CDK13_HUMAN - dbPTM
CDK13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDK13_HUMAN
UniProt AC Q14004
Protein Name Cyclin-dependent kinase 13
Gene Name CDK13
Organism Homo sapiens (Human).
Sequence Length 1512
Subcellular Localization Nucleus speckle .
Protein Description Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef..
Protein Sequence MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGSPASSSGTQRRGEGSERRPRRDRRSSSGRSKERHREHRRRDGQRGGSEASKSRSRHSHSGEERAEVAKSGSSSSSGGRRKSASATSSSSSSRKDRDSKAHRSRTKSSKEPPSAYKEPPKAYREDKTEPKAYRRRRSLSPLGGRDDSPVSHRASQSLRSRKSPSPAGGGSSPYSRRLPRSPSPYSRRRSPSYSRHSSYERGGDVSPSPYSSSSWRRSRSPYSPVLRRSGKSRSRSPYSSRHSRSRSRHRLSRSRSRHSSISPSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEATKAAEAAAKAAKASNTSTPTKGNTETSASASQTNHVKDVKKIKIEHAPSPSSGGTLKNDKAKTKPPLQVTKVENNLIVDKATKKAVIVGKESKSAATKEESVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKEADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHSKRRPKICGPRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDSRTNTPQGVLPSSQLKSQGSSNVAPVKTGPGQHLNHSELAILLNLLQSKTSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATGEKQTDPSTPQQESSKPLGGIQPSSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEASLQLRPPPEPSTPVSGQDDLIQHQDMRILELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKREGGIDYQAGDTYVSTSDYKDNFGSSSFSSAPYVSNDGLGSSSAPPLERRSFIGNSDIQSLDNYSTASSHSGGPPQPSAFSESFPSSVAGYGDIYLNAGPMLFSGDKDHRFEYSHGPIAVLANSSDPSTGPESTHPLPAKMHNYNYGGNLQENPSGPSLMHGQTWTSPAQGPGYSQGYRGHISTSTGRGRGRGLPY
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
3Phosphorylation-----MPSSSDTALG
-----CCCCCCCCCC
55.0923663014
4Phosphorylation----MPSSSDTALGG
----CCCCCCCCCCC
42.8523663014
5Phosphorylation---MPSSSDTALGGG
---CCCCCCCCCCCC
43.2323663014
7Phosphorylation-MPSSSDTALGGGGG
-CCCCCCCCCCCCCC
26.2323663014
16PhosphorylationLGGGGGLSWAEKKLE
CCCCCCCHHHHHHHH
27.7523663014
135PhosphorylationQDGGGGASSGGGVTP
CCCCCCCCCCCCCCC
32.5624275569
136PhosphorylationDGGGGASSGGGVTPL
CCCCCCCCCCCCCCC
40.71-
141PhosphorylationASSGGGVTPLVEYED
CCCCCCCCCCEEEEC
17.7424275569
151PhosphorylationVEYEDVSSQSEQGLL
EEEECCCCHHCCCEE
37.26-
163PhosphorylationGLLLGGASAATAATA
CEECCHHHHHHHHHH
23.0126074081
166PhosphorylationLGGASAATAATAAGG
CCHHHHHHHHHHCCC
19.2826074081
169PhosphorylationASAATAATAAGGTGG
HHHHHHHHHCCCCCC
17.9926074081
174PhosphorylationAATAAGGTGGSGGSP
HHHHCCCCCCCCCCC
37.1326074081
177PhosphorylationAAGGTGGSGGSPASS
HCCCCCCCCCCCCCC
41.1326074081
180PhosphorylationGTGGSGGSPASSSGT
CCCCCCCCCCCCCCC
22.3326074081
183PhosphorylationGSGGSPASSSGTQRR
CCCCCCCCCCCCCCC
28.5526074081
184PhosphorylationSGGSPASSSGTQRRG
CCCCCCCCCCCCCCC
34.5926074081
185PhosphorylationGGSPASSSGTQRRGE
CCCCCCCCCCCCCCC
43.2826074081
