SNUT1_HUMAN - dbPTM
SNUT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNUT1_HUMAN
UniProt AC O43290
Protein Name U4/U6.U5 tri-snRNP-associated protein 1
Gene Name SART1
Organism Homo sapiens (Human).
Sequence Length 800
Subcellular Localization Nucleus . Found in the nucleus of mitogen-activated peripheral blood mononuclear cells (PBMCs), tumor cells, or normal cell lines, but not in normal tissues except testis and fetal liver or in unstimulated PBMCs, suggesting preferential expression in
Protein Description Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA..
Protein Sequence MGSSKKHRGEKEAAGTTAAAGTGGATEQPPRHREHKKHKHRSGGSGGSGGERRKRSRERGGERGSGRRGAEAEARSSTHGRERSQAEPSERRVKREKRDDGYEAAASSKTSSGDASSLSIEETNKLRAKLGLKPLEVNAIKKEAGTKEEPVTADVINPMALRQREELREKLAAAKEKRLLNQKLGKIKTLGEDDPWLDDTAAWIERSRQLQKEKDLAEKRAKLLEEMDQEFGVSTLVEEEFGQRRQDLYSARDLQGLTVEHAIDSFREGETMILTLKDKGVLQEEEDVLVNVNLVDKERAEKNVELRKKKPDYLPYAEDESVDDLAQQKPRSILSKYDEELEGERPHSFRLEQGGTADGLRERELEEIRAKLRLQAQSLSTVGPRLASEYLTPEEMVTFKKTKRRVKKIRKKEKEVVVRADDLLPLGDQTQDGDFGSRLRGRGRRRVSEVEEEKEPVPQPLPSDDTRVENMDISDEEEGGAPPPGSPQVLEEDEAELELQKQLEKGRRLRQLQQLQQLRDSGEKVVEIVKKLESRQRGWEEDEDPERKGAIVFNATSEFCRTLGEIPTYGLAGNREEQEELMDFERDEERSANGGSESDGEENIGWSTVNLDEEKQQQDFSASSTTILDEEPIVNRGLAAALLLCQNKGLLETTVQKVARVKAPNKSLPSAVYCIEDKMAIDDKYSRREEYRGFTQDFKEKDGYKPDVKIEYVDETGRKLTPKEAFRQLSHRFHGKGSGKMKTERRMKKLDEEALLKKMSSSDTPLGTVALLQEKQKAQKTPYIVLSGSGKSMNANTITK
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
12UbiquitinationKKHRGEKEAAGTTAA
CCCCCCHHCCCCCCC
39.1824816145
17PhosphorylationEKEAAGTTAAAGTGG
CHHCCCCCCCCCCCC
17.2425627689
22PhosphorylationGTTAAAGTGGATEQP
CCCCCCCCCCCCCCC
27.9325159151
25UbiquitinationAAAGTGGATEQPPRH
CCCCCCCCCCCCCCC
14.8722817900
27UbiquitinationAGTGGATEQPPRHRE
CCCCCCCCCCCCCCC
61.6323000965
28UbiquitinationGTGGATEQPPRHREH
CCCCCCCCCCCCCCC
49.2822817900
30UbiquitinationGGATEQPPRHREHKK
CCCCCCCCCCCCCCC
44.3922817900
31UbiquitinationGATEQPPRHREHKKH
CCCCCCCCCCCCCCC
48.4521890473
35UbiquitinationQPPRHREHKKHKHRS
CCCCCCCCCCCCCCC
44.4123000965
42PhosphorylationHKKHKHRSGGSGGSG
CCCCCCCCCCCCCCH
47.4230576142
45PhosphorylationHKHRSGGSGGSGGER
CCCCCCCCCCCHHHH
43.4321406692
48PhosphorylationRSGGSGGSGGERRKR
CCCCCCCCHHHHHHH
47.3421406692
56UbiquitinationGGERRKRSRERGGER
HHHHHHHHHHCCCCC
41.3424816145
72UbiquitinationSGRRGAEAEARSSTH
