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Interferon alpha/beta receptor 2 (IFN-R-2) (IFN-alpha binding protein) (IFN-alpha/beta receptor 2) (Interferon alpha binding protein) (Type I interferon receptor 2)

 INAR2_HUMAN             Reviewed;         515 AA.
P48551; A8KAJ4; D3DSE8; D3DSE9; Q15467; Q6FHD7;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 177.
RecName: Full=Interferon alpha/beta receptor 2;
Short=IFN-R-2;
Short=IFN-alpha binding protein;
Short=IFN-alpha/beta receptor 2;
AltName: Full=Interferon alpha binding protein;
AltName: Full=Type I interferon receptor 2;
Flags: Precursor;
Name=IFNAR2; Synonyms=IFNABR, IFNARB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE,
GLYCOSYLATION AT ASN-87 AND ASN-192, FUNCTION, SUBUNIT, INTERACTION
WITH JAK1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT
VAL-10.
TISSUE=Monocyte;
PubMed=8181059; DOI=10.1016/0092-8674(94)90154-6;
Novick D., Cohen B., Rubinstein M.;
"The human interferon alpha/beta receptor: characterization and
molecular cloning.";
Cell 77:391-400(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND
TISSUE SPECIFICITY.
TISSUE=Lymphoblastoma;
PubMed=7588638;
Lutfalla G., Holland S.J., Cinato E., Monneron D., Reboul J.,
Rogers N.C., Smith J.M., Stark G.R., Gardiner K., Mogensen K.E.,
Kerr I.M., Uze G.;
"Mutant U5A cells are complemented by an interferon-alpha beta
receptor subunit generated by alternative processing of a new member
of a cytokine receptor gene cluster.";
EMBO J. 14:5100-5108(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBUNIT.
TISSUE=Myeloma;
PubMed=7665574; DOI=10.1074/jbc.270.37.21606;
Domanski P., Witte M., Kellum M., Rubinstein M., Hackett R., Pitha P.,
Colamonici O.R.;
"Cloning and expression of a long form of the beta subunit of the
interferon alpha beta receptor that is required for signaling.";
J. Biol. Chem. 270:21606-21611(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PARTIAL PROTEIN SEQUENCE,
FUNCTION, INTERACTION WITH JAK1, ALTERNATIVE SPLICING, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND VARIANT VAL-10.
TISSUE=Blood;
PubMed=7759950;
Novick D., Cohen B., Tal N., Rubinstein M.;
"Soluble and membrane-anchored forms of the human IFN-alpha/beta
receptor.";
J. Leukoc. Biol. 57:712-718(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-10.
TISSUE=Blood;
Cohen B., Kim S.H., Novick D., Rubinstein M.;
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-8; VAL-10 AND
VAL-196.
SeattleSNPs variation discovery resource;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[10]
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.
[11]
FUNCTION, AND INTERACTION WITH STAT1 AND STAT2.
PubMed=9121453; DOI=10.1128/MCB.17.4.2048;
Li X., Leung S., Kerr I.M., Stark G.R.;
"Functional subdomains of STAT2 required for preassociation with the
alpha interferon receptor and for signaling.";
Mol. Cell. Biol. 17:2048-2056(1997).
[12]
INTERACTION WITH IFNAR1, AND FUNCTION.
PubMed=10049744; DOI=10.1006/bbrc.1998.0105;
Russell-Harde D., Wagner T.C., Perez H.D., Croze E.;
"Formation of a uniquely stable type I interferon receptor complex by
interferon beta is dependent upon particular interactions between
interferon beta and its receptor and independent of tyrosine
phosphorylation.";
Biochem. Biophys. Res. Commun. 255:539-544(1999).
[13]
FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, AND MUTAGENESIS OF
TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512.
PubMed=11682488; DOI=10.1074/jbc.M108928200;
Wagner T.C., Velichko S., Vogel D., Rani M.R., Leung S.,
Ransohoff R.M., Stark G.R., Perez H.D., Croze E.;
"Interferon signaling is dependent on specific tyrosines located
within the intracellular domain of IFNAR2c. Expression of IFNAR2c
tyrosine mutants in U5A cells.";
J. Biol. Chem. 277:1493-1499(2002).
[14]
FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, AND MUTAGENESIS OF
TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512.
