MATR3_MOUSE - dbPTM
MATR3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MATR3_MOUSE
UniProt AC Q8K310
Protein Name Matrin-3
Gene Name Matr3
Organism Mus musculus (Mouse).
Sequence Length 846
Subcellular Localization Nucleus matrix .
Protein Description May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs (By similarity).; May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. May bind to specific miRNA hairpins (By similarity)..
Protein Sequence MSKSFQQSSLGRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDTDQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNKEWSQHINGASHSRRCQLLLEIYPEWNPDNDTGHTMGDPFMLQQSTNPAPGILGPPPPSFHLGGPAVGPRGNLGAGNGNLQGPRHMQKGRVETSRVVHIMDFQRGKNLRYQLLQLVEPFGVISNHLILNKINEAFIEMATTEDAQAAVDYYTTTPALVFGKPVRVHLSQKYKRIKKPEGKPDQKFDQKQELGRVIHLSNLPHSGYSDSAVLKLAEPYGKIKNYILMRMKSQAFIEMETREDAMAMVDHCLKKALWFQGRCVKVDLSEKYKKLVLRIPNRGIDLLKKDKSRKRSYSPDGKESPSDKKSKTDAQKTESPAEGKEQEEKSGEDGEKDTKDDQTEQEPSMLLESEDELLVDEEEAAALLESGSSVGDETDLANLGDVSSDGKKEPSDKAVKKDPSASATSKKKLKKVDKIEELDQENEAALENGIKNEENTEPGAESAENADDPNKDTSENADGQNDENKEDYTIPDEYRIGPYQPNVPVGIDYVIPKTGFYCKLCSLFYTNEEVAKNTHCSSLPHYQKLKKFLNKLAEERRQKKET
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
2Phosphorylation------MSKSFQQSS
------CCCCCCCHH		36.6930635358
2Acetylation------MSKSFQQSS
------CCCCCCCHH		36.69-
3Acetylation-----MSKSFQQSSL
-----CCCCCCCHHC		54.7323806337
4Phosphorylation----MSKSFQQSSLG
----CCCCCCCHHCC		22.4521082442
8PhosphorylationMSKSFQQSSLGRDSQ
CCCCCCCHHCCCCCC		19.4229472430
9PhosphorylationSKSFQQSSLGRDSQG
CCCCCCHHCCCCCCC		30.4229472430
14PhosphorylationQSSLGRDSQGHGRDL
CHHCCCCCCCCCCCC		36.3827681418
22PhosphorylationQGHGRDLSAAGIGLL
CCCCCCCHHHHHHHH		21.9920415495
37PhosphorylationAAATQSLSMPASLGR
HHHHHHHCCCHHHCC		28.15-
41PhosphorylationQSLSMPASLGRMNQG
HHHCCCHHHCCCCHH		26.03-
98PhosphorylationSRGPLPLSSQHRGDT
CCCCCCCCCCCCCCC		26.4728066266
99PhosphorylationRGPLPLSSQHRGDTD
CCCCCCCCCCCCCCH		37.3728066266
118PhosphorylationILASFGLSARDLDEL
HHHHCCCCHHCHHHH		22.95-
126PhosphorylationARDLDELSRYPEDKI
HHCHHHHHCCCCCCC		27.93-
132UbiquitinationLSRYPEDKITPENLP
HHCCCCCCCCHHHHH		46.98-
146AcetylationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC		30.7922826441
146UbiquitinationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC		30.79-
150PhosphorylationLQLKRRRTEEGPTLS
HHHHHHCCCCCCCCC		36.2623527152
155PhosphorylationRRTEEGPTLSYGRDG
HCCCCCCCCCCCCCC		38.9128833060
157PhosphorylationTEEGPTLSYGRDGRS
CCCCCCCCCCCCCCC		28.1922006019
158PhosphorylationEEGPTLSYGRDGRSA
CCCCCCCCCCCCCCC		21.20-
164PhosphorylationSYGRDGRSATREPPY
CCCCCCCCCCCCCCC		39.2526824392
166PhosphorylationGRDGRSATREPPYRV
CCCCCCCCCCCCCCC		36.4925266776
171PhosphorylationSATREPPYRVPRDDW
CCCCCCCCCCCCCCH		34.6529899451
