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Interferon-induced GTP-binding protein Mx1 (Interferon-induced protein p78) (IFI-78K) (Interferon-regulated resistance GTP-binding protein MxA) (Myxoma resistance protein 1) (Myxovirus resistance protein 1) [Cleaved into: Interferon-induced GTP-binding protein Mx1, N-terminally processed]

 MX1_HUMAN               Reviewed;         662 AA.
P20591; B2RDA5; B3KU10; C9IYV7; C9J8D6; C9JN19; C9JN88; C9JUL1;
C9JZS6; D3DSI8; Q86YP5; Q96CI3;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 4.
20-JUN-2018, entry version 174.
RecName: Full=Interferon-induced GTP-binding protein Mx1;
AltName: Full=Interferon-induced protein p78;
Short=IFI-78K;
AltName: Full=Interferon-regulated resistance GTP-binding protein MxA;
AltName: Full=Myxoma resistance protein 1;
AltName: Full=Myxovirus resistance protein 1;
Contains:
RecName: Full=Interferon-induced GTP-binding protein Mx1, N-terminally processed;
Name=MX1;
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 1), AND VARIANT ILE-379.
PubMed=2481229; DOI=10.1128/MCB.9.11.5062;
Aebi M., Faeh J., Hurt N., Samuel C.E., Thomis D., Bazzigher L.,
Pavlovic J., Haller O., Staeheli P.;
"cDNA structures and regulation of two interferon-induced human Mx
proteins.";
Mol. Cell. Biol. 9:5062-5072(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-379.
PubMed=2154602;
Horisberger M.A., McMaster G.K., Zeller H., Wathelet M.G., Dellis J.,
Content J.;
"Cloning and sequence analyses of cDNAs for interferon- and virus-
induced human Mx proteins reveal that they contain putative guanine
nucleotide-binding sites: functional study of the corresponding gene
promoter.";
J. Virol. 64:1171-1181(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-379, AND POSSIBLE
INVOLVEMENT IN ALLOPECIA AREATA.
PubMed=10942113; DOI=10.1007/s004390000318;
Tazi-Ahnini R., di Giovine F.S., McDonagh A.J., Messenger A.G.,
Amadou C., Cox A., Duff G.W., Cork M.J.;
"Structure and polymorphism of the human gene for the interferon-
induced p78 protein (MX1): evidence of association with alopecia
areata in the Down syndrome region.";
Hum. Genet. 106:639-645(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2),
SUBCELLULAR LOCATION (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=20603636; DOI=10.1038/icb.2010.83;
Ku C.C., Che X.B., Reichelt M., Rajamani J., Schaap-Nutt A.,
Huang K.J., Sommer M.H., Chen Y.S., Chen Y.Y., Arvin A.M.;
"Herpes simplex virus-1 induces expression of a novel MxA isoform that
enhances viral replication.";
Immunol. Cell Biol. 89:173-182(2011).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-379.
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], AND VARIANT ILE-379.
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).
[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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-379.
TISSUE=B-cell, and Uterus;
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).
[9]
PROTEIN SEQUENCE OF 1-10; 84-97 AND 442-481, ACETYLATION AT MET-1, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Prostatic carcinoma;
Bienvenut W.V., Gao M., Leug H.;
Submitted (JUL-2009) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 2-57, AND NUCLEOTIDE SEQUENCE OF 2-124.
Horisberger M.A., Hochkeppel H.K., Content J.;
"Interferon-induced human protein in pure form, monoclonal antibodies
thereto, and test kits containing these antibodies.";
Patent number EP0242329, 21-OCT-1987.
[11]
PROTEIN SEQUENCE OF 2-26.
PubMed=2607176; DOI=10.1089/jir.1989.9.679;
Weitz G., Bekisz J., Zoon K., Arnheiter H.;
"Purification and characterization of a human Mx protein.";
J. Interferon Res. 9:679-689(1989).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 486-569.
Narayan K., Pachner A.R.;
"Inf-induced gene expression analysis in MS patients: Loss of
bioavailability can be caused by either binding or neutralizing
antibodies.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[13]
RESISTANCE TO INFLUENZA VIRUS AND VSV.
