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Pro-neuregulin-1, membrane-bound isoform (Pro-NRG1) [Cleaved into: Neuregulin-1 (Acetylcholine receptor-inducing activity) (ARIA) (Breast cancer cell differentiation factor p45) (Glial growth factor) (Heregulin) (HRG) (Neu differentiation factor) (Sensory and motor neuron-derived factor)]

 NRG1_HUMAN              Reviewed;         640 AA.
Q02297; 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;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 203.
RecName: Full=Pro-neuregulin-1, membrane-bound isoform;
Short=Pro-NRG1;
Contains:
RecName: Full=Neuregulin-1;
AltName: Full=Acetylcholine receptor-inducing activity;
Short=ARIA;
AltName: Full=Breast cancer cell differentiation factor p45;
AltName: Full=Glial growth factor;
AltName: Full=Heregulin;
Short=HRG;
AltName: Full=Neu differentiation factor;
AltName: Full=Sensory and motor neuron-derived factor;
Flags: Precursor;
Name=NRG1; Synonyms=GGF, HGL, HRGA, NDF, SMDF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 7 AND 8), AND PARTIAL
PROTEIN SEQUENCE.
PubMed=1350381; DOI=10.1126/science.256.5060.1205;
Holmes W.E., Sliwkowski M.X., Akita R.W., Henzel W.J., Lee J.,
Park J.W., Yansura D., Abadi N., Raab H., Lewis G.D., Shepard H.M.,
Kuang W.-J., Wood W.I., Goeddel D.V., Vandlen R.L.;
"Identification of heregulin, a specific activator of p185erbB2.";
Science 256:1205-1210(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 6; 7 AND 8).
TISSUE=Kidney adenocarcinoma, and Pituitary;
PubMed=7509448; DOI=10.1128/MCB.14.3.1909;
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.;
"Structural and functional aspects of the multiplicity of Neu
differentiation factors.";
Mol. Cell. Biol. 14:1909-1919(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8 AND 9).
TISSUE=Brain;
PubMed=8096067; DOI=10.1038/362312a0;
Marchionni M.A., Goodearl A.D.J., Chen M.S., Bermingham-McDonogh O.,
Kirk C., Hendricks M., Danehy F., Misumi D., Sudhalter J.,
Kobayashi K., Wroblewski D., Lynch C., Baldasarre M., Hiles I.,
Davis J.B., Hsuan J.J., Totty N.F., Otsu M., McBurney R.N.,
Waterfield M.D., Stroobant P., Gwynne D.;
"Glial growth factors are alternatively spliced erbB2 ligands
expressed in the nervous system.";
Nature 362:312-318(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
TISSUE=Brain stem, and Cerebellum;
PubMed=7782315; DOI=10.1074/jbc.270.24.14523;
Ho W.-H., Armanini M.P., Nuijens A., Phillips H.S., Osheroff P.L.;
"Sensory and motor neuron-derived factor. A novel heregulin variant
highly expressed in sensory and motor neurons.";
J. Biol. Chem. 270:14523-14532(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 10 AND 12), AND
VARIANT THR-289.
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
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.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF GAMMA-HEREGULIN FUSION PROTEIN.
TISSUE=Mammary cancer;
PubMed=9333014; DOI=10.1038/sj.onc.1201317;
Schaefer G., Fitzpatrick V.D., Sliwkowski M.X.;
"Gamma-heregulin: a novel heregulin isoform that is an autocrine
growth factor for the human breast cancer cell line, MDA-MB-175.";
Oncogene 15:1385-1394(1997).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 8 AND 9), AND
SUSCEPTIBILITY TO SCHIZOPHRENIA.
