MATR3_HUMAN - dbPTM
MATR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MATR3_HUMAN
UniProt AC P43243
Protein Name Matrin-3
Gene Name MATR3
Organism Homo sapiens (Human).
Sequence Length 847
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. 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. [PubMed: 28712728 May bind to specific miRNA hairpins]
Protein Sequence MSKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDADQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNKEWSQHINGASHSRRCQLLLEIYPEWNPDNDTGHTMGDPFMLQQSTNPAPGILGPPPPSFHLGGPAVGPRGNLGAGNGNLQGPRHMQKGRVETSRVVHIMDFQRGKNLRYQLLQLVEPFGVISNHLILNKINEAFIEMATTEDAQAAVDYYTTTPALVFGKPVRVHLSQKYKRIKKPEGKPDQKFDQKQELGRVIHLSNLPHSGYSDSAVLKLAEPYGKIKNYILMRMKSQAFIEMETREDAMAMVDHCLKKALWFQGRCVKVDLSEKYKKLVLRIPNRGIDLLKKDKSRKRSYSPDGKESPSDKKSKTDGSQKTESSTEGKEQEEKSGEDGEKDTKDDQTEQEPNMLLESEDELLVDEEEAAALLESGSSVGDETDLANLGDVASDGKKEPSDKAVKKDGSASAAAKKKLKKVDKIEELDQENEAALENGIKNEENTEPGAESSENADDPNKDTSENADGQSDENKDDYTIPDEYRIGPYQPNVPVGIDYVIPKTGFYCKLCSLFYTNEEVAKNTHCSSLPHYQKLKKFLNKLAEERRQKKET
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------MSKSFQQSS
------CCHHHHHHH
36.6922814378
2Phosphorylation------MSKSFQQSS
------CCHHHHHHH
36.6923401153
3Sumoylation-----MSKSFQQSSL
-----CCHHHHHHHC
54.73-
3Acetylation-----MSKSFQQSSL
-----CCHHHHHHHC
54.7319608861
3Methylation-----MSKSFQQSSL
-----CCHHHHHHHC
54.7319608861
3Sumoylation-----MSKSFQQSSL
-----CCHHHHHHHC
54.7328112733
3Ubiquitination-----MSKSFQQSSL
-----CCHHHHHHHC
54.7319608861
4Phosphorylation----MSKSFQQSSLS
----CCHHHHHHHCC
22.4525159151
7Methylation-MSKSFQQSSLSRDS
-CCHHHHHHHCCCCC
32.74-
8PhosphorylationMSKSFQQSSLSRDSQ
CCHHHHHHHCCCCCC
23.5923401153
9PhosphorylationSKSFQQSSLSRDSQG
CHHHHHHHCCCCCCC
26.4823927012
11PhosphorylationSFQQSSLSRDSQGHG
HHHHHHCCCCCCCCC
35.6723401153
14PhosphorylationQSSLSRDSQGHGRDL
HHHCCCCCCCCCCCC
36.6323401153
22PhosphorylationQGHGRDLSAAGIGLL
CCCCCCCHHHHHHHH
21.9921082442
33O-linked_GlycosylationIGLLAAATQSLSMPA
HHHHHHHHHHHCCCH
17.6031373491
33PhosphorylationIGLLAAATQSLSMPA
HHHHHHHHHHHCCCH
17.6024732914
35PhosphorylationLLAAATQSLSMPASL
HHHHHHHHHCCCHHH
20.3228450419
37PhosphorylationAAATQSLSMPASLGR
HHHHHHHCCCHHHCC
28.1524732914
38SulfoxidationAATQSLSMPASLGRM
HHHHHHCCCHHHCCC
3.7928183972
41O-linked_GlycosylationQSLSMPASLGRMNQG
HHHCCCHHHCCCCHH
26.0331373491
41PhosphorylationQSLSMPASLGRMNQG
HHHCCCHHHCCCCHH
26.0326055452
49PhosphorylationLGRMNQGTARLASLM
HCCCCHHHHHHHHHH
9.9924173317
54PhosphorylationQGTARLASLMNLGMS
HHHHHHHHHHHHHCC
32.5128464451
61O-linked_GlycosylationSLMNLGMSSSLNQQG
HHHHHHCCCCCCHHC
18.2531373491
61PhosphorylationSLMNLGMSSSLNQQG
HHHHHHCCCCCCHHC
18.2530108239
62PhosphorylationLMNLGMSSSLNQQGA
HHHHHCCCCCCHHCH
29.9230108239
63PhosphorylationMNLGMSSSLNQQGAH
HHHHCCCCCCHHCHH
24.8328464451
71O-linked_GlycosylationLNQQGAHSALSSAST
CCHHCHHHHHHCCCC
30.3031373491
71PhosphorylationLNQQGAHSALSSAST
CCHHCHHHHHHCCCC
30.3028464451
74O-linked_GlycosylationQGAHSALSSASTSSH
HCHHHHHHCCCCCCC
24.4731373491
74PhosphorylationQGAHSALSSASTSSH
HCHHHHHHCCCCCCC
24.4726657352
75O-linked_GlycosylationGAHSALSSASTSSHN
CHHHHHHCCCCCCCC