PubMed=2161946;
Pavlovic J., Zuercher T., Haller O., Staeheli P.;
"Resistance to influenza virus and vesicular stomatitis virus
conferred by expression of human MxA protein.";
J. Virol. 64:3370-3375(1990).
[14]
MUTAGENESIS OF SER-81 AND LYS-83.
PubMed=8411374;
Pitossi F., Blank A., Schroeder A., Schwarz A., Huessi P.,
Schwemmle M., Pavlovic J., Staeheli P.;
"A functional GTP-binding motif is necessary for antiviral activity of
Mx proteins.";
J. Virol. 67:6726-6732(1993).
[15]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-103.
PubMed=9060610;
Ponten A., Sick C., Weeber M., Haller O., Kochs G.;
"Dominant-negative mutants of human MxA protein: domains in the
carboxy-terminal moiety are important for oligomerization and
antiviral activity.";
J. Virol. 71:2591-2599(1997).
[16]
INTERACTION WITH THOV NUCLEOPROTEIN.
PubMed=9933640; DOI=10.1074/jbc.274.7.4370;
Kochs G., Haller O.;
"GTP-bound human MxA protein interacts with the nucleocapsids of
Thogoto virus (Orthomyxoviridae).";
J. Biol. Chem. 274:4370-4376(1999).
[17]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LACV PROTEIN N, AND
MUTAGENESIS OF GLU-645.
PubMed=11880649; DOI=10.1073/pnas.052430399;
Kochs G., Janzen C., Hohenberg H., Haller O.;
"Antivirally active MxA protein sequesters La Crosse virus
nucleocapsid protein into perinuclear complexes.";
Proc. Natl. Acad. Sci. U.S.A. 99:3153-3158(2002).
[18]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCHFV PROTEIN N, AND
MUTAGENESIS OF GLU-645.
PubMed=15047845; DOI=10.1128/JVI.78.8.4323-4329.2004;
Andersson I., Bladh L., Mousavi-Jazi M., Magnusson K.E., Lundkvist A.,
Haller O., Mirazimi A.;
"Human MxA protein inhibits the replication of Crimean-Congo
hemorrhagic fever virus.";
J. Virol. 78:4323-4329(2004).
[19]
FUNCTION.
PubMed=14752052; DOI=10.1093/nar/gkh192;
Turan K., Mibayashi M., Sugiyama K., Saito S., Numajiri A., Nagata K.;
"Nuclear MxA proteins form a complex with influenza virus NP and
inhibit the transcription of the engineered influenza virus genome.";
Nucleic Acids Res. 32:643-652(2004).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15355513; DOI=10.1111/j.1600-0854.2004.00219.x;
Reichelt M., Stertz S., Krijnse-Locker J., Haller O., Kochs G.;
"Missorting of LaCrosse virus nucleocapsid protein by the interferon-
induced MxA GTPase involves smooth ER membranes.";
Traffic 5:772-784(2004).
[21]
FUNCTION.
PubMed=14687945; DOI=10.1016/j.virusres.2003.10.002;
Bridgen A., Dalrymple D.A., Weber F., Elliott R.M.;
"Inhibition of Dugbe nairovirus replication by human MxA protein.";
Virus Res. 99:47-50(2004).
[22]
FUNCTION, INTERACTION WITH TRPC1; TRPC3; TRPC4; TRPC5; TRPC6 AND
TRPC7, AND MUTAGENESIS OF LYS-83; THR-103 AND LEU-612.
PubMed=15757897; DOI=10.1074/jbc.M500391200;
Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
St-Hilaire M., Pinard M., Boulay G.;
"MxA, a member of the dynamin superfamily, interacts with the ankyrin-
like repeat domain of TRPC.";
J. Biol. Chem. 280:19393-19400(2005).
[23]
FUNCTION, SUBCELLULAR LOCATION, OLIGOMERIZATION, AND INTERACTION WITH
LACV PROTEIN N.
PubMed=16413306; DOI=10.1016/S0076-6879(05)04055-3;
Kochs G., Reichelt M., Danino D., Hinshaw J.E., Haller O.;
"Assay and functional analysis of dynamin-like Mx proteins.";
Methods Enzymol. 404:632-643(2005).