PubMed=12105218; DOI=10.1074/jbc.M204578200;
Velichko S., Wagner T.C., Turkson J., Jove R., Croze E.;
"STAT3 activation by type I interferons is dependent on specific
tyrosines located in the cytoplasmic domain of interferon receptor
chain 2c. Activation of multiple STATS proceeds through the redundant
usage of two tyrosine residues.";
J. Biol. Chem. 277:35635-35641(2002).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
STRUCTURE BY NMR OF 28-237, AND DISULFIDE BONDS.
PubMed=12842042; DOI=10.1016/S0969-2126(03)00120-5;
Chill J.H., Quadt S.R., Levy R., Schreiber G., Anglister J.;
"The human type I interferon receptor: NMR structure reveals the
molecular basis of ligand binding.";
Structure 11:791-802(2003).
[17]
INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION, VARIANTS SER-8 AND
VAL-10, AND CHARACTERIZATION OF VARIANT SER-8.
PubMed=16757563; DOI=10.1073/pnas.0602800103;
Frodsham A.J., Zhang L., Dumpis U., Taib N.A.M., Best S., Durham A.,
Hennig B.J.W., Hellier S., Knapp S., Wright M., Chiaramonte M.,
Bell J.I., Graves M., Whittle H.C., Thomas H.C., Thursz M.R.,
Hill A.V.S.;
"Class II cytokine receptor gene cluster is a major locus for
hepatitis B persistence.";
Proc. Natl. Acad. Sci. U.S.A. 103:9148-9153(2006).
[18]
INTERACTION WITH IFNAR1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S.,
Katlinski K., Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y.,
Greenberg R.A.;
"A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
responses.";
Cell Rep. 5:180-193(2013).
[19]
STRUCTURE BY NMR OF 28-239 IN COMPLEX WITH IFNA2, AND DISULFIDE BONDS.
PubMed=17001036; DOI=10.1110/ps.062283006;
Quadt-Akabayov S.R., Chill J.H., Levy R., Kessler N., Anglister J.;
"Determination of the human type I interferon receptor binding site on
human interferon-alpha2 by cross saturation and an NMR-based model of
the complex.";
Protein Sci. 15:2656-2668(2006).
[20]
STRUCTURE BY NMR OF 28-239 IN COMPLEX WITH IFNA2, AND DISULFIDE BONDS.
PubMed=20496919; DOI=10.1021/bi100041f;
Nudelman I., Akabayov S.R., Schnur E., Biron Z., Levy R., Xu Y.,
Yang D., Anglister J.;
"Intermolecular interactions in a 44 kDa interferon-receptor complex
detected by asymmetric reverse-protonation and two-dimensional
NOESY.";
Biochemistry 49:5117-5133(2010).
[21]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-436 IN COMPLEX WITH
IFNAR1 AND IFNW1, AND DISULFIDE BONDS.
PubMed=21854986; DOI=10.1016/j.cell.2011.06.048;
Thomas C., Moraga I., Levin D., Krutzik P.O., Podoplelova Y.,
Trejo A., Lee C., Yarden G., Vleck S.E., Glenn J.S., Nolan G.P.,
Piehler J., Schreiber G., Garcia K.C.;
"Structural linkage between ligand discrimination and receptor
activation by type I interferons.";
Cell 146:621-632(2011).
[22]
STRUCTURE BY NMR OF 28-237, AND DISULFIDE BONDS.
PubMed=21819146; DOI=10.1021/ja205480v;
Nudelman I., Akabayov S.R., Scherf T., Anglister J.;
"Observation of intermolecular interactions in large protein complexes
by 2D-double difference nuclear Overhauser enhancement spectroscopy:
application to the 44 kDa interferon-receptor complex.";
J. Am. Chem. Soc. 133:14755-14764(2011).
[23]
INVOLVEMENT IN IMD45, AND FUNCTION.
PubMed=26424569; DOI=10.1126/scitranslmed.aac4227;
Duncan C.J., Mohamad S.M., Young D.F., Skelton A.J., Leahy T.R.,
Munday D.C., Butler K.M., Morfopoulou S., Brown J.R., Hubank M.,
Connell J., Gavin P.J., McMahon C., Dempsey E., Lynch N.E.,
Jacques T.S., Valappil M., Cant A.J., Breuer J., Engelhardt K.R.,
Randall R.E., Hambleton S.;
"Human IFNAR2 deficiency: Lessons for antiviral immunity.";
Sci. Transl. Med. 7:307RA154-307RA154(2015).
