PCF11_HUMAN - dbPTM
PCF11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCF11_HUMAN
UniProt AC O94913
Protein Name Pre-mRNA cleavage complex 2 protein Pcf11
Gene Name PCF11
Organism Homo sapiens (Human).
Sequence Length 1555
Subcellular Localization Nucleus.
Protein Description Component of pre-mRNA cleavage complex II..
Protein Sequence MSEQTPAEAGAAGAREDACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYLMDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKKLYALDVRVNSLDPAWPIKPLPPNVNTSSIHVNPKFLNKSPEEPSTPGTVVSSPSISTPPIVPDIQKNLTQEQLIRQQLLAKQKQLLELQQKKLELELEQAKAQLAVSLSVQQETSNLGPGSAPSKLHVSQIPPMAVKAPHQVPVQSEKSRPGPSLQIQDLKGTNRDPRLNRISQHSHGKDQSHRKEFLMNTLNQSDTKTSKTIPSEKLNSSKQEKSKSGEKITKKELDQLDSKSKSKSKSPSPLKNKLSHTKDLKNQESESMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLAGSRNKIINGIVQKQDTITEESEKQGTKPGRSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQRSMSPTSTPKAGKIRQSGAKQSHMEEFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETTNQHSTKSGTEPKENVENWQSSKSAKRWKSGWEENKSLQQVDEHSKPPHLRHRESWSSTKGILSPRAPKQQQHRLSVDANLQIPKELTLASKRELLQKTSERLASGEITQDDFLVVVHQIRQLFQYQEGVREEQRSPFNDRFPLKRPRYEDSDKPFVDSPASRFAGLDTNQRLTALAEDRPLFDGPSRPSVARDGPTKMIFEGPNKLSPRIDGPPTPASLRFDGSPGQMGGGGPLRFEGPQGQLGGGCPLRFEGPPGPVGTPLRFEGPIGQAGGGGFRFEGSPGLRFEGSPGGLRFEGPGGQPVGGLRFEGHRGQPVGGLRFEGPHGQPVGGLRFDNPRGQPVGGLRFEGGHGPSGAAIRFDGPHGQPGGGIRFEGPLLQQGVGMRFEGPHGQSVAGLRFEGQHNQLGGNLRFEGPHGQPGVGIRFEGPLVQQGGGMRFEGPSVPGGGLRIEGPLGQGGPRFEGCHALRFDGQPGQPSLLPRFDGLHGQPGPRFERTPGQPGPQRFDGPPGQQVQPRFDGVPQRFDGPQHQQASRFDIPLGLQGTRFDNHPSQRLESVSFNQTGPYNDPPGNAFNAPSQGLQFQRHEQIFDSPQGPNFNGPHGPGNQSFSNPLNRASGHYFDEKNLQSSQFGNFGNIPAPMTVGNIQASQQVLSGVAQPVAFGQGQQFLPVHPQNPGFVQNPSGALPKAYPDNHLSQVDVNELFSKLLKTGILKLSQTDSATTQVSEVTAQPPPEEEEDQNEDQDVPDLTNFTVEELKQRYDSVINRLYTGIQCYSCGMRFTTSQTDVYADHLDWHYRQNRTEKDVSRKVTHRRWYYSLTDWIEFEEIADLEERAKSQFFEKVHEEVVLKTQEAAKEKEFQSVPAGPAGAVESCEICQEQFEQYWDEEEEEWHLKNAIRVDGKIYHPSCYEDYQNTSSFDCTPSPSKTPVENPLNIMLNIVKNELQEPCDSPKVKEERIDTPPACTEESIATPSEIKTENDTVESV
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------MSEQTPAEA
------CCCCCHHHH
50.1122814378
22PhosphorylationREDACRDYQSSLEDL
HHHHHHHHHHHHHHC
7.3120068231
24PhosphorylationDACRDYQSSLEDLTF
HHHHHHHHHHHHCCC
30.5720068231
25PhosphorylationACRDYQSSLEDLTFN
HHHHHHHHHHHCCCC
21.9120068231
30PhosphorylationQSSLEDLTFNSKPHI
HHHHHHCCCCCCCCC
32.8520068231
33PhosphorylationLEDLTFNSKPHINML
HHHCCCCCCCCCCHH
43.2920068231
56PhosphorylationPFAKEIVSLIEAQTA
