neurotrophin TRK receptor signaling pathway Source: Reactome
    31. peripheral nervous system development Source: Ensembl
    32. phosphatidylinositol-mediated signaling Source: Reactome
    33. positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
    34. positive regulation of cell adhesion Source: BHF-UCL
    35. positive regulation of cell growth Source: BHF-UCL
    36. positive regulation of protein kinase B signaling Source: Ensembl
    37. positive regulation of protein tyrosine kinase activity Source: GOC
    38. positive regulation of Ras protein signal transduction Source: Ensembl
    39. positive regulation of striated muscle cell differentiation Source: BHF-UCL
    40. regulation of protein heterodimerization activity Source: BHF-UCL
    41. regulation of protein homodimerization activity Source: BHF-UCL
    42. synapse assembly Source: Ensembl
    43. transmembrane receptor protein tyrosine kinase signaling pathway Source: BHF-UCL
    44. ventricular cardiac muscle cell differentiation Source: BHF-UCL
    45. ventricular trabecula myocardium morphogenesis Source: BHF-UCL
    46. wound healing Source: BHF-UCL

    Keywords - Molecular functioni

    Growth factor

    Enzyme and pathway databases

    ReactomeiREACT_115596. Signaling by ERBB4.
    REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115854. GRB2 events in ERBB2 signaling.
    REACT_115896. GRB7 events in ERBB2 signaling.
    REACT_115961. PI3K events in ERBB4 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116005. SHC1 events in ERBB4 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_116022. Nuclear signaling by ERBB4.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiQ02297.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pro-neuregulin-1, membrane-bound isoform
    Short name:
    Pro-NRG1
    Cleaved into the following chain:
    Alternative name(s):
    Acetylcholine receptor-inducing activity
    Short name:
    ARIA
    Breast cancer cell differentiation factor p45
    Glial growth factor
    Heregulin
    Short name:
    HRG
    Neu differentiation factor
    Sensory and motor neuron-derived factor
    Gene namesi
    Name:NRG1
    Synonyms:GGF, HGL, HRGA, NDF, SMDF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:7997. NRG1.

    Subcellular locationi

    Isoform 8 : Nucleus
    Note: May be nuclear.
    Isoform 9 : Secreted
    Note: Has a signal peptide.
    Isoform 10 : Membrane; Single-pass type I membrane protein
    Note: May possess an internal uncleaved signal sequence.

    GO - Cellular componenti

    1. apical plasma membrane Source: BHF-UCL
    2. axon Source: Ensembl
    3. cytoplasm Source: Ensembl
    4. extracellular region Source: UniProtKB
    5. extracellular space Source: BHF-UCL
    6. integral component of plasma membrane Source: Ensembl
    7. membrane Source: UniProtKB
    8. neuromuscular junction Source: Ensembl
    9. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving NRG1 produces gamma-heregulin. Translocation t(8;11) with TENM4. The translocation fuses the 5'-end of TENM4 to NRG1 (isoform 8). The product of this translocation was first thought to be an alternatively spliced isoform. Gamma-heregulin is a soluble activating ligand for the ERBB2-ERBB3 receptor complex and acts as an autocrine growth factor in a specific breast cancer cell line (MDA-MB-175). Not detected in breast carcinoma samples, including ductal, lobular, medullary, and mucinous histological types, neither in other breast cancer cell lines.

    Organism-specific databases

    PharmGKBiPA31776.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 19191 PublicationPRO_0000019462Add
    BLAST
    Chaini20 – 640621Pro-neuregulin-1, membrane-bound isoformPRO_0000019463Add
    BLAST
    Chaini20 – 241222Neuregulin-1PRO_0000019464Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi57 ↔ 112By similarity
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi182 ↔ 1961 Publication
    Disulfide bondi190 ↔ 2101 Publication
    Disulfide bondi212 ↔ 2211 Publication

    Post-translational modificationi

    Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.
    N- and O-glycosylated. Extensive glycosylation precedes the proteolytic cleavage By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ02297.
    PaxDbiQ02297.
    PRIDEiQ02297.

    PTM databases

    PhosphoSiteiQ02297.

    Miscellaneous databases

    PMAP-CutDBQ02297.