-!- FUNCTION: Associates with IFNAR1 to form the type I interferon
receptor. Receptor for interferons alpha and beta. Involved in
IFN-mediated STAT1, STAT2 and STAT3 activation (PubMed:26424569).
Isoform 1 and isoform 2 are directly involved in signal
transduction due to their association with the TYR kinase, JAK1
(PubMed:8181059, PubMed:7665574, PubMed:7759950). Isoform 3 is a
potent inhibitor of type I IFN receptor activity (PubMed:7759950).
{ECO:0000269|PubMed:10049744, ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218, ECO:0000269|PubMed:26424569,
ECO:0000269|PubMed:7665574, ECO:0000269|PubMed:7759950,
ECO:0000269|PubMed:8181059}.
-!- SUBUNIT: Heterodimer with IFNAR1 (PubMed:8181059, PubMed:7665574,
PubMed:10049744, PubMed:24075985, PubMed:21854986). Isoform 1
interacts with the transcriptional factors STAT1 and STAT2
(PubMed:9121453). Interacts with JAK1 (PubMed:8181059,
PubMed:7759950). {ECO:0000269|PubMed:10049744,
ECO:0000269|PubMed:17001036, ECO:0000269|PubMed:20496919,
ECO:0000269|PubMed:21854986, ECO:0000269|PubMed:24075985,
ECO:0000269|PubMed:7665574, ECO:0000269|PubMed:7759950,
ECO:0000269|PubMed:8181059, ECO:0000269|PubMed:9121453}.
-!- INTERACTION:
Q92793:CREBBP; NbExp=4; IntAct=EBI-958408, EBI-81215;
Q00978:IRF9; NbExp=6; IntAct=EBI-958408, EBI-626526;
P23458:JAK1; NbExp=3; IntAct=EBI-958408, EBI-1383438;
P63244:RACK1; NbExp=4; IntAct=EBI-958408, EBI-296739;
P42224:STAT1; NbExp=2; IntAct=EBI-958408, EBI-1057697;
P52630:STAT2; NbExp=4; IntAct=EBI-958408, EBI-1546963;
Q9UMW8:USP18; NbExp=4; IntAct=EBI-958408, EBI-356206;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:7665574}; Single-pass type I membrane protein
{ECO:0000269|PubMed:7665574}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:7665574, ECO:0000269|PubMed:7759950,
ECO:0000269|PubMed:8181059}; Single-pass type I membrane protein
{ECO:0000269|PubMed:7665574}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted
{ECO:0000269|PubMed:7759950, ECO:0000269|PubMed:8181059}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long form beta {ECO:0000303|PubMed:7665574},
IFNaR2-2, IFNaR2-1b;
IsoId=P48551-1; Sequence=Displayed;
Name=2; Synonyms=Short form beta {ECO:0000303|PubMed:7665574},
IFNaR2-1, IFNaR2-1a;
IsoId=P48551-2; Sequence=VSP_001738, VSP_001739;
Name=3; Synonyms=IFNaR2-3, IFNaR2-2a, P40
{ECO:0000303|PubMed:8181059};
IsoId=P48551-3; Sequence=VSP_001736, VSP_001737;
Note=Soluble receptor.;
-!- TISSUE SPECIFICITY: Isoform 3 is detected in the urine (at protein
level) (PubMed:8181059, PubMed:7759950). Expressed in blood cells.
Expressed in lymphoblastoid and fibrosarcoma cell lines.
{ECO:0000269|PubMed:7588638, ECO:0000269|PubMed:7759950,
ECO:0000269|PubMed:8181059}.
-!- PTM: Phosphorylated on tyrosine residues upon interferon binding.
Phosphorylation at Tyr-337 or Tyr-512 are sufficient to mediate
interferon dependent activation of STAT1, STAT2 and STAT3 leading
to antiproliferative effects on many different cell types.
{ECO:0000269|PubMed:11682488, ECO:0000269|PubMed:12105218,
ECO:0000269|PubMed:7759950}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:8181059}.
-!- POLYMORPHISM: Genetic variations in IFNAR2 influence
susceptibility to hepatitis B virus (HBV) infection [MIM:610424].
-!- DISEASE: Immunodeficiency 45 (IMD45) [MIM:616669]: An autosomal
recessive disorder characterized by increased susceptibility to
viral infection due to impaired antiviral immunity, resulting in
infection-associated encephalopathy. Affected individuals are at
risk for developing fatal encephalitis after routine
measles/mumps/rubella (MMR) vaccination.
