TR150_MOUSE - dbPTM
TR150_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TR150_MOUSE
UniProt AC Q569Z6
Protein Name Thyroid hormone receptor-associated protein 3
Gene Name Thrap3
Organism Mus musculus (Mouse).
Sequence Length 951
Subcellular Localization Nucleus . Nucleus, nucleoplasm . Nucleus speckle .
Protein Description Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes. [PubMed: 24043798]
Protein Sequence MSKTNKSKSGSRSSRSRSASRSRSRSFSKSRSRSRSVSRSRKRRLSSRSRSRSYSPAHNRERNHPRVYQNRDFRGHNRGYRRPYYFRGRNRGFYPWGQYNRGGYGNYRSNWQNYRQAYSPRRGRSRSRSPKRRSPSPRSRSHSRNSDKSSSDRSRRSSSSRSSSNHSRVESSKRKSTKEKKSSSKDSRPSQAAGDNQGDEAKEQTFSGGTSQDIKGSESSKPWPDATTYGAGSASRASVSDLSPRERSPALKSPLQSVVVRRRSPRPSPVPKPSPPLSNASQMGSSMSGGAGYQSGAHQGQFDHGSGSLSPSKKSPVGKSPPATGSAYGSSQKEESAASGGAAYSKRYLEEQKTENGKDKEQKQTNADKEKLKEKGGFSDADVKMKSDPFAPKTDSEKPFRGSQSPKRYKLRDDFEKKMADFHKEELDEHDKDKSKGRKEPEFDDEPKFMSKVIAGASKNQEEEKSGKWESLHTGKEKQRKAEEMEDEPFTERSRKEERGGSKRSESGHRGFVPEKNFRVTAYKAVQEKSSSPPPRKTSESRDKLGSKGDFSSGKSSFSITREAQVNVRMDSFDEDLARPSGLLAQERKLCRDLVHSNKKEQEFRSIFQHIQSAQSQRSPSELFAQHIVTIVHHVKEHHFGSSGMTLHERFTKYLKRGNEQEAAKNKKSPEIHRRIDISPSTFRKHGLTHEELKSPREPGYKAEGKYKDDPVDLRLDIERRKKHKERDLKRGKSRESVDSRDSSHSRERSTEKTEKTHKGSKKQKKHRRARDRSRSSSSSSQSSHSYKAEEYPEEAEEREESTSGFDKSRLGTKDFVGPNERGGRARGTFQFRARGRGWGRGNYSGNNNNNSNNDFQKRSREEEWDPEYTPKSKKYYLHDDREGEGSDKWMGRGRGRGAFPRGRGRFMFRKSSTSPKWAHDKFSGEEGEIEDDESGTENREEKDSLQPSAE
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------MSKTNKSKS
------CCCCCCCCC
48.46-
13PhosphorylationKSKSGSRSSRSRSAS
CCCCCCCCHHCHHHH
31.6220531401
14PhosphorylationSKSGSRSSRSRSASR
CCCCCCCHHCHHHHH
32.9119854140
16PhosphorylationSGSRSSRSRSASRSR
CCCCCHHCHHHHHHH
32.3220531401
17MethylationGSRSSRSRSASRSRS
CCCCHHCHHHHHHHH
34.82-
38PhosphorylationRSRSRSVSRSRKRRL
HHHHHHHCHHHHHHH
26.2825890499
46PhosphorylationRSRKRRLSSRSRSRS
HHHHHHHHHHHHCCC
23.1523737553
47PhosphorylationSRKRRLSSRSRSRSY
HHHHHHHHHHHCCCC
38.5823737553
49PhosphorylationKRRLSSRSRSRSYSP
HHHHHHHHHCCCCCC
36.2325159016
51PhosphorylationRLSSRSRSRSYSPAH
HHHHHHHCCCCCCCC
27.1627742792
53PhosphorylationSSRSRSRSYSPAHNR
HHHHHCCCCCCCCCC
31.0725521595
54PhosphorylationSRSRSRSYSPAHNRE
HHHHCCCCCCCCCCC
19.9823684622
55PhosphorylationRSRSRSYSPAHNRER
HHHCCCCCCCCCCCC
19.5025521595
66Asymmetric dimethylarginineNRERNHPRVYQNRDF
CCCCCCCCCCCCCCC
32.02-
66MethylationNRERNHPRVYQNRDF
CCCCCCCCCCCCCCC
32.0254560283
71DimethylationHPRVYQNRDFRGHNR
CCCCCCCCCCCCCCC
28.99-
71MethylationHPRVYQNRDFRGHNR