HHHHHHHHHHHHHCC
29.3224144214
62PhosphorylationVSLIEAQTAKAPSSE
HHHHHHHCCCCCCCC
36.8524144214
64UbiquitinationLIEAQTAKAPSSEKL
HHHHHCCCCCCCCCC
65.3029967540
67PhosphorylationAQTAKAPSSEKLPVM
HHCCCCCCCCCCCHH
56.8626552605
68PhosphorylationQTAKAPSSEKLPVMY
HCCCCCCCCCCCHHH
37.3826552605
75PhosphorylationSEKLPVMYLMDSIVK
CCCCCHHHHHHHHHH
10.1026552605
79PhosphorylationPVMYLMDSIVKNVGR
CHHHHHHHHHHHHCH
18.4724719451
114PhosphorylationVDENTRKSLFKLRST
CCCCHHHHHHHHHHC
35.4324719451
120PhosphorylationKSLFKLRSTWDEIFP
HHHHHHHHCHHHHCC
44.26-
121PhosphorylationSLFKLRSTWDEIFPL
HHHHHHHCHHHHCCH
30.42-
129UbiquitinationWDEIFPLKKLYALDV
HHHHCCHHHEEEEEC
40.7629967540
130UbiquitinationDEIFPLKKLYALDVR
HHHCCHHHEEEEECC
55.18-
140PhosphorylationALDVRVNSLDPAWPI
EEECCCCCCCCCCCC
31.15-
164AcetylationSSIHVNPKFLNKSPE
CCEECCHHHCCCCCC
58.2325953088
169PhosphorylationNPKFLNKSPEEPSTP
CHHHCCCCCCCCCCC
36.1523401153
174PhosphorylationNKSPEEPSTPGTVVS
CCCCCCCCCCCCEEC
50.9825159151
175PhosphorylationKSPEEPSTPGTVVSS
CCCCCCCCCCCEECC
36.1325159151
178O-linked_GlycosylationEEPSTPGTVVSSPSI
CCCCCCCCEECCCCC
20.9530379171
178PhosphorylationEEPSTPGTVVSSPSI
CCCCCCCCEECCCCC
20.9525159151
181O-linked_GlycosylationSTPGTVVSSPSISTP
CCCCCEECCCCCCCC
31.9930379171
181PhosphorylationSTPGTVVSSPSISTP
CCCCCEECCCCCCCC
31.9925159151
182PhosphorylationTPGTVVSSPSISTPP
CCCCEECCCCCCCCC
15.8525159151
184PhosphorylationGTVVSSPSISTPPIV
CCEECCCCCCCCCCC
30.9925159151
186PhosphorylationVVSSPSISTPPIVPD
EECCCCCCCCCCCCC
38.9225159151
187PhosphorylationVSSPSISTPPIVPDI
ECCCCCCCCCCCCCH
31.2625159151
196UbiquitinationPIVPDIQKNLTQEQL
CCCCCHHHCCCHHHH
55.0129967540
211UbiquitinationIRQQLLAKQKQLLEL
HHHHHHHHHHHHHHH
58.9829967540
237PhosphorylationAKAQLAVSLSVQQET
HHHHHHHEEECCCCC
14.8722210691
239PhosphorylationAQLAVSLSVQQETSN
HHHHHEEECCCCCCC
15.4622210691
251PhosphorylationTSNLGPGSAPSKLHV
CCCCCCCCCCCCEEC
39.8922210691
259PhosphorylationAPSKLHVSQIPPMAV
CCCCEECCCCCCCCC
16.1922210691
267AcetylationQIPPMAVKAPHQVPV
CCCCCCCCCCCCCCC
46.8125953088
268PhosphorylationIPPMAVKAPHQVPVQ
CCCCCCCCCCCCCCC
10.5418669648
277PhosphorylationHQVPVQSEKSRPGPS
CCCCCCCCCCCCCCC
37.6518669648
279PhosphorylationVPVQSEKSRPGPSLQ
CCCCCCCCCCCCCCC
39.3928555341
280PhosphorylationPVQSEKSRPGPSLQI
CCCCCCCCCCCCCCE
51.7918669648
281PhosphorylationVQSEKSRPGPSLQIQ
CCCCCCCCCCCCCEE
67.1618669648
283PhosphorylationSEKSRPGPSLQIQDL
CCCCCCCCCCCEECC
34.2518669648
285PhosphorylationKSRPGPSLQIQDLKG