{ECO:0000269|PubMed:26424569}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type II cytokine receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ifnar2/";
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EMBL; X77722; CAA54785.1; -; mRNA.
EMBL; L42243; AAB46417.1; -; Genomic_DNA.
EMBL; L42238; AAB46417.1; JOINED; Genomic_DNA.
EMBL; L42239; AAB46417.1; JOINED; Genomic_DNA.
EMBL; L42240; AAB46417.1; JOINED; Genomic_DNA.
EMBL; L42323; AAB46417.1; JOINED; Genomic_DNA.
EMBL; L42241; AAB46417.1; JOINED; Genomic_DNA.
EMBL; L42242; AAB46417.1; JOINED; Genomic_DNA.
EMBL; L42243; AAB46418.1; -; Genomic_DNA.
EMBL; L42238; AAB46418.1; JOINED; Genomic_DNA.
EMBL; L42239; AAB46418.1; JOINED; Genomic_DNA.
EMBL; L42240; AAB46418.1; JOINED; Genomic_DNA.
EMBL; L42323; AAB46418.1; JOINED; Genomic_DNA.
EMBL; L42241; AAB46418.1; JOINED; Genomic_DNA.
EMBL; L42243; AAB46419.1; -; Genomic_DNA.
EMBL; L42238; AAB46419.1; JOINED; Genomic_DNA.
EMBL; L42239; AAB46419.1; JOINED; Genomic_DNA.
EMBL; L42240; AAB46419.1; JOINED; Genomic_DNA.
EMBL; L42323; AAB46419.1; JOINED; Genomic_DNA.
EMBL; L42241; AAB46419.1; JOINED; Genomic_DNA.
EMBL; L42242; AAB46419.1; JOINED; Genomic_DNA.
EMBL; L41942; AAB46413.1; -; mRNA.
EMBL; L41943; AAB46414.1; -; mRNA.
EMBL; L41944; AAB46415.1; -; mRNA.
EMBL; U29584; AAC50202.1; -; mRNA.
EMBL; X89814; CAA61940.1; -; mRNA.
EMBL; X89772; CAA61914.1; -; mRNA.
EMBL; AY740397; AAU21038.1; -; Genomic_DNA.
EMBL; AK293059; BAF85748.1; -; mRNA.
EMBL; CR541817; CAG46616.1; -; mRNA.
EMBL; AP000292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09842.1; -; Genomic_DNA.
EMBL; CH471079; EAX09843.1; -; Genomic_DNA.
EMBL; CH471079; EAX09844.1; -; Genomic_DNA.
EMBL; CH471079; EAX09846.1; -; Genomic_DNA.
CCDS; CCDS13621.1; -. [P48551-1]
CCDS; CCDS13622.1; -. [P48551-2]
CCDS; CCDS74782.1; -. [P48551-3]
PIR; I39073; I39073.
PIR; S59501; S59501.
RefSeq; NP_000865.2; NM_000874.4. [P48551-2]
RefSeq; NP_001276054.1; NM_001289125.1. [P48551-1]
RefSeq; NP_001276055.1; NM_001289126.1. [P48551-3]
RefSeq; NP_001276057.1; NM_001289128.1. [P48551-3]
RefSeq; NP_997467.1; NM_207584.2. [P48551-2]
RefSeq; NP_997468.1; NM_207585.2. [P48551-1]
UniGene; Hs.708195; -.
PDB; 1N6U; NMR; -; A=28-237.
PDB; 1N6V; NMR; -; A=28-237.
PDB; 2HYM; NMR; -; A=28-237.
PDB; 2KZ1; NMR; -; B=28-237.
PDB; 2LAG; NMR; -; B=28-237.
PDB; 3S8W; X-ray; 2.60 A; A/B/C=131-232.
PDB; 3S9D; X-ray; 2.00 A; B/D=37-232.
PDB; 3SE3; X-ray; 4.00 A; C=34-232.
PDB; 3SE4; X-ray; 3.50 A; C=34-232.
PDBsum; 1N6U; -.
PDBsum; 1N6V; -.
PDBsum; 2HYM; -.
PDBsum; 2KZ1; -.
PDBsum; 2LAG; -.
PDBsum; 3S8W; -.
PDBsum; 3S9D; -.
PDBsum; 3SE3; -.
PDBsum; 3SE4; -.
ProteinModelPortal; P48551; -.