[24]
ISGYLATION.
PubMed=16009940; DOI=10.1073/pnas.0504754102;
Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.;
"Human ISG15 conjugation targets both IFN-induced and constitutively
expressed proteins functioning in diverse cellular pathways.";
Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005).
[25]
SUBCELLULAR LOCATION.
PubMed=16978069; DOI=10.1089/jir.2006.26.650;
Stertz S., Reichelt M., Krijnse-Locker J., Mackenzie J., Simpson J.C.,
Haller O., Kochs G.;
"Interferon-induced, antiviral human MxA protein localizes to a
distinct subcompartment of the smooth endoplasmic reticulum.";
J. Interferon Cytokine Res. 26:650-660(2006).
[26]
FUNCTION.
PubMed=16202617; DOI=10.1016/j.nbd.2005.08.015;
Leroy M., Pire G., Baise E., Desmecht D.;
"Expression of the interferon-alpha/beta-inducible bovine Mx1 dynamin
interferes with replication of rabies virus.";
Neurobiol. Dis. 21:515-521(2006).
[27]
FUNCTION.
PubMed=17374778; DOI=10.1099/vir.0.82526-0;
Mundt E.;
"Human MxA protein confers resistance to double-stranded RNA viruses
of two virus families.";
J. Gen. Virol. 88:1319-1323(2007).
[28]
REVIEW, AND INDUCTION.
PubMed=18062906; DOI=10.1016/j.micinf.2007.09.010;
Haller O., Stertz S., Kochs G.;
"The Mx GTPase family of interferon-induced antiviral proteins.";
Microbes Infect. 9:1636-1643(2007).
[29]
FUNCTION.
PubMed=18668195; DOI=10.1007/s00705-008-0168-9;
Yu Z., Wang Z., Chen J., Li H., Lin Z., Zhang F., Zhou Y., Hou J.;
"GTPase activity is not essential for the interferon-inducible MxA
protein to inhibit the replication of hepatitis B virus.";
Arch. Virol. 153:1677-1684(2008).
[30]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19109387; DOI=10.1128/JVI.00781-08;
Netherton C.L., Simpson J., Haller O., Wileman T.E., Takamatsu H.H.,
Monaghan P., Taylor G.;
"Inhibition of a large double-stranded DNA virus by MxA protein.";
J. Virol. 83:2310-2320(2009).
[31]
REVIEW ON STRUCTURE, DOMAIN GED, AND DOMAIN MIDDLE.
PubMed=20538602; DOI=10.1074/jbc.R110.145839;
Haller O., Gao S., von der Malsburg A., Daumke O., Kochs G.;
"Dynamin-like MxA GTPase: structural insights into oligomerization and
implications for antiviral activity.";
J. Biol. Chem. 285:28419-28424(2010).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[33]
SUBCELLULAR LOCATION, AND INTERACTION WITH DDX39A AND DDX39B.
PubMed=21859714; DOI=10.1074/jbc.M111.251843;
Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E.,
Pavlovic J.;
"Interferon-induced antiviral protein MxA interacts with the cellular
RNA helicases UAP56 and URH49.";
J. Biol. Chem. 286:34743-34751(2011).
[34]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-554;
LYS-555; LYS-556 AND LYS-557.
PubMed=21900240; DOI=10.1074/jbc.M111.249037;
von der Malsburg A., Abutbul-Ionita I., Haller O., Kochs G.,
Danino D.;
"Stalk domain of the dynamin-like MxA GTPase protein mediates membrane
binding and liposome tubulation via the unstructured L4 loop.";
J. Biol. Chem. 286:37858-37865(2011).
[35]
REVIEW.
PubMed=21166595; DOI=10.1089/jir.2010.0076;
Haller O., Kochs G.;
"Human MxA protein: an interferon-induced dynamin-like GTPase with
broad antiviral activity.";
J. Interferon Cytokine Res. 31:79-87(2011).
[36]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HSPA5.