CCHHHHHHHHHHCCC
18.4024816145
84PhosphorylationSTHGRERSQAEPSER
CCCCCHHHCCCCCHH
29.0523312004
85UbiquitinationTHGRERSQAEPSERR
CCCCHHHCCCCCHHH
56.8422817900
88UbiquitinationRERSQAEPSERRVKR
CHHHCCCCCHHHHHH
44.5022817900
90UbiquitinationRSQAEPSERRVKREK
HHCCCCCHHHHHHHH
56.0422817900
94SumoylationEPSERRVKREKRDDG
CCCHHHHHHHHCCCC
53.69-
94SumoylationEPSERRVKREKRDDG
CCCHHHHHHHHCCCC
53.69-
102PhosphorylationREKRDDGYEAAASSK
HHHCCCCHHHHHCCC
14.9128796482
108PhosphorylationGYEAAASSKTSSGDA
CHHHHHCCCCCCCCH
34.91-
109UbiquitinationYEAAASSKTSSGDAS
HHHHHCCCCCCCCHH
50.3532015554
110PhosphorylationEAAASSKTSSGDASS
HHHHCCCCCCCCHHH
30.0325159151
111PhosphorylationAAASSKTSSGDASSL
HHHCCCCCCCCHHHC
35.7425159151
112PhosphorylationAASSKTSSGDASSLS
HHCCCCCCCCHHHCC
46.0221815630
116PhosphorylationKTSSGDASSLSIEET
CCCCCCHHHCCHHHH
36.2328985074
116UbiquitinationKTSSGDASSLSIEET
CCCCCCHHHCCHHHH
36.2324816145
119PhosphorylationSGDASSLSIEETNKL
CCCHHHCCHHHHHHH
29.87-
123PhosphorylationSSLSIEETNKLRAKL
HHCCHHHHHHHHHHH
25.5129396449
125AcetylationLSIEETNKLRAKLGL
CCHHHHHHHHHHHCC
46.9325953088
125SumoylationLSIEETNKLRAKLGL
CCHHHHHHHHHHHCC
46.9328112733
125UbiquitinationLSIEETNKLRAKLGL
CCHHHHHHHHHHHCC
46.9323000965
129AcetylationETNKLRAKLGLKPLE
HHHHHHHHHCCCCEE
36.3325953088
129UbiquitinationETNKLRAKLGLKPLE
HHHHHHHHHCCCCEE
36.3323000965
133AcetylationLRAKLGLKPLEVNAI
HHHHHCCCCEEHHEE
45.8423749302
133SumoylationLRAKLGLKPLEVNAI
HHHHHCCCCEEHHEE
45.8428112733
133UbiquitinationLRAKLGLKPLEVNAI
HHHHHCCCCEEHHEE
45.8423000965
141SumoylationPLEVNAIKKEAGTKE
CEEHHEEECCCCCCC
41.99-
141AcetylationPLEVNAIKKEAGTKE
CEEHHEEECCCCCCC
41.9925953088
141SumoylationPLEVNAIKKEAGTKE
CEEHHEEECCCCCCC
41.9925114211
147SumoylationIKKEAGTKEEPVTAD
EECCCCCCCCCCCHH
60.19-
147AcetylationIKKEAGTKEEPVTAD
EECCCCCCCCCCCHH
60.1926051181
147SumoylationIKKEAGTKEEPVTAD
EECCCCCCCCCCCHH
60.1928112733
147UbiquitinationIKKEAGTKEEPVTAD
EECCCCCCCCCCCHH
60.1932015554
159SulfoxidationTADVINPMALRQREE
CHHHHCHHHHHHHHH
4.7921406390
170UbiquitinationQREELREKLAAAKEK
HHHHHHHHHHHHHHH
36.6724816145
171UbiquitinationREELREKLAAAKEKR
HHHHHHHHHHHHHHH
3.1624816145
175SuccinylationREKLAAAKEKRLLNQ
HHHHHHHHHHHHHHH
60.0723954790
1832-HydroxyisobutyrylationEKRLLNQKLGKIKTL
HHHHHHHHHCCCCCC
59.12-
183AcetylationEKRLLNQKLGKIKTL
HHHHHHHHHCCCCCC