PubMed=12145742; DOI=10.1086/342734;
Stefansson H., Sigurdsson E., Steinthorsdottir V., Bjornsdottir S.,
Sigmundsson T., Ghosh S., Brynjolfsson J., Gunnarsdottir S.,
Ivarsson O., Chou T.T., Hjaltason O., Birgisdottir B., Jonsson H.,
Gudnadottir V.G., Gudmundsdottir E., Bjornsson A., Ingvarsson B.,
Ingason A., Sigfusson S., Hardardottir H., Harvey R.P., Brunner D.,
Mutel V., Gonzalo A., Lemke G., Sainz J., Johannesson G.,
Andresson T., Gudbjartsson D., Manolescu A., Frigge M.L., Gurney M.E.,
Kong A., Gulcher J.R., Petursson H., Stefansson K.;
"Neuregulin 1 and susceptibility to Schizophrenia.";
Am. J. Hum. Genet. 71:877-892(2002).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11), ALTERNATIVE SPLICING,
VARIANTS GLN-38 AND THR-289, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Hippocampus, and Prefrontal cortex;
PubMed=17565985; DOI=10.1074/jbc.M702953200;
Tan W., Wang Y., Gold B., Chen J., Dean M., Harrison P.J.,
Weinberger D.R., Law A.J.;
"Molecular cloning of a brain-specific, developmentally regulated
neuregulin 1 (NRG1) isoform and identification of a functional
promoter variant associated with schizophrenia.";
J. Biol. Chem. 282:24343-24351(2007).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 10).
TISSUE=Brain, and Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-211 (ISOFORM 1).
Schoumacher F., Herzer S., Flury N., Kueng W., Mueller H.,
Eppenberger U.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[13]
PROTEIN SEQUENCE OF 20-28.
PubMed=7689552;
Culouscou J.-M., Plowman G.D., Carlton G.W., Green J.M., Shoyab M.;
"Characterization of a breast cancer cell differentiation factor that
specifically activates the HER4/p180erbB4 receptor.";
J. Biol. Chem. 268:18407-18410(1993).
[14]
PARTIAL PROTEIN SEQUENCE (ISOFORM 1), FUNCTION, AND GLYCOSYLATION.
PubMed=1348215; DOI=10.1016/0092-8674(92)90131-U;
Peles E., Bacus S.S., Koski R.A., Lu H.S., Wen D., Ogden S.G.,
Levy R.B., Yarden Y.;
"Isolation of the neu/HER-2 stimulatory ligand: a 44 kd glycoprotein
that induces differentiation of mammary tumor cells.";
Cell 69:205-216(1992).
[15]
BINDING TO ERBB4, AND FUNCTION.
PubMed=7902537; DOI=10.1038/366473a0;
Plowman G.D., Green J.M., Culouscou J.M., Carlton G.W., Rothwell V.M.,
Buckley S.;
"Heregulin induces tyrosine phosphorylation of HER4/p180erbB4.";
Nature 366:473-475(1993).
[16]
CHROMOSOMAL TRANSLOCATION.
PubMed=10523851; DOI=10.1038/sj.onc.1202950;
Wang X.-Z., Jolicoeur E.M., Conte N., Chaffanet M., Zhang Y.,
Mozziconacci M.-J., Feiner H., Birnbaum D., Pebusque M.-J., Ron D.;
"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.";
Oncogene 18:5718-5721(1999).
[17]
CHROMOSOMAL TRANSLOCATION.
PubMed=10597312; DOI=10.1038/sj.onc.1203136;
Liu X., Baker E., Eyre H.J., Sutherland G.R., Zhou M.;
"Gamma-heregulin: a fusion gene of DOC-4 and neuregulin-1 derived from
a chromosome translocation.";
Oncogene 18:7110-7114(1999).
[18]
BINDING TO ERBB4.
PubMed=10867024; DOI=10.1074/jbc.C901015199;
Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C.,
Carraway K.L. III;
"Ligand discrimination in signaling through an ErbB4 receptor
homodimer.";
J. Biol. Chem. 275:19803-19807(2000).
[19]
FUNCTION, BINDING TO ERBB3 AND INTEGRINS, IDENTIFICATION IN A TERNARY
COMPLEX WITH ERBB3 AND INTEGRINS, AND MUTAGENESIS OF LYS-181; LYS-185
AND LYS-187.
PubMed=20682778; DOI=10.1074/jbc.M110.113878;
Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
Wang B., Takada Y.K., Takada Y.;
"Direct binding of the EGF-like domain of neuregulin-1 to integrins
({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
signaling.";
J. Biol. Chem. 285:31388-31398(2010).
[20]
STRUCTURE BY NMR OF 175-241 (ISOFORM 1).
