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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.
26-FEB-2020, entry version 190.
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;
Q08380:LGALS3BP; NbExp=2; IntAct=EBI-929476, EBI-354956;
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]
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; -.
SMR; P20591; -.
BioGrid; 110684; 43.
DIP; DIP-35694N; -.
IntAct; P20591; 21.
STRING; 9606.ENSP00000381601; -.
iPTMnet; P20591; -.
PhosphoSitePlus; P20591; -.
SwissPalm; P20591; -.
BioMuta; MX1; -.
DMDM; 251757499; -.
EPD; P20591; -.
jPOST; P20591; -.
MassIVE; P20591; -.
MaxQB; P20591; -.
PaxDb; P20591; -.
PeptideAtlas; P20591; -.
PRIDE; P20591; -.
ProteomicsDB; 53763; -. [P20591-1]
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; -.
GeneCards; MX1; -.
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; ENSGT00940000155686; -.
HOGENOM; CLU_008964_8_0_1; -.
InParanoid; P20591; -.
KO; K14754; -.
OMA; KATIPCL; -.
OrthoDB; 494748at2759; -.
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; -.
Pharos; P20591; Tbio.
PRO; PR:P20591; -.
Proteomes; UP000005640; Chromosome 21.
RNAct; P20591; protein.
Bgee; ENSG00000157601; Expressed in epithelium of bronchus and 222 other tissues.
ExpressionAtlas; P20591; baseline and differential.
Genevisible; P20591; HS.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
GO; GO:0044327; C:dendritic spine head; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0098844; C:postsynaptic endocytic zone membrane; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0045202; C:synapse; IBA:GO_Central.
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: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:0048285; P:organelle fission; IBA:GO_Central.
GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IBA:GO_Central.
GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
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:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IBA:GO_Central.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd08771; DLP_1; 1.
DisProt; DP01239; -.
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;
Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; GTP-binding;
Immunity; Innate immunity; Membrane; Nucleotide-binding; Nucleus;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1..662
/note="Interferon-induced GTP-binding protein Mx1"
/id="PRO_0000382943"
INIT_MET 1
/note="Removed; alternate"
/evidence="ECO:0000269|PubMed:2607176, ECO:0000269|Ref.10"
CHAIN 2..662
/note="Interferon-induced GTP-binding protein Mx1, N-
terminally processed"
/id="PRO_0000206592"
DOMAIN 67..340
/note="Dynamin-type G"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
DOMAIN 574..662
/note="GED"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
NP_BIND 77..84
/note="GTP"
/evidence="ECO:0000255"
NP_BIND 178..182
/note="GTP"
/evidence="ECO:0000255"
NP_BIND 247..250
/note="GTP"
/evidence="ECO:0000255"
REGION 77..84
/note="G1 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
REGION 102..104
/note="G2 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
REGION 178..181
/note="G3 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
REGION 247..250
/note="G4 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
REGION 279..282
/note="G5 motif"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
REGION 341..366
/note="Bundle signaling element (BSE)"
REGION 366..533
/note="Middle domain"
REGION 367..632
/note="Stalk"
REGION 554..557
/note="Critical for lipid-binding"
MOD_RES 1
/note="N-acetylmethionine; in Interferon-induced GTP-
binding protein Mx1; alternate"
/evidence="ECO:0000269|Ref.9"
VAR_SEQ 425..662
/note="GHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTV
TDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQD
QVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISS
HIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQA
RRRLAQFPG -> GGQQAHLQPHPFDHPVLHAPDVRPAASEGHAAAPAGQGHLQLAPEG
AERHQRQAEVPEGAACTADAGSAPACPVPRLTTLCPAP (in isoform 2)"
/evidence="ECO:0000303|PubMed:20603636"
/id="VSP_042904"
VARIANT 379
/note="V -> I (in dbSNP:rs469390)"
/evidence="ECO:0000269|PubMed:10830953,
ECO:0000269|PubMed:10942113, ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2154602,
ECO:0000269|PubMed:2481229"
/id="VAR_058010"
VARIANT 381
/note="A -> V (in dbSNP:rs34717738)"
/id="VAR_034116"
VARIANT 611
/note="Q -> H (in dbSNP:rs2230454)"
/id="VAR_034117"
MUTAGEN 81
/note="S->C: No effect on GTP-binding, nor on viral
infection."