59.1225953088
183UbiquitinationEKRLLNQKLGKIKTL
HHHHHHHHHCCCCCC
59.1222817900
186UbiquitinationLLNQKLGKIKTLGED
HHHHHHCCCCCCCCC
52.0122817900
188SumoylationNQKLGKIKTLGEDDP
HHHHCCCCCCCCCCC
40.98-
188SumoylationNQKLGKIKTLGEDDP
HHHHCCCCCCCCCCC
40.9828112733
188UbiquitinationNQKLGKIKTLGEDDP
HHHHCCCCCCCCCCC
40.9822817900
189PhosphorylationQKLGKIKTLGEDDPW
HHHCCCCCCCCCCCC
43.3926074081
200PhosphorylationDDPWLDDTAAWIERS
CCCCHHHHHHHHHHH
20.2426074081
207PhosphorylationTAAWIERSRQLQKEK
HHHHHHHHHHHHHHH
16.1626074081
214UbiquitinationSRQLQKEKDLAEKRA
HHHHHHHHHHHHHHH
66.1424816145
219AcetylationKEKDLAEKRAKLLEE
HHHHHHHHHHHHHHH
52.6425953088
231UbiquitinationLEEMDQEFGVSTLVE
HHHHHHHHCHHHHHH
11.0024816145
243UbiquitinationLVEEEFGQRRQDLYS
HHHHHHHHHHHHHHH
42.5824816145
249PhosphorylationGQRRQDLYSARDLQG
HHHHHHHHHHHHHCC
14.47-
250PhosphorylationQRRQDLYSARDLQGL
HHHHHHHHHHHHCCC
24.9123532336
256UbiquitinationYSARDLQGLTVEHAI
HHHHHHCCCCHHHHH
30.5224816145
258PhosphorylationARDLQGLTVEHAIDS
HHHHCCCCHHHHHHH
30.5820044836
265PhosphorylationTVEHAIDSFREGETM
CHHHHHHHHHCCCEE
21.7928122231
271PhosphorylationDSFREGETMILTLKD
HHHHCCCEEEEEECC
21.99-
272SulfoxidationSFREGETMILTLKDK
HHHCCCEEEEEECCC
1.7421406390
275PhosphorylationEGETMILTLKDKGVL
CCCEEEEEECCCCCC
22.3420044836
277SumoylationETMILTLKDKGVLQE
CEEEEEECCCCCCCC
52.7628112733
277UbiquitinationETMILTLKDKGVLQE
CEEEEEECCCCCCCC
52.7632015554
296UbiquitinationLVNVNLVDKERAEKN
EEEEECCCHHHHHHH
50.7124816145
302AcetylationVDKERAEKNVELRKK
CCHHHHHHHHHHHHC
66.3725953088
302UbiquitinationVDKERAEKNVELRKK
CCHHHHHHHHHHHHC
66.37-
303UbiquitinationDKERAEKNVELRKKK
CHHHHHHHHHHHHCC
24.8124816145
309UbiquitinationKNVELRKKKPDYLPY
HHHHHHHCCCCCCCC
64.2029967540
310UbiquitinationNVELRKKKPDYLPYA
HHHHHHCCCCCCCCC
46.2729967540
313PhosphorylationLRKKKPDYLPYAEDE
HHHCCCCCCCCCCCC
20.3623186163
316PhosphorylationKKPDYLPYAEDESVD
CCCCCCCCCCCCCHH
21.7423403867
316UbiquitinationKKPDYLPYAEDESVD
CCCCCCCCCCCCCHH
21.7424816145
321PhosphorylationLPYAEDESVDDLAQQ
CCCCCCCCHHHHHHH
43.0725159151
329AcetylationVDDLAQQKPRSILSK
HHHHHHHCCHHHHHH
30.2526051181
329SumoylationVDDLAQQKPRSILSK
HHHHHHHCCHHHHHH
30.2528112733
329UbiquitinationVDDLAQQKPRSILSK
HHHHHHHCCHHHHHH
30.2524816145
332PhosphorylationLAQQKPRSILSKYDE
HHHHCCHHHHHHCCH
36.0927422710
335PhosphorylationQKPRSILSKYDEELE
