P20591 (MX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Interferon-induced GTP-binding protein Mx1, N-terminally processed

Gene names

Name:

MX1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May regulate the calcium channel activity of TRPCs. Shows activity against influenza virus and VSV, a rhabdovirus. Ref.13
Subunit structure	Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7. Ref.13
Subcellular location	Cytoplasm Ref.12.
Induction	By interferons.
Sequence similarities	Belongs to the dynamin family. Contains 1 GED domain.

Ontologies

Keywords
Biological process	Antiviral defense
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	induction of apoptosis Traceable author statement. Source: ProtInc response to virus Inferred from electronic annotation. Source: UniProtKB-KW type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	GTP binding Traceable author statement. Source: ProtInc GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.13. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRPC3	Q13507	2	EBI-929476,EBI-520807
TRPC4	Q9UBN4	2	EBI-929476,EBI-929504
TRPC6	Q9Y210	4	EBI-929476,EBI-929362

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 662

662

Interferon-induced GTP-binding protein Mx1

PRO_0000382943

Initiator methionine

1

1

Removed; alternate Ref.8 Ref.9

Chain

2 – 662

661

Interferon-induced GTP-binding protein Mx1, N-terminally processed

PRO_0000206592

Regions

Domain

574 – 662

89

GED

Nucleotide binding

77 – 84

8

GTP Potential

Nucleotide binding

178 – 182

5

GTP Potential

Nucleotide binding

247 – 250

4

GTP Potential

Amino acid modifications

Modified residue

1

1

N-acetylmethionine; in Interferon-induced GTP-binding protein Mx1; alternate Ref.7

Modified residue

129

1

Phosphotyrosine Ref.14

Modified residue

451

1

Phosphotyrosine Ref.14

Natural variations

Natural variant

379

1

V → I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs469390 [ dbSNP | Ensembl ].

VAR_058010

Natural variant

381

1

A → V.
Corresponds to variant rs34717738 [ dbSNP | Ensembl ].

VAR_034116

Natural variant

611

1

Q → H.
Corresponds to variant rs2230454 [ dbSNP | Ensembl ].

VAR_034117

Experimental info

Mutagenesis

81

1

S → C: No effect on GTP-binding, nor on viral infection. Ref.11

Mutagenesis

83

1

K → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. Ref.11 Ref.13

Mutagenesis

83

1

K → M: Loss of GTP-binding. Loss of protection against viral infection. Ref.11 Ref.13

Mutagenesis

103

1

T → A: Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection. Ref.12 Ref.13

Mutagenesis

612

1

L → K: Loss of GTP-hydrolysis. No effect on GTP-binding, nor on potentiation of TRPC6 activity. Ref.13

Sequence conflict

164

1

L → R in AAA36337. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

662

Helix Strand Turn

Details...