CCCCCCCCCEECCCC
6.1418669648
286PhosphorylationSRPGPSLQIQDLKGT
CCCCCCCCEECCCCC
35.3218669648
291SumoylationSLQIQDLKGTNRDPR
CCCEECCCCCCCCHH
72.4828112733
303PhosphorylationDPRLNRISQHSHGKD
CHHHHHHHHCCCCCC
20.7129449344
306PhosphorylationLNRISQHSHGKDQSH
HHHHHHCCCCCCHHH
26.7129449344
312PhosphorylationHSHGKDQSHRKEFLM
CCCCCCHHHHHHHHH
35.08-
319SulfoxidationSHRKEFLMNTLNQSD
HHHHHHHHHHCCCCC
4.3521406390
321PhosphorylationRKEFLMNTLNQSDTK
HHHHHHHHCCCCCCC
17.08-
325PhosphorylationLMNTLNQSDTKTSKT
HHHHCCCCCCCCCCC
46.2925159151
327PhosphorylationNTLNQSDTKTSKTIP
HHCCCCCCCCCCCCC
41.28-
328SumoylationTLNQSDTKTSKTIPS
HCCCCCCCCCCCCCH
56.6528112733
337AcetylationSKTIPSEKLNSSKQE
CCCCCHHHHCCCHHH
58.2523749302
355AcetylationSGEKITKKELDQLDS
CCCCCCHHHHHHHHH
55.6626051181
362PhosphorylationKELDQLDSKSKSKSK
HHHHHHHHHCCCCCC
47.6326074081
364PhosphorylationLDQLDSKSKSKSKSP
HHHHHHHCCCCCCCC
46.2226074081
366PhosphorylationQLDSKSKSKSKSPSP
HHHHHCCCCCCCCCH
49.6126074081
368PhosphorylationDSKSKSKSKSPSPLK
HHHCCCCCCCCCHHH
45.5226055452
370PhosphorylationKSKSKSKSPSPLKNK
HCCCCCCCCCHHHHH
37.3925159151
372PhosphorylationKSKSKSPSPLKNKLS
CCCCCCCCHHHHHHH
50.3725159151
379PhosphorylationSPLKNKLSHTKDLKN
CHHHHHHHCCHHHCC
30.6226074081
381PhosphorylationLKNKLSHTKDLKNQE
HHHHHHCCHHHCCCC
23.9126074081
382UbiquitinationKNKLSHTKDLKNQES
HHHHHCCHHHCCCCC
56.4929967540
389PhosphorylationKDLKNQESESMRLSD
HHHCCCCCHHHHHHH
25.8026074081
391PhosphorylationLKNQESESMRLSDMN
HCCCCCHHHHHHHHH
20.6228555341
395PhosphorylationESESMRLSDMNKRDP
CCHHHHHHHHHHCCH
25.1725159151
420UbiquitinationDGKDDDVKEKRKTAE
CCCCCCHHHHHHHHH
65.5924816145
456SumoylationIINGIVQKQDTITEE
HHHHHHHHCCCCCHH
38.97-
456SumoylationIINGIVQKQDTITEE
HHHHHHHHCCCCCHH
38.9728112733
459PhosphorylationGIVQKQDTITEESEK
HHHHHCCCCCHHHHH
27.5723917254
461PhosphorylationVQKQDTITEESEKQG
HHHCCCCCHHHHHCC
35.4723186163
480PhosphorylationRSSTRKRSRSRSPKS
CCCCCHHCCCCCCCC
37.3329743597
482PhosphorylationSTRKRSRSRSPKSRS
CCCHHCCCCCCCCCC
38.0529743597
484PhosphorylationRKRSRSRSPKSRSPI
CHHCCCCCCCCCCCC
37.6222468782
487PhosphorylationSRSRSPKSRSPIIHS
CCCCCCCCCCCCCCC
41.1825159151
489PhosphorylationSRSPKSRSPIIHSPK
CCCCCCCCCCCCCCC
27.7822167270
494PhosphorylationSRSPIIHSPKRRDRR
CCCCCCCCCCCCCCC
23.0022167270
502PhosphorylationPKRRDRRSPKRRQRS
CCCCCCCCHHHHHHC
35.35-
509O-linked_GlycosylationSPKRRQRSMSPTSTP
CHHHHHHCCCCCCCC
18.4430379171
509PhosphorylationSPKRRQRSMSPTSTP