HCCHHHHHHCCHHHC
27.7430108239
336AcetylationKPRSILSKYDEELEG
CCHHHHHHCCHHHCC
53.9625953088
336SumoylationKPRSILSKYDEELEG
CCHHHHHHCCHHHCC
53.9628112733
336UbiquitinationKPRSILSKYDEELEG
CCHHHHHHCCHHHCC
53.9632015554
337PhosphorylationPRSILSKYDEELEGE
CHHHHHHCCHHHCCC
25.8023312004
348PhosphorylationLEGERPHSFRLEQGG
HCCCCCCCEECCCCC
18.1023401153
356PhosphorylationFRLEQGGTADGLRER
EECCCCCCCCCCCHH
28.5320068231
356UbiquitinationFRLEQGGTADGLRER
EECCCCCCCCCCCHH
28.5324816145
373UbiquitinationEEIRAKLRLQAQSLS
HHHHHHHHHHHHHHH
24.8524816145
378PhosphorylationKLRLQAQSLSTVGPR
HHHHHHHHHHCCCHH
27.5728555341
380PhosphorylationRLQAQSLSTVGPRLA
HHHHHHHHCCCHHHH
26.7128555341
385MethylationSLSTVGPRLASEYLT
HHHCCCHHHHHHCCC
36.64115493335
388PhosphorylationTVGPRLASEYLTPEE
CCCHHHHHHCCCHHH
31.2228796482
390NitrationGPRLASEYLTPEEMV
CHHHHHHCCCHHHHH
17.24-
390PhosphorylationGPRLASEYLTPEEMV
CHHHHHHCCCHHHHH
17.2428796482
392PhosphorylationRLASEYLTPEEMVTF
HHHHHCCCHHHHHCC
27.9621712546
398PhosphorylationLTPEEMVTFKKTKRR
CCHHHHHCCHHHHHH
28.5529396449
4002-HydroxyisobutyrylationPEEMVTFKKTKRRVK
HHHHHCCHHHHHHHH
50.60-
400AcetylationPEEMVTFKKTKRRVK
HHHHHCCHHHHHHHH
50.6026051181
400SumoylationPEEMVTFKKTKRRVK
HHHHHCCHHHHHHHH
50.6028112733
400UbiquitinationPEEMVTFKKTKRRVK
HHHHHCCHHHHHHHH
50.6029967540
401UbiquitinationEEMVTFKKTKRRVKK
HHHHCCHHHHHHHHH
55.9024816145
414SumoylationKKIRKKEKEVVVRAD
HHHHHHCCEEEEEHH
65.7628112733
414UbiquitinationKKIRKKEKEVVVRAD
HHHHHHCCEEEEEHH
65.7624816145
430PhosphorylationLLPLGDQTQDGDFGS
CCCCCCCCCCCCHHH
33.1117525332
433UbiquitinationLGDQTQDGDFGSRLR
CCCCCCCCCHHHHCC
23.4824816145
437PhosphorylationTQDGDFGSRLRGRGR
CCCCCHHHHCCCCCC
28.3025159151
448PhosphorylationGRGRRRVSEVEEEKE
CCCCCCCCCCCCCCC
33.8329255136
454UbiquitinationVSEVEEEKEPVPQPL
CCCCCCCCCCCCCCC
71.2724816145
463PhosphorylationPVPQPLPSDDTRVEN
CCCCCCCCCCCCCCC
56.6630266825
466PhosphorylationQPLPSDDTRVENMDI
CCCCCCCCCCCCCCC
41.4230266825
474PhosphorylationRVENMDISDEEEGGA
CCCCCCCCCCCCCCC
34.4030266825
486PhosphorylationGGAPPPGSPQVLEED
CCCCCCCCCHHHCCC
20.2430266825
521PhosphorylationQLQQLRDSGEKVVEI
HHHHHHHCCCHHHHH
42.2826055452
524UbiquitinationQLRDSGEKVVEIVKK
HHHHCCCHHHHHHHH
55.9229967540
5302-HydroxyisobutyrylationEKVVEIVKKLESRQR
CHHHHHHHHHHHHHC
58.25-
530UbiquitinationEKVVEIVKKLESRQR
CHHHHHHHHHHHHHC