    Expressioni

    Tissue specificityi

    Type I isoforms are the predominant forms expressed in the endocardium. Isoform alpha is expressed in breast, ovary, testis, prostate, heart, skeletal muscle, lung, placenta liver, kidney, salivary gland, small intestine and brain, but not in uterus, stomach, pancreas, and spleen. Isoform 3 is the predominant form in mesenchymal cells and in non-neuronal organs, whereas isoform 6 is the major neuronal form. Isoform 8 is expressed in spinal cord and brain. Isoform 9 is the major form in skeletal muscle cells; in the nervous system it is expressed in spinal cord and brain. Also detected in adult heart, placenta, lung, liver, kidney, and pancreas. Isoform 10 is expressed in nervous system: spinal cord motor neurons, dorsal root ganglion neurons, and brain. Predominant isoform expressed in sensory and motor neurons. Not detected in adult heart, placenta, lung, liver, skeletal muscle, kidney, and pancreas. Not expressed in fetal lung, liver and kidney. Type IV isoforms are brain-specific.1 Publication

    Developmental stagei

    Detectable at early embryonic ages. Isoform 10 is highly expressed in developing spinal motor neurons and in developing cranial nerve nuclei. Expression is maintained only in both adult motor neurons and dorsal root ganglion neurons. Type IV isoforms are expressed in fetal brain.1 Publication

    Gene expression databases

    ArrayExpressiQ02297.
    BgeeiQ02297.
    CleanExiHS_NRG1.
    GenevestigatoriQ02297.

    Organism-specific databases

    HPAiHPA010964.

    Interactioni

    Subunit structurei

    The cytoplasmic domain interacts with the LIM domain region of LIMK1 By similarity. Interacts with ERBB3 and ERBB4.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046262EBI-2460927,EBI-641062
    ERBB3P218603EBI-2460927,EBI-720706

    Protein-protein interaction databases

    BioGridi109332. 5 interactions.
    DIPiDIP-355N.
    IntActiQ02297. 5 interactions.
    MINTiMINT-158528.

    Structurei

    Secondary structure

    1
    640
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi179 – 1813
    Turni185 – 1895
    Beta strandi190 – 1934
    Beta strandi195 – 1995
    Beta strandi200 – 2045
    Beta strandi208 – 2125
    Beta strandi216 – 2183
    Beta strandi233 – 2353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HAENMR-A177-239[»]
    1HAFNMR-A177-239[»]
    1HRENMR-A175-241[»]
    1HRFNMR-A175-241[»]
    3U7UX-ray3.03G/H/I/J/K/L175-212[»]
    ProteinModelPortaliQ02297.
    SMRiQ02297. Positions 38-117, 175-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02297.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 242223ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini266 – 640375CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei243 – 26523Helical; Note=Internal signal sequenceSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 12892Ig-like C2-typeAdd
    BLAST
    Domaini178 – 22245EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi165 – 17713Ser/Thr-richAdd
    BLAST

    Domaini

    The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization By similarity.By similarity
    ERBB receptor binding is elicited entirely by the EGF-like domain.

    Sequence similaritiesi

    Belongs to the neuregulin family.Curated
    Contains 1 EGF-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Immunoglobulin domain, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG47801.
    HOVERGENiHBG006531.
    KOiK05455.
    OrthoDBiEOG7F7W86.
    PhylomeDBiQ02297.
    TreeFamiTF332469.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR018250. Neuregulin.
    IPR002154. Neuregulin_1_C.
    [Graphical view]
    PfamiPF12661. hEGF. 1 hit.
    PF07679. I-set. 1 hit.
    PF02158. Neuregulin. 1 hit.
    [Graphical view]
    PRINTSiPR01089. NEUREGULIN.
    SMARTiSM00181. EGF. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequences (11)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 11 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist. Isoforms have been classified as type I NRGs (isoforms with an Ig domain and a glycosylation domain, isoforms 1-8), type II NRGs (isoforms with an Ig domain but no glycosylation domain, isoform 9), type III NRGs (isoforms with a Cys-rich domain, isoform 10) and type IV NRGs (isoforms with additional 5' exons, isoform 11). All these isoforms perform distinct tissue-specific functions.

    Isoform 1 (identifier: Q02297-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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.