27.3931373491
75PhosphorylationGAHSALSSASTSSHN
CHHHHHHCCCCCCCC
27.3926657352
77O-linked_GlycosylationHSALSSASTSSHNLQ
HHHHHCCCCCCCCHH
30.6731373491
77PhosphorylationHSALSSASTSSHNLQ
HHHHHCCCCCCCCHH
30.6726657352
78PhosphorylationSALSSASTSSHNLQS
HHHHCCCCCCCCHHH
33.6826657352
79PhosphorylationALSSASTSSHNLQSI
HHHCCCCCCCCHHHH
27.4026657352
80PhosphorylationLSSASTSSHNLQSIF
HHCCCCCCCCHHHHH
19.2428464451
85O-linked_GlycosylationTSSHNLQSIFNIGSR
CCCCCHHHHHCCCCC
32.1131373491
85PhosphorylationTSSHNLQSIFNIGSR
CCCCCHHHHHCCCCC
32.1120068231
91PhosphorylationQSIFNIGSRGPLPLS
HHHHCCCCCCCCCCC
30.2130108239
92MethylationSIFNIGSRGPLPLSS
HHHCCCCCCCCCCCC
45.6058854767
98PhosphorylationSRGPLPLSSQHRGDA
CCCCCCCCCCCCCCH
26.4720068231
99PhosphorylationRGPLPLSSQHRGDAD
CCCCCCCCCCCCCHH
37.3720068231
109PhosphorylationRGDADQASNILASFG
CCCHHHHHHHHHHCC
20.8320873877
114PhosphorylationQASNILASFGLSARD
HHHHHHHHCCCCHHC
19.1927732954
118PhosphorylationILASFGLSARDLDEL
HHHHCCCCHHCHHHH
22.9521712546
126PhosphorylationARDLDELSRYPEDKI
HHCHHHHHCCCCCCC
27.9320873877
128PhosphorylationDLDELSRYPEDKITP
CHHHHHCCCCCCCCH
13.9620090780
132SumoylationLSRYPEDKITPENLP
HHCCCCCCCCHHHHH
46.98-
1322-HydroxyisobutyrylationLSRYPEDKITPENLP
HHCCCCCCCCHHHHH
46.98-
132AcetylationLSRYPEDKITPENLP
HHCCCCCCCCHHHHH
46.9826051181
132SumoylationLSRYPEDKITPENLP
HHCCCCCCCCHHHHH
46.9828112733
132UbiquitinationLSRYPEDKITPENLP
HHCCCCCCCCHHHHH
46.9821906983
134PhosphorylationRYPEDKITPENLPQI
CCCCCCCCHHHHHHH
30.2325159151
146UbiquitinationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC
30.7921890473
146SumoylationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC
30.79-
1462-HydroxyisobutyrylationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC
30.79-
146AcetylationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC
30.7926051181
146SumoylationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC
30.7928112733
146UbiquitinationPQILLQLKRRRTEEG
HHHHHHHHHHCCCCC
30.7921906983
150PhosphorylationLQLKRRRTEEGPTLS
HHHHHHCCCCCCCCC
36.2621945579
155PhosphorylationRRTEEGPTLSYGRDG
HCCCCCCCCCCCCCC
38.9121945579
157PhosphorylationTEEGPTLSYGRDGRS
CCCCCCCCCCCCCCC
28.1921945579
158PhosphorylationEEGPTLSYGRDGRSA
CCCCCCCCCCCCCCC
21.2021945579
164PhosphorylationSYGRDGRSATREPPY
CCCCCCCCCCCCCCC
39.2523401153
166PhosphorylationGRDGRSATREPPYRV
CCCCCCCCCCCCCCC
36.4925159151
171PhosphorylationSATREPPYRVPRDDW
CCCCCCCCCCCCCCH
34.6517081983
181AcetylationPRDDWEEKRHFRRDS
CCCCHHHHHHHCCCC
39.3923749302
181UbiquitinationPRDDWEEKRHFRRDS
CCCCHHHHHHHCCCC
39.39-
185AcetylationWEEKRHFRRDSFDDR
HHHHHHHCCCCCCCC
35.0619608861
188PhosphorylationKRHFRRDSFDDRGPS
HHHHCCCCCCCCCCC
28.8529255136
192MethylationRRDSFDDRGPSLNPV
CCCCCCCCCCCCCCC
61.85115482655
195PhosphorylationSFDDRGPSLNPVLDY
CCCCCCCCCCCCCCC
43.5329255136
202NitrationSLNPVLDYDHGSRSQ
CCCCCCCCCCCCCCC
12.99-
202PhosphorylationSLNPVLDYDHGSRSQ
CCCCCCCCCCCCCCC
12.9923927012
206PhosphorylationVLDYDHGSRSQESGY
CCCCCCCCCCCCCCC
25.9129255136
208PhosphorylationDYDHGSRSQESGYYD
CCCCCCCCCCCCCCC
39.7425159151
211PhosphorylationHGSRSQESGYYDRMD
CCCCCCCCCCCCCCC
25.1823401153
