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P20591

- MX1_HUMAN

UniProt

P20591 - MX1_HUMAN

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Protein

Interferon-induced GTP-binding protein Mx1

Gene

MX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.13 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 848GTPSequence Analysis
Nucleotide bindingi178 – 1825GTPSequence Analysis
Nucleotide bindingi247 – 2504GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. cytokine-mediated signaling pathway Source: Reactome
  3. defense response Source: ProtInc
  4. defense response to virus Source: UniProtKB-KW
  5. innate immune response Source: UniProtKB
  6. negative regulation of viral genome replication Source: UniProtKB
  7. response to type I interferon Source: UniProtKB
  8. response to virus Source: UniProtKB
  9. signal transduction Source: ProtInc
  10. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_25162. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:MX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:7532. MX1.

Subcellular locationi

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.
Isoform 2 : Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Translocates into the nuclei of HSV-1 infected cells.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. membrane Source: UniProtKB-KW
  5. nucleus Source: UniProtKB-KW
  6. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811S → C: No effect on GTP-binding, nor on viral infection. 1 Publication
Mutagenesisi83 – 831K → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. 2 Publications
Mutagenesisi83 – 831K → M: Loss of GTP-binding. Loss of protection against viral infection. 2 Publications
Mutagenesisi103 – 1031T → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. 2 Publications
Mutagenesisi554 – 5541K → E: Strong liposome-binding reduction. 1 Publication
Mutagenesisi555 – 5551K → E: Strong liposome-binding reduction. 1 Publication
Mutagenesisi556 – 5561K → E: Strong liposome-binding reduction. 1 Publication
Mutagenesisi557 – 5571K → E: Strong liposome-binding reduction. 1 Publication
Mutagenesisi612 – 6121L → K: Loss of GTP-hydrolysis. No effect on GTP-binding, nor on potentiation of TRPC6 activity. 1 Publication
Mutagenesisi632 – 6321E → A: Reduced antiviral activity. 1 Publication
Mutagenesisi640 – 6401R → A: Fails to sequester viral nucleoproteins, no antiviral activity. 1 Publication
Mutagenesisi645 – 6451E → R: Loss of antiviral activity towards CCHFV and LACV. 2 Publications

Organism-specific databases

PharmGKBiPA31333.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 662662Interferon-induced GTP-binding protein Mx1PRO_0000382943Add
BLAST
Initiator methioninei1 – 11Removed; alternate2 Publications
Chaini2 – 662661Interferon-induced GTP-binding protein Mx1, N-terminally processedPRO_0000206592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in Interferon-induced GTP-binding protein Mx1; alternate1 Publication

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiP20591.
PaxDbiP20591.
PRIDEiP20591.

PTM databases

PhosphoSiteiP20591.

Expressioni

Inductioni

By type I and type III interferons. Isoform 2 is induced by HSV-1.1 Publication

Gene expression databases

BgeeiP20591.
CleanExiHS_MX1.
ExpressionAtlasiP20591. baseline and differential.
GenevestigatoriP20591.

Organism-specific databases

HPAiHPA030917.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TRPC3Q135072EBI-929476,EBI-520807
TRPC4Q9UBN42EBI-929476,EBI-929504
TRPC6Q9Y2104EBI-929476,EBI-929362

Protein-protein interaction databases

BioGridi110684. 9 interactions.
DIPiDIP-35694N.
IntActiP20591. 10 interactions.
STRINGi9606.ENSP00000381599.

Structurei

Secondary structure

1
662
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 6217
Helixi83 – 919
Beta strandi107 – 1137
Beta strandi115 – 1184
Beta strandi121 – 1255
Helixi136 – 1405
Helixi143 – 1519
Beta strandi153 – 1553
Beta strandi162 – 17110
Beta strandi174 – 1785
Helixi194 – 20512
Beta strandi208 – 2103
Beta strandi213 – 2219
Turni223 – 2253
Helixi227 – 2359
Beta strandi241 – 2477
Helixi249 – 2513
Beta strandi252 – 2565
Turni286 – 2883
Helixi292 – 2954
Turni296 – 2983
Helixi299 – 3024
Turni303 – 3053
Turni307 – 3093
Helixi311 – 3144
Helixi323 – 35836
Helixi367 – 39024
Helixi403 – 43735
Beta strandi444 – 4463
Helixi451 – 46313
Helixi466 – 49227
Helixi496 – 52833
Helixi574 – 60431
Helixi606 – 61813
Helixi623 – 6253
Helixi626 – 6294
Helixi634 – 65825