CCCCCCCCCCCCCCC
28.9954560307
91DimethylationYYFRGRNRGFYPWGQ
CEECCCCCCCCCCCC
34.93-
91MethylationYYFRGRNRGFYPWGQ
CEECCCCCCCCCCCC
34.9354560291
101Asymmetric dimethylarginineYPWGQYNRGGYGNYR
CCCCCCCCCCCCCCC
34.67-
101MethylationYPWGQYNRGGYGNYR
CCCCCCCCCCCCCCC
34.6724129315
108Asymmetric dimethylarginineRGGYGNYRSNWQNYR
CCCCCCCCCCHHHHH
27.75-
108MethylationRGGYGNYRSNWQNYR
CCCCCCCCCCHHHHH
27.7524129315
114PhosphorylationYRSNWQNYRQAYSPR
CCCCHHHHHHHCCCC
6.7623984901
118PhosphorylationWQNYRQAYSPRRGRS
HHHHHHHCCCCCCCC
15.7425367039
119PhosphorylationQNYRQAYSPRRGRSR
HHHHHHCCCCCCCCC
18.2327087446
125PhosphorylationYSPRRGRSRSRSPKR
CCCCCCCCCCCCCCC
37.1119367708
127PhosphorylationPRRGRSRSRSPKRRS
CCCCCCCCCCCCCCC
38.0519367708
129PhosphorylationRGRSRSRSPKRRSPS
CCCCCCCCCCCCCCC
35.7023384938
134PhosphorylationSRSPKRRSPSPRSRS
CCCCCCCCCCCCCCC
33.4923684622
136PhosphorylationSPKRRSPSPRSRSHS
CCCCCCCCCCCCCCC
33.9023684622
139PhosphorylationRRSPSPRSRSHSRNS
CCCCCCCCCCCCCCC
41.3329899451
167PhosphorylationSRSSSNHSRVESSKR
CCCHHHHHHHHHHHC
42.1220139300
171PhosphorylationSNHSRVESSKRKSTK
HHHHHHHHHHCCCCC
38.0020139300
172PhosphorylationNHSRVESSKRKSTKE
HHHHHHHHHCCCCCC
23.9920139300
182PhosphorylationKSTKEKKSSSKDSRP
CCCCCCCCCCCCCCH
51.4125521595
183PhosphorylationSTKEKKSSSKDSRPS
CCCCCCCCCCCCCHH
50.7324453211
184PhosphorylationTKEKKSSSKDSRPSQ
CCCCCCCCCCCCHHH
47.8025521595
187PhosphorylationKKSSSKDSRPSQAAG
CCCCCCCCCHHHHCC
50.2325521595
190PhosphorylationSSKDSRPSQAAGDNQ
CCCCCCHHHHCCCCC
31.2025521595
205PhosphorylationGDEAKEQTFSGGTSQ
CHHHHHHHCCCCCCC
22.3625159016
207PhosphorylationEAKEQTFSGGTSQDI
HHHHHHCCCCCCCCC
39.4325521595
210PhosphorylationEQTFSGGTSQDIKGS
HHHCCCCCCCCCCCC
27.0923684622
211PhosphorylationQTFSGGTSQDIKGSE
HHCCCCCCCCCCCCC
29.1825521595
217PhosphorylationTSQDIKGSESSKPWP
CCCCCCCCCCCCCCC
29.3325367039
219PhosphorylationQDIKGSESSKPWPDA
CCCCCCCCCCCCCCC
45.4125367039
220PhosphorylationDIKGSESSKPWPDAT
CCCCCCCCCCCCCCC
38.3925367039
221AcetylationIKGSESSKPWPDATT
CCCCCCCCCCCCCCC
61.4522826441
227PhosphorylationSKPWPDATTYGAGSA
CCCCCCCCCCCCCCC
28.1225367039
228PhosphorylationKPWPDATTYGAGSAS
CCCCCCCCCCCCCCC
22.9826745281
229PhosphorylationPWPDATTYGAGSASR
CCCCCCCCCCCCCCC
10.7123984901
233PhosphorylationATTYGAGSASRASVS
CCCCCCCCCCCCCHH
23.6523684622
235PhosphorylationTYGAGSASRASVSDL
CCCCCCCCCCCHHHC
30.0326745281
238PhosphorylationAGSASRASVSDLSPR
CCCCCCCCHHHCCHH
22.5024925903
240PhosphorylationSASRASVSDLSPRER