213PhosphorylationSRSQESGYYDRMDYE
CCCCCCCCCCCCCCC
16.0921945579
214PhosphorylationRSQESGYYDRMDYED
CCCCCCCCCCCCCCC
10.7021945579
216MethylationQESGYYDRMDYEDDR
CCCCCCCCCCCCCCC
12.07115482687
219PhosphorylationGYYDRMDYEDDRLRD
CCCCCCCCCCCCCCC
16.3521945579
223MethylationRMDYEDDRLRDGERC
CCCCCCCCCCCCCCC
43.90115482671
230GlutathionylationRLRDGERCRDDSFFG
CCCCCCCCCCCCCCC
4.9422555962
234AcetylationGERCRDDSFFGETSH
CCCCCCCCCCCCCCC
27.1119608861
234PhosphorylationGERCRDDSFFGETSH
CCCCCCCCCCCCCCC
27.1123401153
234UbiquitinationGERCRDDSFFGETSH
CCCCCCCCCCCCCCC
27.1119608861
239PhosphorylationDDSFFGETSHNYHKF
CCCCCCCCCCCCCCC
35.3527794612
240PhosphorylationDSFFGETSHNYHKFD
CCCCCCCCCCCCCCC
12.8727794612
243PhosphorylationFGETSHNYHKFDSEY
CCCCCCCCCCCCHHH
10.8517081983
245SumoylationETSHNYHKFDSEYER
CCCCCCCCCCHHHHH
40.27-
245AcetylationETSHNYHKFDSEYER
CCCCCCCCCCHHHHH
40.2725825284
245SumoylationETSHNYHKFDSEYER
CCCCCCCCCCHHHHH
40.2728112733
245UbiquitinationETSHNYHKFDSEYER
CCCCCCCCCCHHHHH
40.27-
248PhosphorylationHNYHKFDSEYERMGR
CCCCCCCHHHHHCCC
45.2523401153
250PhosphorylationYHKFDSEYERMGRGP
CCCCCHHHHHCCCCC
16.8825884760
255MethylationSEYERMGRGPGPLQE
HHHHHCCCCCCCHHH
38.50115482679
264PhosphorylationPGPLQERSLFEKKRG
CCCHHHHHHHHHHCC
36.3423186163
269SumoylationERSLFEKKRGAPPSS
HHHHHHHHCCCCCCC
49.1928112733
275PhosphorylationKKRGAPPSSNIEDFH
HHCCCCCCCCHHHHH
34.6530266825
276PhosphorylationKRGAPPSSNIEDFHG
HCCCCCCCCHHHHHC
47.8330266825
283AcetylationSNIEDFHGLLPKGYP
CCHHHHHCCCCCCCC
28.9819608861
283UbiquitinationSNIEDFHGLLPKGYP
CCHHHHHCCCCCCCC
28.9819608861
289PhosphorylationHGLLPKGYPHLCSIC
HCCCCCCCCCEEECC
8.1328152594
294PhosphorylationKGYPHLCSICDLPVH
CCCCCEEECCCCCCC
32.3920873877
302PhosphorylationICDLPVHSNKEWSQH
CCCCCCCCCCHHHHH
50.2420873877
304AcetylationDLPVHSNKEWSQHIN
CCCCCCCCHHHHHCC
64.6723749302
307PhosphorylationVHSNKEWSQHINGAS
CCCCCHHHHHCCCCC
16.99-
326PhosphorylationCQLLLEIYPEWNPDN
HHHHEECCCCCCCCC
5.92-
387MethylationNGNLQGPRHMQKGRV
CCCCCCCCCCCCCCE
44.74115482663
396PhosphorylationMQKGRVETSRVVHIM
CCCCCEEEEEEEEEE
20.9827251275
397PhosphorylationQKGRVETSRVVHIMD
CCCCEEEEEEEEEEE
15.0127251275
403SulfoxidationTSRVVHIMDFQRGKN
EEEEEEEEECCCCCC
2.2621406390
407MethylationVHIMDFQRGKNLRYQ
EEEEECCCCCCHHHH
59.03115482695
413PhosphorylationQRGKNLRYQLLQLVE
CCCCCHHHHHHHHHH
13.4828064214
464UbiquitinationTPALVFGKPVRVHLS
CHHHHCCCCEEEEHH
28.95-
471PhosphorylationKPVRVHLSQKYKRIK
CCEEEEHHHHHHCCC
15.1124719451
473SumoylationVRVHLSQKYKRIKKP
EEEEHHHHHHCCCCC
49.73-
473AcetylationVRVHLSQKYKRIKKP
EEEEHHHHHHCCCCC
49.7325825284
473SumoylationVRVHLSQKYKRIKKP
EEEEHHHHHHCCCCC
49.7319608861
473UbiquitinationVRVHLSQKYKRIKKP
EEEEHHHHHHCCCCC
49.7319608861
474PhosphorylationRVHLSQKYKRIKKPE
EEEHHHHHHCCCCCC
9.6224719451
478AcetylationSQKYKRIKKPEGKPD
HHHHHCCCCCCCCCC
67.3312434983
478SumoylationSQKYKRIKKPEGKPD
HHHHHCCCCCCCCCC
67.3328112733
478UbiquitinationSQKYKRIKKPEGKPD
HHHHHCCCCCCCCCC
67.33-
479AcetylationQKYKRIKKPEGKPDQ
HHHHCCCCCCCCCCC
46.0212434997
479UbiquitinationQKYKRIKKPEGKPDQ
HHHHCCCCCCCCCCC
46.02-
483UbiquitinationRIKKPEGKPDQKFDQ
CCCCCCCCCCCCCCH
43.70-
487SumoylationPEGKPDQKFDQKQEL