    « Hide

    MSERKEGRGK GKGKKKERGS GKKPESAAGS QSPALPPRLK EMKSQESAAG    50
    SKLVLRCETS SEYSSLRFKW FKNGNELNRK NKPQNIKIQK KPGKSELRIN 100
    KASLADSGEY MCKVISKLGN DSASANITIV ESNEIITGMP ASTEGAYVSS 150
    ESPIRISVST EGANTSSSTS TSTTGTSHLV KCAEKEKTFC VNGGECFMVK 200
    DLSNPSRYLC KCQPGFTGAR CTENVPMKVQ NQEKAEELYQ KRVLTITGIC 250
    IALLVVGIMC VVAYCKTKKQ RKKLHDRLRQ SLRSERNNMM NIANGPHHPN 300
    PPPENVQLVN QYVSKNVISS EHIVEREAET SFSTSHYTST AHHSTTVTQT 350
    PSHSWSNGHT ESILSESHSV IVMSSVENSR HSSPTGGPRG RLNGTGGPRE 400
    CNSFLRHARE TPDSYRDSPH SERYVSAMTT PARMSPVDFH TPSSPKSPPS 450
    EMSPPVSSMT VSMPSMAVSP FMEEERPLLL VTPPRLREKK FDHHPQQFSS 500
    FHHNPAHDSN SLPASPLRIV EDEEYETTQE YEPAQEPVKK LANSRRAKRT 550
    KPNGHIANRL EVDSNTSSQS SNSESETEDE RVGEDTPFLG IQNPLAASLE 600
    ATPAFRLADS RTNPAGRFST QEEIQARLSS VIANQDPIAV 640
    Length:640
    Mass (Da):70,392
    Last modified:January 23, 2007 - v3
    Checksum:iC30D3F614AADFF62
    GO
    Isoform 2 (identifier: Q02297-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha1A

    The sequence of this isoform differs from the canonical sequence as follows:
         234-234: K → KHLGIEFIE

    Show »
    Length:648
    Mass (Da):71,331
    Checksum:i775329E1F5FED358
    GO
    Isoform 3 (identifier: Q02297-3) [UniParc]FASTAAdd to Basket

    Also known as: Alpha2B

    The sequence of this isoform differs from the canonical sequence as follows:
         424-462: YVSAMTTPAR...SPPVSSMTVS → HNLIAELRRN...SSIPHLGFIL
         463-640: Missing.

    Show »
    Length:462
    Mass (Da):50,879
    Checksum:i00F513509DED3269
    GO
    Isoform 4 (identifier: Q02297-4) [UniParc]FASTAAdd to Basket

    Also known as: Alpha3

    The sequence of this isoform differs from the canonical sequence as follows:
         234-247: KAEELYQKRVLTIT → SAQMSLLVIAAKTT
         248-640: Missing.

    Show »
    Length:247
    Mass (Da):26,590
    Checksum:i8D44247649C60C67
    GO
    Isoform 6 (identifier: Q02297-6) [UniParc]FASTAAdd to Basket

    Also known as: Beta1, Beta1A

    The sequence of this isoform differs from the canonical sequence as follows:
         213-234: QPGFTGARCTENVPMKVQNQEK → PNEFTGDRCQNYVMASFYKHLGIEFME

    Show »
    Length:645
    Mass (Da):71,157
    Checksum:iD61555DF50325386
    GO
    Isoform 7 (identifier: Q02297-7) [UniParc]FASTAAdd to Basket

    Also known as: Beta2

    The sequence of this isoform differs from the canonical sequence as follows:
         213-233: QPGFTGARCTENVPMKVQNQE → PNEFTGDRCQNYVMASFY

    Show »
    Length:637
    Mass (Da):70,200
    Checksum:iD92B25445628869D
    GO
    Isoform 8 (identifier: Q02297-8) [UniParc]FASTAAdd to Basket

    Also known as: Beta3, GGFHFB1

    The sequence of this isoform differs from the canonical sequence as follows:
         213-241: QPGFTGARCTENVPMKVQNQEKAEELYQK → PNEFTGDRCQNYVMASFYSTSTPFLSLPE
         242-640: Missing.

    Show »
    Length:241
    Mass (Da):26,143
    Checksum:iD2450DB340E6B64D
    GO
    Isoform 9 (identifier: Q02297-9) [UniParc]FASTAAdd to Basket

    Also known as: GGF2, GGFHPP2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MSERKEGRGKGKGKKKERGSGKKPESAAGSQSP → MRWRRAPRRS...EVSRVLCKRC
         134-168: EIITGMPASTEGAYVSSESPIRISVSTEGANTSSS → A
         213-241: QPGFTGARCTENVPMKVQNQEKAEELYQK → PNEFTGDRCQNYVMASFYSTSTPFLSLPE
         242-640: Missing.

    Show »
    Length:422
    Mass (Da):45,141
    Checksum:i3535A1E4AB8EEA8E
    GO
    Isoform 10 (identifier: Q02297-10) [UniParc]FASTAAdd to Basket

    Also known as: SMDF

    The sequence of this isoform differs from the canonical sequence as follows:
         1-166: Missing.
         167-167: S → MEIYSPDMSE...ETNLQTAPKL
         213-241: QPGFTGARCTENVPMKVQNQEKAEELYQK → PNEFTGDRCQNYVMASFYSTSTPFLSLPE
         242-640: Missing.

    Note: Potential internal signal sequence at positions 76-100.