CCCCCCHHHCCHHHC
30.2724925903
243PhosphorylationRASVSDLSPRERSPA
CCCHHHCCHHHCCHH
27.2318388127
248PhosphorylationDLSPRERSPALKSPL
HCCHHHCCHHHCCCC
15.1218388127
252AcetylationRERSPALKSPLQSVV
HHCCHHHCCCCEEEE
52.7322826441
252MethylationRERSPALKSPLQSVV
HHCCHHHCCCCEEEE
52.73-
253PhosphorylationERSPALKSPLQSVVV
HCCHHHCCCCEEEEE
31.5218388127
257PhosphorylationALKSPLQSVVVRRRS
HHCCCCEEEEEECCC
25.2724925903
264PhosphorylationSVVVRRRSPRPSPVP
EEEEECCCCCCCCCC
24.3726824392
268PhosphorylationRRRSPRPSPVPKPSP
ECCCCCCCCCCCCCC
39.5527742792
274PhosphorylationPSPVPKPSPPLSNAS
CCCCCCCCCCCCCHH
45.3226370283
278PhosphorylationPKPSPPLSNASQMGS
CCCCCCCCCHHHCCC
35.8025293948
281PhosphorylationSPPLSNASQMGSSMS
CCCCCCHHHCCCCCC
25.5826160508
285PhosphorylationSNASQMGSSMSGGAG
CCHHHCCCCCCCCCC
19.9526160508
286PhosphorylationNASQMGSSMSGGAGY
CHHHCCCCCCCCCCC
15.9626160508
288PhosphorylationSQMGSSMSGGAGYQS
HHCCCCCCCCCCCCC
35.7026160508
293PhosphorylationSMSGGAGYQSGAHQG
CCCCCCCCCCCCCCC
10.0426160508
295PhosphorylationSGGAGYQSGAHQGQF
CCCCCCCCCCCCCCC
29.4826160508
306PhosphorylationQGQFDHGSGSLSPSK
CCCCCCCCCCCCCCC
23.0726160508
308PhosphorylationQFDHGSGSLSPSKKS
CCCCCCCCCCCCCCC
27.6325266776
310PhosphorylationDHGSGSLSPSKKSPV
CCCCCCCCCCCCCCC
28.9126160508
312PhosphorylationGSGSLSPSKKSPVGK
CCCCCCCCCCCCCCC
49.7126160508
315PhosphorylationSLSPSKKSPVGKSPP
CCCCCCCCCCCCCCC
28.6725521595
320PhosphorylationKKSPVGKSPPATGSA
CCCCCCCCCCCCCCC
30.1327087446
324PhosphorylationVGKSPPATGSAYGSS
CCCCCCCCCCCCCCC
37.1324925903
326PhosphorylationKSPPATGSAYGSSQK
CCCCCCCCCCCCCHH
17.6024925903
328PhosphorylationPPATGSAYGSSQKEE
CCCCCCCCCCCHHHH
21.1624925903
330PhosphorylationATGSAYGSSQKEESA
CCCCCCCCCHHHHHH
19.5424925903
331PhosphorylationTGSAYGSSQKEESAA
CCCCCCCCHHHHHHH
40.6924925903
336PhosphorylationGSSQKEESAASGGAA
CCCHHHHHHHCCCHH
30.1725619855
339PhosphorylationQKEESAASGGAAYSK
HHHHHHHCCCHHHHH
37.1625619855
344PhosphorylationAASGGAAYSKRYLEE
HHCCCHHHHHHHHHH
17.7525619855
345PhosphorylationASGGAAYSKRYLEEQ
HCCCHHHHHHHHHHH
13.1125619855
346AcetylationSGGAAYSKRYLEEQK
CCCHHHHHHHHHHHC
32.1723806337
346MalonylationSGGAAYSKRYLEEQK
CCCHHHHHHHHHHHC
32.1726320211
353AcetylationKRYLEEQKTENGKDK
HHHHHHHCCCCCCCH
62.177615345
354PhosphorylationRYLEEQKTENGKDKE
HHHHHHCCCCCCCHH
34.0821659604
358AcetylationEQKTENGKDKEQKQT
HHCCCCCCCHHHHHH
76.767615357
369AcetylationQKQTNADKEKLKEKG
HHHHHHHHHHHHHHC
55.107615369
375UbiquitinationDKEKLKEKGGFSDAD
HHHHHHHHCCCCHHH