PubMed=8062828;
Nagata K., Kohda D., Hatanaka H., Ichikawa S., Matsuda S.,
Yamamoto T., Suzuki A., Inagaki F.;
"Solution structure of the epidermal growth factor-like domain of
heregulin-alpha, a ligand for p180erbB-4.";
EMBO J. 13:3517-3523(1994).
[21]
STRUCTURE BY NMR OF 177-239 (ISOFORM 1), AND DISULFIDE BONDS.
PubMed=8639490; DOI=10.1021/bi952626l;
Jacobsen N.E., Abadi N., Sliwkowski M.X., Reilly D., Skelton N.J.,
Fairbrother W.J.;
"High-resolution solution structure of the EGF-like domain of
heregulin-alpha.";
Biochemistry 35:3402-3417(1996).
-!- FUNCTION: 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. Binds
to ERBB4 (PubMed:10867024, PubMed:7902537). Binds to ERBB3
(PubMed:20682778). Acts as a ligand for integrins and binds (via
EGF domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding
to integrins and subsequent ternary complex formation with
integrins and ERRB3 are essential for NRG1-ERBB signaling. Induces
the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and
AKT1 (PubMed:20682778). Ligand-dependent ERBB4 endocytosis is
essential for the NRG1-mediated activation of these kinases in
neurons (By similarity). {ECO:0000250|UniProtKB:P43322,
ECO:0000269|PubMed:10867024, ECO:0000269|PubMed:1348215,
ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:7902537}.
-!- SUBUNIT: The cytoplasmic domain interacts with the LIM domain
region of LIMK1 (By similarity). Forms a ternary complex with
ERBB3 and ITGAV:ITGB3 or ITGA6:ITGB4 (PubMed:20682778).
{ECO:0000250|UniProtKB:P43322, ECO:0000269|PubMed:20682778}.
-!- INTERACTION:
P04626:ERBB2; NbExp=2; IntAct=EBI-2460927, EBI-641062;
P21860:ERBB3; NbExp=3; IntAct=EBI-2460927, EBI-720706;
-!- SUBCELLULAR LOCATION: Pro-neuregulin-1, membrane-bound isoform:
Cell membrane; Single-pass type I membrane protein. Note=Does not
seem to be active.
-!- SUBCELLULAR LOCATION: Neuregulin-1: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 8: Nucleus. Note=May be nuclear.
-!- SUBCELLULAR LOCATION: Isoform 9: Secreted. Note=Has a signal
peptide.
-!- SUBCELLULAR LOCATION: Isoform 10: Membrane; Single-pass type I
membrane protein. Note=May possess an internal uncleaved signal
sequence.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=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.;
Name=1; Synonyms=Alpha;
IsoId=Q02297-1; Sequence=Displayed;
Name=2; Synonyms=Alpha1A;
IsoId=Q02297-2; Sequence=VSP_003431;
Name=3; Synonyms=Alpha2B;
IsoId=Q02297-3; Sequence=VSP_003434, VSP_003435;
Name=4; Synonyms=Alpha3;
IsoId=Q02297-4; Sequence=VSP_003432, VSP_003433;
Name=6; Synonyms=Beta1, Beta1A;
IsoId=Q02297-6; Sequence=VSP_003428;
Name=7; Synonyms=Beta2;
IsoId=Q02297-7; Sequence=VSP_003427;
Name=8; Synonyms=Beta3, GGFHFB1;
IsoId=Q02297-8; Sequence=VSP_003429, VSP_003430;
Name=9; Synonyms=GGF2, GGFHPP2;
IsoId=Q02297-9; Sequence=VSP_003425, VSP_003426, VSP_003429,
VSP_003430;
Name=10; Synonyms=SMDF;
IsoId=Q02297-10; Sequence=VSP_037562, VSP_037565, VSP_003429,
VSP_003430;
Note=Potential internal signal sequence at positions 76-100.
Variant in position: 46:G->R (in dbSNP:rs3735774). Variant in
position: 127:A->P (in dbSNP:rs34822181).;
Name=11; Synonyms=Type IV-beta1a;
IsoId=Q02297-11; Sequence=VSP_037563, VSP_037564, VSP_003426,
VSP_003428;
Name=12;
IsoId=Q02297-12; Sequence=VSP_003427, VSP_046417;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:17565985}.