    Show »
    Length:296
    Mass (Da):31,686
    Checksum:i8D41743217F7EB02
    GO
    Isoform 11 (identifier: Q02297-11) [UniParc]FASTAAdd to Basket

    Also known as: Type IV-beta1a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: Missing.
         22-33: KKPESAAGSQSP → MGKGRAGRVGTT
         134-168: EIITGMPASTEGAYVSSESPIRISVSTEGANTSSS → A
         213-234: QPGFTGARCTENVPMKVQNQEK → PNEFTGDRCQNYVMASFYKHLGIEFME

    Show »
    Length:590
    Mass (Da):65,460
    Checksum:iB4DCA7D49EE8117B
    GO
    Isoform 12 (identifier: Q02297-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         213-233: QPGFTGARCTENVPMKVQNQE → PNEFTGDRCQNYVMASFY
         424-640: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:420
    Mass (Da):46,226
    Checksum:iBE6F4EBA41F043A9
    GO

    Sequence cautioni

    The sequence AAA19955.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence AAC51756.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941K → A in AAA19953. (PubMed:7509448)Curated
    Sequence conflicti107 – 1071S → P in ABQ53539. (PubMed:17565985)Curated
    Sequence conflicti261 – 2611V → L in ABQ53540. (PubMed:17565985)Curated
    Sequence conflicti414 – 4141S → F in AAA19953. (PubMed:7509448)Curated
    Sequence conflicti535 – 5351Q → R in AAA19951. (PubMed:7509448)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → Q.1 Publication
    Corresponds to variant rs3924999 [ dbSNP | Ensembl ].
    VAR_009307
    Natural varianti289 – 2891M → T.2 Publications
    Corresponds to variant rs10503929 [ dbSNP | Ensembl ].
    VAR_053531
    Natural varianti463 – 4631M → K.
    VAR_009308
    Isoform 10 (identifier: Q02297-10)
    Natural varianti46 – 461G → R.
    Corresponds to variant rs3735774 [ dbSNP | Ensembl ].
    Natural varianti127 – 1271A → P.
    Corresponds to variant rs34822181 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 166166Missing in isoform 10. 3 PublicationsVSP_037562Add
    BLAST
    Alternative sequencei1 – 3333MSERK…GSQSP → MRWRRAPRRSGRPGPRAQRP GSAARSSPPLPLLPLLLLLG TAALAPGAAAGNEAAPAGAS VCYSSPPSVGSVQELAQRAA VVIEGKVHPQRRQQGALDRK AAAAAGEAGAWGGDREPPAA GPRALGPPAEEPLLAANGTV PSWPTAPVPSAGEPGEEAPY LVKVHQVWAVKAGGLKKDSL LTVRLGTWGHPAFPSCGRLK EDSRYIFFMEPDANSTSRAP AAFRASFPPLETGRNLKKEV SRVLCKRC in isoform 9. 1 PublicationVSP_003425Add
    BLAST
    Alternative sequencei1 – 2121Missing in isoform 11. 1 PublicationVSP_037563Add
    BLAST
    Alternative sequencei22 – 3312KKPES…GSQSP → MGKGRAGRVGTT in isoform 11. 1 PublicationVSP_037564Add
    BLAST
    Alternative sequencei134 – 16835EIITG…NTSSS → A in isoform 9 and isoform 11. 2 PublicationsVSP_003426Add
    BLAST
    Alternative sequencei167 – 1671S → MEIYSPDMSEVAAERSSSPS TQLSADPSLDGLPAAEDMPE PQTEDGRTPGLVGLAVPCCA CLEAERLRGCLNSEKICIVP ILACLVSLCLCIAGLKWVFV DKIFEYDSPTHLDPGGLGQD PIISLDATAASAVWVSSEAY TSPVSRAQSESEVQVTVQGD KAVVSFEPSAAPTPKNRIFA FSFLPSTAPSFPSPTRNPEV RTPKSATQPQTTETNLQTAP KL in isoform 10. 3 PublicationsVSP_037565
    Alternative sequencei213 – 24129QPGFT…ELYQK → PNEFTGDRCQNYVMASFYST STPFLSLPE in isoform 8, isoform 9 and isoform 10. 6 PublicationsVSP_003429Add
    BLAST
    Alternative sequencei213 – 23422QPGFT…QNQEK → PNEFTGDRCQNYVMASFYKH LGIEFME in isoform 6 and isoform 11. 3 PublicationsVSP_003428Add
    BLAST
    Alternative sequencei213 – 23321QPGFT…VQNQE → PNEFTGDRCQNYVMASFY in isoform 7 and isoform 12. 3 PublicationsVSP_003427Add
    BLAST
    Alternative sequencei234 – 24714KAEEL…VLTIT → SAQMSLLVIAAKTT in isoform 4. 1 PublicationVSP_003432Add