PubMed=21992152; DOI=10.1089/jir.2010.0132;
Numajiri Haruki A., Naito T., Nishie T., Saito S., Nagata K.;
"Interferon-inducible antiviral protein MxA enhances cell death
triggered by endoplasmic reticulum stress.";
J. Interferon Cytokine Res. 31:847-856(2011).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[38]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 366-636, AND SUBUNIT.
PubMed=20428112; DOI=10.1038/nature08972;
Gao S., von der Malsburg A., Paeschke S., Behlke J., Haller O.,
Kochs G., Daumke O.;
"Structural basis of oligomerization in the stalk region of dynamin-
like MxA.";
Nature 465:502-506(2010).
[39]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 33-662, SUBUNIT, AND
MUTAGENESIS OF GLU-632 AND ARG-640.
PubMed=21962493; DOI=10.1016/j.immuni.2011.07.012;
Gao S., von der Malsburg A., Dick A., Faelber K., Schroder G.F.,
Haller O., Kochs G., Daumke O.;
"Structure of myxovirus resistance protein a reveals intra- and
intermolecular domain interactions required for the antiviral
function.";
Immunity 35:514-525(2011).
-!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
activity against a wide range of RNA viruses and some DNA viruses.
Its target viruses include negative-stranded RNA viruses and HBV
through binding and inactivation of their ribonucleocapsid. May
also antagonize reoviridae and asfarviridae replication. Inhibits
thogoto virus (THOV) replication by preventing the nuclear import
of viral nucleocapsids. Inhibits La Crosse virus (LACV)
replication by sequestering viral nucleoprotein in perinuclear
complexes, preventing genome amplification, budding, and egress.
Inhibits influenza A virus (IAV) replication by decreasing or
delaying NP synthesis and by blocking endocytic traffic of
incoming virus particles. Enhances ER stress-mediated cell death
after influenza virus infection. May regulate the calcium channel
activity of TRPCs. {ECO:0000269|PubMed:11880649,
ECO:0000269|PubMed:14687945, ECO:0000269|PubMed:14752052,
ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:15355513,
ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16202617,
ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:17374778,
ECO:0000269|PubMed:18668195, ECO:0000269|PubMed:19109387,
ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21992152}.
-!- SUBUNIT: Homotetramer. Oligomerizes into multimeric filamentous or
ring-like structures by virtue of its stalk domain.
Oligomerization is critical for GTPase activity, protein
stability, and recognition of viral target structures. Interacts
with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7. Interacts with
HSPA5. Interacts with DDX39A and DDX39B. Interacts with TUBB/TUBB5
(By similarity). The GTP-bound form interacts (via C-terminus)
with THOV P5 protein. The GTP-bound form interacts with LACV
protein N. Interacts with CCHFV protein N. {ECO:0000250,
ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:15047845,
ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16413306,
ECO:0000269|PubMed:20428112, ECO:0000269|PubMed:21859714,
ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21962493,
ECO:0000269|PubMed:21992152, ECO:0000269|PubMed:9933640}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-929476, EBI-929476;
Q9H9S4:CAB39L; NbExp=3; IntAct=EBI-929476, EBI-1047244;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-929476, EBI-747107;
Q13507:TRPC3; NbExp=2; IntAct=EBI-929476, EBI-520807;
Q9UBN4:TRPC4; NbExp=2; IntAct=EBI-929476, EBI-929504;
Q9Y210:TRPC6; NbExp=4; IntAct=EBI-929476, EBI-929362;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11880649,
ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:21992152,
ECO:0000269|PubMed:9060610}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:16413306,
ECO:0000269|PubMed:21992152}; Peripheral membrane protein
{ECO:0000269|PubMed:16413306}; Cytoplasmic side. Cytoplasm,
perinuclear region {ECO:0000269|PubMed:15047845}. Note=Binds
preferentially to negatively charged phospholipids
(PubMed:21900240). Colocalizes with CCHFV protein N in the
perinuclear region (PubMed:15047845).
{ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:21900240}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:20603636}. Nucleus
{ECO:0000269|PubMed:20603636}. Note=Translocates into the nuclei
of HSV-1 infected cells (PubMed:20603636).