CCCCCCCCCCHHHHH
59.28-
487AcetylationPEGKPDQKFDQKQEL
CCCCCCCCCCHHHHH
59.2827452117
487SumoylationPEGKPDQKFDQKQEL
CCCCCCCCCCHHHHH
59.2828112733
487UbiquitinationPEGKPDQKFDQKQEL
CCCCCCCCCCHHHHH
59.28-
491SumoylationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE
47.81-
4912-HydroxyisobutyrylationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE
47.81-
491AcetylationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE
47.8123749302
491SumoylationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE
47.8128112733
491UbiquitinationPDQKFDQKQELGRVI
CCCCCCHHHHHHCEE
47.8121906983
501PhosphorylationLGRVIHLSNLPHSGY
HHCEEEHHCCCCCCC
23.3528152594
506PhosphorylationHLSNLPHSGYSDSAV
EHHCCCCCCCCHHHH
37.1724043423
508PhosphorylationSNLPHSGYSDSAVLK
HCCCCCCCCHHHHHH
16.6024043423
509PhosphorylationNLPHSGYSDSAVLKL
CCCCCCCCHHHHHHH
28.7224043423
511PhosphorylationPHSGYSDSAVLKLAE
CCCCCCHHHHHHHHC
17.8425159151
515UbiquitinationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH
38.7721890473
515SumoylationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH
38.77-
5152-HydroxyisobutyrylationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH
38.77-
515AcetylationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH
38.7726051181
515MalonylationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH
38.7733225896
515SumoylationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH
38.7728112733
515UbiquitinationYSDSAVLKLAEPYGK
CCHHHHHHHHCCCCH
38.7721890473
520PhosphorylationVLKLAEPYGKIKNYI
HHHHHCCCCHHHHHH
23.6629496907
522UbiquitinationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH
44.6721890473
522SumoylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH
44.67-
5222-HydroxyisobutyrylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH
44.67-
522AcetylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH
44.6719608861
522MalonylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH
44.6726320211
522SumoylationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH
44.6728112733
522UbiquitinationKLAEPYGKIKNYILM
HHHCCCCHHHHHHHH
44.6719608861
5242-HydroxyisobutyrylationAEPYGKIKNYILMRM
HCCCCHHHHHHHHHH
47.38-
524AcetylationAEPYGKIKNYILMRM
HCCCCHHHHHHHHHH
47.3826051181
524SumoylationAEPYGKIKNYILMRM
HCCCCHHHHHHHHHH
47.38-
524UbiquitinationAEPYGKIKNYILMRM
HCCCCHHHHHHHHHH
47.3821906983
526PhosphorylationPYGKIKNYILMRMKS
CCCHHHHHHHHHHHH
7.1618083107
5322-HydroxyisobutyrylationNYILMRMKSQAFIEM
HHHHHHHHHCCEEEE
29.11-
532UbiquitinationNYILMRMKSQAFIEM
HHHHHHHHHCCEEEE
29.1121906983
533PhosphorylationYILMRMKSQAFIEME
HHHHHHHHCCEEEEC
19.8721712546
541AcetylationQAFIEMETREDAMAM
CCEEEECCHHHHHHH
37.7419608861
548AcetylationTREDAMAMVDHCLKK
CHHHHHHHHHHHHHH
2.0319608861
548UbiquitinationTREDAMAMVDHCLKK
CHHHHHHHHHHHHHH
2.0319608861
552GlutathionylationAMAMVDHCLKKALWF
HHHHHHHHHHHHHHH
5.2922555962
5542-HydroxyisobutyrylationAMVDHCLKKALWFQG
HHHHHHHHHHHHHCC
41.20-
554AcetylationAMVDHCLKKALWFQG
HHHHHHHHHHHHHCC
41.2025953088
554SumoylationAMVDHCLKKALWFQG
HHHHHHHHHHHHHCC
41.2028112733
554UbiquitinationAMVDHCLKKALWFQG
HHHHHHHHHHHHHCC