CHHHHHHCCCCCCCC
18.4430266825
511O-linked_GlycosylationKRRQRSMSPTSTPKA
HHHHHCCCCCCCCCC
26.6930379171
511PhosphorylationKRRQRSMSPTSTPKA
HHHHHCCCCCCCCCC
26.6929255136
513PhosphorylationRQRSMSPTSTPKAGK
HHHCCCCCCCCCCCC
37.6230266825
514PhosphorylationQRSMSPTSTPKAGKI
HHCCCCCCCCCCCCC
46.2030266825
515PhosphorylationRSMSPTSTPKAGKIR
HCCCCCCCCCCCCCC
31.1430266825
529PhosphorylationRQSGAKQSHMEEFTP
CCCCCCHHCHHHCCC
24.8923312004
535PhosphorylationQSHMEEFTPPSREDR
HHCHHHCCCCCHHHH
37.2525159151
538PhosphorylationMEEFTPPSREDRNAK
HHHCCCCCHHHHHCC
49.8928985074
547PhosphorylationEDRNAKRSTKQDIRD
HHHHCCCCCHHHHHC
38.9724719451
561PhosphorylationDPRRMKKTEEERPQE
CHHHHHCCHHHCCCC
43.01-
569PhosphorylationEEERPQETTNQHSTK
HHHCCCCCCCCCCCC
26.29-
570PhosphorylationEERPQETTNQHSTKS
HHCCCCCCCCCCCCC
31.93-
588PhosphorylationPKENVENWQSSKSAK
CCHHHHHHHHCHHHH
5.9717081983
593PhosphorylationENWQSSKSAKRWKSG
HHHHHCHHHHHHHHH
40.7617081983
606PhosphorylationSGWEENKSLQQVDEH
HHHHHHHCHHHHCCC
42.8828555341
624PhosphorylationPHLRHRESWSSTKGI
CCCCCCHHHHCCCCC
32.0130576142
626PhosphorylationLRHRESWSSTKGILS
CCCCHHHHCCCCCCC
37.0926055452
627PhosphorylationRHRESWSSTKGILSP
CCCHHHHCCCCCCCC
28.0727251275
628PhosphorylationHRESWSSTKGILSPR
CCHHHHCCCCCCCCC
27.9827251275
633PhosphorylationSSTKGILSPRAPKQQ
HCCCCCCCCCCCCHH
15.4925159151
645PhosphorylationKQQQHRLSVDANLQI
CHHCCCCCCCCCCCC
20.2225159151
654SumoylationDANLQIPKELTLASK
CCCCCCCHHHHHHHH
67.9728112733
661AcetylationKELTLASKRELLQKT
HHHHHHHHHHHHHHH
44.2625953088
661UbiquitinationKELTLASKRELLQKT
HHHHHHHHHHHHHHH
44.2629967540
667UbiquitinationSKRELLQKTSERLAS
HHHHHHHHHHHHHHC
54.72-
705PhosphorylationGVREEQRSPFNDRFP
CCCHHHCCCCCCCCC
33.2729255136
721PhosphorylationKRPRYEDSDKPFVDS
CCCCCCCCCCCCCCC
35.2824732914
723AcetylationPRYEDSDKPFVDSPA
CCCCCCCCCCCCCHH
44.2823236377
723SumoylationPRYEDSDKPFVDSPA
CCCCCCCCCCCCCHH
44.2828112733
723UbiquitinationPRYEDSDKPFVDSPA
CCCCCCCCCCCCCHH
44.2829967540
728PhosphorylationSDKPFVDSPASRFAG
CCCCCCCCHHHHHCC
19.6425159151
731PhosphorylationPFVDSPASRFAGLDT
CCCCCHHHHHCCCCH
31.1724732914
738PhosphorylationSRFAGLDTNQRLTAL
HHHCCCCHHHHHHHH
37.9928555341
756PhosphorylationRPLFDGPSRPSVARD
CCCCCCCCCCCCCCC
63.4524719451
759PhosphorylationFDGPSRPSVARDGPT
CCCCCCCCCCCCCCC
27.5728555341
766PhosphorylationSVARDGPTKMIFEGP
CCCCCCCCEEEEECC
38.48-
775AcetylationMIFEGPNKLSPRIDG
EEEECCCCCCCCCCC
54.1725953088
775UbiquitinationMIFEGPNKLSPRIDG