{ECO:0000269|PubMed:20603636}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P20591-1; Sequence=Displayed;
Name=2; Synonyms=56-kda, varMxA;
IsoId=P20591-2; Sequence=VSP_042904;
-!- INDUCTION: By type I and type III interferons. Isoform 2 is
induced by HSV-1. {ECO:0000269|PubMed:18062906}.
-!- DOMAIN: The C-terminal GTPase effector domain (GED) is involved in
oligomerization and viral target recognition.
{ECO:0000269|PubMed:20538602}.
-!- DOMAIN: The middle domain mediates self-assembly and
oligomerization. {ECO:0000269|PubMed:20538602}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16009940}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
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EMBL; M30817; AAA36337.1; -; mRNA.
EMBL; M33882; AAA36458.1; -; mRNA.
EMBL; AF135187; AAD43063.1; -; Genomic_DNA.
EMBL; AK096355; BAG53272.1; -; mRNA.
EMBL; AK315465; BAG37852.1; -; mRNA.
EMBL; AL163285; CAB90556.1; -; Genomic_DNA.
EMBL; AL773577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL773578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09600.1; -; Genomic_DNA.
EMBL; CH471079; EAX09601.1; -; Genomic_DNA.
EMBL; CH471079; EAX09602.1; -; Genomic_DNA.
EMBL; CH471079; EAX09603.1; -; Genomic_DNA.
EMBL; CH471079; EAX09604.1; -; Genomic_DNA.
EMBL; BC014222; AAH14222.2; -; mRNA.
EMBL; BC032602; AAH32602.1; -; mRNA.
EMBL; AY186254; AAO31807.1; -; mRNA.
CCDS; CCDS13673.1; -. [P20591-1]
CCDS; CCDS74796.1; -. [P20591-2]
PIR; A33481; A33481.
RefSeq; NP_001138397.1; NM_001144925.2. [P20591-1]
RefSeq; NP_001171517.1; NM_001178046.2. [P20591-1]
RefSeq; NP_001269849.1; NM_001282920.1. [P20591-2]
RefSeq; NP_002453.2; NM_002462.4. [P20591-1]
RefSeq; XP_005261035.1; XM_005260978.4. [P20591-1]
RefSeq; XP_005261036.1; XM_005260979.2. [P20591-1]
RefSeq; XP_005261037.1; XM_005260980.2. [P20591-1]
RefSeq; XP_005261038.1; XM_005260981.2. [P20591-1]
RefSeq; XP_005261039.1; XM_005260982.2. [P20591-1]
RefSeq; XP_011527870.1; XM_011529568.2. [P20591-1]
RefSeq; XP_016883838.1; XM_017028349.1. [P20591-1]
RefSeq; XP_016883839.1; XM_017028350.1. [P20591-1]
UniGene; Hs.517307; -.
PDB; 3LJB; X-ray; 2.40 A; A/B=366-636.
PDB; 3SZR; X-ray; 3.50 A; A=33-662.
PDB; 3ZYS; EM; 12.20 A; B/E=1-662.
PDB; 4P4S; X-ray; 3.30 A; A=70-342, B=43-662.
PDB; 4P4T; X-ray; 2.30 A; A=37-366, A=637-662.
PDB; 4P4U; X-ray; 1.90 A; A=37-364, A=632-661.
PDB; 5GTM; X-ray; 2.90 A; A/B=33-662.
PDBsum; 3LJB; -.
PDBsum; 3SZR; -.
PDBsum; 3ZYS; -.
PDBsum; 4P4S; -.
PDBsum; 4P4T; -.
PDBsum; 4P4U; -.
PDBsum; 5GTM; -.
ProteinModelPortal; P20591; -.
SMR; P20591; -.
BioGrid; 110684; 39.
DIP; DIP-35694N; -.
IntAct; P20591; 15.
STRING; 9606.ENSP00000381599; -.
iPTMnet; P20591; -.
PhosphoSitePlus; P20591; -.
BioMuta; MX1; -.
DMDM; 251757499; -.
EPD; P20591; -.
MaxQB; P20591; -.
PaxDb; P20591; -.
PeptideAtlas; P20591; -.