41.20-
555SumoylationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE
35.44-
5552-HydroxyisobutyrylationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE
35.44-
555AcetylationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE
35.4426051181
555MalonylationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE
35.4433225896
555SumoylationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE
35.4428112733
555UbiquitinationMVDHCLKKALWFQGR
HHHHHHHHHHHHCCE
35.4421906983
5652-HydroxyisobutyrylationWFQGRCVKVDLSEKY
HHCCEEEEEECHHHH
33.39-
565AcetylationWFQGRCVKVDLSEKY
HHCCEEEEEECHHHH
33.3923749302
565UbiquitinationWFQGRCVKVDLSEKY
HHCCEEEEEECHHHH
33.39-
5712-HydroxyisobutyrylationVKVDLSEKYKKLVLR
EEEECHHHHHHHHHH
60.02-
571AcetylationVKVDLSEKYKKLVLR
EEEECHHHHHHHHHH
60.0219608861
571UbiquitinationVKVDLSEKYKKLVLR
EEEECHHHHHHHHHH
60.0219608861
573AcetylationVDLSEKYKKLVLRIP
EECHHHHHHHHHHCC
51.187306829
573UbiquitinationVDLSEKYKKLVLRIP
EECHHHHHHHHHHCC
51.18-
588SumoylationNRGIDLLKKDKSRKR
CCCHHHHHHCCCCCC
67.24-
5882-HydroxyisobutyrylationNRGIDLLKKDKSRKR
CCCHHHHHHCCCCCC
67.24-
588AcetylationNRGIDLLKKDKSRKR
CCCHHHHHHCCCCCC
67.2426051181
588SumoylationNRGIDLLKKDKSRKR
CCCHHHHHHCCCCCC
67.24-
588UbiquitinationNRGIDLLKKDKSRKR
CCCHHHHHHCCCCCC
67.24-
589UbiquitinationRGIDLLKKDKSRKRS
CCHHHHHHCCCCCCC
71.06-
592PhosphorylationDLLKKDKSRKRSYSP
HHHHHCCCCCCCCCC
53.8426074081
596PhosphorylationKDKSRKRSYSPDGKE
HCCCCCCCCCCCCCC
32.7626846344
597PhosphorylationDKSRKRSYSPDGKES
CCCCCCCCCCCCCCC
28.4026846344
598PhosphorylationKSRKRSYSPDGKESP
CCCCCCCCCCCCCCC
20.1229255136
602MethylationRSYSPDGKESPSDKK
CCCCCCCCCCCCCCC
63.50-
604PhosphorylationYSPDGKESPSDKKSK
CCCCCCCCCCCCCCC
32.9426846344
606PhosphorylationPDGKESPSDKKSKTD
CCCCCCCCCCCCCCC
71.9326846344
608MethylationGKESPSDKKSKTDGS
CCCCCCCCCCCCCCC
64.38-
610PhosphorylationESPSDKKSKTDGSQK
CCCCCCCCCCCCCCC
46.6726074081
611UbiquitinationSPSDKKSKTDGSQKT
CCCCCCCCCCCCCCC
60.5621906983
612PhosphorylationPSDKKSKTDGSQKTE
CCCCCCCCCCCCCCC
53.3226074081
615PhosphorylationKKSKTDGSQKTESST
CCCCCCCCCCCCCCC
31.1721712546
617SumoylationSKTDGSQKTESSTEG
CCCCCCCCCCCCCCC
56.83-
617AcetylationSKTDGSQKTESSTEG
CCCCCCCCCCCCCCC
56.8323749302
617SumoylationSKTDGSQKTESSTEG
CCCCCCCCCCCCCCC
56.8328112733
617UbiquitinationSKTDGSQKTESSTEG
CCCCCCCCCCCCCCC
56.83-
618PhosphorylationKTDGSQKTESSTEGK
CCCCCCCCCCCCCCH
33.2026074081
620PhosphorylationDGSQKTESSTEGKEQ
CCCCCCCCCCCCHHH
48.0327794612
621PhosphorylationGSQKTESSTEGKEQE
CCCCCCCCCCCHHHH
25.0126055452
622PhosphorylationSQKTESSTEGKEQEE
CCCCCCCCCCHHHHH
59.0230576142
625AcetylationTESSTEGKEQEEKSG
CCCCCCCHHHHHHCC
50.4123749302
625UbiquitinationTESSTEGKEQEEKSG
CCCCCCCHHHHHHCC
50.4121906983
630SumoylationEGKEQEEKSGEDGEK
CCHHHHHHCCCCCCC
64.1128112733
630UbiquitinationEGKEQEEKSGEDGEK
CCHHHHHHCCCCCCC
64.11-
631PhosphorylationGKEQEEKSGEDGEKD
CHHHHHHCCCCCCCC
51.1730576142
639PhosphorylationGEDGEKDTKDDQTEQ
CCCCCCCCCCCCCCC
47.6520068231
640SumoylationEDGEKDTKDDQTEQE
CCCCCCCCCCCCCCC
70.24-
644PhosphorylationKDTKDDQTEQEPNML
CCCCCCCCCCCCCCC
46.7818691976
654PhosphorylationEPNMLLESEDELLVD
