P20591 (MX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Cleaved into the following chain:

1. Interferon-induced GTP-binding protein Mx1, N-terminally processed

Gene names

Name:

MX1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.25 Ref.26 Ref.28 Ref.29 Ref.33 Ref.35
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.32 Ref.33 Ref.35 Ref.36 Ref.37
Subcellular location	Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › perinuclear region. Note: Binds preferentially to negatively charged phospholipids. Co-localizes with CCHFV protein N in the perinuclear region. Ref.4 Ref.15 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.29 Ref.32 Ref.33 Ref.35 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.24 Ref.29 Ref.32 Ref.33 Ref.35
Induction	By type I and type III interferons. Isoform 2 is induced by HSV-1. Ref.27
Domain	The C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition. Ref.30 The middle domain mediates self-assembly and oligomerization. Ref.30
Sequence similarities	Belongs to the dynamin family. Contains 1 GED domain.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Traceable author statement PubMed 9389754. Source: ProtInc negative regulation of viral genome replication Inferred from direct assay Ref.21Ref.18Ref.25. Source: UniProtKB response to virus Inferred from mutant phenotype Ref.18. Source: UniProtKB type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	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_function	GTP binding Traceable author statement Ref.2. Source: ProtInc GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRPC3	Q13507	2	EBI-929476,EBI-520807
TRPC4	Q9UBN4	2	EBI-929476,EBI-929504
TRPC6	Q9Y210	4	EBI-929476,EBI-929362

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 662

662

Interferon-induced GTP-binding protein Mx1

PRO_0000382943

Initiator methionine

1

1

Removed; alternate Ref.10 Ref.11

Chain

2 – 662

661

Interferon-induced GTP-binding protein Mx1, N-terminally processed

PRO_0000206592

Regions

Domain

574 – 662

89

GED

Nucleotide binding

77 – 84

8

GTP Potential

Nucleotide binding

178 – 182

5

GTP Potential

Nucleotide binding

247 – 250

4

GTP Potential

Region

69 – 340

272

GTPase domain (Globular)

Region

341 – 366

26

Bundle signaling element (BSE)

Region

366 – 533

168

Middle domain

Region

367 – 632

266

Stalk

Region

554 – 557

4

Critical for lipid-binding

Amino acid modifications

Modified residue

1

1

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

Natural variations

Alternative sequence

425 – 662

238

GHKIL…AQFPG → GGQQAHLQPHPFDHPVLHAP DVRPAASEGHAAAPAGQGHL QLAPEGAERHQRQAEVPEGA ACTADAGSAPACPVPRLTTL CPAP in isoform 2.

VSP_042904

Natural variant

379

1

V → I. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8
Corresponds to variant rs469390 [ dbSNP | Ensembl ].

VAR_058010

Natural variant

381

1

A → V.
Corresponds to variant rs34717738 [ dbSNP | Ensembl ].

VAR_034116

Natural variant

611

1

Q → H.
Corresponds to variant rs2230454 [ dbSNP | Ensembl ].

VAR_034117

Experimental info

Mutagenesis

81

1

S → C: No effect on GTP-binding, nor on viral infection. Ref.14

Mutagenesis

83

1

K → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. Ref.14 Ref.22

Mutagenesis

83

1

K → M: Loss of GTP-binding. Loss of protection against viral infection. Ref.14 Ref.22

Mutagenesis

103

1

T → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. Ref.15 Ref.22

Mutagenesis

554

1

K → E: Strong liposome-binding reduction. Ref.33

Mutagenesis

555

1

K → E: Strong liposome-binding reduction. Ref.33

Mutagenesis

556

1

K → E: Strong liposome-binding reduction. Ref.33

Mutagenesis

557

1

K → E: Strong liposome-binding reduction. Ref.33

Mutagenesis

612

1

L → K: Loss of GTP-hydrolysis. No effect on GTP-binding, nor on potentiation of TRPC6 activity. Ref.22

Mutagenesis

632

1

E → A: Reduced antiviral activity. Ref.37

Mutagenesis

640

1

R → A: Fails to sequester viral nucleoproteins, no antiviral activity. Ref.37

Mutagenesis

645

1

E → R: Loss of antiviral activity towards CCHFV and LACV. Ref.17 Ref.18

Sequence conflict

164

1

L → R in AAA36337. Ref.1

Sequence conflict

250

1

D → G in BAG53272. Ref.4

Sequence conflict

297

1

Q → H in BAG37852. Ref.4

Sequence conflict

299

1

E → G in BAG53272. Ref.4

Sequence conflict

582

1

M → I in BAG37852. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

662

Helix Strand Turn

Details...

