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P20591 (MX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-induced GTP-binding protein Mx1
Alternative name(s):
Interferon-induced protein p78
Short name=IFI-78K
Interferon-regulated resistance GTP-binding protein MxA
Myxoma resistance protein 1
Myxovirus resistance protein 1
Gene names
Name:MX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26 Ref.27 Ref.29 Ref.30 Ref.34 Ref.36

Subunit structure

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. Ref.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38

Subcellular location

Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmperinuclear region. Note: Binds preferentially to negatively charged phospholipids. Colocalizes with CCHFV protein N in the perinuclear region. Ref.4 Ref.15 Ref.17 Ref.18 Ref.20 Ref.23 Ref.25 Ref.30 Ref.33 Ref.34 Ref.36

Isoform 2: Cytoplasm. Nucleus. Note: Translocates into the nuclei of HSV-1 infected cells. Ref.4 Ref.15 Ref.17 Ref.18 Ref.20 Ref.23 Ref.25 Ref.30 Ref.33 Ref.34 Ref.36

Induction

By type I and type III interferons. Isoform 2 is induced by HSV-1. Ref.28

Domain

The C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition. Ref.31

The middle domain mediates self-assembly and oligomerization. Ref.31

Post-translational modification

ISGylated. Ref.24

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.

Contains 1 dynamin-type G (guanine nucleotide-binding) domain.

Contains 1 GED domain.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement PubMed 9389754. Source: ProtInc

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response

Traceable author statement Ref.2. Source: ProtInc

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement Ref.26. Source: UniProtKB

negative regulation of viral genome replication

Inferred from direct assay Ref.21Ref.18Ref.26. Source: UniProtKB

response to type I interferon

Traceable author statement Ref.33. Source: UniProtKB

response to virus

Inferred from mutant phenotype Ref.18. Source: UniProtKB

signal transduction

Traceable author statement PubMed 9389754. Source: ProtInc

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.33. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 16780588. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay Ref.18. Source: UniProtKB

   Molecular_functionGTP binding

Traceable author statement Ref.2. Source: ProtInc

GTPase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.18Ref.33. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20591-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P20591-2)

Also known as: 56-kda; varMxA;

The sequence of this isoform differs from the canonical sequence as follows:
     425-662: GHKILSRKIQ...ARRRLAQFPG → GGQQAHLQPH...PRLTTLCPAP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Interferon-induced GTP-binding protein Mx1
PRO_0000382943
Initiator methionine11Removed; alternate Ref.10 Ref.11
Chain2 – 662661Interferon-induced GTP-binding protein Mx1, N-terminally processed
PRO_0000206592

Regions

Domain67 – 340274Dynamin-type G
Domain574 – 66289GED
Nucleotide binding77 – 848GTP Potential
Nucleotide binding178 – 1825GTP Potential
Nucleotide binding247 – 2504GTP Potential
Region69 – 340272GTPase domain (Globular)
Region341 – 36626Bundle signaling element (BSE)
Region366 – 533168Middle domain
Region367 – 632266Stalk
Region554 – 5574Critical for lipid-binding

Amino acid modifications

Modified residue11N-acetylmethionine; in Interferon-induced GTP-binding protein Mx1; alternate Ref.9

Natural variations

Alternative sequence425 – 662238GHKIL…AQFPG → GGQQAHLQPHPFDHPVLHAP DVRPAASEGHAAAPAGQGHL QLAPEGAERHQRQAEVPEGA ACTADAGSAPACPVPRLTTL CPAP in isoform 2.
VSP_042904
Natural variant3791V → I. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8
Corresponds to variant rs469390 [ dbSNP | Ensembl ].
VAR_058010
Natural variant3811A → V.
Corresponds to variant rs34717738 [ dbSNP | Ensembl ].
VAR_034116
Natural variant6111Q → H.
Corresponds to variant rs2230454 [ dbSNP | Ensembl ].
VAR_034117

Experimental info

Mutagenesis811S → C: No effect on GTP-binding, nor on viral infection. Ref.14
Mutagenesis831K → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. Ref.14 Ref.22
Mutagenesis831K → M: Loss of GTP-binding. Loss of protection against viral infection. Ref.14 Ref.22
Mutagenesis1031T → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. Ref.15 Ref.22
Mutagenesis5541K → E: Strong liposome-binding reduction. Ref.34
Mutagenesis5551K → E: Strong liposome-binding reduction. Ref.34
Mutagenesis5561K → E: Strong liposome-binding reduction. Ref.34
Mutagenesis5571K → E: Strong liposome-binding reduction. Ref.34
Mutagenesis6121L → K: Loss of GTP-hydrolysis. No effect on GTP-binding, nor on potentiation of TRPC6 activity. Ref.22
Mutagenesis6321E → A: Reduced antiviral activity. Ref.38
Mutagenesis6401R → A: Fails to sequester viral nucleoproteins, no antiviral activity. Ref.38
Mutagenesis6451E → R: Loss of antiviral activity towards CCHFV and LACV. Ref.17 Ref.18
Sequence conflict1641L → R in AAA36337. Ref.1
Sequence conflict2501D → G in BAG53272. Ref.4
Sequence conflict2971Q → H in BAG37852. Ref.4
Sequence conflict2991E → G in BAG53272. Ref.4
Sequence conflict5821M → I in BAG37852. Ref.4

