EWS_MOUSE - dbPTM
EWS_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EWS_MOUSE
UniProt AC Q61545
Protein Name RNA-binding protein EWS
Gene Name Ewsr1
Organism Mus musculus (Mouse).
Sequence Length 655
Subcellular Localization Nucleus. Cytoplasm. Cell membrane. Relocates from cytoplasm to ribosomes upon PTK2B/FAK2 activation..
Protein Description Might function as a transcriptional repressor..
Protein Sequence MASTDYSTYSQAAAQQGYSAYTAQPTQGYAQTTQAYGQQSYGTYGQPTDVSYTQAQTTATYGQTAYATSYGQPPTGYSTPTAPQAYSQPVQGYGTGTYDSTTATVTTTQASYAAQTAYGTQPAYPTYGQQPTATAPTRPQDGNKPAETSQPQSSTGGYNQPSLGYGQSNYSYPQVPGSYPMQPVTAPPSYPPTSYSSSQPTSYDQSSYSQQNTYGQPSSYGQQSSYGQQSSYGQQPPTSYPPQTGSYSQAPSQYSQQSSSYGQQSSFRQDHPSSMGVYGQESGGFSGPGENRSLSGPDNRGRGRGGFDRGGMSRGGRGGGRGGLGAGERGGFNKPGGPMDEGPDLDLGLPIDPDEDSDNSAIYVQGLNDNVTLDDLADFFKQCGVVKMNKRTGQPMIHIYLDKETGKPKGDATVSYEDPPTAKAAVEWFDGKDFQGSKLKVSLARKKPPMNSMRGGMPPREGRGMPPPLRGGPGGPGGPGGPMGRMGGRGGDRGGFPPRGPRGSRGNPSGGGNVQHRAGDWQCPNPGCGNQNFAWRTECNQCKAPKPEGFLPPPFPPPGGDRGRGGPGGMRGGRGGLMDRGGPGGMFRGGRGGDRGGFRGGRGMDRGGFGGGRRGGPGGPPGPLMEQMGGRRGGRGGPGKMDKGEHRQERRDRPY
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
79PhosphorylationQPPTGYSTPTAPQAY
CCCCCCCCCCCCCCC
19.0419076070
266PhosphorylationSSYGQQSSFRQDHPS
CCCCCCCCCCCCCCC
21.80-
295PhosphorylationPGENRSLSGPDNRGR
CCCCCCCCCCCCCCC
49.9122871156
300MethylationSLSGPDNRGRGRGGF
CCCCCCCCCCCCCCC
43.49-
300Asymmetric dimethylarginineSLSGPDNRGRGRGGF
CCCCCCCCCCCCCCC
43.49-
302MethylationSGPDNRGRGRGGFDR
CCCCCCCCCCCCCCC
28.53-
302Asymmetric dimethylarginineSGPDNRGRGRGGFDR
CCCCCCCCCCCCCCC
28.53-
304Asymmetric dimethylargininePDNRGRGRGGFDRGG
CCCCCCCCCCCCCCC
40.47-
304MethylationPDNRGRGRGGFDRGG
CCCCCCCCCCCCCCC
40.47-
309Asymmetric dimethylarginineRGRGGFDRGGMSRGG
CCCCCCCCCCCCCCC
41.10-
309MethylationRGRGGFDRGGMSRGG
CCCCCCCCCCCCCCC
41.10-
314Asymmetric dimethylarginineFDRGGMSRGGRGGGR
CCCCCCCCCCCCCCC
42.57-
314MethylationFDRGGMSRGGRGGGR
CCCCCCCCCCCCCCC
42.57-
317MethylationGGMSRGGRGGGRGGL
CCCCCCCCCCCCCCC
43.33-
317Asymmetric dimethylarginineGGMSRGGRGGGRGGL
CCCCCCCCCCCCCCC
43.33-
321MethylationRGGRGGGRGGLGAGE
CCCCCCCCCCCCCCC
39.00-
321Asymmetric dimethylarginineRGGRGGGRGGLGAGE
CCCCCCCCCCCCCCC
39.00-
423UbiquitinationYEDPPTAKAAVEWFD
CCCCCCCCEEEEEEC
39.08-
432UbiquitinationAVEWFDGKDFQGSKL
EEEEECCCCCCCCEE
58.16-
438AcetylationGKDFQGSKLKVSLAR
CCCCCCCEEEEECCC
60.1823806337
442PhosphorylationQGSKLKVSLARKKPP
CCCEEEEECCCCCCC
18.0929176673
454MethylationKPPMNSMRGGMPPRE
CCCCCCCCCCCCCCC
38.03-
454Asymmetric dimethylarginineKPPMNSMRGGMPPRE
CCCCCCCCCCCCCCC
38.03-
463MethylationGMPPREGRGMPPPLR
CCCCCCCCCCCCCCC
33.22-
463Asymmetric dimethylarginineGMPPREGRGMPPPLR
