VIR_MOUSE - dbPTM
VIR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIR_MOUSE
UniProt AC A2AIV2
Protein Name Protein virilizer homolog {ECO:0000305}
Gene Name Virma {ECO:0000312|MGI:MGI:1913435}
Organism Mus musculus (Mouse).
Sequence Length 1811
Subcellular Localization Nucleus speckle . Nucleus, nucleoplasm . Cytoplasm . Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus (PubMed:29547716).
Protein Description Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs in the 3'-UTR near the stop codon: recruits the catalytic core components METTL3 and METTL14, thereby guiding m6A methylation at specific sites. Required for mRNA polyadenylation via its role in selective m6A methylation: m6A methylation of mRNAs in the 3'-UTR near the stop codon correlating with alternative polyadenylation (APA)..
Protein Sequence MAVDSSMELLFLDTFKHPSAEQSSHIDVVRFPCVVYINEVRVIPPGVRAHSGLPDNRAYGETSPHTFQLDLFFNNVSKPSAPVFDRLGSLEYDENTSIIFRPNSKVNTDGLVLRGWYNCLTLAIYGSVDRVISHDRDSPPPPPPPPPPPQPQPTLKRNLKHADGEKEDQFNGSPPRPQPRGPRTPPGPPPPDDDEDDPMSLPVSGDKEEDVPHREDYFEPISPDRNSVPQEGQYSDEGEVEEEPQEEGEDDEDDVDVEEEEDEDEDDCHTVDSIPDDEEEDEEEEGEEDEEGEGDDGYEQISSDEDGIADLERETFKYPNFDVEYTPEDLASVPPMTYDPYDRELAPLLYFSCPYKTTFEIEISRMKDQGPDKENSGAVEASVKLTELLDLYQEDRGAKWVTALEEIPSLIIKGLSYLQLKNTEQDSLGQLVDWTMQALNLQVAFRQPIALNVRQLKAGTKLVTSLAECGAPGVTELLQAGVINVLFDLLFADHVSSSLKLNAFKALDSVISMTEGMEAFLRSTQNEKSGYQRLLELILLDQTVRVVTAGSAILQKCHFYEILSEIKRLGDHIAEKTSAVPNHSEPDQDTDAVLERANPDYENEVEASMDMDLLESSIISEGEIEKLTNLLEEVFHVMETAPHTMTQPPVKSFPTIARITGPPERDDPYPVLFRYLHSHHFLELVTLLLSIPITSAHQGVLQATKDVLKFLAQSQKGLLFFMSEYEATNLLIRALCHLYDQDEEEGLQSDGADDAFALWLQDSTQTLQCITELFSHFQRCTASEETDHSDLLGTLHNLYLITFNPVGRSAVGHVFSLDKNLQSLITLMEYYSKEALGDSKSKKSVAYNYACVLTLVVAQSSSGVQMLEQHAASLLKLCKADENNAKLQELGKWLEPLKNLRFEINCIPNLIEYVKQNIDNLMTAEGVGLTTALRVLCNVACPPPPVEGQQKDLKWNLAVIQLFSAEGMDTFIRVLQKLNSILTQPWRLHVNMGTTLHRVTTISMARCTLTLLKTMLTELLRGGSFEFKDMRVPSALVTLHMLLCSIPLSGRLDSDEQKIQNDIIDILLTFTQGVNEKLTISEETLANNTWSLMLKEVLSSILKVPEGFFSGLILLSELLPLPLPMQTTQVIEPHDISVALNTRKLWSMHLHVQAKLLQEIVRSFSGTTCQPIQHMLRRICVQLCDLASPTALLIMRTVLDLIVEDLQSTSEDKEKQYTSQTTRLLALLDALASHKACKLAILHLINGTIKGDERYAEIFQDLLALVRSPGDSVTRQQCVEYVTSILQSLCDQDIALILPSPSEGPASELEQLSNSLPSKELMTAICDCLLATLANSESSYNCLLTCVRTMMFLAEHDYGLFHLKSSLRKNSSALHSLLKRVVSTFSKDTGELASASLDFMRQILNADAMGCCGDDSGLMEVEGAHPPRTMSLNAAELKQLLQSKEESPESLFLELEKLVLEHSKDDDSLESLLDNVIGLKQMLESSGEPLPLSDQDVEPVLSAPESLQNLFNNRTAYVLADVMDDQLKSMWFTPFQAEEIDTDLDLVKVDLIELSEKCCSDFDLHSELERSFLSEPSSPGRSKTTKGFKLGKHKHETFITSSGKSEYIEPAKRAHVVPPPRGRGRGGFGQGIRPHDIFRQRKQNTSRPPSMHVDDFVAAESKEVVPQDGIPPPKRPLKVSQKISSRGGFSGNRGGRGAFHSQNRFFTPPASKGNYSRREGTRGSSWSAQNTPRGNYNESRGGQSNFNRGPLPPLRPLSSTGYRPSPRDRASRGRGGLGPSWASTNSGSGGSRGKFVSGGSGRGRHVRSFTR
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
2Acetylation------MAVDSSMEL
------CCCCCCCEE		25.73-
133PhosphorylationGSVDRVISHDRDSPP
CCCCCHHCCCCCCCC		19.2421082442
138PhosphorylationVISHDRDSPPPPPPP
HHCCCCCCCCCCCCC		39.9526824392
154PhosphorylationPPPQPQPTLKRNLKH
CCCCCCCCCCCCCCC		39.4024704852