58.2529967540
531UbiquitinationKVVEIVKKLESRQRG
HHHHHHHHHHHHHCC
46.7424816145
548SumoylationEDEDPERKGAIVFNA
CCCCHHHCCCEEEEC
51.5428112733
560GlutathionylationFNATSEFCRTLGEIP
EECCHHHHHHHCCCC
2.5922555962
569PhosphorylationTLGEIPTYGLAGNRE
HHCCCCCCCCCCCHH
12.5627642862
591PhosphorylationFERDEERSANGGSES
HHHHHHHHCCCCCCC
29.3923927012
596PhosphorylationERSANGGSESDGEEN
HHHCCCCCCCCCCCC
35.0130266825
598PhosphorylationSANGGSESDGEENIG
HCCCCCCCCCCCCCC
53.2523927012
607PhosphorylationGEENIGWSTVNLDEE
CCCCCCCEEECCCHH
19.7723403867
608PhosphorylationEENIGWSTVNLDEEK
CCCCCCEEECCCHHH
13.6023403867
621PhosphorylationEKQQQDFSASSTTIL
HHHHHCCCCCCCCCC
35.2124275569
623PhosphorylationQQQDFSASSTTILDE
HHHCCCCCCCCCCCC
27.3327251275
624PhosphorylationQQDFSASSTTILDEE
HHCCCCCCCCCCCCC
29.3224275569
625PhosphorylationQDFSASSTTILDEEP
HCCCCCCCCCCCCCC
18.5024275569
626PhosphorylationDFSASSTTILDEEPI
CCCCCCCCCCCCCCC
22.8424275569
648AcetylationALLLCQNKGLLETTV
HHHHHHCCCHHHHHH
25.6726051181
648SumoylationALLLCQNKGLLETTV
HHHHHHCCCHHHHHH
25.6728112733
648UbiquitinationALLLCQNKGLLETTV
HHHHHHCCCHHHHHH
25.6729967540
654PhosphorylationNKGLLETTVQKVARV
CCCHHHHHHHHHHCC
16.1528555341
657AcetylationLLETTVQKVARVKAP
HHHHHHHHHHCCCCC
33.2625953088
657SumoylationLLETTVQKVARVKAP
HHHHHHHHHHCCCCC
33.2628112733
657UbiquitinationLLETTVQKVARVKAP
HHHHHHHHHHCCCCC
33.2633845483
662AcetylationVQKVARVKAPNKSLP
HHHHHCCCCCCCCCC
53.2025953088
666AcetylationARVKAPNKSLPSAVY
HCCCCCCCCCCCCEE
52.9225953088
666UbiquitinationARVKAPNKSLPSAVY
HCCCCCCCCCCCCEE
52.9229967540
667PhosphorylationRVKAPNKSLPSAVYC
CCCCCCCCCCCCEEE
52.7526552605
670PhosphorylationAPNKSLPSAVYCIED
CCCCCCCCCEEECCC
35.3426552605
673PhosphorylationKSLPSAVYCIEDKMA
CCCCCCEEECCCHHC
6.3426552605
674GlutathionylationSLPSAVYCIEDKMAI
CCCCCEEECCCHHCC
1.9022555962
678UbiquitinationAVYCIEDKMAIDDKY
CEEECCCHHCCCCCC
19.9029967540
684AcetylationDKMAIDDKYSRREEY
CHHCCCCCCCCHHHH
41.1825953088
684SumoylationDKMAIDDKYSRREEY
CHHCCCCCCCCHHHH
41.1828112733
684UbiquitinationDKMAIDDKYSRREEY
CHHCCCCCCCCHHHH
41.1829967540
685PhosphorylationKMAIDDKYSRREEYR
HHCCCCCCCCHHHHC
17.88-
686PhosphorylationMAIDDKYSRREEYRG
HCCCCCCCCHHHHCC
30.51-
692MethylationYSRREEYRGFTQDFK
CCCHHHHCCCCHHHH
36.71115493343
695PhosphorylationREEYRGFTQDFKEKD
HHHHCCCCHHHHHHC
30.0117525332
699SumoylationRGFTQDFKEKDGYKP
