PRP4B_HUMAN - dbPTM
PRP4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRP4B_HUMAN
UniProt AC Q13523
Protein Name Serine/threonine-protein kinase PRP4 homolog
Gene Name PRPF4B
Organism Homo sapiens (Human).
Sequence Length 1007
Subcellular Localization Nucleus.
Protein Description Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF..
Protein Sequence MAAAETQSLREQPEMEDANSEKSINEENGEVSEDQSQNKHSRHKKKKHKHRSKHKKHKHSSEEDKDKKHKHKHKHKKHKRKEIIDASDKEGMSPAKRTKLDDLALLEDLEKQRALIKAELDNELMEGKVQSGMGLILQGYESGSEEEGEIHEKARNGNRSSTRSSSTKGKLELVDNKITTKKRSKSRSKERTRHRSDKKKSKGGIEIVKEKTTRSKSKERKKSKSPSKRSKSQDQARKSKSPTLRRRSQEKIGKARSPTDDKVKIEDKSKSKDRKKSPIINESRSRDRGKKSRSPVDLRGKSKDRRSRSKERKSKRSETDKEKKPIKSPSKDASSGKENRSPSRRPGRSPKRRSLSPKPRDKSRRSRSPLLNDRRSKQSKSPSRTLSPGRRAKSRSLERKRREPERRRLSSPRTRPRDDILSRRERSKDASPINRWSPTRRRSRSPIRRRSRSPLRRSRSPRRRSRSPRRRDRGRRSRSRLRRRSRSRGGRRRRSRSKVKEDKFKGSLSEGMKVEQESSSDDNLEDFDVEEEDEEALIEQRRIQRQAIVQKYKYLAEDSNMSVPSEPSSPQSSTRTRSPSPDDILERVAADVKEYERENVDTFEASVKAKHNLMTVEQNNGSSQKKLLAPDMFTESDDMFAAYFDSARLRAAGIGKDFKENPNLRDNWTDAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDNARANQEVAVKIIRNNELMQKTGLKELEFLKKLNDADPDDKFHCLRLFRHFYHKQHLCLVFEPLSMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILHADIKPDNILVNESKTILKLCDFGSASHVADNDITPYLVSRFYRAPEIIIGKSYDYGIDMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGKMPNKMIRKGVFKDQHFDQNLNFMYIEVDKVTEREKVTVMSTINPTKDLLADLIGCQRLPEDQRKKVHQLKDLLDQILMLDPAKRISINQALQHAFIQEKI
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------MAAAETQSL
------CCHHHHHHH
27.0422223895
6Phosphorylation--MAAAETQSLREQP
--CCHHHHHHHHHCC
20.8023401153
8PhosphorylationMAAAETQSLREQPEM
CCHHHHHHHHHCCCC
36.4923401153
20O-linked_GlycosylationPEMEDANSEKSINEE
CCCCCCCCCCCCCCC
48.3930379171
20PhosphorylationPEMEDANSEKSINEE
CCCCCCCCCCCCCCC
48.3929255136
23PhosphorylationEDANSEKSINEENGE
CCCCCCCCCCCCCCC
26.9629255136
32PhosphorylationNEENGEVSEDQSQNK
CCCCCCCCHHHHHCH
31.0229255136
36PhosphorylationGEVSEDQSQNKHSRH
CCCCHHHHHCHHHHH
48.3029255136
41PhosphorylationDQSQNKHSRHKKKKH
HHHHCHHHHHHHHHH
37.3828387310
60PhosphorylationKHKKHKHSSEEDKDK
HHHHCCCCCHHHHHH
44.2230576142
61PhosphorylationHKKHKHSSEEDKDKK
HHHCCCCCHHHHHHH
44.7326657352
87PhosphorylationRKEIIDASDKEGMSP
HHHHCCCHHCCCCCH
45.5328176443
93PhosphorylationASDKEGMSPAKRTKL
CHHCCCCCHHHHCCH
32.3423927012
98PhosphorylationGMSPAKRTKLDDLAL
CCCHHHHCCHHHHHH
34.9426074081
99AcetylationMSPAKRTKLDDLALL
CCHHHHCCHHHHHHH
54.6925953088
99SumoylationMSPAKRTKLDDLALL
CCHHHHCCHHHHHHH
54.6928112733
99UbiquitinationMSPAKRTKLDDLALL
CCHHHHCCHHHHHHH
54.69-
111AcetylationALLEDLEKQRALIKA
HHHHHHHHHHHHHHH
53.0026051181