SMR; P48551; -.
BioGrid; 109677; 12.
CORUM; P48551; -.
DIP; DIP-945N; -.
IntAct; P48551; 14.
MINT; MINT-196715; -.
STRING; 9606.ENSP00000343957; -.
ChEMBL; CHEMBL2364170; -.
DrugBank; DB00011; Interferon alfa-n1.
DrugBank; DB00018; Interferon alfa-n3.
DrugBank; DB00069; Interferon alfacon-1.
DrugBank; DB00060; Interferon beta-1a.
DrugBank; DB00068; Interferon beta-1b.
DrugBank; DB05472; omega interferon.
DrugBank; DB00008; Peginterferon alfa-2a.
DrugBank; DB00022; Peginterferon alfa-2b.
iPTMnet; P48551; -.
PhosphoSitePlus; P48551; -.
BioMuta; IFNAR2; -.
DMDM; 1352466; -.
MaxQB; P48551; -.
PaxDb; P48551; -.
PeptideAtlas; P48551; -.
PRIDE; P48551; -.
DNASU; 3455; -.
Ensembl; ENST00000342101; ENSP00000343289; ENSG00000159110. [P48551-3]
Ensembl; ENST00000342136; ENSP00000343957; ENSG00000159110. [P48551-1]
Ensembl; ENST00000382264; ENSP00000371699; ENSG00000159110. [P48551-2]
Ensembl; ENST00000404220; ENSP00000384309; ENSG00000159110. [P48551-2]
GeneID; 3455; -.
KEGG; hsa:3455; -.
UCSC; uc002yrb.5; human. [P48551-1]
CTD; 3455; -.
DisGeNET; 3455; -.
EuPathDB; HostDB:ENSG00000159110.19; -.
GeneCards; IFNAR2; -.
HGNC; HGNC:5433; IFNAR2.
HPA; CAB025889; -.
MIM; 602376; gene.
MIM; 610424; phenotype.
MIM; 616669; phenotype.
neXtProt; NX_P48551; -.
OpenTargets; ENSG00000159110; -.
PharmGKB; PA29671; -.
eggNOG; ENOG410IHB9; Eukaryota.
eggNOG; ENOG410YTXY; LUCA.
GeneTree; ENSGT00510000049322; -.
HOGENOM; HOG000013219; -.
HOVERGEN; HBG053907; -.
InParanoid; P48551; -.
KO; K05131; -.
OMA; KVWDYNY; -.
OrthoDB; EOG091G09YY; -.
PhylomeDB; P48551; -.
TreeFam; TF335897; -.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-912694; Regulation of IFNA signaling.
SignaLink; P48551; -.
SIGNOR; P48551; -.
ChiTaRS; IFNAR2; human.
EvolutionaryTrace; P48551; -.
GeneWiki; IFNAR2; -.
GenomeRNAi; 3455; -.
PMAP-CutDB; Q6FHD7; -.
PRO; PR:P48551; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000159110; -.
CleanEx; HS_IFNAR2; -.
ExpressionAtlas; P48551; baseline and differential.
Genevisible; P48551; HS.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019962; F:type I interferon binding; IPI:UniProtKB.
GO; GO:0004905; F:type I interferon receptor activity; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB.
GO; GO:0035456; P:response to interferon-beta; IMP:UniProtKB.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
GO; GO:0060337; P:type I interferon signaling pathway; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015373; Interferon/interleukin_rcp_dom.
Pfam; PF09294; Interfer-bind; 1.
Pfam; PF01108; Tissue_fac; 1.
SUPFAM; SSF49265; SSF49265; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 26
CHAIN 27 515 Interferon alpha/beta receptor 2.
/FTId=PRO_0000011006.
TOPO_DOM 27 243 Extracellular. {ECO:0000255}.
TRANSMEM 244 264 Helical. {ECO:0000255}.
TOPO_DOM 265 515 Cytoplasmic. {ECO:0000255}.
MOD_RES 337 337 Phosphotyrosine.
{ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000250|UniProtKB:O35664}.
MOD_RES 512 512 Phosphotyrosine.
{ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8181059}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8181059}.
DISULFID 39 122 {ECO:0000244|PDB:1N6U,
ECO:0000244|PDB:1N6V,
ECO:0000244|PDB:2HYM,
ECO:0000244|PDB:2KZ1,
ECO:0000244|PDB:2LAG,
ECO:0000244|PDB:3S9D,
ECO:0000244|PDB:3SE3,
ECO:0000244|PDB:3SE4,
ECO:0000269|PubMed:17001036,
ECO:0000269|PubMed:20496919,
ECO:0000269|PubMed:21819146,
ECO:0000269|PubMed:21854986}.