Secondary structure

...................................................................... 662
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 7, 2009. Version 4.
Checksum: 626A7DD946F89384

FASTA66275,520
        10         20         30         40         50         60 
MVVSEVDIAK ADPAAASHPL LLNGDATVAQ KNPGSVAENN LCSQYEEKVR PCIDLIDSLR 

        70         80         90        100        110        120 
ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKKLVNEDKW 

       130        140        150        160        170        180 
RGKVSYQDYE IEISDASEVE KEINKAQNAI AGEGMGISHE LITLEISSRD VPDLTLIDLP 

       190        200        210        220        230        240 
GITRVAVGNQ PADIGYKIKT LIKKYIQRQE TISLVVVPSN VDIATTEALS MAQEVDPEGD 

       250        260        270        280        290        300 
RTIGILTKPD LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK 

       310        320        330        340        350        360 
IFFENHPYFR DLLEEGKATV PCLAEKLTSE LITHICKSLP LLENQIKETH QRITEELQKY 

       370        380        390        400        410        420 
GVDIPEDENE KMFFLIDKVN AFNQDITALM QGEETVGEED IRLFTRLRHE FHKWSTIIEN 

       430        440        450        460        470        480 
NFQEGHKILS RKIQKFENQY RGRELPGFVN YRTFETIVKQ QIKALEEPAV DMLHTVTDMV 

       490        500        510        520        530        540 
RLAFTDVSIK NFEEFFNLHR TAKSKIEDIR AEQEREGEKL IRLHFQMEQI VYCQDQVYRG 

       550        560        570        580        590        600 
ALQKVREKEL EEEKKKKSWD FGAFQSSSAT DSSMEEIFQH LMAYHQEASK RISSHIPLII 

       610        620        630        640        650        660 
QFFMLQTYGQ QLQKAMLQLL QDKDTYSWLL KERSDTSDKR KFLKERLARL TQARRRLAQF 


PG 

« Hide

Isoform 2 (56-kda) (varMxA) [UniParc].

Checksum: 4681FED66E2F8C21
Show »