CCCCCCCCCCCEECC
50.7617081983
671PhosphorylationEAAALLESGSSVGDE
HHHHHHHCCCCCCCC
43.9017081983
673PhosphorylationAALLESGSSVGDETD
HHHHHCCCCCCCCCH
31.0017081983
674PhosphorylationALLESGSSVGDETDL
HHHHCCCCCCCCCHH
33.3817081983
679PhosphorylationGSSVGDETDLANLGD
CCCCCCCCHHHCHHH
40.8420068231
689PhosphorylationANLGDVASDGKKEPS
HCHHHHCCCCCCCCC
46.9017192257
692AcetylationGDVASDGKKEPSDKA
HHHCCCCCCCCCCHH
59.9830582879
692SumoylationGDVASDGKKEPSDKA
HHHCCCCCCCCCCHH
59.98-
696PhosphorylationSDGKKEPSDKAVKKD
CCCCCCCCCHHHHCC
53.4817081983
698AcetylationGKKEPSDKAVKKDGS
CCCCCCCHHHHCCCC
60.4623749302
702AcetylationPSDKAVKKDGSASAA
CCCHHHHCCCCHHHH
61.8030582897
702UbiquitinationPSDKAVKKDGSASAA
CCCHHHHCCCCHHHH
61.80-
705PhosphorylationKAVKKDGSASAAAKK
HHHHCCCCHHHHHHH
29.2328985074
707PhosphorylationVKKDGSASAAAKKKL
HHCCCCHHHHHHHHH
21.8228176443
711AcetylationGSASAAAKKKLKKVD
CCHHHHHHHHHHHCH
45.7925953088
712AcetylationSASAAAKKKLKKVDK
CHHHHHHHHHHHCHH
59.6225953088
713AcetylationASAAAKKKLKKVDKI
HHHHHHHHHHHCHHH
65.9030582885
715SumoylationAAAKKKLKKVDKIEE
HHHHHHHHHCHHHHH
60.68-
716AcetylationAAKKKLKKVDKIEEL
HHHHHHHHCHHHHHH
67.1325953088
716SumoylationAAKKKLKKVDKIEEL
HHHHHHHHCHHHHHH
67.13-
719SumoylationKKLKKVDKIEELDQE
HHHHHCHHHHHHHHH
55.81-
719SumoylationKKLKKVDKIEELDQE
HHHHHCHHHHHHHHH
55.8128112733
719UbiquitinationKKLKKVDKIEELDQE
HHHHHCHHHHHHHHH
55.81-
736SumoylationAALENGIKNEENTEP
HHHHHCCCCCCCCCC
60.76-
736SumoylationAALENGIKNEENTEP
HHHHHCCCCCCCCCC
60.7628112733
741PhosphorylationGIKNEENTEPGAESS
CCCCCCCCCCCCCCC
47.0025159151
747PhosphorylationNTEPGAESSENADDP
CCCCCCCCCCCCCCC
42.2828355574
748PhosphorylationTEPGAESSENADDPN
CCCCCCCCCCCCCCC
26.7825159151
758PhosphorylationADDPNKDTSENADGQ
CCCCCCCCCCCCCCC
39.2823927012
759PhosphorylationDDPNKDTSENADGQS
CCCCCCCCCCCCCCC
38.7023927012
766PhosphorylationSENADGQSDENKDDY
CCCCCCCCCCCCCCC
53.0425159151
770SumoylationDGQSDENKDDYTIPD
CCCCCCCCCCCCCCC
50.3428112733
770UbiquitinationDGQSDENKDDYTIPD
CCCCCCCCCCCCCCC
50.3421906983
773PhosphorylationSDENKDDYTIPDEYR
CCCCCCCCCCCCCCC
19.3923927012
774PhosphorylationDENKDDYTIPDEYRI
CCCCCCCCCCCCCCC
32.7823927012
779PhosphorylationDYTIPDEYRIGPYQP
CCCCCCCCCCCCCCC
18.2123403867
784PhosphorylationDEYRIGPYQPNVPVG
CCCCCCCCCCCCCCC
31.24-
794PhosphorylationNVPVGIDYVIPKTGF
CCCCCCCEEEECCCC
9.81-
798AcetylationGIDYVIPKTGFYCKL
CCCEEEECCCCEEEH
50.5926051181
798UbiquitinationGIDYVIPKTGFYCKL
CCCEEEECCCCEEEH
50.59-
799PhosphorylationIDYVIPKTGFYCKLC
CCEEEECCCCEEEHH
27.4622210691
802PhosphorylationVIPKTGFYCKLCSLF
EEECCCCEEEHHHHH
7.0425884760
804AcetylationPKTGFYCKLCSLFYT
ECCCCEEEHHHHHCC
40.9425953088
804MethylationPKTGFYCKLCSLFYT
ECCCCEEEHHHHHCC
40.94-
806S-nitrosocysteineTGFYCKLCSLFYTNE
CCCEEEHHHHHCCCH
1.71-
806GlutathionylationTGFYCKLCSLFYTNE
CCCEEEHHHHHCCCH
1.7122555962
806S-nitrosylationTGFYCKLCSLFYTNE
CCCEEEHHHHHCCCH
1.7122178444
807PhosphorylationGFYCKLCSLFYTNEE
CCEEEHHHHHCCCHH
31.7628348404
810PhosphorylationCKLCSLFYTNEEVAK
EEHHHHHCCCHHHHH
17.5928152594
811PhosphorylationKLCSLFYTNEEVAKN
EHHHHHCCCHHHHHC
28.9021815630
817AcetylationYTNEEVAKNTHCSSL
CCCHHHHHCCCCCCC
68.5025953088