-!- DEVELOPMENTAL STAGE: 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.
{ECO:0000269|PubMed:17565985}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- DOMAIN: ERBB receptor binding is elicited entirely by the EGF-like
domain.
-!- PTM: Proteolytic cleavage close to the plasma membrane on the
external face leads to the release of the soluble growth factor
form.
-!- PTM: N- and O-glycosylated. Extensive glycosylation precedes the
proteolytic cleavage (By similarity). {ECO:0000250}.
-!- DISEASE: Note=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.
-!- SIMILARITY: Belongs to the neuregulin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA19955.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=AAC51756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Tipping the mind
- Issue 129 of June 2011;
URL="http://web.expasy.org/spotlight/back_issues/129";
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EMBL; M94165; AAA58638.1; -; mRNA.
EMBL; M94166; AAA58639.1; -; mRNA.
EMBL; M94167; AAA58640.1; -; mRNA.
EMBL; M94168; AAA58641.1; -; mRNA.
EMBL; U02325; AAA19950.1; -; mRNA.
EMBL; U02326; AAA19951.1; -; mRNA.
EMBL; U02327; AAA19952.1; -; mRNA.
EMBL; U02328; AAA19953.1; -; mRNA.
EMBL; U02329; AAA19954.1; -; mRNA.
EMBL; U02330; AAA19955.1; ALT_SEQ; mRNA.
EMBL; L12260; AAB59622.1; -; mRNA.
EMBL; L12261; AAB59358.1; -; mRNA.
EMBL; L41827; AAC41764.1; -; mRNA.
EMBL; AK289927; BAF82616.1; -; mRNA.
EMBL; AK298132; BAH12729.1; -; mRNA.
EMBL; AC021909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC023948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC083977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC113209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF009227; AAC51756.1; ALT_INIT; mRNA.
EMBL; AF491780; AAM71137.1; -; Genomic_DNA.
EMBL; AF491780; AAM71139.1; -; Genomic_DNA.
EMBL; AF491780; AAM71140.1; -; Genomic_DNA.
EMBL; EF372273; ABQ53539.1; -; mRNA.
EMBL; EF372274; ABQ53540.1; -; mRNA.
EMBL; CH471080; EAW63411.1; -; Genomic_DNA.
EMBL; BC064587; AAH64587.1; -; mRNA.
EMBL; BC073871; AAH73871.1; -; mRNA.
EMBL; AF026146; AAD01795.1; -; mRNA.
EMBL; BK000383; DAA00044.1; -; Genomic_DNA.
EMBL; BK000383; DAA00045.1; -; Genomic_DNA.
EMBL; BK000383; DAA00046.1; -; Genomic_DNA.
EMBL; BK000383; DAA00047.1; -; Genomic_DNA.
CCDS; CCDS47836.1; -. [Q02297-9]
CCDS; CCDS55218.1; -. [Q02297-11]
CCDS; CCDS55219.1; -. [Q02297-12]
CCDS; CCDS6083.1; -. [Q02297-6]
CCDS; CCDS6084.1; -. [Q02297-7]
CCDS; CCDS6085.1; -. [Q02297-1]
CCDS; CCDS6086.1; -. [Q02297-3]
CCDS; CCDS6087.1; -. [Q02297-10]
PIR; A43273; A43273.
PIR; A56943; A56943.
PIR; B43273; B43273.
PIR; C43273; C43273.
PIR; D43273; D43273.
PIR; I38403; I38403.
PIR; I38404; I38404.
PIR; I38408; I38408.
PIR; S32357; S32357.
RefSeq; NP_001153467.1; NM_001159995.2.
RefSeq; NP_001153471.1; NM_001159999.2.
RefSeq; NP_001153473.1; NM_001160001.2. [Q02297-11]
RefSeq; NP_001153477.1; NM_001160005.1.
RefSeq; NP_001153480.1; NM_001160008.1. [Q02297-12]
RefSeq; NP_001309134.1; NM_001322205.1.
RefSeq; NP_001309135.1; NM_001322206.1.
RefSeq; NP_001309136.1; NM_001322207.1.