EEEECCCCCCCCCCC
54.1724816145
777PhosphorylationFEGPNKLSPRIDGPP
EECCCCCCCCCCCCC
17.4729255136
779MethylationGPNKLSPRIDGPPTP
CCCCCCCCCCCCCCC
35.93115486619
785PhosphorylationPRIDGPPTPASLRFD
CCCCCCCCCCCEEEC
34.3230266825
788PhosphorylationDGPPTPASLRFDGSP
CCCCCCCCEEECCCC
22.6830266825
790MethylationPPTPASLRFDGSPGQ
CCCCCCEEECCCCCC
25.7281452609
794PhosphorylationASLRFDGSPGQMGGG
CCEEECCCCCCCCCC
27.9229255136
804PhosphorylationQMGGGGPLRFEGPQG
CCCCCCCCEEECCCC
12.7018220336
805Asymmetric dimethylarginineMGGGGPLRFEGPQGQ
CCCCCCCEEECCCCC
30.61-
805MethylationMGGGGPLRFEGPQGQ
CCCCCCCEEECCCCC
30.6124129315
820Asymmetric dimethylarginineLGGGCPLRFEGPPGP
CCCCCCCEECCCCCC
16.83-
820MethylationLGGGCPLRFEGPPGP
CCCCCCCEECCCCCC
16.8324129315
827PhosphorylationRFEGPPGPVGTPLRF
EECCCCCCCCCCEEE
27.4318669648
830PhosphorylationGPPGPVGTPLRFEGP
CCCCCCCCCEEEECC
21.2721815630
833Asymmetric dimethylarginineGPVGTPLRFEGPIGQ
CCCCCCEEEECCCCC
28.86-
833MethylationGPVGTPLRFEGPIGQ
CCCCCCEEEECCCCC
28.8624129315
847DimethylationQAGGGGFRFEGSPGL
CCCCCCCEECCCCCC
31.79-
847MethylationQAGGGGFRFEGSPGL
CCCCCCCEECCCCCC
31.79115383869
851PhosphorylationGGFRFEGSPGLRFEG
CCCEECCCCCCEECC
14.4830266825
854UbiquitinationRFEGSPGLRFEGSPG
EECCCCCCEECCCCC
6.8629967540
855DimethylationFEGSPGLRFEGSPGG
ECCCCCCEECCCCCC
33.22-
855MethylationFEGSPGLRFEGSPGG
ECCCCCCEECCCCCC
33.2280702721
859PhosphorylationPGLRFEGSPGGLRFE
CCCEECCCCCCEEEE
17.1121815630
864DimethylationEGSPGGLRFEGPGGQ
CCCCCCEEEECCCCC
30.74-
864MethylationEGSPGGLRFEGPGGQ
CCCCCCEEEECCCCC
30.7418968905
876PhosphorylationGGQPVGGLRFEGHRG
CCCCCCCEEEECCCC
4.6918669648
877DimethylationGQPVGGLRFEGHRGQ
CCCCCCEEEECCCCC
30.74-
877MethylationGQPVGGLRFEGHRGQ
CCCCCCEEEECCCCC
30.7480702729
882DimethylationGLRFEGHRGQPVGGL
CEEEECCCCCEECCE
57.19-
882MethylationGLRFEGHRGQPVGGL
CEEEECCCCCEECCE
57.1982797519
884PhosphorylationRFEGHRGQPVGGLRF
EEECCCCCEECCEEE
29.4818220336
890DimethylationGQPVGGLRFEGPHGQ
CCEECCEEEECCCCC
30.74-
890MethylationGQPVGGLRFEGPHGQ
CCEECCEEEECCCCC
30.74115383877
903DimethylationGQPVGGLRFDNPRGQ
CCCCCCEEEECCCCC
39.90-
903MethylationGQPVGGLRFDNPRGQ
CCCCCCEEEECCCCC
39.9054549441
906UbiquitinationVGGLRFDNPRGQPVG
CCCEEEECCCCCEEC
26.0024816145
908MethylationGLRFDNPRGQPVGGL
CEEEECCCCCEECCE
63.73115383885
929Asymmetric dimethylarginineGPSGAAIRFDGPHGQ
CCCCCEEEECCCCCC
20.90-
929MethylationGPSGAAIRFDGPHGQ
CCCCCEEEECCCCCC
20.9024129315
942Asymmetric dimethylarginineGQPGGGIRFEGPLLQ
