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Q02297

- NRG1_HUMAN

UniProt

Q02297 - NRG1_HUMAN

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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

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 tyrosine kinase activator activity Source: BHF-UCL
  5. receptor binding Source: BHF-UCL
  6. receptor tyrosine kinase binding Source: UniProtKB
  7. transcription cofactor activity Source: MGI
  8. 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 242223ExtracellularSequence AnalysisAdd
BLAST
Transmembranei243 – 26523Helical; Note=Internal signal sequenceSequence AnalysisAdd
BLAST
Topological domaini266 – 640375CytoplasmicSequence AnalysisAdd
BLAST

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-KW
Complete GO annotation...

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

BgeeiQ02297.
CleanExiHS_NRG1.
ExpressionAtlasiQ02297. baseline and differential.
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. 63 interactions.
DIPiDIP-355N.
IntActiQ02297. 6 interactions.
MINTiMINT-158528.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 35-135, 175-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02297.

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.
GeneTreeiENSGT00710000106660.
HOVERGENiHBG006531.
InParanoidiQ02297.
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

        10         20         30         40         50
MSERKEGRGK GKGKKKERGS GKKPESAAGS QSPALPPRLK EMKSQESAAG
60 70 80 90 100
SKLVLRCETS SEYSSLRFKW FKNGNELNRK NKPQNIKIQK KPGKSELRIN
110 120 130 140 150
KASLADSGEY MCKVISKLGN DSASANITIV ESNEIITGMP ASTEGAYVSS
160 170 180 190 200
ESPIRISVST EGANTSSSTS TSTTGTSHLV KCAEKEKTFC VNGGECFMVK
210 220 230 240 250
DLSNPSRYLC KCQPGFTGAR CTENVPMKVQ NQEKAEELYQ KRVLTITGIC
260 270 280 290 300
IALLVVGIMC VVAYCKTKKQ RKKLHDRLRQ SLRSERNNMM NIANGPHHPN
310 320 330 340 350
PPPENVQLVN QYVSKNVISS EHIVEREAET SFSTSHYTST AHHSTTVTQT
360 370 380 390 400
PSHSWSNGHT ESILSESHSV IVMSSVENSR HSSPTGGPRG RLNGTGGPRE
410 420 430 440 450
CNSFLRHARE TPDSYRDSPH SERYVSAMTT PARMSPVDFH TPSSPKSPPS
460 470 480 490 500
EMSPPVSSMT VSMPSMAVSP FMEEERPLLL VTPPRLREKK FDHHPQQFSS
510 520 530 540 550
FHHNPAHDSN SLPASPLRIV EDEEYETTQE YEPAQEPVKK LANSRRAKRT
560 570 580 590 600
KPNGHIANRL EVDSNTSSQS SNSESETEDE RVGEDTPFLG IQNPLAASLE
610 620 630 640
ATPAFRLADS RTNPAGRFST QEEIQARLSS VIANQDPIAV
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.Curated
The sequence AAC51756.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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]
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]
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:
EMBLi
GenBanki
DDBJi
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 ]
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:
PDBei
RCSB PDBi
PDBji
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 35-135, 175-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109332. 63 interactions.
DIPi DIP-355N.
IntActi Q02297. 6 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 ]
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.
GeneTreei ENSGT00710000106660.
HOVERGENi HBG006531.
InParanoidi Q02297.
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

Bgeei Q02297.
CleanExi HS_NRG1.
ExpressionAtlasi Q02297. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 177 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