63.8527667366
379PhosphorylationLKEKGGFSDADVKMK
HHHHCCCCHHHCCCC
34.8527087446
386AcetylationSDADVKMKSDPFAPK
CHHHCCCCCCCCCCC
46.0923806337
387PhosphorylationDADVKMKSDPFAPKT
HHHCCCCCCCCCCCC
47.2027717184
394PhosphorylationSDPFAPKTDSEKPFR
CCCCCCCCCCCCCCC
43.6423429704
396PhosphorylationPFAPKTDSEKPFRGS
CCCCCCCCCCCCCCC
53.3923429704
398AcetylationAPKTDSEKPFRGSQS
CCCCCCCCCCCCCCC
54.1023806337
403PhosphorylationSEKPFRGSQSPKRYK
CCCCCCCCCCCCCCC
24.1918388127
405PhosphorylationKPFRGSQSPKRYKLR
CCCCCCCCCCCCCCH
33.8018388127
417AcetylationKLRDDFEKKMADFHK
CCHHHHHHHHHHHHH
48.0922826441
432AcetylationEELDEHDKDKSKGRK
HHHHHHCHHHCCCCC
69.8023806337
452AcetylationDEPKFMSKVIAGASK
CCHHHHHHHHHHCCC
26.3523806337
466PhosphorylationKNQEEEKSGKWESLH
CCHHHHHHCCCHHCC
49.2118779572
468AcetylationQEEEKSGKWESLHTG
HHHHHHCCCHHCCCH
55.6823806337
471PhosphorylationEKSGKWESLHTGKEK
HHHCCCHHCCCHHHH
25.0829514104
476AcetylationWESLHTGKEKQRKAE
CHHCCCHHHHHHHHH
63.9923806337
502PhosphorylationRKEERGGSKRSESGH
HHHHCCCCCCCCCCC
27.9327717184
505PhosphorylationERGGSKRSESGHRGF
HCCCCCCCCCCCCCC
39.5926745281
507PhosphorylationGGSKRSESGHRGFVP
CCCCCCCCCCCCCCC
40.9426745281
516AcetylationHRGFVPEKNFRVTAY
CCCCCCCCCEEEEEH
56.1423806337
524AcetylationNFRVTAYKAVQEKSS
CEEEEEHHHHHHHCC
39.3523806337
524MalonylationNFRVTAYKAVQEKSS
CEEEEEHHHHHHHCC
39.3526320211
530PhosphorylationYKAVQEKSSSPPPRK
HHHHHHHCCCCCCCC
34.9827087446
531PhosphorylationKAVQEKSSSPPPRKT
HHHHHHCCCCCCCCC
58.9125263469
532PhosphorylationAVQEKSSSPPPRKTS
HHHHHCCCCCCCCCC
48.8227087446
538PhosphorylationSSPPPRKTSESRDKL
CCCCCCCCCHHHHHH
38.7223375375
541PhosphorylationPPRKTSESRDKLGSK
CCCCCCHHHHHHCCC
45.6123375375
547PhosphorylationESRDKLGSKGDFSSG
HHHHHHCCCCCCCCC
43.8527681418
548MalonylationSRDKLGSKGDFSSGK
HHHHHCCCCCCCCCC
61.7826320211
552PhosphorylationLGSKGDFSSGKSSFS
HCCCCCCCCCCCCEE
42.8127149854
553PhosphorylationGSKGDFSSGKSSFSI
CCCCCCCCCCCCEEE
50.6729899451
555AcetylationKGDFSSGKSSFSITR
CCCCCCCCCCEEEEE
44.8923806337
555MalonylationKGDFSSGKSSFSITR
CCCCCCCCCCEEEEE
44.8926320211
555UbiquitinationKGDFSSGKSSFSITR
CCCCCCCCCCEEEEE
44.89-
556PhosphorylationGDFSSGKSSFSITRE
CCCCCCCCCEEEEEE
39.8926239621
557PhosphorylationDFSSGKSSFSITREA
CCCCCCCCEEEEEEE
26.8826239621
559PhosphorylationSSGKSSFSITREAQV
CCCCCCEEEEEEEEE
25.6228973931
561PhosphorylationGKSSFSITREAQVNV
CCCCEEEEEEEEEEE
22.6629899451
572PhosphorylationQVNVRMDSFDEDLAR
EEEEECCCCCHHHHC
25.8424925903
581PhosphorylationDEDLARPSGLLAQER