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LJBX-ray2.40A/B366-636[»]
3SZRX-ray3.50A33-662[»]
3ZYSelectron microscopy12.20B/E1-662[»]
ProteinModelPortaliP20591.
SMRiP20591. Positions 45-662.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20591.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 340274Dynamin-type GAdd
BLAST
Domaini574 – 66289GEDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 340272GTPase domain (Globular)Add
BLAST
Regioni341 – 36626Bundle signaling element (BSE)Add
BLAST
Regioni366 – 533168Middle domainAdd
BLAST
Regioni367 – 632266StalkAdd
BLAST
Regioni554 – 5574Critical for lipid-binding

Domaini

The C-terminal GTPase effector domain (GED) is involved in oligomerization and viral target recognition.1 Publication
The middle domain mediates self-assembly and oligomerization.1 Publication

Sequence similaritiesi

Contains 1 GED domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0699.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000213785.
HOVERGENiHBG008788.
InParanoidiP20591.
KOiK14754.
OMAiLHTVTDM.
OrthoDBiEOG7034GF.
PhylomeDBiP20591.
TreeFamiTF331484.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000375. 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]
PANTHERiPTHR11566. PTHR11566. 1 hit.
PfamiPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20591-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVVSEVDIAK ADPAAASHPL LLNGDATVAQ KNPGSVAENN LCSQYEEKVR
60 70 80 90 100
PCIDLIDSLR ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG
110 120 130 140 150
IVTRCPLVLK LKKLVNEDKW RGKVSYQDYE IEISDASEVE KEINKAQNAI
160 170 180 190 200
AGEGMGISHE LITLEISSRD VPDLTLIDLP GITRVAVGNQ PADIGYKIKT
210 220 230 240 250
LIKKYIQRQE TISLVVVPSN VDIATTEALS MAQEVDPEGD RTIGILTKPD
260 270 280 290 300
LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK
310 320 330 340 350
IFFENHPYFR DLLEEGKATV PCLAEKLTSE LITHICKSLP LLENQIKETH
360 370 380 390 400
QRITEELQKY GVDIPEDENE KMFFLIDKVN AFNQDITALM QGEETVGEED
410 420 430 440 450
IRLFTRLRHE FHKWSTIIEN NFQEGHKILS RKIQKFENQY RGRELPGFVN
460 470 480 490 500
YRTFETIVKQ QIKALEEPAV DMLHTVTDMV RLAFTDVSIK NFEEFFNLHR
510 520 530 540 550
TAKSKIEDIR AEQEREGEKL IRLHFQMEQI VYCQDQVYRG ALQKVREKEL
560 570 580 590 600
EEEKKKKSWD FGAFQSSSAT DSSMEEIFQH LMAYHQEASK RISSHIPLII
610 620 630 640 650
QFFMLQTYGQ QLQKAMLQLL QDKDTYSWLL KERSDTSDKR KFLKERLARL
660
TQARRRLAQF PG
Length:662
Mass (Da):75,520
Last modified:July 7, 2009 - v4
Checksum:i626A7DD946F89384
GO
Isoform 2 (identifier: P20591-2) [UniParc]FASTAAdd to Basket

Also known as: 56-kda, varMxA

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

Show »
Length:508
Mass (Da):55,661
Checksum:i4681FED66E2F8C21
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641L → R in AAA36337. (PubMed:2481229)Curated
Sequence conflicti250 – 2501D → G in BAG53272. (PubMed:20603636)Curated
Sequence conflicti297 – 2971Q → H in BAG37852. (PubMed:20603636)Curated
Sequence conflicti299 – 2991E → G in BAG53272. (PubMed:20603636)Curated
Sequence conflicti582 – 5821M → I in BAG37852. (PubMed:20603636)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti379 – 3791V → I.6 Publications
Corresponds to variant rs469390 [ dbSNP | Ensembl ].
VAR_058010
Natural varianti381 – 3811A → V.
Corresponds to variant rs34717738 [ dbSNP | Ensembl ].
VAR_034116
Natural varianti611 – 6111Q → H.
Corresponds to variant rs2230454 [ dbSNP | Ensembl ].
VAR_034117

