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Protein

Interferon-induced GTP-binding protein Mx1

Gene

MX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Nucleotide bindingi77 – 84GTPSequence analysis8
Nucleotide bindingi178 – 182GTPSequence analysis5
Nucleotide bindingi247 – 250GTPSequence analysis4

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: ProtInc
  • identical protein binding Source: IntAct
  • microtubule binding Source: GO_Central

GO - Biological processi

  • apoptotic process Source: ProtInc
  • defense response Source: ProtInc
  • defense response to virus Source: UniProtKB
  • dynamin family protein polymerization involved in mitochondrial fission Source: GO_Central
  • innate immune response Source: UniProtKB
  • membrane fusion Source: GO_Central
  • mitochondrial fission Source: GO_Central
  • negative regulation of viral genome replication Source: UniProtKB
  • response to type I interferon Source: UniProtKB
  • response to virus Source: UniProtKB
  • signal transduction Source: ProtInc
  • type I interferon signaling pathway Source: Reactome

Keywordsi

Biological processAntiviral defense, Immunity, Innate immunity
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1169408 ISG15 antiviral mechanism
R-HSA-909733 Interferon alpha/beta signaling
SIGNORiP20591

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
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

EuPathDBiHostDB:ENSG00000157601.13
HGNCiHGNC:7532 MX1
MIMi147150 gene
neXtProtiNX_P20591

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi81S → C: No effect on GTP-binding, nor on viral infection. 1 Publication1
Mutagenesisi83K → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. 2 Publications1
Mutagenesisi83K → M: Loss of GTP-binding. Loss of protection against viral infection. 2 Publications1
Mutagenesisi103T → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. 2 Publications1
Mutagenesisi554K → E: Strong liposome-binding reduction. 1 Publication1
Mutagenesisi555K → E: Strong liposome-binding reduction. 1 Publication1
Mutagenesisi556K → E: Strong liposome-binding reduction. 1 Publication1
Mutagenesisi557K → E: Strong liposome-binding reduction. 1 Publication1
Mutagenesisi612L → K: Loss of GTP-hydrolysis. No effect on GTP-binding, nor on potentiation of TRPC6 activity. 1 Publication1
Mutagenesisi632E → A: Reduced antiviral activity. 1 Publication1
Mutagenesisi640R → A: Fails to sequester viral nucleoproteins, no antiviral activity. 1 Publication1
Mutagenesisi645E → R: Loss of antiviral activity towards CCHFV and LACV. 2 Publications1

Organism-specific databases

DisGeNETi4599
OpenTargetsiENSG00000157601
PharmGKBiPA31333

Polymorphism and mutation databases

BioMutaiMX1
DMDMi251757499

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003829431 – 662Interferon-induced GTP-binding protein Mx1Add BLAST662
Initiator methionineiRemoved; alternate2 Publications
ChainiPRO_00002065922 – 662Interferon-induced GTP-binding protein Mx1, N-terminally processedAdd BLAST661

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine; in Interferon-induced GTP-binding protein Mx1; alternate1 Publication1

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

EPDiP20591
MaxQBiP20591
PaxDbiP20591
PeptideAtlasiP20591
PRIDEiP20591

PTM databases

iPTMnetiP20591
PhosphoSitePlusiP20591

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000157601
CleanExiHS_MX1
ExpressionAtlasiP20591 baseline and differential
GenevisibleiP20591 HS

Organism-specific databases

HPAiHPA030917
HPA030918
HPA049724

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • microtubule binding Source: GO_Central

Protein-protein interaction databases

BioGridi110684, 36 interactors
DIPiDIP-35694N
IntActiP20591, 15 interactors
STRINGi9606.ENSP00000381599

