FUS_MOUSE - dbPTM
FUS_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUS_MOUSE
UniProt AC P56959
Protein Name RNA-binding protein FUS
Gene Name Fus
Organism Mus musculus (Mouse).
Sequence Length 518
Subcellular Localization Nucleus.
Protein Description Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity (By similarity)..
Protein Sequence MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYGQSADTSGYGQSSYGSSYGQTQNTGYGTQSAPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGGSSQSSSYGQPQSGGYGQQSGYGGQQQSYGQQQSSYNPPQGYGQQNQYNSSSGGGGGGGGGNYGQDQSSMSGGGGGGGYGNQDQSGGGGGGYGGGQQDRGGRGRGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY
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
217Asymmetric dimethylarginineGQQDRGGRGRGGGGG
CCCCCCCCCCCCCCC		34.16-
217MethylationGQQDRGGRGRGGGGG
CCCCCCCCCCCCCCC		34.162617643
219Asymmetric dimethylarginineQDRGGRGRGGGGGYN
CCCCCCCCCCCCCCC		38.94-
219MethylationQDRGGRGRGGGGGYN
CCCCCCCCCCCCCCC		38.9418935173
227MethylationGGGGGYNRSSGGYEP
CCCCCCCCCCCCCCC		24.5816287775
235Asymmetric dimethylarginineSSGGYEPRGRGGGRG
CCCCCCCCCCCCCCC		35.19-
235MethylationSSGGYEPRGRGGGRG
CCCCCCCCCCCCCCC		35.1930759973
237Asymmetric dimethylarginineGGYEPRGRGGGRGGR
CCCCCCCCCCCCCCC		41.69-
237MethylationGGYEPRGRGGGRGGR
CCCCCCCCCCCCCCC		41.6954540521
241Asymmetric dimethylargininePRGRGGGRGGRGGMG
CCCCCCCCCCCCCCC		47.90-
241MethylationPRGRGGGRGGRGGMG
CCCCCCCCCCCCCCC		47.9082797545
244Asymmetric dimethylarginineRGGGRGGRGGMGGSD
CCCCCCCCCCCCCCC		41.12-
244MethylationRGGGRGGRGGMGGSD
CCCCCCCCCCCCCCC		41.1254540505
252MethylationGGMGGSDRGGFNKFG
CCCCCCCCCCCCCCC		49.1624395515
252Asymmetric dimethylarginineGGMGGSDRGGFNKFG
CCCCCCCCCCCCCCC		49.16-
266PhosphorylationGGPRDQGSRHDSEQD
CCCCCCCCCCCCCCC		22.3225266776
270PhosphorylationDQGSRHDSEQDNSDN
CCCCCCCCCCCCCCC		30.9121149613
275PhosphorylationHDSEQDNSDNNTIFV
CCCCCCCCCCCEEEE		50.4325293948
279PhosphorylationQDNSDNNTIFVQGLG
CCCCCCCEEEEECCC		23.2625293948
305MalonylationFKQIGIIKTNKKTGQ
HHHCCEEECCCCCCC		44.0926320211
309UbiquitinationGIIKTNKKTGQPMIN
CEEECCCCCCCCCEE		61.02-
309MalonylationGIIKTNKKTGQPMIN
CEEECCCCCCCCCEE		61.0226320211
325AcetylationYTDRETGKLKGEATV
EECCCCCCCCCEEEE		55.2123236377
327AcetylationDRETGKLKGEATVSF
CCCCCCCCCEEEEEC		59.1822826441
327UbiquitinationDRETGKLKGEATVSF
CCCCCCCCCEEEEEC		59.1822790023
331PhosphorylationGKLKGEATVSFDDPP
CCCCCEEEEECCCCC		16.6328066266
333PhosphorylationLKGEATVSFDDPPSA
CCCEEEEECCCCCCC		20.7130635358
339PhosphorylationVSFDDPPSAKAAIDW
EECCCCCCCCEEEEE		48.0328066266
341UbiquitinationFDDPPSAKAAIDWFD
CCCCCCCCEEEEECC		42.5622790023
350AcetylationAIDWFDGKEFSGNPI
EEEECCCCCCCCCCE		58.3822826441
350UbiquitinationAIDWFDGKEFSGNPI
EEEECCCCCCCCCCE		58.3822790023
353PhosphorylationWFDGKEFSGNPIKVS
ECCCCCCCCCCEEEE		38.4625338131
358UbiquitinationEFSGNPIKVSFATRR
CCCCCCEEEEEEECC		32.8422790023
370Asymmetric dimethylarginineTRRADFNRGGGNGRG
ECCCCCCCCCCCCCC		45.16-
370MethylationTRRADFNRGGGNGRG
ECCCCCCCCCCCCCC		45.16-
376MethylationNRGGGNGRGGRGRGG
CCCCCCCCCCCCCCC		48.68-
376Asymmetric dimethylarginineNRGGGNGRGGRGRGG
CCCCCCCCCCCCCCC		48.68-
379MethylationGGNGRGGRGRGGPMG
CCCCCCCCCCCCCCC		34.16-
379Asymmetric dimethylarginineGGNGRGGRGRGGPMG
CCCCCCCCCCCCCCC		34.16-
381Asymmetric dimethylarginineNGRGGRGRGGPMGRG
CCCCCCCCCCCCCCC		45.60-
381MethylationNGRGGRGRGGPMGRG
CCCCCCCCCCCCCCC		45.60-
387MethylationGRGGPMGRGGYGGGG
CCCCCCCCCCCCCCC		29.1624129315
387Asymmetric dimethylarginineGRGGPMGRGGYGGGG
CCCCCCCCCCCCCCC		29.16-
390PhosphorylationGPMGRGGYGGGGSGG