PRIDE; P20591; -.
ProteomicsDB; 53763; -.
ProteomicsDB; 53764; -. [P20591-2]
DNASU; 4599; -.
Ensembl; ENST00000398598; ENSP00000381599; ENSG00000157601. [P20591-1]
Ensembl; ENST00000398600; ENSP00000381601; ENSG00000157601. [P20591-1]
Ensembl; ENST00000455164; ENSP00000410523; ENSG00000157601. [P20591-1]
Ensembl; ENST00000619682; ENSP00000478441; ENSG00000157601. [P20591-2]
GeneID; 4599; -.
KEGG; hsa:4599; -.
UCSC; uc002yzh.5; human. [P20591-1]
CTD; 4599; -.
DisGeNET; 4599; -.
EuPathDB; HostDB:ENSG00000157601.13; -.
GeneCards; MX1; -.
H-InvDB; HIX0027784; -.
HGNC; HGNC:7532; MX1.
HPA; HPA030917; -.
HPA; HPA030918; -.
HPA; HPA049724; -.
MIM; 147150; gene.
neXtProt; NX_P20591; -.
OpenTargets; ENSG00000157601; -.
PharmGKB; PA31333; -.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000213785; -.
HOVERGEN; HBG008788; -.
InParanoid; P20591; -.
KO; K14754; -.
OMA; AVDMLHT; -.
OrthoDB; EOG091G080G; -.
PhylomeDB; P20591; -.
TreeFam; TF331484; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
SIGNOR; P20591; -.
ChiTaRS; MX1; human.
EvolutionaryTrace; P20591; -.
GeneWiki; MX1; -.
GenomeRNAi; 4599; -.
PRO; PR:P20591; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000157601; -.
CleanEx; HS_MX1; -.
ExpressionAtlas; P20591; baseline and differential.
Genevisible; P20591; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; TAS:ProtInc.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0006952; P:defense response; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0034340; P:response to type I interferon; TAS:UniProtKB.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd08771; DLP_1; 1.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Direct protein sequencing;
Endoplasmic reticulum; GTP-binding; Immunity; Innate immunity;
Membrane; Nucleotide-binding; Nucleus; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 662 Interferon-induced GTP-binding protein
Mx1.
/FTId=PRO_0000382943.
INIT_MET 1 1 Removed; alternate.
{ECO:0000269|PubMed:2607176,
ECO:0000269|Ref.10}.
CHAIN 2 662 Interferon-induced GTP-binding protein
Mx1, N-terminally processed.
/FTId=PRO_0000206592.
DOMAIN 67 340 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
DOMAIN 574 662 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 77 84 GTP. {ECO:0000255}.
NP_BIND 178 182 GTP. {ECO:0000255}.
NP_BIND 247 250 GTP. {ECO:0000255}.
REGION 77 84 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 102 104 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 178 181 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 247 250 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 279 282 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 341 366 Bundle signaling element (BSE).
REGION 366 533 Middle domain.
REGION 367 632 Stalk.
REGION 554 557 Critical for lipid-binding.
MOD_RES 1 1 N-acetylmethionine; in Interferon-induced
GTP-binding protein Mx1; alternate.
{ECO:0000269|Ref.9}.
VAR_SEQ 425 662 GHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKAL
EEPAVDMLHTVTDMVRLAFTDVSIKNFEEFFNLHRTAKSKI
EDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVRE
KELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEA
SKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWL
LKERSDTSDKRKFLKERLARLTQARRRLAQFPG -> GGQQ
AHLQPHPFDHPVLHAPDVRPAASEGHAAAPAGQGHLQLAPE
GAERHQRQAEVPEGAACTADAGSAPACPVPRLTTLCPAP
(in isoform 2).
{ECO:0000303|PubMed:20603636}.
/FTId=VSP_042904.
VARIANT 379 379 V -> I (in dbSNP:rs469390).
{ECO:0000269|PubMed:10830953,
ECO:0000269|PubMed:10942113,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2154602,
ECO:0000269|PubMed:2481229}.
/FTId=VAR_058010.
VARIANT 381 381 A -> V (in dbSNP:rs34717738).