CCCCHHHHHHCCCCC
72.6228112733
699UbiquitinationRGFTQDFKEKDGYKP
CCCCHHHHHHCCCCC
72.6229967540
7012-HydroxyisobutyrylationFTQDFKEKDGYKPDV
CCHHHHHHCCCCCCC
57.98-
705AcetylationFKEKDGYKPDVKIEY
HHHHCCCCCCCEEEE
40.0326051181
709SumoylationDGYKPDVKIEYVDET
CCCCCCCEEEEECCC
36.88-
709SumoylationDGYKPDVKIEYVDET
CCCCCCCEEEEECCC
36.8828112733
712PhosphorylationKPDVKIEYVDETGRK
CCCCEEEEECCCCCC
19.37-
716PhosphorylationKIEYVDETGRKLTPK
EEEEECCCCCCCCHH
37.5123898821
719UbiquitinationYVDETGRKLTPKEAF
EECCCCCCCCHHHHH
59.0429967540
721PhosphorylationDETGRKLTPKEAFRQ
CCCCCCCCHHHHHHH
35.0424719451
723SumoylationTGRKLTPKEAFRQLS
CCCCCCHHHHHHHHH
57.3428112733
723UbiquitinationTGRKLTPKEAFRQLS
CCCCCCHHHHHHHHH
57.3433845483
730PhosphorylationKEAFRQLSHRFHGKG
HHHHHHHHHHHCCCC
12.32-
742SumoylationGKGSGKMKTERRMKK
CCCCCCHHHHHHHHH
51.20-
742SumoylationGKGSGKMKTERRMKK
CCCCCCHHHHHHHHH
51.20-
749SumoylationKTERRMKKLDEEALL
HHHHHHHHCCHHHHH
52.4028112733
749UbiquitinationKTERRMKKLDEEALL
HHHHHHHHCCHHHHH
52.4029967540
7572-HydroxyisobutyrylationLDEEALLKKMSSSDT
CCHHHHHHHHCCCCC
47.48-
757MethylationLDEEALLKKMSSSDT
CCHHHHHHHHCCCCC
47.48115977547
758SumoylationDEEALLKKMSSSDTP
CHHHHHHHHCCCCCC
43.94-
758MethylationDEEALLKKMSSSDTP
CHHHHHHHHCCCCCC
43.94110876121
758SumoylationDEEALLKKMSSSDTP
CHHHHHHHHCCCCCC
43.9428112733
758UbiquitinationDEEALLKKMSSSDTP
CHHHHHHHHCCCCCC
43.9429967540
760PhosphorylationEALLKKMSSSDTPLG
HHHHHHHCCCCCCCH
35.2529255136
761PhosphorylationALLKKMSSSDTPLGT
HHHHHHCCCCCCCHH
28.8329255136
762PhosphorylationLLKKMSSSDTPLGTV
HHHHHCCCCCCCHHH
37.8929255136
764PhosphorylationKKMSSSDTPLGTVAL
HHHCCCCCCCHHHHH
23.5129255136
768PhosphorylationSSDTPLGTVALLQEK
CCCCCCHHHHHHHHH
15.4129255136
775SumoylationTVALLQEKQKAQKTP
HHHHHHHHHHCCCCC
44.1028112733
775UbiquitinationTVALLQEKQKAQKTP
HHHHHHHHHHCCCCC
44.1029967540
780AcetylationQEKQKAQKTPYIVLS
HHHHHCCCCCEEEEC
57.2225953088
780SumoylationQEKQKAQKTPYIVLS
HHHHHCCCCCEEEEC
57.2228112733
781PhosphorylationEKQKAQKTPYIVLSG
HHHHCCCCCEEEECC
14.8320068231
783PhosphorylationQKAQKTPYIVLSGSG
HHCCCCCEEEECCCC
14.6417360941
787PhosphorylationKTPYIVLSGSGKSMN
CCCEEEECCCCCCCC
21.7325159151
789PhosphorylationPYIVLSGSGKSMNAN
CEEEECCCCCCCCCC
39.4125159151
791AcetylationIVLSGSGKSMNANTI
EEECCCCCCCCCCCC
48.5126051181
791SumoylationIVLSGSGKSMNANTI
EEECCCCCCCCCCCC