111SumoylationALLEDLEKQRALIKA
HHHHHHHHHHHHHHH
53.0028112733
111UbiquitinationALLEDLEKQRALIKA
HHHHHHHHHHHHHHH
53.00-
117SumoylationEKQRALIKAELDNEL
HHHHHHHHHHHCHHH
36.34-
117SumoylationEKQRALIKAELDNEL
HHHHHHHHHHHCHHH
36.3425114211
125SulfoxidationAELDNELMEGKVQSG
HHHCHHHHHCCCCCC
5.3521406390
131PhosphorylationLMEGKVQSGMGLILQ
HHHCCCCCCCEEHHH
33.4622167270
140PhosphorylationMGLILQGYESGSEEE
CEEHHHCCCCCCCCC
8.2529255136
142PhosphorylationLILQGYESGSEEEGE
EHHHCCCCCCCCCHH
38.8529255136
144PhosphorylationLQGYESGSEEEGEIH
HHCCCCCCCCCHHHH
51.6329255136
162PhosphorylationRNGNRSSTRSSSTKG
HCCCCCCCCCCCCCC
35.50-
164PhosphorylationGNRSSTRSSSTKGKL
CCCCCCCCCCCCCCE
28.8230108239
165PhosphorylationNRSSTRSSSTKGKLE
CCCCCCCCCCCCCEE
38.4430108239
166PhosphorylationRSSTRSSSTKGKLEL
CCCCCCCCCCCCEEE
35.0723401153
167PhosphorylationSSTRSSSTKGKLELV
CCCCCCCCCCCEEEE
45.8523401153
168AcetylationSTRSSSTKGKLELVD
CCCCCCCCCCEEEEC
56.877266923
170SumoylationRSSSTKGKLELVDNK
CCCCCCCCEEEECCC
40.10-
170AcetylationRSSSTKGKLELVDNK
CCCCCCCCEEEECCC
40.1023749302
170SumoylationRSSSTKGKLELVDNK
CCCCCCCCEEEECCC
40.1028112733
177AcetylationKLELVDNKITTKKRS
CEEEECCCCCCCCHH
36.6512432463
177SumoylationKLELVDNKITTKKRS
CEEEECCCCCCCCHH
36.6528112733
179PhosphorylationELVDNKITTKKRSKS
EEECCCCCCCCHHHH
33.8826074081
180PhosphorylationLVDNKITTKKRSKSR
EECCCCCCCCHHHHH
37.7326074081
182UbiquitinationDNKITTKKRSKSRSK
CCCCCCCCHHHHHCH
60.87-
184PhosphorylationKITTKKRSKSRSKER
CCCCCCHHHHHCHHH
43.8126074081
186PhosphorylationTTKKRSKSRSKERTR
CCCCHHHHHCHHHHC
42.9326074081
188PhosphorylationKKRSKSRSKERTRHR
CCHHHHHCHHHHCCH
46.0626074081
196PhosphorylationKERTRHRSDKKKSKG
HHHHCCHHHCCCCCC
47.89-
200AcetylationRHRSDKKKSKGGIEI
CCHHHCCCCCCCCCC
64.247296833
201PhosphorylationHRSDKKKSKGGIEIV
CHHHCCCCCCCCCCC
45.4723312004
202AcetylationRSDKKKSKGGIEIVK
HHHCCCCCCCCCCCE
70.777296845
209AcetylationKGGIEIVKEKTTRSK
CCCCCCCEECCCCCC
60.1926051181
230PhosphorylationSKSPSKRSKSQDQAR
CCCCCHHHHHHHHHH
40.1630242111
232PhosphorylationSPSKRSKSQDQARKS
CCCHHHHHHHHHHHC
39.9930576142
239PhosphorylationSQDQARKSKSPTLRR
HHHHHHHCCCHHHHH
32.5830266825
241PhosphorylationDQARKSKSPTLRRRS
HHHHHCCCHHHHHHH
30.1530266825
243PhosphorylationARKSKSPTLRRRSQE
HHHCCCHHHHHHHHH
39.7330266825
248PhosphorylationSPTLRRRSQEKIGKA
CHHHHHHHHHHHHCC
40.6626074081
257PhosphorylationEKIGKARSPTDDKVK
HHHHCCCCCCCCCCC
36.6922167270
259PhosphorylationIGKARSPTDDKVKIE
HHCCCCCCCCCCCCC
59.0630266825
277PhosphorylationKSKDRKKSPIINESR
CCCCCCCCCCCCCHH
25.1129255136
283PhosphorylationKSPIINESRSRDRGK
CCCCCCCHHCCCCCC
30.9429255136
285PhosphorylationPIINESRSRDRGKKS
CCCCCHHCCCCCCCC