/FTId=VAR_034116.
VARIANT 611 611 Q -> H (in dbSNP:rs2230454).
/FTId=VAR_034117.
MUTAGEN 81 81 S->C: No effect on GTP-binding, nor on
viral infection.
{ECO:0000269|PubMed:8411374}.
MUTAGEN 83 83 K->A: Loss of GTP-binding. Loss of
potentiation of TRPC6 activity. Loss of
protection against viral infection.
{ECO:0000269|PubMed:15757897,
ECO:0000269|PubMed:8411374}.
MUTAGEN 83 83 K->M: Loss of GTP-binding. Loss of
protection against viral infection.
{ECO:0000269|PubMed:15757897,
ECO:0000269|PubMed:8411374}.
MUTAGEN 103 103 T->A: Loss of GTP-binding. Loss of
potentiation of TRPC6 activity. Loss of
protection against viral infection.
{ECO:0000269|PubMed:15757897,
ECO:0000269|PubMed:9060610}.
MUTAGEN 554 554 K->E: Strong liposome-binding reduction.
{ECO:0000269|PubMed:21900240}.
MUTAGEN 555 555 K->E: Strong liposome-binding reduction.
{ECO:0000269|PubMed:21900240}.
MUTAGEN 556 556 K->E: Strong liposome-binding reduction.
{ECO:0000269|PubMed:21900240}.
MUTAGEN 557 557 K->E: Strong liposome-binding reduction.
{ECO:0000269|PubMed:21900240}.
MUTAGEN 612 612 L->K: Loss of GTP-hydrolysis. No effect
on GTP-binding, nor on potentiation of
TRPC6 activity.
{ECO:0000269|PubMed:15757897}.
MUTAGEN 632 632 E->A: Reduced antiviral activity.
{ECO:0000269|PubMed:21962493}.
MUTAGEN 640 640 R->A: Fails to sequester viral
nucleoproteins, no antiviral activity.
{ECO:0000269|PubMed:21962493}.
MUTAGEN 645 645 E->R: Loss of antiviral activity towards
CCHFV and LACV.
{ECO:0000269|PubMed:11880649,
ECO:0000269|PubMed:15047845}.
CONFLICT 164 164 L -> R (in Ref. 1; AAA36337).
{ECO:0000305}.
CONFLICT 250 250 D -> G (in Ref. 4; BAG53272).
{ECO:0000305}.
CONFLICT 297 297 Q -> H (in Ref. 4; BAG37852).
{ECO:0000305}.
CONFLICT 299 299 E -> G (in Ref. 4; BAG53272).
{ECO:0000305}.
CONFLICT 582 582 M -> I (in Ref. 4; BAG37852).
{ECO:0000305}.
TURN 47 49 {ECO:0000244|PDB:4P4U}.
HELIX 50 61 {ECO:0000244|PDB:4P4U}.
HELIX 64 66 {ECO:0000244|PDB:4P4U}.
STRAND 72 78 {ECO:0000244|PDB:4P4U}.
HELIX 83 91 {ECO:0000244|PDB:4P4U}.
STRAND 99 101 {ECO:0000244|PDB:4P4S}.
STRAND 107 113 {ECO:0000244|PDB:4P4U}.
STRAND 115 117 {ECO:0000244|PDB:4P4S}.
STRAND 121 126 {ECO:0000244|PDB:4P4U}.
STRAND 129 133 {ECO:0000244|PDB:4P4U}.
HELIX 136 138 {ECO:0000244|PDB:4P4U}.
HELIX 139 150 {ECO:0000244|PDB:4P4U}.
STRAND 153 155 {ECO:0000244|PDB:4P4S}.
STRAND 162 168 {ECO:0000244|PDB:4P4U}.
STRAND 173 178 {ECO:0000244|PDB:4P4U}.
HELIX 195 206 {ECO:0000244|PDB:5GTM}.
STRAND 208 210 {ECO:0000244|PDB:3SZR}.
STRAND 211 218 {ECO:0000244|PDB:5GTM}.
TURN 223 225 {ECO:0000244|PDB:5GTM}.