    BLAST
    Alternative sequencei234 – 2341K → KHLGIEFIE in isoform 2. 1 PublicationVSP_003431
    Alternative sequencei242 – 640399Missing in isoform 8, isoform 9 and isoform 10. 6 PublicationsVSP_003430Add
    BLAST
    Alternative sequencei248 – 640393Missing in isoform 4. 1 PublicationVSP_003433Add
    BLAST
    Alternative sequencei424 – 640217Missing in isoform 12. 1 PublicationVSP_046417Add
    BLAST
    Alternative sequencei424 – 46239YVSAM…SMTVS → HNLIAELRRNKAHRSKCMQI QLSATHLRSSSIPHLGFIL in isoform 3. 1 PublicationVSP_003434Add
    BLAST
    Alternative sequencei463 – 640178Missing in isoform 3. 1 PublicationVSP_003435Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94165 mRNA. Translation: AAA58638.1.
    M94166 mRNA. Translation: AAA58639.1.
    M94167 mRNA. Translation: AAA58640.1.
    M94168 mRNA. Translation: AAA58641.1.
    U02325 mRNA. Translation: AAA19950.1.
    U02326 mRNA. Translation: AAA19951.1.
    U02327 mRNA. Translation: AAA19952.1.
    U02328 mRNA. Translation: AAA19953.1.
    U02329 mRNA. Translation: AAA19954.1.
    U02330 mRNA. Translation: AAA19955.1. Sequence problems.
    L12260 mRNA. Translation: AAB59622.1.
    L12261 mRNA. Translation: AAB59358.1.
    L41827 mRNA. Translation: AAC41764.1.
    AK289927 mRNA. Translation: BAF82616.1.
    AK298132 mRNA. Translation: BAH12729.1.
    AC021909 Genomic DNA. No translation available.
    AC022833 Genomic DNA. No translation available.
    AC022850 Genomic DNA. No translation available.
    AC023948 Genomic DNA. No translation available.
    AC068359 Genomic DNA. No translation available.
    AC068931 Genomic DNA. No translation available.
    AC083977 Genomic DNA. No translation available.
    AC103675 Genomic DNA. No translation available.
    AC104000 Genomic DNA. No translation available.
    AC104029 Genomic DNA. No translation available.
    AC113209 Genomic DNA. No translation available.
    AF009227 mRNA. Translation: AAC51756.1. Different initiation.
    AF491780 Genomic DNA. Translation: AAM71137.1.
    AF491780 Genomic DNA. Translation: AAM71139.1.
    AF491780 Genomic DNA. Translation: AAM71140.1.
    EF372273 mRNA. Translation: ABQ53539.1.
    EF372274 mRNA. Translation: ABQ53540.1.
    CH471080 Genomic DNA. Translation: EAW63411.1.
    BC064587 mRNA. Translation: AAH64587.1.
    BC073871 mRNA. Translation: AAH73871.1.
    AF026146 mRNA. Translation: AAD01795.1.
    BK000383 Genomic DNA. Translation: DAA00044.1.
    BK000383 Genomic DNA. Translation: DAA00045.1.
    BK000383 Genomic DNA. Translation: DAA00046.1.
    BK000383 Genomic DNA. Translation: DAA00047.1.
    CCDSiCCDS47836.1. [Q02297-9]
    CCDS55218.1. [Q02297-11]
    CCDS55219.1. [Q02297-12]
    CCDS6083.1. [Q02297-6]
    CCDS6084.1. [Q02297-7]
    CCDS6085.1. [Q02297-1]
    CCDS6086.1. [Q02297-3]
    CCDS6087.1. [Q02297-10]
    PIRiA43273.
    A56943.
    B43273.
    C43273.
    D43273.
    I38403.
    I38404.
    I38408.
    S32357.
    RefSeqiNP_001153467.1. NM_001159995.1.
    NP_001153471.1. NM_001159999.1.
    NP_001153473.1. NM_001160001.1. [Q02297-11]
    NP_001153477.1. NM_001160005.1.
    NP_001153480.1. NM_001160008.1. [Q02297-12]
    NP_039250.2. NM_013956.3. [Q02297-6]
    NP_039251.2. NM_013957.3. [Q02297-7]
    NP_039252.2. NM_013958.3. [Q02297-8]
    NP_039253.1. NM_013959.3. [Q02297-10]
    NP_039254.1. NM_013960.3. [Q02297-3]
    NP_039256.2. NM_013962.2. [Q02297-9]
    NP_039258.1. NM_013964.3. [Q02297-1]
    UniGeneiHs.453951.
    Hs.668810.