48.5128112733

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 SNUT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNUT1_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 SNUT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBL5_HUMANUBL5physical
21614000
PRP8_HUMANPRPF8physical
11350945
PRPF3_HUMANPRPF3physical
11350945
PRP4_HUMANPRPF4physical
11350945
SNUT1_HUMANSART1physical
16723661
PRPF3_HUMANPRPF3physical
16723661
U520_HUMANSNRNP200physical
16723661
PRP6_HUMANPRPF6physical
16723661
A4_HUMANAPPphysical
21832049
U2AF2_HUMANU2AF2physical
22939629
U2AF1_HUMANU2AF1physical
22939629
SRRM2_HUMANSRRM2physical
22939629
SRPK1_HUMANSRPK1physical
22939629
TPR_HUMANTPRphysical
22939629
TIM10_HUMANTIMM10physical
22939629
TR112_HUMANTRMT112physical
22939629
TIM9_HUMANTIMM9physical
22939629
TR150_HUMANTHRAP3physical
22939629
RBM25_HUMANRBM25physical
22365833
CHERP_HUMANCHERPphysical
22365833
SNW1_HUMANSNW1physical
22365833
MFAP1_HUMANMFAP1physical
22365833
UBL5_HUMANUBL5physical
22365833
SRSF4_HUMANSRSF4physical
22365833
ZCH10_HUMANZCCHC10physical
22365833
UBL5_HUMANUBL5physical
24872507
U5S1_HUMANEFTUD2physical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP4_HUMANPABPC4physical
26344197
PRP19_HUMANPRPF19physical
26344197
PRPF3_HUMANPRPF3physical
26344197
PR40A_HUMANPRPF40Aphysical
26344197
SF3A3_HUMANSF3A3physical
26344197
SF3B3_HUMANSF3B3physical
26344197
SMD3_HUMANSNRPD3physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNUT1_HUMAN

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Related Literatures of Post-Translational Modification
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 THR-430; SER-448 ANDTHR-764, AND MASS SPECTROMETRY.
"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 THR-392; SER-448; SER-474AND SER-486, AND MASS 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-448, 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-448, 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-448; SER-591; SER-596AND SER-598, 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 THR-764, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-430 AND THR-695, 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 THR-392, AND MASSSPECTROMETRY.

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