RefSeq; NP_039250.2; NM_013956.4. [Q02297-6]
RefSeq; NP_039251.2; NM_013957.4. [Q02297-7]
RefSeq; NP_039252.2; NM_013958.3. [Q02297-8]
RefSeq; NP_039253.1; NM_013959.3. [Q02297-10]
RefSeq; NP_039254.1; NM_013960.4. [Q02297-3]
RefSeq; NP_039256.2; NM_013962.2. [Q02297-9]
RefSeq; NP_039258.1; NM_013964.4. [Q02297-1]
UniGene; Hs.453951; -.
UniGene; Hs.668810; -.
PDB; 1HAE; NMR; -; A=177-239.
PDB; 1HAF; NMR; -; A=177-239.
PDB; 1HRE; NMR; -; A=175-241.
PDB; 1HRF; NMR; -; A=175-241.
PDB; 3U7U; X-ray; 3.03 A; G/H/I/J/K/L=175-212.
PDBsum; 1HAE; -.
PDBsum; 1HAF; -.
PDBsum; 1HRE; -.
PDBsum; 1HRF; -.
PDBsum; 3U7U; -.
ProteinModelPortal; Q02297; -.
SMR; Q02297; -.
BioGrid; 109332; 70.
DIP; DIP-355N; -.
IntAct; Q02297; 13.
MINT; MINT-158528; -.
STRING; 9606.ENSP00000349275; -.
iPTMnet; Q02297; -.
PhosphoSitePlus; Q02297; -.
BioMuta; NRG1; -.
DMDM; 9297018; -.
MaxQB; Q02297; -.
PaxDb; Q02297; -.
PeptideAtlas; Q02297; -.
PRIDE; Q02297; -.
DNASU; 3084; -.
Ensembl; ENST00000287842; ENSP00000287842; ENSG00000157168. [Q02297-6]
Ensembl; ENST00000356819; ENSP00000349275; ENSG00000157168. [Q02297-7]
Ensembl; ENST00000405005; ENSP00000384620; ENSG00000157168. [Q02297-1]
Ensembl; ENST00000519301; ENSP00000429582; ENSG00000157168. [Q02297-11]
Ensembl; ENST00000520407; ENSP00000434640; ENSG00000157168. [Q02297-9]
Ensembl; ENST00000520502; ENSP00000433289; ENSG00000157168. [Q02297-10]
Ensembl; ENST00000521670; ENSP00000428828; ENSG00000157168. [Q02297-3]
Ensembl; ENST00000523079; ENSP00000430120; ENSG00000157168. [Q02297-12]
GeneID; 3084; -.
KEGG; hsa:3084; -.
UCSC; uc003xip.4; human. [Q02297-1]
CTD; 3084; -.
DisGeNET; 3084; -.
GeneCards; NRG1; -.
HGNC; HGNC:7997; NRG1.
HPA; HPA010964; -.
MalaCards; NRG1; -.
MIM; 142445; gene.
neXtProt; NX_Q02297; -.
OpenTargets; ENSG00000157168; -.
PharmGKB; PA31776; -.
eggNOG; ENOG410IEU9; Eukaryota.
eggNOG; ENOG4110ST7; LUCA.
GeneTree; ENSGT00800000124099; -.
HOGENOM; HOG000273863; -.
HOVERGEN; HBG006531; -.
InParanoid; Q02297; -.
KO; K05455; -.
PhylomeDB; Q02297; -.
TreeFam; TF332469; -.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1236394; Signaling by ERBB4.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling.
Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1306955; GRB7 events in ERBB2 signaling.
Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
SignaLink; Q02297; -.
SIGNOR; Q02297; -.
ChiTaRS; NRG1; human.
EvolutionaryTrace; Q02297; -.
GeneWiki; Neuregulin_1; -.
GenomeRNAi; 3084; -.
PMAP-CutDB; Q02297; -.
PRO; PR:Q02297; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000157168; -.
CleanEx; HS_NRG1; -.
ExpressionAtlas; Q02297; baseline and differential.
Genevisible; Q02297; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0030673; C:axolemma; IEA:Ensembl.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; TAS:BHF-UCL.
GO; GO:0005176; F:ErbB-2 class receptor binding; IEA:Ensembl.