    Genome annotation databases

    EnsembliENST00000287842; ENSP00000287842; ENSG00000157168. [Q02297-7]
    ENST00000356819; ENSP00000349275; ENSG00000157168. [Q02297-6]
    ENST00000405005; ENSP00000384620; ENSG00000157168. [Q02297-1]
    ENST00000519301; ENSP00000429582; ENSG00000157168. [Q02297-11]
    ENST00000520407; ENSP00000434640; ENSG00000157168. [Q02297-9]
    ENST00000520502; ENSP00000433289; ENSG00000157168. [Q02297-10]
    ENST00000521670; ENSP00000428828; ENSG00000157168. [Q02297-3]
    ENST00000523079; ENSP00000430120; ENSG00000157168. [Q02297-12]
    GeneIDi3084.
    KEGGihsa:3084.
    UCSCiuc003xip.3. human. [Q02297-9]
    uc003xis.3. human. [Q02297-8]
    uc003xit.2. human. [Q02297-3]
    uc003xiu.2. human. [Q02297-6]
    uc003xiv.2. human. [Q02297-1]
    uc003xiw.2. human. [Q02297-7]
    uc003xix.3. human. [Q02297-4]
    uc003xiy.3. human. [Q02297-10]
    uc003xja.2. human. [Q02297-2]
    uc010lvp.2. human. [Q02297-11]

    Polymorphism databases

    DMDMi9297018.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Tipping the mind - Issue 129 of June 2011

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94165 mRNA. Translation: AAA58638.1 .
    M94166 mRNA. Translation: AAA58639.1 .
    M94167 mRNA. Translation: AAA58640.1 .
    M94168 mRNA. Translation: AAA58641.1 .
    U02325 mRNA. Translation: AAA19950.1 .
    U02326 mRNA. Translation: AAA19951.1 .
    U02327 mRNA. Translation: AAA19952.1 .
    U02328 mRNA. Translation: AAA19953.1 .
    U02329 mRNA. Translation: AAA19954.1 .
    U02330 mRNA. Translation: AAA19955.1 . Sequence problems.
    L12260 mRNA. Translation: AAB59622.1 .
    L12261 mRNA. Translation: AAB59358.1 .
    L41827 mRNA. Translation: AAC41764.1 .
    AK289927 mRNA. Translation: BAF82616.1 .
    AK298132 mRNA. Translation: BAH12729.1 .
    AC021909 Genomic DNA. No translation available.
    AC022833 Genomic DNA. No translation available.
    AC022850 Genomic DNA. No translation available.
    AC023948 Genomic DNA. No translation available.
    AC068359 Genomic DNA. No translation available.
    AC068931 Genomic DNA. No translation available.
    AC083977 Genomic DNA. No translation available.
    AC103675 Genomic DNA. No translation available.
    AC104000 Genomic DNA. No translation available.
    AC104029 Genomic DNA. No translation available.
    AC113209 Genomic DNA. No translation available.
    AF009227 mRNA. Translation: AAC51756.1 . Different initiation.
    AF491780 Genomic DNA. Translation: AAM71137.1 .
    AF491780 Genomic DNA. Translation: AAM71139.1 .
    AF491780 Genomic DNA. Translation: AAM71140.1 .
    EF372273 mRNA. Translation: ABQ53539.1 .
    EF372274 mRNA. Translation: ABQ53540.1 .
    CH471080 Genomic DNA. Translation: EAW63411.1 .
    BC064587 mRNA. Translation: AAH64587.1 .
    BC073871 mRNA. Translation: AAH73871.1 .
    AF026146 mRNA. Translation: AAD01795.1 .
    BK000383 Genomic DNA. Translation: DAA00044.1 .
    BK000383 Genomic DNA. Translation: DAA00045.1 .
    BK000383 Genomic DNA. Translation: DAA00046.1 .
    BK000383 Genomic DNA. Translation: DAA00047.1 .
    CCDSi CCDS47836.1. [Q02297-9 ]
    CCDS55218.1. [Q02297-11 ]
    CCDS55219.1. [Q02297-12 ]
    CCDS6083.1. [Q02297-6 ]
    CCDS6084.1. [Q02297-7 ]
    CCDS6085.1. [Q02297-1 ]
    CCDS6086.1. [Q02297-3 ]
    CCDS6087.1. [Q02297-10 ]
    PIRi A43273.
    A56943.
    B43273.
    C43273.
    D43273.
    I38403.
    I38404.
    I38408.
    S32357.
    RefSeqi NP_001153467.1. NM_001159995.1.
    NP_001153471.1. NM_001159999.1.
    NP_001153473.1. NM_001160001.1. [Q02297-11 ]
    NP_001153477.1. NM_001160005.1.
    NP_001153480.1. NM_001160008.1. [Q02297-12 ]
    NP_039250.2. NM_013956.3. [Q02297-6 ]
    NP_039251.2. NM_013957.3. [Q02297-7 ]
    NP_039252.2. NM_013958.3. [Q02297-8 ]
    NP_039253.1. NM_013959.3. [Q02297-10 ]
    NP_039254.1. NM_013960.3. [Q02297-3 ]
    NP_039256.2. NM_013962.2. [Q02297-9 ]
    NP_039258.1. NM_013964.3. [Q02297-1 ]
    UniGenei Hs.453951.
    Hs.668810.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HAE NMR - A 177-239 [» ]
    1HAF NMR - A 177-239 [» ]
    1HRE NMR - A 175-241 [» ]
    1HRF NMR - A 175-241 [» ]
    3U7U X-ray 3.03 G/H/I/J/K/L 175-212 [» ]
    ProteinModelPortali Q02297.
    SMRi Q02297. Positions 38-117, 175-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109332. 5 interactions.
    DIPi DIP-355N.
    IntActi Q02297. 5 interactions.
    MINTi MINT-158528.