187PhosphorylationSPASSSGTQRRGEGS
CCCCCCCCCCCCCCC
22.3526074081
204PhosphorylationRPRRDRRSSSGRSKE
CCCCCCCCCCCCCHH
29.74-
205PhosphorylationPRRDRRSSSGRSKER
CCCCCCCCCCCCHHH
34.69-
209PhosphorylationRRSSSGRSKERHREH
CCCCCCCCHHHHHHH
42.25-
229PhosphorylationQRGGSEASKSRSRHS
CCCCCHHHHHHCCCC
27.4117081983
233PhosphorylationSEASKSRSRHSHSGE
CHHHHHHCCCCCCHH
41.2423312004
236PhosphorylationSKSRSRHSHSGEERA
HHHHCCCCCCHHHHH
20.4530576142
238PhosphorylationSRSRHSHSGEERAEV
HHCCCCCCHHHHHHH
51.4130576142
248PhosphorylationERAEVAKSGSSSSSG
HHHHHHHCCCCCCCC
33.8823401153
250PhosphorylationAEVAKSGSSSSSGGR
HHHHHCCCCCCCCCC
33.8523401153
251PhosphorylationEVAKSGSSSSSGGRR
HHHHCCCCCCCCCCC
37.4523401153
252PhosphorylationVAKSGSSSSSGGRRK
HHHCCCCCCCCCCCC
30.1623401153
253PhosphorylationAKSGSSSSSGGRRKS
HHCCCCCCCCCCCCC
34.6423401153
254PhosphorylationKSGSSSSSGGRRKSA
HCCCCCCCCCCCCCC
47.4123401153
260PhosphorylationSSGGRRKSASATSSS
CCCCCCCCCCCCCCC
26.1624275569
262PhosphorylationGGRRKSASATSSSSS
CCCCCCCCCCCCCCC
38.8925849741
264PhosphorylationRRKSASATSSSSSSR
CCCCCCCCCCCCCCC
27.0130387612
268PhosphorylationASATSSSSSSRKDRD
CCCCCCCCCCCHHHC
33.99-
276PhosphorylationSSRKDRDSKAHRSRT
CCCHHHCHHHHHHHC
32.41-
281PhosphorylationRDSKAHRSRTKSSKE
HCHHHHHHHCCCCCC
34.14-
283PhosphorylationSKAHRSRTKSSKEPP
HHHHHHHCCCCCCCC
36.2027794612
285PhosphorylationAHRSRTKSSKEPPSA
HHHHHCCCCCCCCHH
46.1328985074
286PhosphorylationHRSRTKSSKEPPSAY
HHHHCCCCCCCCHHH
42.4628674419
291PhosphorylationKSSKEPPSAYKEPPK
CCCCCCCHHHCCCCC
55.7525159151
293PhosphorylationSKEPPSAYKEPPKAY
CCCCCHHHCCCCCCC
21.8826074081
315PhosphorylationKAYRRRRSLSPLGGR
HHHHHHHCCCCCCCC
31.2429255136
317PhosphorylationYRRRRSLSPLGGRDD
HHHHHCCCCCCCCCC
21.2329255136
325PhosphorylationPLGGRDDSPVSHRAS
CCCCCCCCCCCHHHH
31.3329255136
328PhosphorylationGRDDSPVSHRASQSL
CCCCCCCCHHHHHHH
15.6130266825
332PhosphorylationSPVSHRASQSLRSRK
CCCCHHHHHHHHHCC
21.9121406692
334PhosphorylationVSHRASQSLRSRKSP
CCHHHHHHHHHCCCC
24.2121406692
337PhosphorylationRASQSLRSRKSPSPA
HHHHHHHHCCCCCCC
49.7221955146
340PhosphorylationQSLRSRKSPSPAGGG
HHHHHCCCCCCCCCC
29.5122617229
342PhosphorylationLRSRKSPSPAGGGSS
HHHCCCCCCCCCCCC
34.1822617229
348PhosphorylationPSPAGGGSSPYSRRL
CCCCCCCCCCCHHCC
31.2621955146
349PhosphorylationSPAGGGSSPYSRRLP
CCCCCCCCCCHHCCC
31.0021955146
351PhosphorylationAGGGSSPYSRRLPRS
CCCCCCCCHHCCCCC
19.4322115753
352PhosphorylationGGGSSPYSRRLPRSP
CCCCCCCHHCCCCCC
17.8222115753
358PhosphorylationYSRRLPRSPSPYSRR
CHHCCCCCCCCCCCC
27.9923927012
360PhosphorylationRRLPRSPSPYSRRRS
HCCCCCCCCCCCCCC
37.4023927012
362PhosphorylationLPRSPSPYSRRRSPS
CCCCCCCCCCCCCCC
21.1023927012
363PhosphorylationPRSPSPYSRRRSPSY
CCCCCCCCCCCCCCC
23.7723927012