Helix

46 – 62

17

Helix

83 – 91

9

Beta strand

107 – 113

7

Beta strand

115 – 118

4

Beta strand

121 – 125

5

Helix

136 – 140

5

Helix

143 – 151

9

Beta strand

153 – 155

3

Beta strand

162 – 171

10

Beta strand

174 – 178

5

Helix

194 – 205

12

Beta strand

208 – 210

3

Beta strand

213 – 221

9

Turn

223 – 225

3

Helix

227 – 235

9

Beta strand

241 – 247

7

Helix

249 – 251

3

Beta strand

252 – 256

5

Turn

286 – 288

3

Helix

292 – 295

4

Turn

296 – 298

3

Helix

299 – 302

4

Turn

303 – 305

3

Turn

307 – 309

3

Helix

311 – 314

4

Helix

323 – 358

36

Helix

367 – 390

24

Helix

403 – 437

35

Beta strand

444 – 446

3

Helix

451 – 463

13

Helix

466 – 492

27

Helix

496 – 528

33

Helix

574 – 604

31

Helix

606 – 618

13

Helix

623 – 625

3

Helix

626 – 629

4

Helix

634 – 658

25

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 7, 2009. Version 4. Checksum: 626A7DD946F89384	FASTA	662	75,520
	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
	Isoform 2 (56-kda) (varMxA) [UniParc]. Checksum: 4681FED66E2F8C21	FASTA	508	55,661
	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 NFQEGGQQAH LQPHPFDHPV LHAPDVRPAA SEGHAAAPAG QGHLQLAPEG AERHQRQAEV 490 500 PEGAACTADA GSAPACPVPR LTTLCPAP

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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].
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.

IPI

IPI00167949.

PIR

A33481.

RefSeq

NP_001138397.1. NM_001144925.1.
NP_001171517.1. NM_001178046.1.
NP_002453.2. NM_002462.3.

UniGene

Hs.517307.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LJB	X-ray	2.40	A/B	366-636	[»]
3SZR	X-ray	3.50	A	33-662	[»]
3ZYS	electron microscopy	12.20	B/E	1-662	[»]

ProteinModelPortal

P20591.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35694N.

IntAct

P20591. 9 interactions.

STRING

9606.ENSP00000381599.

PTM databases

PhosphoSite

P20591.

Polymorphism databases

DMDM

251757499.

Proteomic databases

PaxDb

P20591.

PRIDE

P20591.

Protocols and materials databases

DNASU

4599.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398598; ENSP00000381599; ENSG00000157601.
ENST00000398600; ENSP00000381601; ENSG00000157601.
ENST00000455164; ENSP00000410523; ENSG00000157601.

GeneID

4599.

KEGG

hsa:4599.

UCSC

uc002yzh.3. human.

Organism-specific databases

CTD

4599.

GeneCards

GC21P042792.

H-InvDB

HIX0027784.

HGNC

HGNC:7532. MX1.

HPA

HPA030917.

MIM

147150. gene.

neXtProt

NX_P20591.

PharmGKB

PA31333.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0699.

HOGENOM

HOG000213785.

HOVERGEN

HBG008788.

InParanoid

P20591.

KO

K14754.

OMA

AVDMLHT.

OrthoDB

EOG495ZRP.

PhylomeDB

P20591.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P20591.

Bgee

P20591.

CleanEx

HS_MX1.

Genevestigator

P20591.

GermOnline

ENSG00000157601. Homo sapiens.

Family and domain databases

InterPro

IPR022812. Dynamin.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR015577. Interferon-induced_Mx.
[Graphical view]

PANTHER

PTHR11566. PTHR11566. 1 hit.
PTHR11566:SF13. PTHR11566:SF13. 1 hit.

Pfam

PF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]

PRINTS

PR00195. DYNAMIN.

SMART

SM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]

PROSITE

PS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20591.

GenomeRNAi

4599.

NextBio

17684.

SOURCE

Search...

Entry information

Entry name

MX1_HUMAN

Accession

Primary (citable) accession number: P20591
Secondary accession number(s): B2RDA5 , 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:	May 1, 2013
This is version 122 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.