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei425 – 662238GHKIL…AQFPG → GGQQAHLQPHPFDHPVLHAP DVRPAASEGHAAAPAGQGHL QLAPEGAERHQRQAEVPEGA ACTADAGSAPACPVPRLTTL CPAP in isoform 2. 1 PublicationVSP_042904Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13673.1. [P20591-1]
CCDS74796.1. [P20591-2]
PIRiA33481.
RefSeqiNP_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]
UniGeneiHs.517307.

Genome annotation databases

EnsembliENST00000398598; ENSP00000381599; ENSG00000157601. [P20591-1]
ENST00000398600; ENSP00000381601; ENSG00000157601. [P20591-1]
ENST00000455164; ENSP00000410523; ENSG00000157601. [P20591-1]
ENST00000619682; ENSP00000478441; ENSG00000157601. [P20591-2]
GeneIDi4599.
KEGGihsa:4599.
UCSCiuc002yzh.3. human. [P20591-1]

Polymorphism databases

DMDMi251757499.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13673.1. [P20591-1 ]
CCDS74796.1. [P20591-2 ]
PIRi A33481.
RefSeqi NP_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 ]
UniGenei Hs.517307.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P20591.
SMRi P20591. Positions 45-662.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110684. 9 interactions.
DIPi DIP-35694N.
IntActi P20591. 10 interactions.
STRINGi 9606.ENSP00000381599.

PTM databases

PhosphoSitei P20591.

Polymorphism databases

DMDMi 251757499.

Proteomic databases

MaxQBi P20591.
PaxDbi P20591.
PRIDEi P20591.

Protocols and materials databases

DNASUi 4599.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398598 ; ENSP00000381599 ; ENSG00000157601 . [P20591-1 ]
ENST00000398600 ; ENSP00000381601 ; ENSG00000157601 . [P20591-1 ]
ENST00000455164 ; ENSP00000410523 ; ENSG00000157601 . [P20591-1 ]
ENST00000619682 ; ENSP00000478441 ; ENSG00000157601 . [P20591-2 ]
GeneIDi 4599.
KEGGi hsa:4599.
UCSCi uc002yzh.3. human. [P20591-1 ]

Organism-specific databases

CTDi 4599.
GeneCardsi GC21P042792.
H-InvDB HIX0027784.
HGNCi HGNC:7532. MX1.
HPAi HPA030917.
MIMi 147150. gene.
neXtProti NX_P20591.
PharmGKBi PA31333.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0699.
GeneTreei ENSGT00760000119213.
HOGENOMi HOG000213785.
HOVERGENi HBG008788.
InParanoidi P20591.
KOi K14754.
OMAi LHTVTDM.
OrthoDBi EOG7034GF.
PhylomeDBi P20591.
TreeFami TF331484.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_25162. Interferon alpha/beta signaling.

Miscellaneous databases

EvolutionaryTracei P20591.
GeneWikii MX1.
GenomeRNAii 4599.
NextBioi 17684.
PROi P20591.
SOURCEi Search...

Gene expression databases

Bgeei P20591.
CleanExi HS_MX1.
ExpressionAtlasi P20591. baseline and differential.
Genevestigatori P20591.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000375. 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 ]
PANTHERi PTHR11566. PTHR11566. 1 hit.
Pfami PF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view ]
PRINTSi PR00195. DYNAMIN.
SMARTi SM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiMX1_HUMAN
AccessioniPrimary (citable) accession number: P20591
Secondary accession number(s): B2RDA5
, B3KU10, C9IYV7, C9J8D6, C9JN19, C9JN88, C9JUL1, C9JZS6, D3DSI8, Q86YP5, Q96CI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 7, 2009
Last modified: October 29, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3