FASTA50855,661

References

« Hide 'large scale' references
[1]"cDNA structures and regulation of two interferon-induced human Mx proteins."
Aebi M., Faeh J., Hurt N., Samuel C.E., Thomis D., Bazzigher L., Pavlovic J., Haller O., Staeheli P.
Mol. Cell. Biol. 9:5062-5072(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-379.
[2]"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."
Horisberger M.A., McMaster G.K., Zeller H., Wathelet M.G., Dellis J., Content J.
J. Virol. 64:1171-1181(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-379.
[3]"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."
Tazi-Ahnini R., di Giovine F.S., McDonagh A.J., Messenger A.G., Amadou C., Cox A., Duff G.W., Cork M.J.
Hum. Genet. 106:639-645(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-379, POSSIBLE INVOLVEMENT IN ALLOPECIA AREATA.
[4]"Herpes simplex virus-1 induces expression of a novel MxA isoform that enhances viral replication."
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.
Immunol. Cell Biol. 89:173-182(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORM 2), ALTERNATIVE SPLICING.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-379.
[6]"The DNA sequence of human chromosome 21."
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. expand/collapse author list , 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.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-379.
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-379.
Tissue: B-cell and Uterus.
[9]Bienvenut W.V., Gao M., Leug H.
Submitted (JUL-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-10; 84-97 AND 442-481, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Prostatic carcinoma.
[10]"Interferon-induced human protein in pure form, monoclonal antibodies thereto, and test kits containing these antibodies."
Horisberger M.A., Hochkeppel H.K., Content J.
Patent number EP0242329, 21-OCT-1987
Cited for: PROTEIN SEQUENCE OF 2-57, NUCLEOTIDE SEQUENCE OF 2-124.
[11]"Purification and characterization of a human Mx protein."
Weitz G., Bekisz J., Zoon K., Arnheiter H.
J. Interferon Res. 9:679-689(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.
[12]"Inf-induced gene expression analysis in MS patients: Loss of bioavailability can be caused by either binding or neutralizing antibodies."
Narayan K., Pachner A.R.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 486-569.
[13]"Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein."
Pavlovic J., Zuercher T., Haller O., Staeheli P.
J. Virol. 64:3370-3375(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: RESISTANCE TO INFLUENZA VIRUS AND VSV.
[14]"A functional GTP-binding motif is necessary for antiviral activity of Mx proteins."
Pitossi F., Blank A., Schroeder A., Schwarz A., Huessi P., Schwemmle M., Pavlovic J., Staeheli P.
J. Virol. 67:6726-6732(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-81 AND LYS-83.
[15]"Dominant-negative mutants of human MxA protein: domains in the carboxy-terminal moiety are important for oligomerization and antiviral activity."
Ponten A., Sick C., Weeber M., Haller O., Kochs G.
J. Virol. 71:2591-2599(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THR-103.
[16]"GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae)."
Kochs G., Haller O.
J. Biol. Chem. 274:4370-4376(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THOV NUCLEOPROTEIN.
[17]"Antivirally active MxA protein sequesters La Crosse virus nucleocapsid protein into perinuclear complexes."
Kochs G., Janzen C., Hohenberg H., Haller O.
Proc. Natl. Acad. Sci. U.S.A. 99:3153-3158(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LACV PROTEIN N, MUTAGENESIS OF GLU-645.
[18]"Human MxA protein inhibits the replication of Crimean-Congo hemorrhagic fever virus."
Andersson I., Bladh L., Mousavi-Jazi M., Magnusson K.E., Lundkvist A., Haller O., Mirazimi A.
J. Virol. 78:4323-4329(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCHFV PROTEIN N, MUTAGENESIS OF GLU-645.
[19]"Nuclear MxA proteins form a complex with influenza virus NP and inhibit the transcription of the engineered influenza virus genome."
Turan K., Mibayashi M., Sugiyama K., Saito S., Numajiri A., Nagata K.
Nucleic Acids Res. 32:643-652(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"Missorting of LaCrosse virus nucleocapsid protein by the interferon-induced MxA GTPase involves smooth ER membranes."
Reichelt M., Stertz S., Krijnse-Locker J., Haller O., Kochs G.
Traffic 5:772-784(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[21]"Inhibition of Dugbe nairovirus replication by human MxA protein."
Bridgen A., Dalrymple D.A., Weber F., Elliott R.M.
Virus Res. 99:47-50(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC."
Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N., St-Hilaire M., Pinard M., Boulay G.
J. Biol. Chem. 280:19393-19400(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRPC1; TRPC3; TRPC4; TRPC5; TRPC6 AND TRPC7, MUTAGENESIS OF LYS-83; THR-103 AND LEU-612.
[23]"Assay and functional analysis of dynamin-like Mx proteins."
Kochs G., Reichelt M., Danino D., Hinshaw J.E., Haller O.
Methods Enzymol. 404:632-643(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH LACV PROTEIN N.
[24]"Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways."
Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[25]"Interferon-induced, antiviral human MxA protein localizes to a distinct subcompartment of the smooth endoplasmic reticulum."
Stertz S., Reichelt M., Krijnse-Locker J., Mackenzie J., Simpson J.C., Haller O., Kochs G.
J. Interferon Cytokine Res. 26:650-660(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[26]"Expression of the interferon-alpha/beta-inducible bovine Mx1 dynamin interferes with replication of rabies virus."
Leroy M., Pire G., Baise E., Desmecht D.
Neurobiol. Dis. 21:515-521(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"Human MxA protein confers resistance to double-stranded RNA viruses of two virus families."
Mundt E.
J. Gen. Virol. 88:1319-1323(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"The Mx GTPase family of interferon-induced antiviral proteins."
Haller O., Stertz S., Kochs G.
Microbes Infect. 9:1636-1643(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, INDUCTION.
[29]"GTPase activity is not essential for the interferon-inducible MxA protein to inhibit the replication of hepatitis B virus."
Yu Z., Wang Z., Chen J., Li H., Lin Z., Zhang F., Zhou Y., Hou J.
Arch. Virol. 153:1677-1684(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"Inhibition of a large double-stranded DNA virus by MxA protein."
Netherton C.L., Simpson J., Haller O., Wileman T.E., Takamatsu H.H., Monaghan P., Taylor G.
J. Virol. 83:2310-2320(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[31]"Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity."
Haller O., Gao S., von der Malsburg A., Daumke O., Kochs G.
J. Biol. Chem. 285:28419-28424(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON STRUCTURE, DOMAIN GED, DOMAIN MIDDLE.
[32]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Interferon-induced antiviral protein MxA interacts with the cellular RNA helicases UAP56 and URH49."
Wisskirchen C., Ludersdorfer T.H., Mueller D.A., Moritz E., Pavlovic J.
J. Biol. Chem. 286:34743-34751(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DDX39A AND DDX39B.
[34]"Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop."
von der Malsburg A., Abutbul-Ionita I., Haller O., Kochs G., Danino D.
J. Biol. Chem. 286:37858-37865(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-554; LYS-555; LYS-556 AND LYS-557.
[35]"Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity."
Haller O., Kochs G.
J. Interferon Cytokine Res. 31:79-87(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[36]"Interferon-inducible antiviral protein MxA enhances cell death triggered by endoplasmic reticulum stress."
Numajiri Haruki A., Naito T., Nishie T., Saito S., Nagata K.
J. Interferon Cytokine Res. 31:847-856(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA5.
[37]"Structural basis of oligomerization in the stalk region of dynamin-like MxA."
Gao S., von der Malsburg A., Paeschke S., Behlke J., Haller O., Kochs G., Daumke O.
Nature 465:502-506(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 366-636, SUBUNIT.
[38]"Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function."
Gao S., von der Malsburg A., Dick A., Faelber K., Schroder G.F., Haller O., Kochs G., Daumke O.
Immunity 35:514-525(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 33-662, SUBUNIT, MUTAGENESIS OF GLU-632 AND ARG-640.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30817 mRNA. Translation: AAA36337.1.
M33882 mRNA. Translation: AAA36458.1.
AF135187 Genomic DNA. Translation: AAD43063.1.
AK096355 mRNA. Translation: BAG53272.1.
AK315465 mRNA. Translation: BAG37852.1.
AL163285 Genomic DNA. Translation: CAB90556.1.
AL773577 Genomic DNA. No translation available.
AL773578 Genomic DNA. No translation available.
AP001610 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09600.1.
CH471079 Genomic DNA. Translation: EAX09601.1.
CH471079 Genomic DNA. Translation: EAX09602.1.
CH471079 Genomic DNA. Translation: EAX09603.1.
CH471079 Genomic DNA. Translation: EAX09604.1.
BC014222 mRNA. Translation: AAH14222.2.
BC032602 mRNA. Translation: AAH32602.1.
AY186254 mRNA. Translation: AAO31807.1.
CCDSCCDS13673.1. [P20591-1]
PIRA33481.
RefSeqNP_001138397.1. NM_001144925.2. [P20591-1]
NP_001171517.1. NM_001178046.2. [P20591-1]
NP_001269849.1. NM_001282920.1. [P20591-2]
NP_002453.2. NM_002462.4. [P20591-1]
XP_005261035.1. XM_005260978.2. [P20591-1]
XP_005261036.1. XM_005260979.1. [P20591-1]
XP_005261037.1. XM_005260980.1. [P20591-1]
XP_005261038.1. XM_005260981.1. [P20591-1]
XP_005261039.1. XM_005260982.1. [P20591-1]
UniGeneHs.517307.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LJBX-ray2.40A/B366-636[»]
3SZRX-ray3.50A33-662[»]
3ZYSelectron microscopy12.20B/E1-662[»]
ProteinModelPortalP20591.
SMRP20591. Positions 45-662.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110684. 9 interactions.
DIPDIP-35694N.
IntActP20591. 10 interactions.
STRING9606.ENSP00000381599.