48.0520363803
292PhosphorylationSRDRGKKSRSPVDLR
CCCCCCCCCCCCCCC
41.2929255136
294PhosphorylationDRGKKSRSPVDLRGK
CCCCCCCCCCCCCCC
36.0429255136
302PhosphorylationPVDLRGKSKDRRSRS
CCCCCCCCCCHHHHH
42.4826437602
314PhosphorylationSRSKERKSKRSETDK
HHHHHHHHHCCCCHH
39.2526074081
317PhosphorylationKERKSKRSETDKEKK
HHHHHHCCCCHHCCC
48.8926074081
319PhosphorylationRKSKRSETDKEKKPI
HHHHCCCCHHCCCCC
54.3326074081
328PhosphorylationKEKKPIKSPSKDASS
HCCCCCCCCCCCCCC
34.8222167270
330PhosphorylationKKPIKSPSKDASSGK
CCCCCCCCCCCCCCC
50.7022167270
334PhosphorylationKSPSKDASSGKENRS
CCCCCCCCCCCCCCC
50.1624732914
335PhosphorylationSPSKDASSGKENRSP
CCCCCCCCCCCCCCC
56.4526657352
341PhosphorylationSSGKENRSPSRRPGR
CCCCCCCCCCCCCCC
38.5226552605
343PhosphorylationGKENRSPSRRPGRSP
CCCCCCCCCCCCCCC
42.0126074081
349PhosphorylationPSRRPGRSPKRRSLS
CCCCCCCCCCCCCCC
40.4630266825
354PhosphorylationGRSPKRRSLSPKPRD
CCCCCCCCCCCCCCC
36.9122167270
356O-linked_GlycosylationSPKRRSLSPKPRDKS
CCCCCCCCCCCCCCC
31.9330379171
356PhosphorylationSPKRRSLSPKPRDKS
CCCCCCCCCCCCCCC
31.9322167270
358AcetylationKRRSLSPKPRDKSRR
CCCCCCCCCCCCCHH
49.6719608861
366PhosphorylationPRDKSRRSRSPLLND
CCCCCHHCCCHHHCC
35.6829255136
368PhosphorylationDKSRRSRSPLLNDRR
CCCHHCCCHHHCCHH
22.5829255136
376PhosphorylationPLLNDRRSKQSKSPS
HHHCCHHHCCCCCCC
35.6224300666
379PhosphorylationNDRRSKQSKSPSRTL
CCHHHCCCCCCCCCC
38.5530576142
381PhosphorylationRRSKQSKSPSRTLSP
HHHCCCCCCCCCCCC
33.1028355574
383PhosphorylationSKQSKSPSRTLSPGR
HCCCCCCCCCCCCCH
45.0125159151
385PhosphorylationQSKSPSRTLSPGRRA
CCCCCCCCCCCCHHH
35.6120164059
387PhosphorylationKSPSRTLSPGRRAKS
CCCCCCCCCCHHHHH
25.3730266825
394PhosphorylationSPGRRAKSRSLERKR
CCCHHHHHHHHHHHH
26.5622167270
396PhosphorylationGRRAKSRSLERKRRE
CHHHHHHHHHHHHHH
41.4922167270
410PhosphorylationEPERRRLSSPRTRPR
HHHHHHCCCCCCCCH
36.1623927012
411PhosphorylationPERRRLSSPRTRPRD
HHHHHCCCCCCCCHH
24.0023927012
414PhosphorylationRRLSSPRTRPRDDIL
HHCCCCCCCCHHHHH
48.7023403867
422PhosphorylationRPRDDILSRRERSKD
CCHHHHHHHHHHCCC
29.6220068231
427PhosphorylationILSRRERSKDASPIN
HHHHHHHCCCCCCCC
30.0922167270
431PhosphorylationRERSKDASPINRWSP
HHHCCCCCCCCCCCC
36.1229255136
437PhosphorylationASPINRWSPTRRRSR
CCCCCCCCCCCCCCC
17.1022167270
439PhosphorylationPINRWSPTRRRSRSP
CCCCCCCCCCCCCCC
31.1522167270
443PhosphorylationWSPTRRRSRSPIRRR
CCCCCCCCCCCCHHH
34.9930576142
445PhosphorylationPTRRRSRSPIRRRSR
CCCCCCCCCCHHHCC
26.4030576142
451PhosphorylationRSPIRRRSRSPLRRS
CCCCHHHCCCCCCCC
34.9922167270
453PhosphorylationPIRRRSRSPLRRSRS
CCHHHCCCCCCCCCC
29.5422167270
458PhosphorylationSRSPLRRSRSPRRRS
CCCCCCCCCCCCCCC