HELIX 227 235 {ECO:0000244|PDB:5GTM}.
STRAND 239 247 {ECO:0000244|PDB:5GTM}.
HELIX 249 251 {ECO:0000244|PDB:4P4S}.
STRAND 252 256 {ECO:0000244|PDB:3SZR}.
HELIX 257 264 {ECO:0000244|PDB:5GTM}.
STRAND 275 277 {ECO:0000244|PDB:5GTM}.
HELIX 283 288 {ECO:0000244|PDB:5GTM}.
HELIX 292 305 {ECO:0000244|PDB:5GTM}.
TURN 307 309 {ECO:0000244|PDB:5GTM}.
HELIX 310 314 {ECO:0000244|PDB:5GTM}.
HELIX 320 358 {ECO:0000244|PDB:5GTM}.
HELIX 367 390 {ECO:0000244|PDB:3LJB}.
HELIX 403 437 {ECO:0000244|PDB:3LJB}.
STRAND 444 446 {ECO:0000244|PDB:3SZR}.
HELIX 449 452 {ECO:0000244|PDB:4P4U}.
HELIX 454 462 {ECO:0000244|PDB:4P4U}.
HELIX 463 465 {ECO:0000244|PDB:3SZR}.
STRAND 467 474 {ECO:0000244|PDB:4P4U}.
HELIX 479 481 {ECO:0000244|PDB:4P4U}.
HELIX 483 490 {ECO:0000244|PDB:4P4U}.
STRAND 495 502 {ECO:0000244|PDB:4P4U}.
HELIX 504 506 {ECO:0000244|PDB:4P4U}.
HELIX 513 520 {ECO:0000244|PDB:4P4U}.
STRAND 523 525 {ECO:0000244|PDB:4P4U}.
HELIX 543 546 {ECO:0000244|PDB:4P4U}.
HELIX 551 561 {ECO:0000244|PDB:4P4U}.
HELIX 564 566 {ECO:0000244|PDB:4P4T}.
TURN 568 570 {ECO:0000244|PDB:4P4U}.
HELIX 571 575 {ECO:0000244|PDB:4P4U}.
HELIX 581 596 {ECO:0000244|PDB:4P4U}.
HELIX 599 601 {ECO:0000244|PDB:4P4U}.
TURN 602 604 {ECO:0000244|PDB:4P4U}.
HELIX 605 621 {ECO:0000244|PDB:4P4U}.
HELIX 623 625 {ECO:0000244|PDB:3LJB}.
HELIX 626 629 {ECO:0000244|PDB:3LJB}.
HELIX 635 658 {ECO:0000244|PDB:4P4U}.
TURN 659 661 {ECO:0000244|PDB:4P4U}.
SEQUENCE 662 AA; 75520 MW; 626A7DD946F89384 CRC64;
MVVSEVDIAK ADPAAASHPL LLNGDATVAQ KNPGSVAENN LCSQYEEKVR PCIDLIDSLR
ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKKLVNEDKW
RGKVSYQDYE IEISDASEVE KEINKAQNAI AGEGMGISHE LITLEISSRD VPDLTLIDLP
GITRVAVGNQ PADIGYKIKT LIKKYIQRQE TISLVVVPSN VDIATTEALS MAQEVDPEGD
RTIGILTKPD LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK
IFFENHPYFR DLLEEGKATV PCLAEKLTSE LITHICKSLP LLENQIKETH QRITEELQKY
GVDIPEDENE KMFFLIDKVN AFNQDITALM QGEETVGEED IRLFTRLRHE FHKWSTIIEN
NFQEGHKILS RKIQKFENQY RGRELPGFVN YRTFETIVKQ QIKALEEPAV DMLHTVTDMV
RLAFTDVSIK NFEEFFNLHR TAKSKIEDIR AEQEREGEKL IRLHFQMEQI VYCQDQVYRG
ALQKVREKEL EEEKKKKSWD FGAFQSSSAT DSSMEEIFQH LMAYHQEASK RISSHIPLII
QFFMLQTYGQ QLQKAMLQLL QDKDTYSWLL KERSDTSDKR KFLKERLARL TQARRRLAQF
PG


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