Structurei

Secondary structure

1662
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni47 – 49Combined sources3
Helixi50 – 61Combined sources12
Helixi64 – 66Combined sources3
Beta strandi72 – 78Combined sources7
Helixi83 – 91Combined sources9
Beta strandi99 – 101Combined sources3
Beta strandi107 – 113Combined sources7
Beta strandi115 – 117Combined sources3
Beta strandi121 – 126Combined sources6
Beta strandi129 – 133Combined sources5
Helixi136 – 138Combined sources3
Helixi139 – 150Combined sources12
Beta strandi153 – 155Combined sources3
Beta strandi162 – 168Combined sources7
Beta strandi173 – 178Combined sources6
Helixi195 – 206Combined sources12
Beta strandi208 – 210Combined sources3
Beta strandi211 – 218Combined sources8
Turni223 – 225Combined sources3
Helixi227 – 235Combined sources9
Beta strandi239 – 247Combined sources9
Helixi249 – 251Combined sources3
Beta strandi252 – 256Combined sources5
Helixi257 – 264Combined sources8
Beta strandi275 – 277Combined sources3
Helixi283 – 288Combined sources6
Helixi292 – 305Combined sources14
Turni307 – 309Combined sources3
Helixi310 – 314Combined sources5
Helixi320 – 358Combined sources39
Helixi367 – 390Combined sources24
Helixi403 – 437Combined sources35
Beta strandi444 – 446Combined sources3
Helixi449 – 452Combined sources4
Helixi454 – 462Combined sources9
Helixi463 – 465Combined sources3
Beta strandi467 – 474Combined sources8
Helixi479 – 481Combined sources3
Helixi483 – 490Combined sources8
Beta strandi495 – 502Combined sources8
Helixi504 – 506Combined sources3
Helixi513 – 520Combined sources8
Beta strandi523 – 525Combined sources3
Helixi543 – 546Combined sources4
Helixi551 – 561Combined sources11
Helixi564 – 566Combined sources3
Turni568 – 570Combined sources3
Helixi571 – 575Combined sources5
Helixi581 – 596Combined sources16
Helixi599 – 601Combined sources3
Turni602 – 604Combined sources3
Helixi605 – 621Combined sources17
Helixi623 – 625Combined sources3
Helixi626 – 629Combined sources4
Helixi635 – 658Combined sources24
Turni659 – 661Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LJBX-ray2.40A/B366-636[»]
3SZRX-ray3.50A33-662[»]
3ZYSelectron microscopy12.20B/E1-662[»]
4P4SX-ray3.30A70-342[»]
B43-662[»]
4P4TX-ray2.30A37-366[»]
A637-662[»]
4P4UX-ray1.90A37-364[»]
A632-661[»]
5GTMX-ray2.90A/B33-662[»]
ProteinModelPortaliP20591
SMRiP20591
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20591

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini67 – 340Dynamin-type GPROSITE-ProRule annotationAdd BLAST274
Domaini574 – 662GEDPROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 84G1 motifPROSITE-ProRule annotation8
Regioni102 – 104G2 motifPROSITE-ProRule annotation3
Regioni178 – 181G3 motifPROSITE-ProRule annotation4
Regioni247 – 250G4 motifPROSITE-ProRule annotation4
Regioni279 – 282G5 motifPROSITE-ProRule annotation4
Regioni341 – 366Bundle signaling element (BSE)Add BLAST26
Regioni366 – 533Middle domainAdd BLAST168
Regioni367 – 632StalkAdd BLAST266
Regioni554 – 557Critical for lipid-binding4

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

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

Phylogenomic databases

eggNOGiKOG0446 Eukaryota
COG0699 LUCA
GeneTreeiENSGT00760000119213
HOGENOMiHOG000213785
HOVERGENiHBG008788
InParanoidiP20591
KOiK14754
OMAiAVDMLHT
OrthoDBiEOG091G080G
PhylomeDBiP20591
TreeFamiTF331484

Family and domain databases

CDDicd08771 DLP_1, 1 hit
InterProiView protein in InterPro
IPR000375 Dynamin_central
IPR001401 Dynamin_GTPase
IPR019762 Dynamin_GTPase_CS
IPR022812 Dynamin_SF
IPR030381 G_DYNAMIN_dom
IPR003130 GED
IPR020850 GED_dom
IPR027417 P-loop_NTPase
PANTHERiPTHR11566 PTHR11566, 1 hit
PfamiView protein in Pfam
PF01031 Dynamin_M, 1 hit
PF00350 Dynamin_N, 1 hit
PF02212 GED, 1 hit
PRINTSiPR00195 DYNAMIN
SMARTiView protein in SMART
SM00053 DYNc, 1 hit
SM00302 GED, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00410 G_DYNAMIN_1, 1 hit
PS51718 G_DYNAMIN_2, 1 hit
PS51388 GED, 1 hit

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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti164L → R in AAA36337 (PubMed:2481229).Curated1
Sequence conflicti250D → G in BAG53272 (PubMed:20603636).Curated1
Sequence conflicti297Q → H in BAG37852 (PubMed:20603636).Curated1
Sequence conflicti299E → G in BAG53272 (PubMed:20603636).Curated1
Sequence conflicti582M → I in BAG37852 (PubMed:20603636).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058010379V → I6 PublicationsCorresponds to variant dbSNP:rs469390Ensembl.1
Natural variantiVAR_034116381A → V. Corresponds to variant dbSNP:rs34717738Ensembl.1
Natural variantiVAR_034117611Q → H. Corresponds to variant dbSNP:rs2230454Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_042904425 – 662GHKIL…AQFPG → GGQQAHLQPHPFDHPVLHAP DVRPAASEGHAAAPAGQGHL QLAPEGAERHQRQAEVPEGA ACTADAGSAPACPVPRLTTL CPAP in isoform 2. 1 PublicationAdd BLAST238

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005260978.4 [P20591-1]
XP_005261036.1, XM_005260979.2 [P20591-1]
XP_005261037.1, XM_005260980.2 [P20591-1]
XP_005261038.1, XM_005260981.2 [P20591-1]
XP_005261039.1, XM_005260982.2 [P20591-1]
XP_011527870.1, XM_011529568.2 [P20591-1]
XP_016883838.1, XM_017028349.1 [P20591-1]
XP_016883839.1, XM_017028350.1 [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.5 human [P20591-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 7, 2009
Last modified: May 23, 2018
This is version 173 of the entry and version 4 of the sequence. See 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

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