    PTM databases

    PhosphoSitei Q02297.

    Polymorphism databases

    DMDMi 9297018.

    Proteomic databases

    MaxQBi Q02297.
    PaxDbi Q02297.
    PRIDEi Q02297.

    Protocols and materials databases

    DNASUi 3084.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287842 ; ENSP00000287842 ; ENSG00000157168 . [Q02297-7 ]
    ENST00000356819 ; ENSP00000349275 ; ENSG00000157168 . [Q02297-6 ]
    ENST00000405005 ; ENSP00000384620 ; ENSG00000157168 . [Q02297-1 ]
    ENST00000519301 ; ENSP00000429582 ; ENSG00000157168 . [Q02297-11 ]
    ENST00000520407 ; ENSP00000434640 ; ENSG00000157168 . [Q02297-9 ]
    ENST00000520502 ; ENSP00000433289 ; ENSG00000157168 . [Q02297-10 ]
    ENST00000521670 ; ENSP00000428828 ; ENSG00000157168 . [Q02297-3 ]
    ENST00000523079 ; ENSP00000430120 ; ENSG00000157168 . [Q02297-12 ]
    GeneIDi 3084.
    KEGGi hsa:3084.
    UCSCi uc003xip.3. human. [Q02297-9 ]
    uc003xis.3. human. [Q02297-8 ]
    uc003xit.2. human. [Q02297-3 ]
    uc003xiu.2. human. [Q02297-6 ]
    uc003xiv.2. human. [Q02297-1 ]
    uc003xiw.2. human. [Q02297-7 ]
    uc003xix.3. human. [Q02297-4 ]
    uc003xiy.3. human. [Q02297-10 ]
    uc003xja.2. human. [Q02297-2 ]
    uc010lvp.2. human. [Q02297-11 ]

    Organism-specific databases

    CTDi 3084.
    GeneCardsi GC08P031554.
    HGNCi HGNC:7997. NRG1.
    HPAi HPA010964.
    MIMi 142445. gene.
    neXtProti NX_Q02297.
    PharmGKBi PA31776.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47801.
    HOVERGENi HBG006531.
    KOi K05455.
    OrthoDBi EOG7F7W86.
    PhylomeDBi Q02297.
    TreeFami TF332469.

    Enzyme and pathway databases

    Reactomei REACT_115596. Signaling by ERBB4.
    REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115854. GRB2 events in ERBB2 signaling.
    REACT_115896. GRB7 events in ERBB2 signaling.
    REACT_115961. PI3K events in ERBB4 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116005. SHC1 events in ERBB4 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_116022. Nuclear signaling by ERBB4.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki Q02297.