30.5820068231
460PhosphorylationSPLRRSRSPRRRSRS
CCCCCCCCCCCCCCC
24.8120068231
465PhosphorylationSRSPRRRSRSPRRRD
CCCCCCCCCCCCHHH
34.9930576142
467PhosphorylationSPRRRSRSPRRRDRG
CCCCCCCCCCHHHHH
24.8130576142
485PhosphorylationRSRLRRRSRSRGGRR
HHHHHHHHHHHCCCC
32.5626074081
487PhosphorylationRLRRRSRSRGGRRRR
HHHHHHHHHCCCCCC
36.2026074081
495PhosphorylationRGGRRRRSRSKVKED
HCCCCCCCHHHHCCH
38.8126074081
497PhosphorylationGRRRRSRSKVKEDKF
CCCCCCHHHHCCHHH
42.9426074081
505MethylationKVKEDKFKGSLSEGM
HHCCHHHCCCCCCCC
54.02115975717
507PhosphorylationKEDKFKGSLSEGMKV
CCHHHCCCCCCCCCC
29.3425137130
509PhosphorylationDKFKGSLSEGMKVEQ
HHHCCCCCCCCCCEE
33.5325850435
518PhosphorylationGMKVEQESSSDDNLE
CCCCEECCCCCCCHH
34.5328102081
519PhosphorylationMKVEQESSSDDNLED
CCCEECCCCCCCHHH
36.7128102081
520PhosphorylationKVEQESSSDDNLEDF
CCEECCCCCCCHHHC
59.2628102081
551UbiquitinationQRQAIVQKYKYLAED
HHHHHHHHHHHHHCC
32.58-
552PhosphorylationRQAIVQKYKYLAEDS
HHHHHHHHHHHHCCC
6.4322468782
554PhosphorylationAIVQKYKYLAEDSNM
HHHHHHHHHHCCCCC
14.1920068231
559PhosphorylationYKYLAEDSNMSVPSE
HHHHHCCCCCCCCCC
26.4123663014
562PhosphorylationLAEDSNMSVPSEPSS
HHCCCCCCCCCCCCC
34.8226055452
565PhosphorylationDSNMSVPSEPSSPQS
CCCCCCCCCCCCCCC
61.0425159151
568PhosphorylationMSVPSEPSSPQSSTR
CCCCCCCCCCCCCCC
51.0725159151
569PhosphorylationSVPSEPSSPQSSTRT
CCCCCCCCCCCCCCC
37.3625159151
572PhosphorylationSEPSSPQSSTRTRSP
CCCCCCCCCCCCCCC
36.7425159151
573PhosphorylationEPSSPQSSTRTRSPS
CCCCCCCCCCCCCCC
19.3622115753
574PhosphorylationPSSPQSSTRTRSPSP
CCCCCCCCCCCCCCH
41.1121712546
576PhosphorylationSPQSSTRTRSPSPDD
CCCCCCCCCCCCHHH
35.2729255136
578PhosphorylationQSSTRTRSPSPDDIL
CCCCCCCCCCHHHHH
29.1729255136
580PhosphorylationSTRTRSPSPDDILER
CCCCCCCCHHHHHHH
42.0529255136
5932-HydroxyisobutyrylationERVAADVKEYERENV
HHHHHHHHHHHHHCC
55.94-
593SumoylationERVAADVKEYERENV
HHHHHHHHHHHHHCC
55.9428112733
595PhosphorylationVAADVKEYERENVDT
HHHHHHHHHHHCCCC
17.9928064214
602PhosphorylationYERENVDTFEASVKA
HHHHCCCCHHHHHHH
21.0621815630
606PhosphorylationNVDTFEASVKAKHNL
CCCCHHHHHHHHHHC
19.5621815630
615PhosphorylationKAKHNLMTVEQNNGS
HHHHHCEEEEECCCC
24.8529888752
622PhosphorylationTVEQNNGSSQKKLLA
EEEECCCCCCCEECC
31.5520068231
623PhosphorylationVEQNNGSSQKKLLAP
EEECCCCCCCEECCC
47.6320068231
625AcetylationQNNGSSQKKLLAPDM
ECCCCCCCEECCCCC
47.5425953088
634PhosphorylationLLAPDMFTESDDMFA
ECCCCCCCCCHHHHH
28.1328464451
636PhosphorylationAPDMFTESDDMFAAY
CCCCCCCCHHHHHHH
35.5322115753
643PhosphorylationSDDMFAAYFDSARLR
CHHHHHHHHHHHHHH
12.4227732954
646PhosphorylationMFAAYFDSARLRAAG
HHHHHHHHHHHHHCC
12.8527732954