188PhosphorylationKRHFRRDSFDDRGPS
HHHHCCCCCCCCCCC		28.8524925903
195PhosphorylationSFDDRGPSLNPVLDY
CCCCCCCCCCCCCCC		43.5325521595
202PhosphorylationSLNPVLDYDHGSRSQ
CCCCCCCCCCCCCCC		12.9924925903
206PhosphorylationVLDYDHGSRSQESGY
CCCCCCCCCCCCCCC		25.9124925903
208PhosphorylationDYDHGSRSQESGYYD
CCCCCCCCCCCCCCC		39.7425521595
211PhosphorylationHGSRSQESGYYDRMD
CCCCCCCCCCCCCCC		25.1821082442
213PhosphorylationSRSQESGYYDRMDYE
CCCCCCCCCCCCCCC		16.0923737553
214PhosphorylationRSQESGYYDRMDYED
CCCCCCCCCCCCCCC		10.7026643407
219PhosphorylationGYYDRMDYEDDRLRD
CCCCCCCCCCCCCCC		16.3525159016
234PhosphorylationGERCRDDSFFGETSH
CCCCCCCCCCCCCCC		27.1125159016
240PhosphorylationDSFFGETSHNYHKFD
CCCCCCCCCCCCCCC		12.8725266776
248PhosphorylationHNYHKFDSEYERMGR
CCCCCCCHHHHHCCC		45.2526525534
250PhosphorylationYHKFDSEYERMGRGP
CCCCCHHHHHCCCCC		16.8825367039
264PhosphorylationPGPLQERSLFEKKRG
CCCHHHHHHHHHHCC		36.3429899451
275PhosphorylationKKRGAPPSSNIEDFH
HHCCCCCCCCHHHHH		34.65-
391AcetylationQGPRHMQKGRVETSR
CCCCCCCCCCEEEEE		40.906569395
426PhosphorylationVEPFGVISNHLILNK
HHHHCHHCCHHHHHH		18.7822802335
443PhosphorylationEAFIEMATTEDAQAA
HHHHHHHCCCCHHHH		29.4322802335
444PhosphorylationAFIEMATTEDAQAAV
HHHHHHCCCCHHHHH		23.4822802335
453PhosphorylationDAQAAVDYYTTTPAL
CHHHHHHHHCCCHHH		8.9822802335
454PhosphorylationAQAAVDYYTTTPALV
HHHHHHHHCCCHHHH		7.9822802335
455PhosphorylationQAAVDYYTTTPALVF
HHHHHHHCCCHHHHC		20.2622802335
456PhosphorylationAAVDYYTTTPALVFG
HHHHHHCCCHHHHCC		18.0522802335
457PhosphorylationAVDYYTTTPALVFGK
HHHHHCCCHHHHCCC		9.9622802335
471PhosphorylationKPVRVHLSQKYKRIK
CCEEEEHHHHHHCCC		15.1122802335
474PhosphorylationRVHLSQKYKRIKKPE
EEEHHHHHHCCCCCC		9.62-
491AcetylationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE		47.8123806337
491UbiquitinationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE		47.81-
491MalonylationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE		47.8126320211
501PhosphorylationLGRVIHLSNLPHSGY
HHCEEEHHCCCCCCC		23.3519854140
509PhosphorylationNLPHSGYSDSAVLKL
CCCCCCCCHHHHHHH		28.72-
511PhosphorylationPHSGYSDSAVLKLAE
CCCCCCHHHHHHHHC		17.8426370283
515UbiquitinationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH		38.77-
515AcetylationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH		38.7722826441
522SuccinylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH		44.6723806337
522MalonylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH		44.6726320211
522AcetylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH		44.6723806337
522UbiquitinationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH		44.67-
526PhosphorylationPYGKIKNYILMRMKS
CCCHHHHHHHHHHHH		7.1629109428
533PhosphorylationYILMRMKSQAFIEME
HHHHHHHHCCEEEEC		19.8725521595
555UbiquitinationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE		35.44-
555MalonylationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE		35.4426320211
565MalonylationWFQGRCVKVDLSEKY
HHCCEEEEEECHHHH		33.3926320211
571AcetylationVKVDLSEKYKKLVLR
EEEECHHHHHHHHHH		60.02-
592PhosphorylationDLLKKDKSRKRSYSP
HHHHHCCCCCCCCCC		53.84-
596PhosphorylationKDKSRKRSYSPDGKE
HCCCCCCCCCCCCCC		32.7625521595
597PhosphorylationDKSRKRSYSPDGKES
CCCCCCCCCCCCCCC		28.4025521595
598PhosphorylationKSRKRSYSPDGKESP
CCCCCCCCCCCCCCC		20.1227087446
604PhosphorylationYSPDGKESPSDKKSK
CCCCCCCCCCCCCCC		32.9426824392
606PhosphorylationPDGKESPSDKKSKTD
CCCCCCCCCCCCCCC		71.9327742792
610PhosphorylationESPSDKKSKTDAQKT
CCCCCCCCCCCHHHC		46.6727717184
612PhosphorylationPSDKKSKTDAQKTES
CCCCCCCCCHHHCCC		43.5925159016
617PhosphorylationSKTDAQKTESPAEGK
CCCCHHHCCCCCCCH		29.6127087446
619PhosphorylationTDAQKTESPAEGKEQ
CCHHHCCCCCCCHHH		34.3425521595
630PhosphorylationGKEQEEKSGEDGEKD
CHHHHHHCCCCCCCC		51.1730352176
638PhosphorylationGEDGEKDTKDDQTEQ
CCCCCCCCCCCCCCC		47.6520531401
643PhosphorylationKDTKDDQTEQEPSML
CCCCCCCCCCCHHHC		46.7820531401
648PhosphorylationDQTEQEPSMLLESED
CCCCCCHHHCCCCCC		22.7020531401
653PhosphorylationEPSMLLESEDELLVD
CHHHCCCCCCCEECC		50.7620531401
670PhosphorylationEAAALLESGSSVGDE
HHHHHHHCCCCCCCC		43.9020531401
672PhosphorylationAALLESGSSVGDETD
HHHHHCCCCCCCCCH		31.0020531401
673PhosphorylationALLESGSSVGDETDL
HHHHCCCCCCCCCHH		33.3820531401
678PhosphorylationGSSVGDETDLANLGD
CCCCCCCCHHHHHCC		40.8420531401
687PhosphorylationLANLGDVSSDGKKEP
HHHHCCCCCCCCCCC		27.7020531401
688PhosphorylationANLGDVSSDGKKEPS
HHHCCCCCCCCCCCC		50.6720531401
695PhosphorylationSDGKKEPSDKAVKKD
CCCCCCCCCCCCCCC		53.48-
706PhosphorylationVKKDPSASATSKKKL
CCCCCCCCCCCHHHH		36.1027149854
740PhosphorylationGIKNEENTEPGAESA
CCCCCCCCCCCHHHH		47.0029472430
746PhosphorylationNTEPGAESAENADDP
CCCCCHHHHHCCCCC		40.1125521595
757PhosphorylationADDPNKDTSENADGQ
CCCCCCCCCCCCCCC		39.2825521595
758PhosphorylationDDPNKDTSENADGQN
CCCCCCCCCCCCCCC		38.7027087446
835AcetylationKLKKFLNKLAEERRQ
HHHHHHHHHHHHHHH		51.7423806337
835UbiquitinationKLKKFLNKLAEERRQ
HHHHHHHHHHHHHHH		51.74-
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 MATR3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MATR3_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 MATR3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MATR3_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MATR3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND MASSSPECTROMETRY.
"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-188 AND SER-598, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-598, ANDMASS SPECTROMETRY.

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