CCCCCCCCCCCCCCC
33.22-
470MethylationRGMPPPLRGGPGGPG
CCCCCCCCCCCCCCC
54.5224129315
470Asymmetric dimethylarginineRGMPPPLRGGPGGPG
CCCCCCCCCCCCCCC
54.52-
485MethylationGPGGPMGRMGGRGGD
CCCCCCCCCCCCCCC
17.8324129315
489Asymmetric dimethylargininePMGRMGGRGGDRGGF
CCCCCCCCCCCCCCC
39.94-
489MethylationPMGRMGGRGGDRGGF
CCCCCCCCCCCCCCC
39.94-
493Asymmetric dimethylarginineMGGRGGDRGGFPPRG
CCCCCCCCCCCCCCC
50.86-
493MethylationMGGRGGDRGGFPPRG
CCCCCCCCCCCCCCC
50.86-
499Asymmetric dimethylarginineDRGGFPPRGPRGSRG
CCCCCCCCCCCCCCC
68.90-
499MethylationDRGGFPPRGPRGSRG
CCCCCCCCCCCCCCC
68.90-
502MethylationGFPPRGPRGSRGNPS
CCCCCCCCCCCCCCC
59.5524129315
502Asymmetric dimethylarginineGFPPRGPRGSRGNPS
CCCCCCCCCCCCCCC
59.55-
505MethylationPRGPRGSRGNPSGGG
CCCCCCCCCCCCCCC
52.2924129315
505Asymmetric dimethylargininePRGPRGSRGNPSGGG
CCCCCCCCCCCCCCC
52.29-
528GlutathionylationWQCPNPGCGNQNFAW
CCCCCCCCCCCCCEE
4.9524333276
562Asymmetric dimethylarginineFPPPGGDRGRGGPGG
CCCCCCCCCCCCCCC
39.73-
562MethylationFPPPGGDRGRGGPGG
CCCCCCCCCCCCCCC
39.73-
564Asymmetric dimethylargininePPGGDRGRGGPGGMR
CCCCCCCCCCCCCCC
48.03-
564MethylationPPGGDRGRGGPGGMR
CCCCCCCCCCCCCCC
48.03-
571MethylationRGGPGGMRGGRGGLM
CCCCCCCCCCCCCCC
47.92-
571Asymmetric dimethylarginineRGGPGGMRGGRGGLM
CCCCCCCCCCCCCCC
47.92-
574Asymmetric dimethylargininePGGMRGGRGGLMDRG
CCCCCCCCCCCCCCC
38.54-
574MethylationPGGMRGGRGGLMDRG
CCCCCCCCCCCCCCC
38.54-
580Asymmetric dimethylarginineGRGGLMDRGGPGGMF
CCCCCCCCCCCCCCC
37.69-
580MethylationGRGGLMDRGGPGGMF
CCCCCCCCCCCCCCC
37.69-
588Asymmetric dimethylarginineGGPGGMFRGGRGGDR
CCCCCCCCCCCCCCC
37.45-
588MethylationGGPGGMFRGGRGGDR
CCCCCCCCCCCCCCC
37.45-
591Asymmetric dimethylarginineGGMFRGGRGGDRGGF
CCCCCCCCCCCCCCC
49.06-
591MethylationGGMFRGGRGGDRGGF
CCCCCCCCCCCCCCC
49.06-
595MethylationRGGRGGDRGGFRGGR
CCCCCCCCCCCCCCC
50.86-
595Asymmetric dimethylarginineRGGRGGDRGGFRGGR
CCCCCCCCCCCCCCC
50.86-
599Asymmetric dimethylarginineGGDRGGFRGGRGMDR
CCCCCCCCCCCCCCC
50.35-
599MethylationGGDRGGFRGGRGMDR
CCCCCCCCCCCCCCC
50.35-
602MethylationRGGFRGGRGMDRGGF
CCCCCCCCCCCCCCC
39.84-
602Asymmetric dimethylarginineRGGFRGGRGMDRGGF
CCCCCCCCCCCCCCC
39.84-
606MethylationRGGRGMDRGGFGGGR
CCCCCCCCCCCCCCC
37.94-
606Asymmetric dimethylarginineRGGRGMDRGGFGGGR
CCCCCCCCCCCCCCC
37.94-
614MethylationGGFGGGRRGGPGGPP
CCCCCCCCCCCCCCC
58.6624129315
614Asymmetric dimethylarginineGGFGGGRRGGPGGPP
CCCCCCCCCCCCCCC
58.66-
632MethylationMEQMGGRRGGRGGPG
HHHCCCCCCCCCCCC
56.01-
632Asymmetric dimethylarginineMEQMGGRRGGRGGPG
HHHCCCCCCCCCCCC
56.01-
635Asymmetric dimethylarginineMGGRRGGRGGPGKMD
CCCCCCCCCCCCCCC
50.12-
635MethylationMGGRRGGRGGPGKMD
CCCCCCCCCCCCCCC
50.12-