Helix

367 – 390

24

Helix

403 – 423

21

Helix

427 – 437

11

Helix

451 – 463

13

Helix

466 – 492

27

Helix

496 – 515

20

Helix

519 – 528

10

Helix

574 – 604

31

Turn

605 – 607

3

Helix

611 – 618

8

Helix

623 – 625

3

Helix

626 – 629

4

Sequences

	Sequence		Length	Mass (Da)
	P20591 [UniParc]. Last modified July 7, 2009. Version 4. Checksum: 626A7DD946F89384	FASTA	662	75,520
	10 20 30 40 50 60 MVVSEVDIAK ADPAAASHPL LLNGDATVAQ KNPGSVAENN LCSQYEEKVR PCIDLIDSLR 70 80 90 100 110 120 ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKKLVNEDKW 130 140 150 160 170 180 RGKVSYQDYE IEISDASEVE KEINKAQNAI AGEGMGISHE LITLEISSRD VPDLTLIDLP 190 200 210 220 230 240 GITRVAVGNQ PADIGYKIKT LIKKYIQRQE TISLVVVPSN VDIATTEALS MAQEVDPEGD 250 260 270 280 290 300 RTIGILTKPD LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK 310 320 330 340 350 360 IFFENHPYFR DLLEEGKATV PCLAEKLTSE LITHICKSLP LLENQIKETH QRITEELQKY 370 380 390 400 410 420 GVDIPEDENE KMFFLIDKVN AFNQDITALM QGEETVGEED IRLFTRLRHE FHKWSTIIEN 430 440 450 460 470 480 NFQEGHKILS RKIQKFENQY RGRELPGFVN YRTFETIVKQ QIKALEEPAV DMLHTVTDMV 490 500 510 520 530 540 RLAFTDVSIK NFEEFFNLHR TAKSKIEDIR AEQEREGEKL IRLHFQMEQI VYCQDQVYRG 550 560 570 580 590 600 ALQKVREKEL EEEKKKKSWD FGAFQSSSAT DSSMEEIFQH LMAYHQEASK RISSHIPLII 610 620 630 640 650 660 QFFMLQTYGQ QLQKAMLQLL QDKDTYSWLL KERSDTSDKR KFLKERLARL TQARRRLAQF PG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2481229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 2154602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-379.
[3]	"Organization of the human MX1 gene." Tazi Ahnini R., Cork M., di Giovine F.S. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-379.
[4]	"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: 10830953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-379.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-379. Tissue: Uterus.
[7]	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, MASS SPECTROMETRY. Tissue: Prostatic carcinoma.
[8]	"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.
[9]	"Purification and characterization of a human Mx protein." Weitz G., Bekisz J., Zoon K., Arnheiter H. J. Interferon Res. 9:679-689(1989) [PubMed: 2607176] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.
[10]	"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: 2161946] [Abstract] Cited for: RESISTANCE TO INFLUENZA VIRUS AND VSV.
[11]	"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: 8411374] [Abstract] Cited for: MUTAGENESIS OF SER-81 AND LYS-83.
[12]	"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: 9060610] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THR-103.
[13]	"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: 15757897] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRPC1; TRPC3; TRPC4; TRPC5; TRPC6 AND TRPC7, MUTAGENESIS OF LYS-83; THR-103 AND LEU-612.
[14]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND TYR-451, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M30817 mRNA. Translation: AAA36337.1.
M33882 mRNA. Translation: AAA36458.1.
AF135187 Genomic DNA. Translation: AAD43063.1.
AL163285 Genomic DNA. Translation: CAB90556.1.
AL773577 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.
BC032602 mRNA. Translation: AAH32602.1.

IPI

IPI00167949.

PIR

A33481.

RefSeq

NP_001138397.1. NM_001144925.1.
NP_001171517.1. NM_001178046.1.
NP_002453.2. NM_002462.3.

UniGene

Hs.517307.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P20591.

SMR

P20591. Positions 47-657.

ModBase

Search...

Protein-protein interaction databases

IntAct

P20591. 9 interactions.

STRING

P20591.

PTM databases

PhosphoSite

P20591.

Polymorphism databases

DMDM

251757499.

Proteomic databases

PRIDE

P20591.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000398598; ENSP00000381599; ENSG00000157601.
ENST00000398600; ENSP00000381601; ENSG00000157601.
ENST00000455164; ENSP00000410523; ENSG00000157601.

GeneID

4599.

KEGG

hsa:4599.

UCSC

uc002yzi.1. human.

Organism-specific databases

CTD

4599.

GeneCards

GC21P042792.

H-InvDB

HIX0027784.

HGNC

HGNC:7532. MX1.

HPA

HPA030917.

MIM

147150. gene.

neXtProt

NX_P20591.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16755.

HOGENOM

HBG445127.

HOVERGEN

HBG008788.

InParanoid

P20591.

OMA

AVDMLHT.

OrthoDB

EOG495ZRP.

PhylomeDB

P20591.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P20591.

Bgee

P20591.

CleanEx

HS_MX1.

Genevestigator

P20591.

GermOnline

ENSG00000157601. Homo sapiens.

Family and domain databases

InterPro

IPR022812. Dynamin.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR015577. Interferon-induced_Mx.
[Graphical view]

KO

K14754.

PANTHER

PTHR11566:SF13. Interferon_mx. 1 hit.

Pfam

PF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]

PRINTS

PR00195. DYNAMIN.

SMART

SM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]

PROSITE

PS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

17684.

SOURCE

Search...

Entry information

Entry name

MX1_HUMAN

Accession

Primary (citable) accession number: P20591
Secondary accession number(s): D3DSI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 7, 2009
Last modified:	January 25, 2012
This is version 107 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.