GO; GO:0043125; F:ErbB-3 class receptor binding; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:BHF-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0030971; F:receptor tyrosine kinase binding; NAS:UniProtKB.
GO; GO:0003712; F:transcription cofactor activity; IDA:MGI.
GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; NAS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IMP:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; IMP:UniProtKB.
GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IDA:BHF-UCL.
GO; GO:0008366; P:axon ensheathment; IEA:Ensembl.
GO; GO:0003161; P:cardiac conduction system development; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:BHF-UCL.
GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IDA:BHF-UCL.
GO; GO:0007154; P:cell communication; TAS:BHF-UCL.
GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IDA:BHF-UCL.
GO; GO:0043624; P:cellular protein complex disassembly; IGI:MGI.
GO; GO:0021842; P:chemorepulsion involved in interneuron migration from the subpallium to the cortex; IEA:Ensembl.
GO; GO:0009790; P:embryo development; IEA:InterPro.
GO; GO:0060956; P:endocardial cell differentiation; IDA:BHF-UCL.
GO; GO:0038127; P:ERBB signaling pathway; IDA:BHF-UCL.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038129; P:ERBB3 signaling pathway; IDA:CAFA.
GO; GO:0021781; P:glial cell fate commitment; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; TAS:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:1901185; P:negative regulation of ERBB signaling pathway; TAS:Reactome.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:BHF-UCL.
GO; GO:2001223; P:negative regulation of neuron migration; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0051048; P:negative regulation of secretion; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0007399; P:nervous system development; TAS:BHF-UCL.
GO; GO:0014032; P:neural crest cell development; TAS:BHF-UCL.
GO; GO:0048663; P:neuron fate commitment; IEA:Ensembl.
GO; GO:0045213; P:neurotransmitter receptor metabolic process; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0043497; P:regulation of protein heterodimerization activity; IDA:BHF-UCL.
GO; GO:0043496; P:regulation of protein homodimerization activity; TAS:BHF-UCL.
GO; GO:0001964; P:startle response; IEA:Ensembl.
GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:BHF-UCL.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IDA:BHF-UCL.
GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR002154; Neuregulin_C.
InterPro; IPR018250; NRG1.
PANTHER; PTHR11100:SF30; PTHR11100:SF30; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF07679; I-set; 1.
Pfam; PF02158; Neuregulin; 1.
PRINTS; PR01089; NEUREGULIN.
SMART; SM00181; EGF; 1.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane;
Chromosomal rearrangement; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Glycoprotein; Growth factor; Immunoglobulin domain; Membrane; Nucleus;
Polymorphism; Reference proteome; Secreted; Transmembrane;
Transmembrane helix.
PROPEP 1 19 {ECO:0000269|PubMed:7689552}.
/FTId=PRO_0000019462.
CHAIN 20 640 Pro-neuregulin-1, membrane-bound isoform.
/FTId=PRO_0000019463.
CHAIN 20 241 Neuregulin-1.
/FTId=PRO_0000019464.
TOPO_DOM 20 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 265 Helical; Note=Internal signal sequence.
{ECO:0000255}.
TOPO_DOM 266 640 Cytoplasmic. {ECO:0000255}.
DOMAIN 37 128 Ig-like C2-type.
DOMAIN 178 222 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
COMPBIAS 165 177 Ser/Thr-rich.
SITE 34 34 Breakpoint for translocation to form
gamma-heregulin.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 112 {ECO:0000250}.
DISULFID 182 196 {ECO:0000269|PubMed:8639490}.
DISULFID 190 210 {ECO:0000269|PubMed:8639490}.
DISULFID 212 221 {ECO:0000269|PubMed:8639490}.
VAR_SEQ 1 166 Missing (in isoform 10).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7782315}.
/FTId=VSP_037562.
VAR_SEQ 1 33 MSERKEGRGKGKGKKKERGSGKKPESAAGSQSP -> MRWR
RAPRRSGRPGPRAQRPGSAARSSPPLPLLPLLLLLGTAALA
PGAAAGNEAAPAGASVCYSSPPSVGSVQELAQRAAVVIEGK
VHPQRRQQGALDRKAAAAAGEAGAWGGDREPPAAGPRALGP
PAEEPLLAANGTVPSWPTAPVPSAGEPGEEAPYLVKVHQVW
AVKAGGLKKDSLLTVRLGTWGHPAFPSCGRLKEDSRYIFFM
EPDANSTSRAPAAFRASFPPLETGRNLKKEVSRVLCKRC
(in isoform 9).