/evidence="ECO:0000269|PubMed:8411374"
MUTAGEN 83
/note="K->A: Loss of GTP-binding. Loss of potentiation of
TRPC6 activity. Loss of protection against viral
infection."
/evidence="ECO:0000269|PubMed:15757897,
ECO:0000269|PubMed:8411374"
MUTAGEN 83
/note="K->M: Loss of GTP-binding. Loss of protection
against viral infection."
/evidence="ECO:0000269|PubMed:15757897,
ECO:0000269|PubMed:8411374"
MUTAGEN 103
/note="T->A: Loss of GTP-binding. Loss of potentiation of
TRPC6 activity. Loss of protection against viral
infection."
/evidence="ECO:0000269|PubMed:15757897,
ECO:0000269|PubMed:9060610"
MUTAGEN 554
/note="K->E: Strong liposome-binding reduction."
/evidence="ECO:0000269|PubMed:21900240"
MUTAGEN 555
/note="K->E: Strong liposome-binding reduction."
/evidence="ECO:0000269|PubMed:21900240"
MUTAGEN 556
/note="K->E: Strong liposome-binding reduction."
/evidence="ECO:0000269|PubMed:21900240"
MUTAGEN 557
/note="K->E: Strong liposome-binding reduction."
/evidence="ECO:0000269|PubMed:21900240"
MUTAGEN 612
/note="L->K: Loss of GTP-hydrolysis. No effect on GTP-
binding, nor on potentiation of TRPC6 activity."
/evidence="ECO:0000269|PubMed:15757897"
MUTAGEN 632
/note="E->A: Reduced antiviral activity."
/evidence="ECO:0000269|PubMed:21962493"
MUTAGEN 640
/note="R->A: Fails to sequester viral nucleoproteins, no
antiviral activity."
/evidence="ECO:0000269|PubMed:21962493"
MUTAGEN 645
/note="E->R: Loss of antiviral activity towards CCHFV and
LACV."
/evidence="ECO:0000269|PubMed:11880649,
ECO:0000269|PubMed:15047845"
CONFLICT 164
/note="L -> R (in Ref. 1; AAA36337)"
/evidence="ECO:0000305"
CONFLICT 250
/note="D -> G (in Ref. 4; BAG53272)"
/evidence="ECO:0000305"
CONFLICT 297
/note="Q -> H (in Ref. 4; BAG37852)"
/evidence="ECO:0000305"
CONFLICT 299
/note="E -> G (in Ref. 4; BAG53272)"
/evidence="ECO:0000305"
CONFLICT 582
/note="M -> I (in Ref. 4; BAG37852)"
/evidence="ECO:0000305"
TURN 47..49
/evidence="ECO:0000244|PDB:4P4U"
HELIX 50..61
/evidence="ECO:0000244|PDB:4P4U"
HELIX 64..66
/evidence="ECO:0000244|PDB:4P4U"
STRAND 72..78
/evidence="ECO:0000244|PDB:4P4U"
HELIX 83..91
/evidence="ECO:0000244|PDB:4P4U"
STRAND 99..101
/evidence="ECO:0000244|PDB:4P4S"
STRAND 107..113
/evidence="ECO:0000244|PDB:4P4U"
STRAND 115..117
/evidence="ECO:0000244|PDB:4P4S"
STRAND 121..126
/evidence="ECO:0000244|PDB:4P4U"
STRAND 129..133
/evidence="ECO:0000244|PDB:4P4U"
HELIX 136..138
/evidence="ECO:0000244|PDB:4P4U"
HELIX 139..150
/evidence="ECO:0000244|PDB:4P4U"
STRAND 153..155
/evidence="ECO:0000244|PDB:4P4S"
STRAND 162..168
/evidence="ECO:0000244|PDB:4P4U"
STRAND 173..178
/evidence="ECO:0000244|PDB:4P4U"
HELIX 194..206
/evidence="ECO:0000244|PDB:4P4U"
STRAND 208..210
/evidence="ECO:0000244|PDB:3SZR"
STRAND 211..218
/evidence="ECO:0000244|PDB:4P4U"
HELIX 223..225
/evidence="ECO:0000244|PDB:4P4U"
HELIX 227..235
/evidence="ECO:0000244|PDB:4P4U"
STRAND 240..247
/evidence="ECO:0000244|PDB:4P4U"
HELIX 249..251
/evidence="ECO:0000244|PDB:4P4U"
STRAND 252..256
/evidence="ECO:0000244|PDB:3SZR"
HELIX 257..264
/evidence="ECO:0000244|PDB:4P4U"
STRAND 267..269
/evidence="ECO:0000244|PDB:4P4U"
STRAND 275..277
/evidence="ECO:0000244|PDB:4P4U"
HELIX 283..287
/evidence="ECO:0000244|PDB:4P4U"
HELIX 292..304
/evidence="ECO:0000244|PDB:4P4U"
TURN 307..309
/evidence="ECO:0000244|PDB:4P4U"
HELIX 310..314
/evidence="ECO:0000244|PDB:4P4U"
HELIX 320..338
/evidence="ECO:0000244|PDB:4P4U"
TURN 339..341
/evidence="ECO:0000244|PDB:4P4U"
HELIX 342..358
/evidence="ECO:0000244|PDB:4P4U"
HELIX 367..390