173PhosphorylationKEDQFNGSPPRPQPR
CCCCCCCCCCCCCCC		32.6027087446
184PhosphorylationPQPRGPRTPPGPPPP
CCCCCCCCCCCCCCC		36.6525521595
200PhosphorylationDDEDDPMSLPVSGDK
CCCCCCCCCCCCCCC		34.6025293948
204PhosphorylationDPMSLPVSGDKEEDV
CCCCCCCCCCCCCCC		39.0625293948
217PhosphorylationDVPHREDYFEPISPD
CCCCCHHCCCCCCCC		12.7025293948
222PhosphorylationEDYFEPISPDRNSVP
HHCCCCCCCCCCCCC		31.3128973931
373AcetylationMKDQGPDKENSGAVE
CHHCCCCCCCCCCHH		63.036568231
376PhosphorylationQGPDKENSGAVEASV
CCCCCCCCCCHHHHH		29.2622871156
382PhosphorylationNSGAVEASVKLTELL
CCCCHHHHHHHHHHH		13.2822871156
392PhosphorylationLTELLDLYQEDRGAK
HHHHHHHHHHCCCCC		14.9922871156
416PhosphorylationSLIIKGLSYLQLKNT
HHHHHHCCEEEECCC		32.25-
417PhosphorylationLIIKGLSYLQLKNTE
HHHHHCCEEEECCCC		11.96-
584PhosphorylationTSAVPNHSEPDQDTD
CCCCCCCCCCCCCHH		58.4225619855
608PhosphorylationYENEVEASMDMDLLE
HHHCHHHHCCHHHHH		11.21-
892UbiquitinationAKLQELGKWLEPLKN
HHHHHHHHHHHHHHH		62.32-
913PhosphorylationCIPNLIEYVKQNIDN
CHHHHHHHHHHHHHH		13.12-
1371PhosphorylationKSSLRKNSSALHSLL
HHHHHCCHHHHHHHH		21.7427841257
1438UbiquitinationSLNAAELKQLLQSKE
CCCHHHHHHHHHCCC		30.33-
1517PhosphorylationLFNNRTAYVLADVMD
HCCCCHHHHHHHHCC		8.7222802335
1560PhosphorylationELSEKCCSDFDLHSE
HHHHHHCCCCCCCHH		51.27-
1571PhosphorylationLHSELERSFLSEPSS
CCHHHHHHHHCCCCC		22.5925619855
1574PhosphorylationELERSFLSEPSSPGR
HHHHHHHCCCCCCCC		45.5124925903
1577PhosphorylationRSFLSEPSSPGRSKT
HHHHCCCCCCCCCCC		45.1524925903
1578PhosphorylationSFLSEPSSPGRSKTT
HHHCCCCCCCCCCCC		41.9324925903
1582PhosphorylationEPSSPGRSKTTKGFK
CCCCCCCCCCCCCEE		40.0225266776
1645PhosphorylationFRQRKQNTSRPPSMH
HHHHHCCCCCCCCCC		24.5020531401
1646PhosphorylationRQRKQNTSRPPSMHV
HHHHCCCCCCCCCCH		50.7920531401
1650PhosphorylationQNTSRPPSMHVDDFV
CCCCCCCCCCHHHHH		24.9729514104
1674AcetylationQDGIPPPKRPLKVSQ
CCCCCCCCCCCCCCH		72.8619858985
1678AcetylationPPPKRPLKVSQKISS
CCCCCCCCCCHHHHH		42.3919858995
1707PhosphorylationHSQNRFFTPPASKGN
CCCCCCCCCCCCCCC		26.1726643407
1722MethylationYSRREGTRGSSWSAQ
CCCCCCCCCCCCCCC		54.5824129315
1740MethylationRGNYNESRGGQSNFN
CCCCCCCCCCCCCCC		47.2724129315
1740Asymmetric dimethylarginineRGNYNESRGGQSNFN
CCCCCCCCCCCCCCC		47.27-
1772MethylationSPRDRASRGRGGLGP
CHHCCCCCCCCCCCC		37.5324129315
1772Asymmetric dimethylarginineSPRDRASRGRGGLGP
CHHCCCCCCCCCCCC		37.53-
1774Asymmetric dimethylarginineRDRASRGRGGLGPSW
HCCCCCCCCCCCCCC		34.59-
1774MethylationRDRASRGRGGLGPSW
HCCCCCCCCCCCCCC		34.5924129315
1792Asymmetric dimethylarginineNSGSGGSRGKFVSGG
CCCCCCCCCCCCCCC		56.44-
1792MethylationNSGSGGSRGKFVSGG
CCCCCCCCCCCCCCC		56.4424129315
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 VIR_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIR_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 VIR_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VIR_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VIR_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.

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