{ECO:0000303|PubMed:8096067}.
/FTId=VSP_003425.
VAR_SEQ 1 21 Missing (in isoform 11).
{ECO:0000303|PubMed:17565985}.
/FTId=VSP_037563.
VAR_SEQ 22 33 KKPESAAGSQSP -> MGKGRAGRVGTT (in isoform
11). {ECO:0000303|PubMed:17565985}.
/FTId=VSP_037564.
VAR_SEQ 134 168 EIITGMPASTEGAYVSSESPIRISVSTEGANTSSS -> A
(in isoform 9 and isoform 11).
{ECO:0000303|PubMed:17565985,
ECO:0000303|PubMed:8096067}.
/FTId=VSP_003426.
VAR_SEQ 167 167 S -> MEIYSPDMSEVAAERSSSPSTQLSADPSLDGLPAAE
DMPEPQTEDGRTPGLVGLAVPCCACLEAERLRGCLNSEKIC
IVPILACLVSLCLCIAGLKWVFVDKIFEYDSPTHLDPGGLG
QDPIISLDATAASAVWVSSEAYTSPVSRAQSESEVQVTVQG
DKAVVSFEPSAAPTPKNRIFAFSFLPSTAPSFPSPTRNPEV
RTPKSATQPQTTETNLQTAPKL (in isoform 10).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7782315}.
/FTId=VSP_037565.
VAR_SEQ 213 241 QPGFTGARCTENVPMKVQNQEKAEELYQK -> PNEFTGDR
CQNYVMASFYSTSTPFLSLPE (in isoform 8,
isoform 9 and isoform 10).
{ECO:0000303|PubMed:1350381,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7509448,
ECO:0000303|PubMed:7782315,
ECO:0000303|PubMed:8096067}.
/FTId=VSP_003429.
VAR_SEQ 213 234 QPGFTGARCTENVPMKVQNQEK -> PNEFTGDRCQNYVMA
SFYKHLGIEFME (in isoform 6 and isoform
11). {ECO:0000303|PubMed:1350381,
ECO:0000303|PubMed:17565985,
ECO:0000303|PubMed:7509448}.
/FTId=VSP_003428.
VAR_SEQ 213 233 QPGFTGARCTENVPMKVQNQE -> PNEFTGDRCQNYVMAS
FY (in isoform 7 and isoform 12).
{ECO:0000303|PubMed:1350381,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7509448}.
/FTId=VSP_003427.
VAR_SEQ 234 247 KAEELYQKRVLTIT -> SAQMSLLVIAAKTT (in
isoform 4). {ECO:0000303|PubMed:7509448}.
/FTId=VSP_003432.
VAR_SEQ 234 234 K -> KHLGIEFIE (in isoform 2).
{ECO:0000303|PubMed:7509448}.
/FTId=VSP_003431.
VAR_SEQ 242 640 Missing (in isoform 8, isoform 9 and
isoform 10). {ECO:0000303|PubMed:1350381,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7509448,
ECO:0000303|PubMed:7782315,
ECO:0000303|PubMed:8096067}.
/FTId=VSP_003430.
VAR_SEQ 248 640 Missing (in isoform 4).
{ECO:0000303|PubMed:7509448}.
/FTId=VSP_003433.
VAR_SEQ 424 640 Missing (in isoform 12).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046417.
VAR_SEQ 424 462 YVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVS
-> HNLIAELRRNKAHRSKCMQIQLSATHLRSSSIPHLGFI
L (in isoform 3).
{ECO:0000303|PubMed:7509448}.
/FTId=VSP_003434.
VAR_SEQ 463 640 Missing (in isoform 3).
{ECO:0000303|PubMed:7509448}.
/FTId=VSP_003435.
VARIANT 38 38 R -> Q (in dbSNP:rs3924999).
{ECO:0000269|PubMed:17565985}.
/FTId=VAR_009307.
