MX1_HUMAN - dbPTM
MX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MX1_HUMAN
UniProt AC P20591
Protein Name Interferon-induced GTP-binding protein Mx1
Gene Name MX1
Organism Homo sapiens (Human).
Sequence Length 662
Subcellular Localization Cytoplasm . Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasm, perinuclear region . Binds preferentially to negatively charged phospholipids (PubMed:21900240). Colocalizes with CCHFV protein N in the perinucle
Protein Description 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..
Protein Sequence MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLLEEGKATVPCLAEKLTSELITHICKSLPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTIIENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQARRRLAQFPG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MVVSEVDI
-------CCCCEEEH		6.40-
4Phosphorylation----MVVSEVDIAKA
----CCCCEEEHHHC		22.0828355574
17PhosphorylationKADPAAASHPLLLNG
HCCHHHHCCCEEECC		22.4028348404
31UbiquitinationGDATVAQKNPGSVAE
CCCEECCCCCCCHHH		56.2022817900
35PhosphorylationVAQKNPGSVAENNLC
ECCCCCCCHHHCCHH		21.2923403867
52S-palmitoylationYEEKVRPCIDLIDSL
HHHHHHHHHHHHHHH		2.3729575903
58PhosphorylationPCIDLIDSLRALGVE
HHHHHHHHHHHCCCC		16.8628348404
80PhosphorylationIAVIGDQSSGKSSVL
EEEEECCCCCHHHHH		45.8827251275
83UbiquitinationIGDQSSGKSSVLEAL
EECCCCCHHHHHHHH		41.3222817900
84PhosphorylationGDQSSGKSSVLEALS
ECCCCCHHHHHHHHH		29.2420068231
85PhosphorylationDQSSGKSSVLEALSG
CCCCCHHHHHHHHHC		33.9220068231
91PhosphorylationSSVLEALSGVALPRG
HHHHHHHHCCCCCCC		37.9624719451
99PhosphorylationGVALPRGSGIVTRCP
CCCCCCCCCHHHCCH		26.9928857561
110UbiquitinationTRCPLVLKLKKLVNE
HCCHHHHHHHHHHCC		51.2722817900
112UbiquitinationCPLVLKLKKLVNEDK
CHHHHHHHHHHCCCC		42.3422817900
113UbiquitinationPLVLKLKKLVNEDKW
HHHHHHHHHHCCCCC		69.0122817900
119UbiquitinationKKLVNEDKWRGKVSY
HHHHCCCCCCCCCCC		32.3922817900
123UbiquitinationNEDKWRGKVSYQDYE
CCCCCCCCCCCCEEE		21.3122817900
125PhosphorylationDKWRGKVSYQDYEIE
CCCCCCCCCCEEEEE		22.1430108239
126PhosphorylationKWRGKVSYQDYEIEI
CCCCCCCCCEEEEEE		14.3730108239
129PhosphorylationGKVSYQDYEIEISDA
CCCCCCEEEEEECCH		11.8630108239
134PhosphorylationQDYEIEISDASEVEK
CEEEEEECCHHHHHH		17.8430108239
137PhosphorylationEIEISDASEVEKEIN
EEEECCHHHHHHHHH		47.3630108239
196PhosphorylationNQPADIGYKIKTLIK
CCCCCHHHHHHHHHH		15.18-
197UbiquitinationQPADIGYKIKTLIKK
CCCCHHHHHHHHHHH		32.2922817900
199UbiquitinationADIGYKIKTLIKKYI
CCHHHHHHHHHHHHH		32.8822817900
273UbiquitinationNLVFHLKKGYMIVKC
HHHHHHCCCEEEEEE		62.7321906983
279UbiquitinationKKGYMIVKCRGQQEI
CCCEEEEEECCCHHH		13.80-
291PhosphorylationQEIQDQLSLSEALQR
HHHHHHCCHHHHHHH		24.9828348404
308PhosphorylationIFFENHPYFRDLLEE
HHCCCCHHHHHHHHH		12.05-
317UbiquitinationRDLLEEGKATVPCLA
HHHHHHCCCHHHHHH		44.1322817900
337UbiquitinationELITHICKSLPLLEN
HHHHHHHHHHHHHHH		55.19-
359UbiquitinationRITEELQKYGVDIPE
HHHHHHHHHCCCCCC		57.50-
427UbiquitinationNNFQEGHKILSRKIQ
CCCHHHHHHHHHHHH		57.0822817900
430PhosphorylationQEGHKILSRKIQKFE
HHHHHHHHHHHHHHH		34.6928258704