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
266SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
266SPhosphorylation

-

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 EWS_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JARD2_MOUSEJarid2physical
20211142
MECP2_MOUSEMecp2physical
20211142
MTF2_MOUSEMtf2physical
20211142
PER1_MOUSEPer1physical
20211142
REST_MOUSERestphysical
20211142
RORG_MOUSERorcphysical
20211142
RPA1_MOUSEPolr1aphysical
20211142
KDM5D_MOUSEKdm5dphysical
20211142
SRBP1_MOUSESrebf1physical
20211142
PHF1_MOUSEPhf1physical
20211142
DEDD_MOUSEDeddphysical
20211142
UBIP1_MOUSEUbp1physical
20211142
ZFP42_MOUSEZfp42physical
20211142
ZN292_MOUSEZfp292physical
20211142
TRIP4_MOUSETrip4physical
20211142
ANR49_MOUSEAnkrd49physical
20211142
MED20_MOUSEMed20physical
20211142
SIR2_MOUSESirt2physical
20211142
ZDHC6_MOUSEZdhhc6physical
20211142
SYF1_MOUSEXab2physical
20211142
ANRA2_MOUSEAnkra2physical
20211142
RPC6_MOUSEPolr3fphysical
20211142
CERS5_MOUSECers5physical
20211142
ERCC8_MOUSEErcc8physical
20211142
MMS19_MOUSEMms19physical
20211142
NKD2_MOUSENkd2physical
20211142
ASB6_MOUSEAsb6physical
20211142
ANKR7_MOUSEAnkrd7physical
20211142
RAI14_MOUSERai14physical
20211142
CERS2_MOUSECers2physical
20211142
NKRF_MOUSENkrfphysical
20211142
ABTB1_MOUSEAbtb1physical
20211142
SMCA1_MOUSESmarca1physical
20211142
PWP1_MOUSEPwp1physical
20211142
CHD4_MOUSEChd4physical
20211142
TLE6_MOUSETle6physical
20211142
RFXAP_MOUSERfxapphysical
20211142
HDA10_MOUSEHdac10physical
20211142
ASH1L_MOUSEAsh1lphysical
20211142
ZSWM4_MOUSEZswim4physical
20211142
MED16_MOUSEMed16physical
20211142
SNPC4_MOUSESnapc4physical
20211142
RPB2_MOUSEPolr2bphysical
20211142
ZBT24_MOUSEZbtb24physical
20211142
ZFP82_MOUSEZfp82physical
20211142
K2C5_HUMANKRT5physical
26496610
MED24_HUMANMED24physical
26496610
ATG2A_HUMANATG2Aphysical
26496610
KLH12_HUMANKLHL12physical
26496610
NUD18_HUMANNUDT18physical
26496610
PRGC1_MOUSEPpargc1aphysical
25918410

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EWS_MOUSE

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Related Literatures of Post-Translational Modification

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