6562-HydroxyisobutyrylationLRAAGIGKDFKENPN
HHHCCCCCCCCCCCC
59.06-
656AcetylationLRAAGIGKDFKENPN
HHHCCCCCCCCCCCC
59.0623749302
656UbiquitinationLRAAGIGKDFKENPN
HHHCCCCCCCCCCCC
59.06-
659AcetylationAGIGKDFKENPNLRD
CCCCCCCCCCCCCCC
67.7126051181
659SumoylationAGIGKDFKENPNLRD
CCCCCCCCCCCCCCC
67.7128112733
659UbiquitinationAGIGKDFKENPNLRD
CCCCCCCCCCCCCCC
67.71-
674PhosphorylationNWTDAEGYYRVNIGE
CCCCCCCEEECCHHH
4.60-
6852-HydroxyisobutyrylationNIGEVLDKRYNVYGY
CHHHHHHCCCCEECE
53.25-
685AcetylationNIGEVLDKRYNVYGY
CHHHHHHCCCCEECE
53.2523749302
685MalonylationNIGEVLDKRYNVYGY
CHHHHHHCCCCEECE
53.2526320211
685UbiquitinationNIGEVLDKRYNVYGY
CHHHHHHCCCCEECE
53.25-
687PhosphorylationGEVLDKRYNVYGYTG
HHHHHCCCCEECEEC
18.0828152594
690PhosphorylationLDKRYNVYGYTGQGV
HHCCCCEECEECCCH
10.7728152594
717AcetylationANQEVAVKIIRNNEL
CCHHHHHHHHHCCHH
23.7619608861
7272-HydroxyisobutyrylationRNNELMQKTGLKELE
HCCHHHHHHCHHHHH
30.51-
727AcetylationRNNELMQKTGLKELE
HCCHHHHHHCHHHHH
30.5125953088
727UbiquitinationRNNELMQKTGLKELE
HCCHHHHHHCHHHHH
30.51-
731AcetylationLMQKTGLKELEFLKK
HHHHHCHHHHHHHHH
62.6926051181
731UbiquitinationLMQKTGLKELEFLKK
HHHHHCHHHHHHHHH
62.69-
737AcetylationLKELEFLKKLNDADP
HHHHHHHHHHCCCCC
61.6123749302
7472-HydroxyisobutyrylationNDADPDDKFHCLRLF
CCCCCCCHHHHHHHH
44.37-
747AcetylationNDADPDDKFHCLRLF
CCCCCCCHHHHHHHH
44.3725825284
794PhosphorylationLHIKAVRSYSQQLFL
HHHHHHHHHHHHHHH
23.65-
795PhosphorylationHIKAVRSYSQQLFLA
HHHHHHHHHHHHHHH
10.4322210691
817AcetylationNILHADIKPDNILVN
CEECCCCCCCCEEEC
47.0326051181
817UbiquitinationNILHADIKPDNILVN
CEECCCCCCCCEEEC
47.03-
837PhosphorylationLKLCDFGSASHVADN
HHHCCCCCHHHCCCC
26.9621945579
839PhosphorylationLCDFGSASHVADNDI
HCCCCCHHHCCCCCC
21.8621945579
847PhosphorylationHVADNDITPYLVSRF
HCCCCCCHHHHHHHH
14.5629255136
848PhosphorylationVADNDITPYLVSRFY
CCCCCCHHHHHHHHH
22.3117016520
849PhosphorylationADNDITPYLVSRFYR
CCCCCHHHHHHHHHC
15.8729255136
852PhosphorylationDITPYLVSRFYRAPE
CCHHHHHHHHHCCCE
17.6829255136
855PhosphorylationPYLVSRFYRAPEIII
HHHHHHHHCCCEEEE
12.5422817900
892UbiquitinationGKILFPGKTNNHMLK
CCEECCCCCCHHHHH
48.60-
905AcetylationLKLAMDLKGKMPNKM
HHHHHHHCCCCCCHH
52.8219608861
907AcetylationLAMDLKGKMPNKMIR
HHHHHCCCCCCHHHH
49.9919608861
938PhosphorylationYIEVDKVTEREKVTV
EEEEEECCCCEEEEE
34.7623322592
944PhosphorylationVTEREKVTVMSTINP
CCCCEEEEEEECCCC
22.8923322592
946SulfoxidationEREKVTVMSTINPTK
CCEEEEEEECCCCCH
1.8221406390
947PhosphorylationREKVTVMSTINPTKD
CEEEEEEECCCCCHH
23.0729978859
948PhosphorylationEKVTVMSTINPTKDL
EEEEEEECCCCCHHH
13.4823322592
952PhosphorylationVMSTINPTKDLLADL
EEECCCCCHHHHHHH
32.4721601212