    Miscellaneous databases

    ChiTaRSi NRG1. human.
    EvolutionaryTracei Q02297.
    GeneWikii Neuregulin_1.
    GenomeRNAii 3084.
    NextBioi 12227.
    PMAP-CutDB Q02297.
    PROi Q02297.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02297.
    Bgeei Q02297.
    CleanExi HS_NRG1.
    Genevestigatori Q02297.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR018250. Neuregulin.
    IPR002154. Neuregulin_1_C.
    [Graphical view ]
    Pfami PF12661. hEGF. 1 hit.
    PF07679. I-set. 1 hit.
    PF02158. Neuregulin. 1 hit.
    [Graphical view ]
    PRINTSi PR01089. NEUREGULIN.
    SMARTi SM00181. EGF. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 7 AND 8), PARTIAL PROTEIN SEQUENCE.
    2. "Structural and functional aspects of the multiplicity of Neu differentiation factors."
      Wen D., Suggs S.V., Karunagaran D., Liu N., Cupples R.L., Luo Y., Janssen A.M., Ben-Baruch N., Trollinger D.B., Jacobsen V.L., Meng S.-Y., Lu H.S., Hu S., Chang D., Yang W., Yanigahara D., Koski R.A., Yarden Y.
      Mol. Cell. Biol. 14:1909-1919(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 6; 7 AND 8).
      Tissue: Kidney adenocarcinoma and Pituitary.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8 AND 9).
      Tissue: Brain.
    4. "Sensory and motor neuron-derived factor. A novel heregulin variant highly expressed in sensory and motor neurons."
      Ho W.-H., Armanini M.P., Nuijens A., Phillips H.S., Osheroff P.L.
      J. Biol. Chem. 270:14523-14532(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
      Tissue: Brain stem and Cerebellum.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 10 AND 12), VARIANT THR-289.
      Tissue: Hippocampus.
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Gamma-heregulin: a novel heregulin isoform that is an autocrine growth factor for the human breast cancer cell line, MDA-MB-175."
      Schaefer G., Fitzpatrick V.D., Sliwkowski M.X.
      Oncogene 15:1385-1394(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF GAMMA-HEREGULIN FUSION PROTEIN.
      Tissue: Mammary cancer.
    9. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 8 AND 9), SUSCEPTIBILITY TO SCHIZOPHRENIA.
    10. "Molecular cloning of a brain-specific, developmentally regulated neuregulin 1 (NRG1) isoform and identification of a functional promoter variant associated with schizophrenia."
      Tan W., Wang Y., Gold B., Chen J., Dean M., Harrison P.J., Weinberger D.R., Law A.J.
      J. Biol. Chem. 282:24343-24351(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11), ALTERNATIVE SPLICING, VARIANTS GLN-38 AND THR-289, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Hippocampus and Prefrontal cortex.
    11. "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 1 AND 10).
      Tissue: Brain and Duodenum.
    12. Schoumacher F., Herzer S., Flury N., Kueng W., Mueller H., Eppenberger U.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-211 (ISOFORM 1).
    13. "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: PROTEIN SEQUENCE OF 20-28.
    14. "Isolation of the neu/HER-2 stimulatory ligand: a 44 kd glycoprotein that induces differentiation of mammary tumor cells."
      Peles E., Bacus S.S., Koski R.A., Lu H.S., Wen D., Ogden S.G., Levy R.B., Yarden Y.
      Cell 69:205-216(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE (ISOFORM 1), FUNCTION, GLYCOSYLATION.
    15. "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 ERBB4, FUNCTION.
    16. "Gamma-heregulin is the product of a chromosomal translocation fusing the DOC4 and HGL/NRG1 genes in the MDA-MB-175 breast cancer cell line."
      Wang X.-Z., Jolicoeur E.M., Conte N., Chaffanet M., Zhang Y., Mozziconacci M.-J., Feiner H., Birnbaum D., Pebusque M.-J., Ron D.
      Oncogene 18:5718-5721(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION.
    17. "Gamma-heregulin: a fusion gene of DOC-4 and neuregulin-1 derived from a chromosome translocation."
      Liu X., Baker E., Eyre H.J., Sutherland G.R., Zhou M.
      Oncogene 18:7110-7114(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION.
    18. "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: INTERACTION WITH ERBB4.
    19. "Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4."
      Nagata K., Kohda D., Hatanaka H., Ichikawa S., Matsuda S., Yamamoto T., Suzuki A., Inagaki F.
      EMBO J. 13:3517-3523(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 175-241 (ISOFORM 1).
    20. "High-resolution solution structure of the EGF-like domain of heregulin-alpha."
      Jacobsen N.E., Abadi N., Sliwkowski M.X., Reilly D., Skelton N.J., Fairbrother W.J.
      Biochemistry 35:3402-3417(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 177-239 (ISOFORM 1), DISULFIDE BONDS.

    Entry informationi

    Entry nameiNRG1_HUMAN
    AccessioniPrimary (citable) accession number: Q02297
    Secondary accession number(s): A5YAK4
    , A5YAK5, A8K1L2, B7Z4Z3, E9PHH4, O14667, P98202, Q02298, Q02299, Q07110, Q07111, Q12779, Q12780, Q12781, Q12782, Q12783, Q12784, Q15491, Q7RTV9, Q7RTW0, Q7RTW1, Q7RTW2, Q8NFN1, Q8NFN2, Q8NFN3, Q9UPE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 175 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3