CHHHHCCCCHHHHHH
36.2028833060
597PhosphorylationLCRDLVHSNKKEQEF
HHHHHHHCCHHHHHH
42.75-
613PhosphorylationSIFQHIQSAQSQRSP
HHHHHHHHHHHCCCH
27.8926643407
616PhosphorylationQHIQSAQSQRSPSEL
HHHHHHHHCCCHHHH
27.5526643407
619PhosphorylationQSAQSQRSPSELFAQ
HHHHHCCCHHHHHHH
25.7425521595
621PhosphorylationAQSQRSPSELFAQHI
HHHCCCHHHHHHHHH
48.4525521595
630PhosphorylationLFAQHIVTIVHHVKE
HHHHHHHHHHHHHHH
19.3720415495
653UbiquitinationTLHERFTKYLKRGNE
HHHHHHHHHHHHCCH
45.9627667366
669PhosphorylationEAAKNKKSPEIHRRI
HHHHHCCCHHHHHHC
29.4025521595
679PhosphorylationIHRRIDISPSTFRKH
HHHHCCCCHHHHHHC
14.7318388127
681PhosphorylationRRIDISPSTFRKHGL
HHCCCCHHHHHHCCC
33.1324925903
682PhosphorylationRIDISPSTFRKHGLT
HCCCCHHHHHHCCCC
30.7324925903
685AcetylationISPSTFRKHGLTHEE
CCHHHHHHCCCCHHH
37.5223806337
689PhosphorylationTFRKHGLTHEELKSP
HHHHCCCCHHHHCCC
31.6525619855
695PhosphorylationLTHEELKSPREPGYK
CCHHHHCCCCCCCCC
41.6426824392
701PhosphorylationKSPREPGYKAEGKYK
CCCCCCCCCCCCCCC
20.1025159016
706AcetylationPGYKAEGKYKDDPVD
CCCCCCCCCCCCCCH
40.4023806337
734PhosphorylationRDLKRGKSRESVDSR
HHHHCCCCCHHHHCC
44.0727087446
737PhosphorylationKRGKSRESVDSRDSS
HCCCCCHHHHCCCCC
30.0725159016
740PhosphorylationKSRESVDSRDSSHSR
CCCHHHHCCCCCCCC
35.5127087446
743PhosphorylationESVDSRDSSHSRERS
HHHHCCCCCCCCCCC
28.9225159016
744PhosphorylationSVDSRDSSHSRERST
HHHCCCCCCCCCCCC
29.7625159016
746PhosphorylationDSRDSSHSRERSTEK
HCCCCCCCCCCCCHH
37.4725159016
750PhosphorylationSSHSRERSTEKTEKT
CCCCCCCCCHHCHHH
35.8422817900
776PhosphorylationRARDRSRSSSSSSQS
HHHHHCCCCCCCCCC
35.5023684622
777PhosphorylationARDRSRSSSSSSQSS
HHHHCCCCCCCCCCC
32.8825195567
778PhosphorylationRDRSRSSSSSSQSSH
HHHCCCCCCCCCCCC
35.1729895711
781PhosphorylationSRSSSSSSQSSHSYK
CCCCCCCCCCCCCCC
35.7129895711
783PhosphorylationSSSSSSQSSHSYKAE
CCCCCCCCCCCCCHH
31.7829895711
784PhosphorylationSSSSSQSSHSYKAEE
CCCCCCCCCCCCHHH
14.6029895711
786PhosphorylationSSSQSSHSYKAEEYP
CCCCCCCCCCHHHCH
30.2129895711
802PhosphorylationEAEEREESTSGFDKS
HHHHHHHHCCCCCHH
24.1025521595
803PhosphorylationAEEREESTSGFDKSR
HHHHHHHCCCCCHHH
35.8323375375
804PhosphorylationEEREESTSGFDKSRL
HHHHHHCCCCCHHHC
46.9027841257
808AcetylationESTSGFDKSRLGTKD
HHCCCCCHHHCCCCC
34.90-
825DimethylationGPNERGGRARGTFQF
CCCCCCCCCCEEEEE
24.76-
825MethylationGPNERGGRARGTFQF
CCCCCCCCCCEEEEE
24.7682954755
827DimethylationNERGGRARGTFQFRA
CCCCCCCCEEEEEEE
43.24-
827MethylationNERGGRARGTFQFRA
CCCCCCCCEEEEEEE
43.2424395871