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 PRP4B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRP4B_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 PRP4B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PININ_HUMANPNNphysical
12077342
PRP8_HUMANPRPF8physical
22939629
U5S1_HUMANEFTUD2physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
RS11_HUMANRPS11physical
22939629
RL5_HUMANRPL5physical
22939629
MK12_HUMANMAPK12physical
23602568
SRRM2_HUMANSRRM2physical
23602568
PININ_HUMANPNNphysical
23602568
PRP8_HUMANPRPF8physical
23602568
PRP6_HUMANPRPF6physical
23602568
U520_HUMANSNRNP200physical
23602568
DDX23_HUMANDDX23physical
23602568
U5S1_HUMANEFTUD2physical
23602568
SNUT1_HUMANSART1physical
23602568
SNUT2_HUMANUSP39physical
23602568
PRP4_HUMANPRPF4physical
23602568
SNR40_HUMANSNRNP40physical
23602568
PRP31_HUMANPRPF31physical
23602568
RSMB_HUMANSNRPBphysical
23602568
SMD1_HUMANSNRPD1physical
23602568
CPSF5_HUMANNUDT21physical
23602568

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 PRP4B_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87; SER-93; SER-142 ANDSER-144, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6 AND SER-8, ACETYLATION[LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-358 AND LYS-717, AND MASSSPECTROMETRY.
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-20; SER-23; SER-32;TYR-140; SER-142; SER-144; SER-518; SER-519; SER-520; SER-578 ANDSER-580, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87; SER-93; SER-142 ANDSER-144, 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 SER-20; SER-23; SER-32;SER-87; SER-93; TYR-140; SER-142; SER-144; SER-257; SER-277; SER-292;SER-294; SER-427; SER-431; SER-437; SER-518; SER-519; SER-520;SER-569; SER-578; SER-580 AND TYR-849, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6 AND SER-8, ACETYLATION[LARGE SCALE ANALYSIS] AT ALA-2, AND MASS 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-277; SER-366 ANDSER-368, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-294, ANDMASS SPECTROMETRY.
"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-20; SER-23; SER-32;SER-87; SER-93; SER-239; SER-241; SER-257; SER-277; SER-292; SER-294;SER-328; SER-366; SER-368; SER-381; THR-385; SER-387; SER-410;SER-411; SER-431; SER-437; THR-576; SER-578; SER-580 AND TYR-849, 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-20; SER-23; SER-32;SER-36; SER-277; SER-294; SER-354; SER-356; SER-366; SER-368; SER-387;SER-431; SER-437; SER-569; SER-578 AND SER-580, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-849, AND MASSSPECTROMETRY.

TOP