367PhosphorylationSPYSRRRSPSYSRHS
CCCCCCCCCCCCCCC
19.1828102081
369PhosphorylationYSRRRSPSYSRHSSY
CCCCCCCCCCCCCCC
36.6720363803
370PhosphorylationSRRRSPSYSRHSSYE
CCCCCCCCCCCCCCC
17.0717081983
371PhosphorylationRRRSPSYSRHSSYER
CCCCCCCCCCCCCCC
28.0520363803
374PhosphorylationSPSYSRHSSYERGGD
CCCCCCCCCCCCCCC
33.2424247654
375PhosphorylationPSYSRHSSYERGGDV
CCCCCCCCCCCCCCC
25.5330576142
376PhosphorylationSYSRHSSYERGGDVS
CCCCCCCCCCCCCCC
16.80-
383PhosphorylationYERGGDVSPSPYSSS
CCCCCCCCCCCCCCC
25.1319664994
385PhosphorylationRGGDVSPSPYSSSSW
CCCCCCCCCCCCCCC
29.0322167270
387PhosphorylationGDVSPSPYSSSSWRR
CCCCCCCCCCCCCHH
26.0622167270
388PhosphorylationDVSPSPYSSSSWRRS
CCCCCCCCCCCCHHC
27.4222167270
389PhosphorylationVSPSPYSSSSWRRSR
CCCCCCCCCCCHHCC
23.6522167270
390PhosphorylationSPSPYSSSSWRRSRS
CCCCCCCCCCHHCCC
28.1622167270
391PhosphorylationPSPYSSSSWRRSRSP
CCCCCCCCCHHCCCC
26.9222167270
395PhosphorylationSSSSWRRSRSPYSPV
CCCCCHHCCCCCCHH
28.6522167270
397PhosphorylationSSWRRSRSPYSPVLR
CCCHHCCCCCCHHHH
29.4522167270
399PhosphorylationWRRSRSPYSPVLRRS
CHHCCCCCCHHHHCC
27.1822167270
400PhosphorylationRRSRSPYSPVLRRSG
HHCCCCCCHHHHCCC
16.3622167270
406PhosphorylationYSPVLRRSGKSRSRS
CCHHHHCCCCCCCCC
44.1024719451
409PhosphorylationVLRRSGKSRSRSPYS
HHHCCCCCCCCCCCC
38.7320363803
411PhosphorylationRRSGKSRSRSPYSSR
HCCCCCCCCCCCCCC
44.1727362937
413PhosphorylationSGKSRSRSPYSSRHS
CCCCCCCCCCCCCCH
29.4527362937
415PhosphorylationKSRSRSPYSSRHSRS
CCCCCCCCCCCCHHH
22.1123312004
416PhosphorylationSRSRSPYSSRHSRSR
CCCCCCCCCCCHHHH
25.0423663014
417PhosphorylationRSRSPYSSRHSRSRS
CCCCCCCCCCHHHHH
28.3320363803
420PhosphorylationSPYSSRHSRSRSRHR
CCCCCCCHHHHHHHH
30.7320068231
422PhosphorylationYSSRHSRSRSRHRLS
CCCCCHHHHHHHHHH
37.3117081983
429PhosphorylationSRSRHRLSRSRSRHS
HHHHHHHHHHHHCCC
28.3228102081
431PhosphorylationSRHRLSRSRSRHSSI
HHHHHHHHHHCCCCC
31.0921406692
433PhosphorylationHRLSRSRSRHSSISP
HHHHHHHHCCCCCCH
35.2826055452
436PhosphorylationSRSRSRHSSISPSTL
HHHHHCCCCCCHHHH
28.4029255136
437PhosphorylationRSRSRHSSISPSTLT
HHHHCCCCCCHHHHH
22.4419664994
439PhosphorylationRSRHSSISPSTLTLK
HHCCCCCCHHHHHHH
18.1029255136
441PhosphorylationRHSSISPSTLTLKSS
CCCCCCHHHHHHHHH
29.2919664994
442PhosphorylationHSSISPSTLTLKSSL
CCCCCHHHHHHHHHH
27.4429255136
444PhosphorylationSISPSTLTLKSSLAA
CCCHHHHHHHHHHHH
32.0322167270
490O-linked_GlycosylationAAKAAKASNTSTPTK
HHHHHHHCCCCCCCC
39.6830059200
490PhosphorylationAAKAAKASNTSTPTK
HHHHHHHCCCCCCCC
39.6823927012
492PhosphorylationKAAKASNTSTPTKGN
HHHHHCCCCCCCCCC
31.3323927012
493PhosphorylationAAKASNTSTPTKGNT
HHHHCCCCCCCCCCC
36.3223927012
494PhosphorylationAKASNTSTPTKGNTE
HHHCCCCCCCCCCCC
32.7023927012
496PhosphorylationASNTSTPTKGNTETS