CCCCCCCCCCCCCCC		18.5430165576
395PhosphorylationGGYGGGGSGGGGRGG
CCCCCCCCCCCCCCC		37.2225890499
400MethylationGGSGGGGRGGFPSGG
CCCCCCCCCCCCCCC		45.3924129315
400Asymmetric dimethylarginineGGSGGGGRGGFPSGG
CCCCCCCCCCCCCCC		45.39-
405PhosphorylationGGRGGFPSGGGGGGG
CCCCCCCCCCCCCCC		48.0530165576
455PhosphorylationPGGGPGGSHMGGNYG
CCCCCCCCCCCCCCC		19.0629514104
461PhosphorylationGSHMGGNYGDDRRGR
CCCCCCCCCCCCCCC		25.80-
466MethylationGNYGDDRRGRGGYDR
CCCCCCCCCCCCCCC		46.27-
466Asymmetric dimethylarginineGNYGDDRRGRGGYDR
CCCCCCCCCCCCCCC		46.27-
468Asymmetric dimethylarginineYGDDRRGRGGYDRGG
CCCCCCCCCCCCCCC		33.29-
468MethylationYGDDRRGRGGYDRGG
CCCCCCCCCCCCCCC		33.29-
473Asymmetric dimethylarginineRGRGGYDRGGYRGRG
CCCCCCCCCCCCCCC		31.77-
473MethylationRGRGGYDRGGYRGRG
CCCCCCCCCCCCCCC		31.77-
477MethylationGYDRGGYRGRGGDRG
CCCCCCCCCCCCCCC		31.44-
477Asymmetric dimethylarginineGYDRGGYRGRGGDRG
CCCCCCCCCCCCCCC		31.44-
479Asymmetric dimethylarginineDRGGYRGRGGDRGGF
CCCCCCCCCCCCCCC		36.60-
479MethylationDRGGYRGRGGDRGGF
CCCCCCCCCCCCCCC		36.60-
483Asymmetric dimethylarginineYRGRGGDRGGFRGGR
CCCCCCCCCCCCCCC		50.86-
483MethylationYRGRGGDRGGFRGGR
CCCCCCCCCCCCCCC		50.86-
487Asymmetric dimethylarginineGGDRGGFRGGRGGGD
CCCCCCCCCCCCCCC		50.35-
487MethylationGGDRGGFRGGRGGGD
CCCCCCCCCCCCCCC		50.35-
490MethylationRGGFRGGRGGGDRGG
CCCCCCCCCCCCCCC		43.33-
490Asymmetric dimethylarginineRGGFRGGRGGGDRGG
CCCCCCCCCCCCCCC		43.33-
495Asymmetric dimethylarginineGGRGGGDRGGFGPGK
CCCCCCCCCCCCCCC		50.86-
495MethylationGGRGGGDRGGFGPGK
CCCCCCCCCCCCCCC		50.8616288429
505PhosphorylationFGPGKMDSRGEHRQD
CCCCCCCCCCCCCCC		38.3925521595
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 FUS_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FUS_MOUSE !!
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 FUS_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRS10_MOUSESrsf10physical
9774382
SRSF2_MOUSESrsf2physical
9774382
DSRAD_HUMANADARphysical
26496610
DDX1_HUMANDDX1physical
26496610
DDX3X_HUMANDDX3Xphysical
26496610
DDX5_HUMANDDX5physical
26496610
DHX9_HUMANDHX9physical
26496610
ROA1_HUMANHNRNPA1physical
26496610
ROA2_HUMANHNRNPA2B1physical
26496610
HNRH3_HUMANHNRNPH3physical
26496610
HNRPK_HUMANHNRNPKphysical
26496610
HNRPL_HUMANHNRNPLphysical
26496610
ILF3_HUMANILF3physical
26496610
ITPR1_HUMANITPR1physical
26496610
HNRPM_HUMANHNRNPMphysical
26496610
NRDC_HUMANNRD1physical
26496610
PP1A_HUMANPPP1CAphysical
26496610
PCP_HUMANPRCPphysical
26496610
RBM3_HUMANRBM3physical
26496610
SAFB1_HUMANSAFBphysical
26496610
RBP56_HUMANTAF15physical
26496610
TNK1_HUMANTNK1physical
26496610
ABC3B_HUMANAPOBEC3Bphysical
26496610
SAFB2_HUMANSAFB2physical
26496610
HNRDL_HUMANHNRNPDLphysical
26496610
RBM6_HUMANRBM6physical
26496610
HNRPR_HUMANHNRNPRphysical
26496610
RBM14_HUMANRBM14physical
26496610
DDX17_HUMANDDX17physical
26496610
KHDR1_HUMANKHDRBS1physical
26496610
ROA0_HUMANHNRNPA0physical
26496610
HNRL1_HUMANHNRNPUL1physical
26496610
FA98A_HUMANFAM98Aphysical
26496610
TRUB2_HUMANTRUB2physical
26496610
RBMX_HUMANRBMXphysical
26496610
ZN638_HUMANZNF638physical
26496610
NIN_HUMANNINphysical
26496610
PPHLN_HUMANPPHLN1physical
26496610
KI16B_HUMANKIF16Bphysical
26496610
YLPM1_HUMANYLPM1physical
26496610
NCOA5_HUMANNCOA5physical
26496610
SLTM_HUMANSLTMphysical
26496610
ROA3_HUMANHNRNPA3physical
26496610
ZN326_HUMANZNF326physical
26496610
RB12B_HUMANRBM12Bphysical
26496610
RMXL1_HUMANRBMXL1physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FUS_MOUSE

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