CCCCCCEEEECCCHH
27.17-
942MethylationGQPGGGIRFEGPLLQ
CCCCCCEEEECCCHH
27.1724129315
950PhosphorylationFEGPLLQQGVGMRFE
EECCCHHCCCCEEEE
48.8118669648
955Asymmetric dimethylarginineLQQGVGMRFEGPHGQ
HHCCCCEEEECCCCC
22.12-
955MethylationLQQGVGMRFEGPHGQ
HHCCCCEEEECCCCC
22.1224129315
963PhosphorylationFEGPHGQSVAGLRFE
EECCCCCCEEEEEEE
20.6624719451
968MethylationGQSVAGLRFEGQHNQ
CCCEEEEEEECCCCC
27.01115383893
981Asymmetric dimethylarginineNQLGGNLRFEGPHGQ
CCCCCEEEEECCCCC
31.41-
981MethylationNQLGGNLRFEGPHGQ
CCCCCEEEEECCCCC
31.4124129315
994Asymmetric dimethylarginineGQPGVGIRFEGPLVQ
CCCCCEEEEECCEEE
20.03-
994MethylationGQPGVGIRFEGPLVQ
CCCCCEEEEECCEEE
20.0324129315
1007Asymmetric dimethylarginineVQQGGGMRFEGPSVP
EEECCCCCCCCCCCC
29.73-
1007MethylationVQQGGGMRFEGPSVP
EEECCCCCCCCCCCC
29.7324129315
1019MethylationSVPGGGLRIEGPLGQ
CCCCCCEEEECCCCC
28.34115383829
1030DimethylationPLGQGGPRFEGCHAL
CCCCCCCCCCCCEEE
45.59-
1030MethylationPLGQGGPRFEGCHAL
CCCCCCCCCCCCEEE
45.5952717377
1038MethylationFEGCHALRFDGQPGQ
CCCCEEEEECCCCCC
28.52115383845
1047PhosphorylationDGQPGQPSLLPRFDG
CCCCCCCCCCCCCCC
34.3524719451
1051DimethylationGQPSLLPRFDGLHGQ
CCCCCCCCCCCCCCC
42.11-
1051MethylationGQPSLLPRFDGLHGQ
CCCCCCCCCCCCCCC
42.1154548651
1062DimethylationLHGQPGPRFERTPGQ
CCCCCCCCCCCCCCC
52.56-
1062MethylationLHGQPGPRFERTPGQ
CCCCCCCCCCCCCCC
52.5654549763
1065DimethylationQPGPRFERTPGQPGP
CCCCCCCCCCCCCCC
43.43-
1065MethylationQPGPRFERTPGQPGP
CCCCCCCCCCCCCCC
43.43115382791
1074DimethylationPGQPGPQRFDGPPGQ
CCCCCCCCCCCCCCC
34.45-
1074MethylationPGQPGPQRFDGPPGQ
CCCCCCCCCCCCCCC
34.4518600801
1086DimethylationPGQQVQPRFDGVPQR
CCCCCCCCCCCCCCC
25.79-
1086MethylationPGQQVQPRFDGVPQR
CCCCCCCCCCCCCCC
25.79115382771
1093Asymmetric dimethylarginineRFDGVPQRFDGPQHQ
CCCCCCCCCCCCCCC
26.08-
1093MethylationRFDGVPQRFDGPQHQ
CCCCCCCCCCCCCCC
26.0824129315
1104Asymmetric dimethylargininePQHQQASRFDIPLGL
CCCCCCCCCCCCCCC
35.95-
1104MethylationPQHQQASRFDIPLGL
CCCCCCCCCCCCCCC
35.9524129315
1114PhosphorylationIPLGLQGTRFDNHPS
CCCCCCCCCCCCCHH
18.4021406692
1115MethylationPLGLQGTRFDNHPSQ
CCCCCCCCCCCCHHH
43.69115486603
1135PhosphorylationSFNQTGPYNDPPGNA
ECCCCCCCCCCCCCC
33.2828555341
1161PhosphorylationRHEQIFDSPQGPNFN
EHHHHCCCCCCCCCC
14.3625159151
1177PhosphorylationPHGPGNQSFSNPLNR
CCCCCCCCCCCHHHH
34.3426055452
1179PhosphorylationGPGNQSFSNPLNRAS
CCCCCCCCCHHHHHC
42.6727174698
1186PhosphorylationSNPLNRASGHYFDEK