VARIANT 289 289 M -> T (in dbSNP:rs10503929).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17565985}.
/FTId=VAR_053531.
VARIANT 463 463 M -> K.
/FTId=VAR_009308.
MUTAGEN 181 181 K->E: Defective in integrin-binding and
in inducing ERBB3 phosphorylation; when
associated with or without E-185 or E-
187. No effect on ERBB3-binding,
defective in integrin-binding and in
ternary complex formation with ERBB3 and
integrins, and defective in inducing
NRG1-ERBB signaling; when associated with
E-185 and E-187.
{ECO:0000269|PubMed:20682778}.
MUTAGEN 185 185 K->E: Defective in integrin-binding and
in inducing ERBB3 phosphorylation; when
associated with or without E-181 or E-
187. No effect on ERBB3-binding,
defective in integrin-binding and in
ternary complex formation with ERBB3 and
integrins, and defective in inducing
NRG1-ERBB signaling; when associated with
E-181 and E-187.
{ECO:0000269|PubMed:20682778}.
MUTAGEN 187 187 K->E: Defective in integrin-binding and
in inducing ERBB3 phosphorylation; when
associated with or without E-181 or E-
185. No effect on ERBB3-binding,
defective in integrin-binding and in
ternary complex formation with ERBB3 and
integrins, and defective in inducing
NRG1-ERBB signaling; when associated with
E-181 and E-185.
{ECO:0000269|PubMed:20682778}.
CONFLICT 94 94 K -> A (in Ref. 2; AAA19953).
{ECO:0000305}.
CONFLICT 107 107 S -> P (in Ref. 10; ABQ53539).
{ECO:0000305}.
CONFLICT 261 261 V -> L (in Ref. 10; ABQ53540).
{ECO:0000305}.
CONFLICT 414 414 S -> F (in Ref. 2; AAA19953).
{ECO:0000305}.
CONFLICT 535 535 Q -> R (in Ref. 2; AAA19951).
{ECO:0000305}.
STRAND 179 181 {ECO:0000244|PDB:3U7U}.
TURN 185 189 {ECO:0000244|PDB:3U7U}.
STRAND 190 193 {ECO:0000244|PDB:1HRE}.
STRAND 195 199 {ECO:0000244|PDB:3U7U}.
STRAND 200 204 {ECO:0000244|PDB:1HRE}.
STRAND 208 212 {ECO:0000244|PDB:3U7U}.
STRAND 216 218 {ECO:0000244|PDB:1HAE}.
STRAND 233 235 {ECO:0000244|PDB:1HAF}.
SEQUENCE 640 AA; 70392 MW; C30D3F614AADFF62 CRC64;
MSERKEGRGK GKGKKKERGS GKKPESAAGS QSPALPPRLK EMKSQESAAG SKLVLRCETS
SEYSSLRFKW FKNGNELNRK NKPQNIKIQK KPGKSELRIN KASLADSGEY MCKVISKLGN
DSASANITIV ESNEIITGMP ASTEGAYVSS ESPIRISVST EGANTSSSTS TSTTGTSHLV
KCAEKEKTFC VNGGECFMVK DLSNPSRYLC KCQPGFTGAR CTENVPMKVQ NQEKAEELYQ
KRVLTITGIC IALLVVGIMC VVAYCKTKKQ RKKLHDRLRQ SLRSERNNMM NIANGPHHPN
PPPENVQLVN QYVSKNVISS EHIVEREAET SFSTSHYTST AHHSTTVTQT PSHSWSNGHT
ESILSESHSV IVMSSVENSR HSSPTGGPRG RLNGTGGPRE CNSFLRHARE TPDSYRDSPH
SERYVSAMTT PARMSPVDFH TPSSPKSPPS EMSPPVSSMT VSMPSMAVSP FMEEERPLLL
VTPPRLREKK FDHHPQQFSS FHHNPAHDSN SLPASPLRIV EDEEYETTQE YEPAQEPVKK
LANSRRAKRT KPNGHIANRL EVDSNTSSQS SNSESETEDE RVGEDTPFLG IQNPLAASLE
ATPAFRLADS RTNPAGRFST QEEIQARLSS VIANQDPIAV


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