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P20591

- MX1_HUMAN

UniProt

P20591 - MX1_HUMAN

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
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 4 (07 Jul 2009)
      Previous versions | rss
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    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
    3. protein binding Source: UniProtKB

    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

    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 membrane Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB-SubCell
    5. perinuclear region of cytoplasm Source: UniProtKB

    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

    ArrayExpressiP20591.
    BgeeiP20591.
    CleanExiHS_MX1.
    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.
    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

    MVVSEVDIAK ADPAAASHPL LLNGDATVAQ KNPGSVAENN LCSQYEEKVR    50
    PCIDLIDSLR ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG 100
    IVTRCPLVLK LKKLVNEDKW RGKVSYQDYE IEISDASEVE KEINKAQNAI 150
    AGEGMGISHE LITLEISSRD VPDLTLIDLP GITRVAVGNQ PADIGYKIKT 200
    LIKKYIQRQE TISLVVVPSN VDIATTEALS MAQEVDPEGD RTIGILTKPD 250
    LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK 300
    IFFENHPYFR DLLEEGKATV PCLAEKLTSE LITHICKSLP LLENQIKETH 350
    QRITEELQKY GVDIPEDENE KMFFLIDKVN AFNQDITALM QGEETVGEED 400
    IRLFTRLRHE FHKWSTIIEN NFQEGHKILS RKIQKFENQY RGRELPGFVN 450
    YRTFETIVKQ QIKALEEPAV DMLHTVTDMV RLAFTDVSIK NFEEFFNLHR 500
    TAKSKIEDIR AEQEREGEKL IRLHFQMEQI VYCQDQVYRG ALQKVREKEL 550
    EEEKKKKSWD FGAFQSSSAT DSSMEEIFQH LMAYHQEASK RISSHIPLII 600
    QFFMLQTYGQ QLQKAMLQLL QDKDTYSWLL KERSDTSDKR KFLKERLARL 650
    TQARRRLAQF PG 662
    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]
    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]
    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 ]
    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 ]
    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.
    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

    ArrayExpressi P20591.
    Bgeei P20591.
    CleanExi HS_MX1.
    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

    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 1, 2014
    This is version 137 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