DISULFID 85 93 {ECO:0000244|PDB:1N6U,
ECO:0000244|PDB:1N6V,
ECO:0000244|PDB:2HYM,
ECO:0000244|PDB:2KZ1,
ECO:0000244|PDB:2LAG,
ECO:0000244|PDB:3S9D,
ECO:0000244|PDB:3SE3,
ECO:0000244|PDB:3SE4,
ECO:0000269|PubMed:17001036,
ECO:0000269|PubMed:20496919,
ECO:0000269|PubMed:21819146,
ECO:0000269|PubMed:21854986}.
DISULFID 207 227 {ECO:0000244|PDB:1N6U,
ECO:0000244|PDB:1N6V,
ECO:0000244|PDB:2HYM,
ECO:0000244|PDB:2KZ1,
ECO:0000244|PDB:2LAG,
ECO:0000244|PDB:3S8W,
ECO:0000244|PDB:3S9D,
ECO:0000244|PDB:3SE3,
ECO:0000244|PDB:3SE4,
ECO:0000269|PubMed:17001036,
ECO:0000269|PubMed:20496919,
ECO:0000269|PubMed:21819146,
ECO:0000269|PubMed:21854986}.
VAR_SEQ 238 239 SA -> FS (in isoform 3).
{ECO:0000303|PubMed:7588638,
ECO:0000303|PubMed:7759950}.
/FTId=VSP_001736.
VAR_SEQ 240 515 Missing (in isoform 3).
{ECO:0000303|PubMed:7588638,
ECO:0000303|PubMed:7759950}.
/FTId=VSP_001737.
VAR_SEQ 281 331 NFHNFLAWPFPNLPPLEAMDMVEVIYINRKKKVWDYNYDDE
SDSDTEAAPR -> RQGLAKGWNAVAIHRCSHNALQSETPE
LKQSSCLSFPSSWDYKRASLCPSD (in isoform 2).
{ECO:0000303|PubMed:7588638,
ECO:0000303|PubMed:8181059,
ECO:0000303|Ref.8}.
/FTId=VSP_001738.
VAR_SEQ 332 515 Missing (in isoform 2).
{ECO:0000303|PubMed:7588638,
ECO:0000303|PubMed:8181059,
ECO:0000303|Ref.8}.
/FTId=VSP_001739.
VARIANT 8 8 F -> S (associated with susceptibility to
HVB infection; lower cell surface levels;
lower induction of MHC class 1 expression
by INF-alpha; dbSNP:rs2229207).
{ECO:0000269|PubMed:16757563,
ECO:0000269|Ref.6}.
/FTId=VAR_020521.
VARIANT 10 10 F -> V (in dbSNP:rs1051393).
{ECO:0000269|PubMed:16757563,
ECO:0000269|PubMed:7759950,
ECO:0000269|PubMed:8181059,
ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
/FTId=VAR_020522.
VARIANT 196 196 I -> V (in dbSNP:rs17860223).
{ECO:0000269|Ref.6}.
/FTId=VAR_020523.
MUTAGEN 269 269 Y->F: Does not inhibit STAT1, STAT2 and
STAT3 activation by IFN. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-306; F-316; F-318; F-
337; F-411 and F-512. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-306; F-316; F-318; F-
411 and F-512. Does not inhibit STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-306; F-316; F-318 and
F-337. {ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
MUTAGEN 306 306 Y->F: Does not inhibit STAT1, STAT2 and
STAT3 activation by IFN. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-316; F-318; F-
337; F-411 and F-512. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-316; F-318; F-
411 and F-512. Does not inhibit STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-512. Does not inhibit
STAT1, STAT2 and STAT3 activation by IFN;
when associated with F-269; F-316; F-318
and F-337. {ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
MUTAGEN 316 316 Y->F: Does not inhibit STAT1, STAT2 and
STAT3 activation by IFN. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-318; F-
337; F-411 and F-512. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-318; F-
411 and F-512. Does not inhibit STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-512. Does not inhibit
STAT1, STAT2 and STAT3 activation by IFN;
when associated with F-269; F-306; F-318
and F-337. {ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
MUTAGEN 318 318 Y->F: Does not inhibit STAT1, STAT2 and
STAT3 activation by IFN. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-316; F-
337; F-411 and F-512. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-316; F-
411 and F-512. Does not inhibit STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-512. Does not inhibit
STAT1, STAT2 and STAT3 activation by IFN;
when associated with F-269; F-306; F-316
and F-337. {ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
MUTAGEN 337 337 Y->F: Does not inhibit STAT1, STAT2 and
STAT3 activation by IFN. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-316; F-
318; F-411 and F-512. Does not inhibit
STAT1, STAT2 and STAT3 activation by IFN;
when associated with F-512. Does not
inhibit STAT1, STAT2 and STAT3 activation
by IFN; when associated with F-269; F-
306; F-316 and F-318.
{ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
MUTAGEN 411 411 Y->F: Does not inhibit STAT1, STAT2 and
STAT3 activation by IFN. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-316; F-
318; F-337 and F-512. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-316; F-
318 and F-512. Does not inhibit STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-512.
{ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
MUTAGEN 512 512 Y->F: Does not inhibit STAT1, STAT2 and
STAT3 activation by IFN. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-316; F-
318; F-337 and F-411. Inhibits STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-269; F-306; F-316; F-
318 and F-411. Does not inhibit STAT1,
STAT2 and STAT3 activation by IFN; when
associated with F-411.
{ECO:0000269|PubMed:11682488,
ECO:0000269|PubMed:12105218}.
CONFLICT 151 151 M -> V (in Ref. 3; AAC50202).
{ECO:0000305}.
STRAND 40 46 {ECO:0000244|PDB:3S9D}.
STRAND 49 55 {ECO:0000244|PDB:3S9D}.
STRAND 59 61 {ECO:0000244|PDB:1N6U}.
STRAND 65 75 {ECO:0000244|PDB:3S9D}.
HELIX 83 85 {ECO:0000244|PDB:3S9D}.
STRAND 86 89 {ECO:0000244|PDB:3S9D}.
STRAND 91 94 {ECO:0000244|PDB:3S9D}.
TURN 96 98 {ECO:0000244|PDB:3S9D}.
STRAND 102 104 {ECO:0000244|PDB:3S9D}.
STRAND 106 113 {ECO:0000244|PDB:3S9D}.
STRAND 119 126 {ECO:0000244|PDB:3S9D}.
HELIX 128 131 {ECO:0000244|PDB:3S9D}.
STRAND 138 143 {ECO:0000244|PDB:3S9D}.
STRAND 148 153 {ECO:0000244|PDB:3S9D}.
HELIX 159 161 {ECO:0000244|PDB:1N6U}.
STRAND 167 174 {ECO:0000244|PDB:3S9D}.
STRAND 177 181 {ECO:0000244|PDB:3S9D}.
STRAND 186 188 {ECO:0000244|PDB:3S8W}.
STRAND 191 197 {ECO:0000244|PDB:3S9D}.
STRAND 205 213 {ECO:0000244|PDB:3S9D}.
STRAND 226 229 {ECO:0000244|PDB:3S9D}.
SEQUENCE 515 AA; 57759 MW; 4D7730D93AA739F4 CRC64;
MLLSQNAFIF RSLNLVLMVY ISLVFGISYD SPDYTDESCT FKISLRNFRS ILSWELKNHS
IVPTHYTLLY TIMSKPEDLK VVKNCANTTR SFCDLTDEWR STHEAYVTVL EGFSGNTTLF
SCSHNFWLAI DMSFEPPEFE IVGFTNHINV MVKFPSIVEE ELQFDLSLVI EEQSEGIVKK
HKPEIKGNMS GNFTYIIDKL IPNTNYCVSV YLEHSDEQAV IKSPLKCTLL PPGQESESAE
SAKIGGIITV FLIALVLTST IVTLKWIGYI CLRNSLPKVL NFHNFLAWPF PNLPPLEAMD
MVEVIYINRK KKVWDYNYDD ESDSDTEAAP RTSGGGYTMH GLTVRPLGQA SATSTESQLI
DPESEEEPDL PEVDVELPTM PKDSPQQLEL LSGPCERRKS PLQDPFPEED YSSTEGSGGR
ITFNVDLNSV FLRVLDDEDS DDLEAPLMLS SHLEEMVDPE DPDNVQSNHL LASGEGTQPT
FPSPSSEGLW SEDAPSDQSD TSESDVDLGD GYIMR


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