CCHHHHHCCCCCCHH
23.9025159151
1189PhosphorylationLNRASGHYFDEKNLQ
HHHHCCCCCCHHCCC
19.0926074081
1211PhosphorylationGNIPAPMTVGNIQAS
CCCCCCEECCHHHHH
24.97-
1218PhosphorylationTVGNIQASQQVLSGV
ECCHHHHHHHHHHCC
12.55-
1274PhosphorylationVDVNELFSKLLKTGI
CCHHHHHHHHHHHCC
34.7124719451
1275AcetylationDVNELFSKLLKTGIL
CHHHHHHHHHHHCCH
50.9723954790
1275UbiquitinationDVNELFSKLLKTGIL
CHHHHHHHHHHHCCH
50.9729967540
1278SumoylationELFSKLLKTGILKLS
HHHHHHHHHCCHHHH
55.96-
1278SumoylationELFSKLLKTGILKLS
HHHHHHHHHCCHHHH
55.9628112733
1278UbiquitinationELFSKLLKTGILKLS
HHHHHHHHHCCHHHH
55.9629967540
1376PhosphorylationNRTEKDVSRKVTHRR
CCCCCHHHHHHHCHH
36.2024719451
1406PhosphorylationDLEERAKSQFFEKVH
CHHHHHHHHHHHHHH
31.1028555341
1406UbiquitinationDLEERAKSQFFEKVH
CHHHHHHHHHHHHHH
31.1029967540
1409UbiquitinationERAKSQFFEKVHEEV
HHHHHHHHHHHHHHH
7.4329967540
1418UbiquitinationKVHEEVVLKTQEAAK
HHHHHHHHHHHHHHH
6.3329967540
1419SumoylationVHEEVVLKTQEAAKE
HHHHHHHHHHHHHHH
36.2328112733
1419UbiquitinationVHEEVVLKTQEAAKE
HHHHHHHHHHHHHHH
36.2329967540
1420PhosphorylationHEEVVLKTQEAAKEK
HHHHHHHHHHHHHHH
27.73-
1474PhosphorylationIRVDGKIYHPSCYED
EEECCEEECHHHHCC
15.9127732954
1477PhosphorylationDGKIYHPSCYEDYQN
CCEEECHHHHCCCCC
18.9327732954
1479PhosphorylationKIYHPSCYEDYQNTS
EEECHHHHCCCCCCC
19.0327732954
1482PhosphorylationHPSCYEDYQNTSSFD
CHHHHCCCCCCCCCC
7.5420873877
1485PhosphorylationCYEDYQNTSSFDCTP
HHCCCCCCCCCCCCC
15.3823663014
1486PhosphorylationYEDYQNTSSFDCTPS
HCCCCCCCCCCCCCC
36.2422617229
1487PhosphorylationEDYQNTSSFDCTPSP
CCCCCCCCCCCCCCC
24.0622617229
1491PhosphorylationNTSSFDCTPSPSKTP
CCCCCCCCCCCCCCC
28.7522617229
1493PhosphorylationSSFDCTPSPSKTPVE
CCCCCCCCCCCCCCC
24.5323401153
1495PhosphorylationFDCTPSPSKTPVENP
CCCCCCCCCCCCCCH
54.2025159151
1497PhosphorylationCTPSPSKTPVENPLN
CCCCCCCCCCCCHHH
36.5828464451
1511SumoylationNIMLNIVKNELQEPC
HHHHHHHHHHCCCCC
40.69-
1511SumoylationNIMLNIVKNELQEPC
HHHHHHHHHHCCCCC
40.6928112733
1520PhosphorylationELQEPCDSPKVKEER
HCCCCCCCCCCCHHH
33.0829255136
1524SumoylationPCDSPKVKEERIDTP
CCCCCCCCHHHCCCC
61.04-
1524SumoylationPCDSPKVKEERIDTP
CCCCCCCCHHHCCCC
61.0428112733
1529PhosphorylationKVKEERIDTPPACTE
CCCHHHCCCCCCCCC
60.4232142685
1530PhosphorylationVKEERIDTPPACTEE
CCHHHCCCCCCCCCC
28.8829255136
1535PhosphorylationIDTPPACTEESIATP
CCCCCCCCCCCCCCH
44.9123663014
1538PhosphorylationPPACTEESIATPSEI
CCCCCCCCCCCHHHC
15.9923663014
1541PhosphorylationCTEESIATPSEIKTE