432UbiquitinationGHKILSRKIQKFENQ
HHHHHHHHHHHHHHH		46.2221906983
435UbiquitinationILSRKIQKFENQYRG
HHHHHHHHHHHHHCC		59.1121906983
437UbiquitinationSRKIQKFENQYRGRE
HHHHHHHHHHHCCCC		50.9222817900
450UbiquitinationRELPGFVNYRTFETI
CCCCCCCCHHHHHHH		20.5022817900
451PhosphorylationELPGFVNYRTFETIV
CCCCCCCHHHHHHHH		13.0118083107
452UbiquitinationLPGFVNYRTFETIVK
CCCCCCHHHHHHHHH		27.9522817900
453PhosphorylationPGFVNYRTFETIVKQ
CCCCCHHHHHHHHHH		18.5728348404
456PhosphorylationVNYRTFETIVKQQIK
CCHHHHHHHHHHHHH		27.2127251275
459UbiquitinationRTFETIVKQQIKALE
HHHHHHHHHHHHHHC		32.4122817900
463UbiquitinationTIVKQQIKALEEPAV
HHHHHHHHHHCCCHH		42.4522817900
466UbiquitinationKQQIKALEEPAVDML
HHHHHHHCCCHHHHH		67.7925015289
490UbiquitinationAFTDVSIKNFEEFFN
HCCCCCCCCHHHHHH		48.3422817900
503UbiquitinationFNLHRTAKSKIEDIR
HHHHHHHHHHHHHHH		52.2322817900
505UbiquitinationLHRTAKSKIEDIRAE
HHHHHHHHHHHHHHH		49.7821906983
519UbiquitinationEQEREGEKLIRLHFQ
HHHHHHHHHHHHEEE		61.1325015289
558PhosphorylationEEEKKKKSWDFGAFQ
HHHHHHHCCCCCCCC		40.5328348404
578UbiquitinationDSSMEEIFQHLMAYH
CCCHHHHHHHHHHHH		4.1822817900
593PhosphorylationQEASKRISSHIPLII
HHHHHHHHHHHHHHH		21.6427174698
594PhosphorylationEASKRISSHIPLIIQ
HHHHHHHHHHHHHHH		24.0627174698
607PhosphorylationIQFFMLQTYGQQLQK
HHHHHHHHHHHHHHH		26.1727174698
608PhosphorylationQFFMLQTYGQQLQKA
HHHHHHHHHHHHHHH		10.4427174698
631UbiquitinationDTYSWLLKERSDTSD
HHHHHHHHHCCCCHH		49.2422817900
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MX1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAXX_HUMANDAXXphysical
11716541
SUMO1_HUMANSUMO1physical
11716541
PIAS1_HUMANPIAS1physical
11716541
SP100_HUMANSP100physical
11716541
BLM_HUMANBLMphysical
11716541
ISG15_HUMANISG15physical
16009940
A4_HUMANAPPphysical
21832049
MX1_HUMANMX1physical
25416956
SIAH1_HUMANSIAH1physical
25416956
CB39L_HUMANCAB39Lphysical
25416956
DAXX_HUMANDAXXphysical
25447205
TF65_HUMANRELAphysical
25447205
SUMO1_HUMANSUMO1physical
25447205
EPMIP_HUMANEPM2AIP1physical
25447205
MX1_HUMANMX1physical
25447205
ZBT16_HUMANZBTB16physical
25447205
UBC9_HUMANUBE2Iphysical
25447205
KI26B_HUMANKIF26Bphysical
25447205
ZN251_HUMANZNF251physical
25447205
C8AP2_HUMANCASP8AP2physical
25447205
ZN623_HUMANZNF623physical
25447205
PSD3_HUMANPSD3physical
25447205
ZCH12_HUMANZCCHC12physical
25447205
PIAS1_HUMANPIAS1physical
25447205
CBX4_HUMANCBX4physical
25447205
KLH35_HUMANKLHL35physical
25447205
CG025_HUMANC7orf25physical
25447205
CHD3_HUMANCHD3physical
25447205
ADRM1_HUMANADRM1physical
25447205
BRD7_HUMANBRD7physical
25447205
TDG_HUMANTDGphysical
25447205
PLRG1_HUMANPLRG1physical
25447205
TBA1A_HUMANTUBA1Aphysical
25447205
HMGX4_HUMANHMGXB4physical
25447205
MPCP_HUMANSLC25A3physical
25447205
LRC4B_HUMANLRRC4Bphysical
25447205
GMEB1_HUMANGMEB1physical
25447205
BCS1_HUMANBCS1Lphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MX1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND TYR-451, ANDMASS SPECTROMETRY.

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