817UbiquitinationYTNEEVAKNTHCSSL
CCCHHHHHCCCCCCC
68.50-
823PhosphorylationAKNTHCSSLPHYQKL
HHCCCCCCCHHHHHH
51.8428152594
827PhosphorylationHCSSLPHYQKLKKFL
CCCCCHHHHHHHHHH
12.8528152594
829AcetylationSSLPHYQKLKKFLNK
CCCHHHHHHHHHHHH
55.9223749302
829UbiquitinationSSLPHYQKLKKFLNK
CCCHHHHHHHHHHHH
55.9219608861
831AcetylationLPHYQKLKKFLNKLA
CHHHHHHHHHHHHHH
48.8125953088
836UbiquitinationKLKKFLNKLAEERRQ
HHHHHHHHHHHHHHH
51.7421890473
836AcetylationKLKKFLNKLAEERRQ
HHHHHHHHHHHHHHH
51.7419608861
836MalonylationKLKKFLNKLAEERRQ
HHHHHHHHHHHHHHH
51.7433225896
836SumoylationKLKKFLNKLAEERRQ
HHHHHHHHHHHHHHH
51.7428112733
836UbiquitinationKLKKFLNKLAEERRQ
HHHHHHHHHHHHHHH
51.7421890473

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
4SPhosphorylationKinaseCHEK1O14757
GPS
150TPhosphorylationKinaseCHEK1O14757
GPS
195SPhosphorylationKinaseCHEK1O14757
GPS
208SPhosphorylationKinaseATMQ13315
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MATR3_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 MATR3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMU1_HUMANSMU1physical
22939629
SAP18_HUMANSAP18physical
22939629
STML2_HUMANSTOML2physical
22939629
RBP2_HUMANRANBP2physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
SYIM_HUMANIARS2physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
PPT2_HUMANPPT2physical
22939629
S10A9_HUMANS100A9physical
22939629
SYSM_HUMANSARS2physical
22939629
RRS1_HUMANRRS1physical
22939629
NAA15_HUMANNAA15physical
22939629
CAVN3_HUMANPRKCDBPphysical
22939629
MYOF_HUMANMYOFphysical
22939629
RM19_HUMANMRPL19physical
22939629
PTBP2_HUMANPTBP2physical
22365833
MATR3_HUMANMATR3physical
25416956
RASD1_HUMANRASD1physical
25416956
BTF3_HUMANBTF3physical
26344197
CALR_HUMANCALRphysical
26344197
EF1D_HUMANEEF1Dphysical
26344197
HNRPU_HUMANHNRNPUphysical
26344197
PUF60_HUMANPUF60physical
26344197
RL7_HUMANRPL7physical
26344197
RUVB1_HUMANRUVBL1physical
26344197
SF3A3_HUMANSF3A3physical
26344197
RU17_HUMANSNRNP70physical
26344197
RU1C_HUMANSNRPCphysical
26344197
SRSF3_HUMANSRSF3physical
26344197
TCP4_HUMANSUB1physical
26344197
YBOX1_HUMANYBX1physical
26344197
DSRAD_HUMANADARphysical
26496610
COPA_HUMANCOPAphysical
26496610
DDX3X_HUMANDDX3Xphysical
26496610
DDX5_HUMANDDX5physical
26496610
DHX9_HUMANDHX9physical
26496610
EWS_HUMANEWSR1physical
26496610
FUS_HUMANFUSphysical
26496610
ROA1_HUMANHNRNPA1physical
26496610
ROA2_HUMANHNRNPA2B1physical
26496610
HNRPC_HUMANHNRNPCphysical
26496610
HNRPF_HUMANHNRNPFphysical
26496610
HNRH1_HUMANHNRNPH1physical
26496610
HNRH2_HUMANHNRNPH2physical
26496610
HNRH3_HUMANHNRNPH3physical
26496610
HNRPK_HUMANHNRNPKphysical
26496610
HNRPL_HUMANHNRNPLphysical
26496610
ILF2_HUMANILF2physical
26496610
ILF3_HUMANILF3physical
26496610
HNRPM_HUMANHNRNPMphysical
26496610
NP1L4_HUMANNAP1L4physical
26496610
NUMA1_HUMANNUMA1physical
26496610
PKP2_HUMANPKP2physical
26496610
PP1A_HUMANPPP1CAphysical
26496610
PP1B_HUMANPPP1CBphysical
26496610
PTBP1_HUMANPTBP1physical
26496610
RBM3_HUMANRBM3physical
26496610
RCN1_HUMANRCN1physical
26496610
SAFB1_HUMANSAFBphysical
26496610
SET_HUMANSETphysical
26496610