PTM databases

PhosphoSiteP20591.

Polymorphism databases

DMDM251757499.

Proteomic databases

MaxQBP20591.
PaxDbP20591.
PRIDEP20591.

Protocols and materials databases

DNASU4599.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398598; ENSP00000381599; ENSG00000157601. [P20591-1]
ENST00000398600; ENSP00000381601; ENSG00000157601. [P20591-1]
ENST00000455164; ENSP00000410523; ENSG00000157601. [P20591-1]
GeneID4599.
KEGGhsa:4599.
UCSCuc002yzh.3. human. [P20591-1]

Organism-specific databases

CTD4599.
GeneCardsGC21P042792.
H-InvDBHIX0027784.
HGNCHGNC:7532. MX1.
HPAHPA030917.
MIM147150. gene.
neXtProtNX_P20591.
PharmGKBPA31333.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0699.
HOGENOMHOG000213785.
HOVERGENHBG008788.
InParanoidP20591.
KOK14754.
OMALHTVTDM.
OrthoDBEOG7034GF.
PhylomeDBP20591.
TreeFamTF331484.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP20591.
BgeeP20591.
CleanExHS_MX1.
GenevestigatorP20591.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 1 hit.
PfamPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSPR00195. DYNAMIN.
SMARTSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20591.
GeneWikiMX1.
GenomeRNAi4599.
NextBio17684.
PROP20591.
SOURCESearch...

Entry information

Entry nameMX1_HUMAN
AccessionPrimary (citable) accession number: P20591
Secondary accession number(s): B2RDA5 expand/collapse secondary AC list , B3KU10, C9IYV7, C9J8D6, C9JN19, C9JN88, C9JUL1, C9JZS6, D3DSI8, Q86YP5, Q96CI3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM