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Protein

Interferon-induced GTP-binding protein Mx1

Gene

MX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)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
  • microtubule binding Source: GO_Central

GO - Biological processi

  • apoptotic process Source: ProtInc
  • defense response Source: ProtInc
  • defense response to virus Source: GO_Central
  • innate immune response Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
  • organelle fission Source: GO_Central
  • response to type I interferon Source: UniProtKB
  • response to virus Source: UniProtKB
  • signal transduction Source: ProtInc
  • 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

BioCyciZFISH:ENSG00000157601-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-909733. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:7532. MX1.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • nuclear membrane Source: HPA
  • nucleus Source: GO_Central
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

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.
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

WithEntry#Exp.IntActNotes
CAB39LQ9H9S43EBI-929476,EBI-1047244
SIAH1Q8IUQ43EBI-929476,EBI-747107
TRPC3Q135072EBI-929476,EBI-520807
TRPC4Q9UBN42EBI-929476,EBI-929504
TRPC6Q9Y2104EBI-929476,EBI-929362

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110684. 36 interactors.
DIPiDIP-35694N.
IntActiP20591. 13 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
Helixi194 – 206Combined sources13
Beta strandi208 – 210Combined sources3
Beta strandi211 – 218Combined sources8
Helixi223 – 225Combined sources3
Helixi227 – 235Combined sources9
Beta strandi240 – 247Combined sources8
Helixi249 – 251Combined sources3
Beta strandi252 – 256Combined sources5
Helixi257 – 264Combined sources8
Beta strandi267 – 269Combined sources3
Beta strandi275 – 277Combined sources3
Helixi283 – 287Combined sources5
Helixi292 – 304Combined sources13
Turni307 – 309Combined sources3
Helixi310 – 314Combined sources5
Helixi320 – 338Combined sources19
Turni339 – 341Combined sources3
Helixi342 – 358Combined sources17
Helixi367 – 390Combined sources24
Helixi403 – 437Combined sources35
Beta strandi444 – 446Combined sources3
Helixi451 – 463Combined sources13
Helixi466 – 492Combined sources27
Helixi496 – 528Combined sources33
Helixi574 – 604Combined sources31
Helixi606 – 618Combined sources13
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[»]
ProteinModelPortaliP20591.
SMRiP20591.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20591.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 340GTPase domain (Globular)Add BLAST272
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

Contains 1 GED domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000213785.
HOVERGENiHBG008788.
InParanoidiP20591.
KOiK14754.
OMAiLHTVTDM.
OrthoDBiEOG091G080G.
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.
IPR030381. G_DYNAMIN_dom.
IPR003130. GED.
IPR020850. GED_dom.
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. 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 → I.6 PublicationsCorresponds to variant rs469390dbSNPEnsembl.1
Natural variantiVAR_034116381A → V.Corresponds to variant rs34717738dbSNPEnsembl.1
Natural variantiVAR_034117611Q → H.Corresponds to variant rs2230454dbSNPEnsembl.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

Cross-referencesi

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.

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[»]
ProteinModelPortaliP20591.
SMRiP20591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110684. 36 interactors.
DIPiDIP-35694N.
IntActiP20591. 13 interactors.
STRINGi9606.ENSP00000381599.

PTM databases

iPTMnetiP20591.
PhosphoSitePlusiP20591.

Polymorphism and mutation databases

BioMutaiMX1.
DMDMi251757499.

Proteomic databases

EPDiP20591.
MaxQBiP20591.
PaxDbiP20591.
PeptideAtlasiP20591.
PRIDEiP20591.

Protocols and materials databases

DNASUi4599.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi4599.
DisGeNETi4599.
GeneCardsiMX1.
H-InvDBHIX0027784.
HGNCiHGNC:7532. MX1.
HPAiHPA030917.
HPA049724.
MIMi147150. gene.
neXtProtiNX_P20591.
OpenTargetsiENSG00000157601.
PharmGKBiPA31333.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157601-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-909733. Interferon alpha/beta signaling.

Miscellaneous databases

ChiTaRSiMX1. human.
EvolutionaryTraceiP20591.
GeneWikiiMX1.
GenomeRNAii4599.
PROiP20591.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157601.
CleanExiHS_MX1.
ExpressionAtlasiP20591. baseline and differential.
GenevisibleiP20591. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000375. 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.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 161 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.