SNRPA_HUMANSNRPAphysical
26496610
RBP56_HUMANTAF15physical
26496610
PKP4_HUMANPKP4physical
26496610
EIF3D_HUMANEIF3Dphysical
26496610
SRSF9_HUMANSRSF9physical
26496610
TNK1_HUMANTNK1physical
26496610
FUBP3_HUMANFUBP3physical
26496610
ABC3B_HUMANAPOBEC3Bphysical
26496610
SAFB2_HUMANSAFB2physical
26496610
PUM1_HUMANPUM1physical
26496610
HNRDL_HUMANHNRNPDLphysical
26496610
PTBP3_HUMANPTBP3physical
26496610
DNJB6_HUMANDNAJB6physical
26496610
SUGP2_HUMANSUGP2physical
26496610
RBM6_HUMANRBM6physical
26496610
THOC4_HUMANALYREFphysical
26496610
HNRPR_HUMANHNRNPRphysical
26496610
AKAP8_HUMANAKAP8physical
26496610
RBM14_HUMANRBM14physical
26496610
DDX17_HUMANDDX17physical
26496610
KHDR1_HUMANKHDRBS1physical
26496610
ROA0_HUMANHNRNPA0physical
26496610
HNRL1_HUMANHNRNPUL1physical
26496610
PKP3_HUMANPKP3physical
26496610
RALY_HUMANRALYphysical
26496610
F120A_HUMANFAM120Aphysical
26496610
TASOR_HUMANFAM208Aphysical
26496610
RFOX2_HUMANRBFOX2physical
26496610
TIM13_HUMANTIMM13physical
26496610
AKP8L_HUMANAKAP8Lphysical
26496610
STAU2_HUMANSTAU2physical
26496610
RBMX_HUMANRBMXphysical
26496610
ZN638_HUMANZNF638physical
26496610
RB15B_HUMANRBM15Bphysical
26496610
RTCB_HUMANRTCBphysical
26496610
PPHLN_HUMANPPHLN1physical
26496610
CN166_HUMANC14orf166physical
26496610
MPP8_HUMANMPHOSPH8physical
26496610
RPC2_HUMANPOLR3Bphysical
26496610
DDX28_HUMANDDX28physical
26496610
YLPM1_HUMANYLPM1physical
26496610
NCOA5_HUMANNCOA5physical
26496610
SQOR_HUMANSQRDLphysical
26496610
ZN106_HUMANZNF106physical
26496610
ZN668_HUMANZNF668physical
26496610
SLTM_HUMANSLTMphysical
26496610
PRR3_HUMANPRR3physical
26496610
RBM4B_HUMANRBM4Bphysical
26496610
HASP_HUMANGSG2physical
26496610
DPY30_HUMANDPY30physical
26496610
NALP5_HUMANNLRP5physical
26496610
ESCO2_HUMANESCO2physical
26496610
ROA3_HUMANHNRNPA3physical
26496610
HNRL2_HUMANHNRNPUL2physical
26496610
BCLA3_HUMANCXorf23physical
26496610
ZN326_HUMANZNF326physical
26496610
RB12B_HUMANRBM12Bphysical
26496610
E2AK4_HUMANEIF2AK4physical
26496610
RMXL1_HUMANRBMXL1physical
26496610
LMNA_HUMANLMNAphysical
25948554

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606070Amyotrophic lateral sclerosis 21 (ALS21)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MATR3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-473; LYS-522; LYS-571AND LYS-836, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-118 AND SER-208,AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598 AND SER-604, ANDMASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-195; SER-208;SER-533; SER-598 AND SER-604, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND TYR-773, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-195 ANDSER-206, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-195, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-397; SER-654;SER-671; SER-673; SER-674 AND SER-696, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598 AND SER-604, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-596; SER-598AND SER-604, AND MASS SPECTROMETRY.

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