841Asymmetric dimethylarginineARGRGWGRGNYSGNN
ECCCCCCCCCCCCCC
24.55-
841MethylationARGRGWGRGNYSGNN
ECCCCCCCCCCCCCC
24.5524129315
860PhosphorylationNNDFQKRSREEEWDP
CCCHHHHHHHHHCCC
51.5918388127
869PhosphorylationEEEWDPEYTPKSKKY
HHHCCCCCCCCCCCE
33.4625619855
870PhosphorylationEEWDPEYTPKSKKYY
HHCCCCCCCCCCCEE
23.6825521595
887PhosphorylationDDREGEGSDKWMGRG
CCCCCCCCCCCCCCC
31.5426643407
904DimethylationRGAFPRGRGRFMFRK
CCCCCCCCCCEEEEC
34.10-
904MethylationRGAFPRGRGRFMFRK
CCCCCCCCCCEEEEC
34.1054541805
906DimethylationAFPRGRGRFMFRKSS
CCCCCCCCEEEECCC
20.63-
906MethylationAFPRGRGRFMFRKSS
CCCCCCCCEEEECCC
20.6354541801
912PhosphorylationGRFMFRKSSTSPKWA
CCEEEECCCCCCCCC
34.2923684622
913PhosphorylationRFMFRKSSTSPKWAH
CEEEECCCCCCCCCC
35.6223684622
914PhosphorylationFMFRKSSTSPKWAHD
EEEECCCCCCCCCCC
57.0223684622
915PhosphorylationMFRKSSTSPKWAHDK
EEECCCCCCCCCCCC
26.8218779572
924PhosphorylationKWAHDKFSGEEGEIE
CCCCCCCCCCCCCCC
51.5427087446
935PhosphorylationGEIEDDESGTENREE
CCCCCCCCCCCCHHH
58.9927087446
937PhosphorylationIEDDESGTENREEKD
CCCCCCCCCCHHHHH
39.0925521595
945PhosphorylationENREEKDSLQPSAE-
CCHHHHHHCCCCCC-
39.7225159016
949PhosphorylationEKDSLQPSAE-----
HHHHCCCCCC-----
31.8825159016

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 TR150_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TR150_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 TR150_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TR150_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TR150_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-243; SER-248; SER-253;SER-572 AND SER-679, AND MASS SPECTROMETRY.
"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-119; SER-134; SER-238;SER-243; SER-248; SER-379; SER-572; SER-679; SER-695 AND SER-924, 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-51; SER-53; SER-55;SER-264; SER-268; SER-315; SER-320; SER-403; SER-405; SER-572; SER-860AND SER-924, AND MASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-679, ANDMASS SPECTROMETRY.
"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-248; SER-253; SER-315;SER-320; THR-324; SER-679; SER-924; SER-935 AND THR-937, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-253, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572 AND SER-935, ANDMASS SPECTROMETRY.
"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-572, AND MASSSPECTROMETRY.

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