CCCCCCCCHHHCCCC
26.1925159151
1543PhosphorylationEESIATPSEIKTEND
CCCCCCHHHCCCCCC
47.8229396449
1546SumoylationIATPSEIKTENDTVE
CCCHHHCCCCCCCCC
45.8128112733
1547PhosphorylationATPSEIKTENDTVES
CCHHHCCCCCCCCCC
45.7626552605
1549UbiquitinationPSEIKTENDTVESV-
HHHCCCCCCCCCCC-
56.3229967540
1550UbiquitinationSEIKTENDTVESV--
HHCCCCCCCCCCC--
45.9929967540
1551PhosphorylationEIKTENDTVESV---
HCCCCCCCCCCC---
37.4426552605
1554PhosphorylationTENDTVESV------
CCCCCCCCC------
28.8828985074
1619Phosphorylation-----------------------------------------------------------------------
-----------------------------------------------------------------------
18669648
1629Phosphorylation---------------------------------------------------------------------------------
---------------------------------------------------------------------------------
15302935
1660Phosphorylation----------------------------------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------------------------------
32142685
1661Phosphorylation-----------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------
32142685

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
120SPhosphorylationKinaseWNK1Q9H4A3
PSP
121TPhosphorylationKinaseWNK1Q9H4A3
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCF11_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 PCF11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THOC4_HUMANALYREFphysical
19110458
PLCB1_HUMANPLCB1physical
22939629
TXND9_HUMANTXNDC9physical
22939629
ATF7_HUMANATF7physical
26344197
SPF27_HUMANBCAS2physical
26344197
CLP1_HUMANCLP1physical
26344197
CPSF2_HUMANCPSF2physical
26344197
SELB_HUMANEEFSECphysical
26344197
PLRG1_HUMANPLRG1physical
26344197
SAE2_HUMANUBA2physical
26344197
WDR33_HUMANWDR33physical
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 PCF11_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 SER-182, AND MASSSPECTROMETRY.
"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-184, 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-169; SER-182; SER-186;SER-728; SER-777; SER-851 AND SER-1520, AND MASS 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-489 AND SER-494, ANDMASS SPECTROMETRY.
"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 THR-785, AND MASSSPECTROMETRY.
"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-1530, AND MASSSPECTROMETRY.

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