MX1
entrez
4599
canonical
uniprot
P20591
canonical
ensembl
ENSG00000157601
resolver
ensp
ENSP00000381599
resolver
ensp
ENSP00000381601
resolver
ensp
ENSP00000400923
resolver
ensp
ENSP00000402215
resolver
ensp
ENSP00000410523
resolver
ensp
ENSP00000478441
resolver
ensp
ENSP00000505051
resolver
ensp
ENSP00000505269
resolver
ensp
ENSP00000506220
resolver
ensp
ENSP00000506348
resolver
ensp
ENSP00000506512
resolver
ensp
ENSP00000506712
resolver
ensp
ENSP00000566084
resolver
ensp
ENSP00000566085
resolver
ensp
ENSP00000566086
resolver
ensp
ENSP00000566087
resolver
ensp
ENSP00000566092
resolver
ensp
ENSP00000566093
resolver
ensp
ENSP00000566097
resolver
ensp
ENSP00000585353
resolver
ensp
ENSP00000637526
resolver
ensp
ENSP00000637538
resolver
ensp
ENSP00000637539
resolver
ensp
ENSP00000785155
resolver
enst
ENST00000424365
resolver
enst
ENST00000679408
resolver
enst
ENST00000896025
resolver
enst
ENST00000896038
resolver
enst
ENST00000915294
resolver
enst
ENST00000967479
resolver
enst
ENST00000967480
resolver
genesymbol
MX1
resolver
hgnc
HGNC:7532
resolver
uniprot
B2RDA5
resolver
uniprot
B3KU10
resolver
uniprot
C9IYV7
resolver
uniprot
C9J8D6
resolver
uniprot
C9JN19
resolver
uniprot
C9JN88
resolver
uniprot
C9JUL1
resolver
uniprot
C9JZS6
resolver
uniprot
D3DSI8
resolver
uniprot
H9KVC7
resolver
uniprot
Q86YP5
resolver
uniprot
Q96CI3
resolver
uniprot_entry
H9KVC7_HUMAN
resolver
uniprot_entry
MX1_HUMAN
resolver
uniprot_sec
B2RDA5
resolver
uniprot_sec
B3KU10
resolver
uniprot_sec
C9IYV7
resolver
uniprot_sec
C9J8D6
resolver
uniprot_sec
C9JN19
resolver
uniprot_sec
C9JN88
resolver
uniprot_sec
C9JUL1
resolver
uniprot_sec
C9JZS6
resolver
uniprot_sec
D3DSI8
resolver
uniprot_sec
Q86YP5
resolver
uniprot_sec
Q96CI3
resolver
amino_acid_sequence
MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLLEEGKATVPCLAEKLTSELITHICKSLPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTIIENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQARRRLAQFPG
uniprot
proteins
function
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. {ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:14687945, ECO:0000269|PubMed:14752052, ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16202617, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:17374778, ECO:0000269|PubMed:18668195, ECO:0000269|PubMed:19109387, ECO:0000269|PubMed:21900240, ECO:0000269|PubMed:21992152}.
uniprot
proteins
mass_dalton
75520
uniprot
proteins
mutagenesis
MUTAGEN 81; /note="S->C: No effect on GTP-binding, nor on viral infection."; /evidence="ECO:0000269|PubMed:8411374"; MUTAGEN 83; /note="K->A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection."; /evidence="ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:8411374"; MUTAGEN 83; /note="K->M: Loss of GTP-binding. Loss of protection against viral infection."; /evidence="ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:8411374"; MUTAGEN 103; /note="T->A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection."; /evidence="ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:9060610"; MUTAGEN 554; /note="K->E: Strong liposome-binding reduction."; /evidence="ECO:0000269|PubMed:21900240"; MUTAGEN 555; /note="K->E: Strong liposome-binding reduction."; /evidence="ECO:0000269|PubMed:21900240"; MUTAGEN 556; /note="K->E: Strong liposome-binding reduction."; /evidence="ECO:0000269|PubMed:21900240"; MUTAGEN 557; /note="K->E: Strong liposome-binding reduction."; /evidence="ECO:0000269|PubMed:21900240"; MUTAGEN 612; /note="L->K: Loss of GTP-hydrolysis. No effect on GTP-binding, nor on potentiation of TRPC6 activity."; /evidence="ECO:0000269|PubMed:15757897"; MUTAGEN 632; /note="E->A: Reduced antiviral activity."; /evidence="ECO:0000269|PubMed:21962493"; MUTAGEN 640; /note="R->A: Fails to sequester viral nucleoproteins, no antiviral activity."; /evidence="ECO:0000269|PubMed:21962493"; MUTAGEN 645; /note="E->R: Loss of antiviral activity towards CCHFV and LACV."; /evidence="ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:15047845
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000269|PubMed:16009940}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
10942113
uniprot
proteins
pubmed
11880649
uniprot
proteins
pubmed
14687945
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14752052
uniprot
proteins
pubmed
15047845
uniprot
proteins
pubmed
15355513
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15757897
uniprot
proteins
pubmed
16009940
uniprot
proteins
pubmed
16202617
uniprot
proteins
pubmed
16413306
uniprot
proteins
pubmed
16978069
uniprot
proteins
pubmed
17374778
uniprot
proteins
pubmed
18062906
uniprot
proteins
pubmed
18668195
uniprot
proteins
pubmed
19109387
uniprot
proteins
pubmed
20428112
uniprot
proteins
pubmed
20538602
uniprot
proteins
pubmed
20603636
uniprot
proteins
pubmed
21166595
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2154602
uniprot
proteins
pubmed
2161946
uniprot
proteins
pubmed
21859714
uniprot
proteins
pubmed
21900240
uniprot
proteins
pubmed
21962493
uniprot
proteins
pubmed
21992152
uniprot
proteins
pubmed
2481229
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
2607176
uniprot
proteins
pubmed
8411374
uniprot
proteins
pubmed
9060610
uniprot
proteins
pubmed
9933640
uniprot
proteins
sequence_length
662
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11880649, ECO:0000269|PubMed:21859714, ECO:0000269|PubMed:21992152, ECO:0000269|PubMed:9060610}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15355513, ECO:0000269|PubMed:16413306, ECO:0000269|PubMed:21992152}; Peripheral membrane protein {ECO:0000269|PubMed:16413306}; Cytoplasmic side. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15047845}. Note=Binds preferentially to negatively charged phospholipids (PubMed:21900240). Colocalizes with CCHFV protein N in the perinuclear region (PubMed:15047845). {ECO:0000269|PubMed:15047845, ECO:0000269|PubMed:21900240}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:20603636}. Nucleus {ECO:0000269|PubMed:20603636}. Note=Translocates into the nuclei of HSV-1 infected cells (PubMed:20603636). {ECO:0000269|PubMed:20603636}.
uniprot
proteins