/evidence="ECO:0000244|PDB:4P4U"
HELIX 403..437
/evidence="ECO:0000244|PDB:3LJB"
STRAND 444..446
/evidence="ECO:0000244|PDB:3SZR"
HELIX 451..463
/evidence="ECO:0000244|PDB:3LJB"
HELIX 466..492
/evidence="ECO:0000244|PDB:3LJB"
STRAND 493..495
/evidence="ECO:0000244|PDB:5GTM"
HELIX 496..528
/evidence="ECO:0000244|PDB:3LJB"
HELIX 574..604
/evidence="ECO:0000244|PDB:3LJB"
HELIX 606..618
/evidence="ECO:0000244|PDB:3LJB"
HELIX 623..625
/evidence="ECO:0000244|PDB:3LJB"
HELIX 626..629
/evidence="ECO:0000244|PDB:3LJB"
HELIX 634..659
/evidence="ECO:0000244|PDB:5GTM"
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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WP1673: Naphthalene and anthracene degradation
WP2203: TSLP Signaling Pathway
WP1502: Mitochondrial biogenesis
WP1613: 1,4-Dichlorobenzene degradation
WP1888: Post-translational protein modification
WP1678: Nucleotide excision repair
WP1690: Propanoate metabolism
WP2324: AGE/RAGE pathway

Related Genes :
[MX1] 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] Interferon-induced GTP-binding protein Mx1 (Interferon-regulated resistance GTP-binding protein MxA) (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[Mx1] Interferon-induced GTP-binding protein Mx1 (Influenza resistance protein) (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[Mx1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX2] Interferon-induced GTP-binding protein Mx2 (Interferon-regulated resistance GTP-binding protein MxB) (Myxovirus resistance protein 2) (p78-related protein)
[MX1 MX] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1) (Oligodendrocyte GTP-binding protein)
[Mx2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[MX1] Interferon-induced GTP-binding protein Mx1
[MX2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[Mx2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[MX2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[MX2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[MX1 MX] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1 MX] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1 MX] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[MX1] Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1)
[ISG15 G1P2 UCRP] Ubiquitin-like protein ISG15 (Interferon-induced 15 kDa protein) (Interferon-induced 17 kDa protein) (IP17) (Ubiquitin cross-reactive protein) (hUCRP)
[mxa] Interferon-induced GTP-binding protein MxA (IFN-inducible antiviral protein MxA) (Interferon-inducible MxA protein)
[MX] Interferon-induced GTP-binding protein Mx (Interferon-inducible Mx protein)
[Mx3] Interferon-induced GTP-binding protein Mx3 (Myxovirus resistance protein 3)
[MX2] Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2)
[IFITM1 CD225 IFI17] Interferon-induced transmembrane protein 1 (Dispanin subfamily A member 2a) (DSPA2a) (Interferon-induced protein 17) (Interferon-inducible protein 9-27) (Leu-13 antigen) (CD antigen CD225)
[IFIT1 G10P1 IFI56 IFNAI1 ISG56] Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Interferon-induced 56 kDa protein) (IFI-56K) (P56)
[IFI27] Interferon alpha-inducible protein 27, mitochondrial (p27) (Interferon alpha-induced 11.5 kDa protein) (Interferon-stimulated gene 12a protein) (ISG12(a)) (ISG12A)
[Ifit1 Garg16 Ifi56 Isg56] Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Glucocorticoid-attenuated response gene 16 protein) (GARG-16) (Interferon-induced 56 kDa protein) (IFI-56K) (P56)
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)

Bibliography :