HCCCCCCCCCCCCCC
52.2323927012
500PhosphorylationSTPTKGNTETSASAS
CCCCCCCCCCCCCHH
49.6723927012
502PhosphorylationPTKGNTETSASASQT
CCCCCCCCCCCHHCC
27.7923927012
503PhosphorylationTKGNTETSASASQTN
CCCCCCCCCCHHCCC
17.6230108239
505PhosphorylationGNTETSASASQTNHV
CCCCCCCCHHCCCCC
28.3728450419
507PhosphorylationTETSASASQTNHVKD
CCCCCCHHCCCCCCC
34.7323927012
509PhosphorylationTSASASQTNHVKDVK
CCCCHHCCCCCCCCE
25.4625627689
519SumoylationVKDVKKIKIEHAPSP
CCCCEEEEEEECCCC
51.42-
519SumoylationVKDVKKIKIEHAPSP
CCCCEEEEEEECCCC
51.4228112733
525PhosphorylationIKIEHAPSPSSGGTL
EEEEECCCCCCCCCC
37.8929255136
527PhosphorylationIEHAPSPSSGGTLKN
EEECCCCCCCCCCCC
46.0529255136
528PhosphorylationEHAPSPSSGGTLKND
EECCCCCCCCCCCCC
44.6325159151
531PhosphorylationPSPSSGGTLKNDKAK
CCCCCCCCCCCCCCC
37.7826055452
539PhosphorylationLKNDKAKTKPPLQVT
CCCCCCCCCCCCEEE
54.3526074081
547SumoylationKPPLQVTKVENNLIV
CCCCEEEEEECCEEE
49.0128112733
556AcetylationENNLIVDKATKKAVI
ECCEEECCCCCEEEE
47.2419608861
566AcetylationKKAVIVGKESKSAAT
CEEEEEECCCCCCCC
48.1725953088
583AcetylationESVSLKEKTKPLTPS
HCCCHHHCCCCCCCC
61.3319666929
584PhosphorylationSVSLKEKTKPLTPSI
CCCHHHCCCCCCCCC
38.7023403867
585AcetylationVSLKEKTKPLTPSIG
CCHHHCCCCCCCCCC
49.4519666941
588PhosphorylationKEKTKPLTPSIGAKE
HHCCCCCCCCCCCCH
24.4225159151
590PhosphorylationKTKPLTPSIGAKEKE
CCCCCCCCCCCCHHH
28.5525159151
624PhosphorylationPEDKEADSLRGNISV
CCCHHHCCCCCCCCH
27.3220068231
630PhosphorylationDSLRGNISVKAVKKE
CCCCCCCCHHHHHHH
22.89-
632UbiquitinationLRGNISVKAVKKEVE
CCCCCCHHHHHHHHH
40.44-
662PhosphorylationLPGGDDLSKSPEEKK
CCCCCCCCCCHHHHH
37.7730278072
664PhosphorylationGGDDLSKSPEEKKTA
CCCCCCCCHHHHHHH
33.8822617229
670PhosphorylationKSPEEKKTATQLHSK
CCHHHHHHHHHHHHC
46.1126074081
672PhosphorylationPEEKKTATQLHSKRR
HHHHHHHHHHHHCCC
36.5726074081
677AcetylationTATQLHSKRRPKICG
HHHHHHHCCCCCCCC
41.5025953088
687PhosphorylationPKICGPRYGETKEKD
CCCCCCCCCCCCHHC
23.58-
699UbiquitinationEKDIDWGKRCVDKFD
HHCCCHHHHHCCCCC
38.07-
716PhosphorylationGIIGEGTYGQVYKAR
EEEECCCCCEEEEEE
19.2022817900
725AcetylationQVYKARDKDTGEMVA
EEEEEECCCCCCEEE
52.1919413330
742UbiquitinationKVRLDNEKEGFPITA
EEECCCCCCCCCCHH
70.19-
748PhosphorylationEKEGFPITAIREIKI
CCCCCCCHHHHHHHH
19.1020068231
774AcetylationMKEIVTDKEDALDFK
HHHHCCCHHHHHHHC
48.4025953088
774UbiquitinationMKEIVTDKEDALDFK
HHHHCCCHHHHHHHC
48.40-
781UbiquitinationKEDALDFKKDKGAFY
HHHHHHHCCCCCCEE
60.78-
827PhosphorylationQLMEGLDYCHKKNFL
HHHHHHHHHHHCCCC
11.0720860994
862PhosphorylationDFGLARLYSSEESRP
HHHHCCCCCCCCCCC
12.4723403867
863PhosphorylationFGLARLYSSEESRPY
HHHCCCCCCCCCCCC
35.5523927012
864PhosphorylationGLARLYSSEESRPYT
HHCCCCCCCCCCCCC
31.6523927012
867PhosphorylationRLYSSEESRPYTNKV
CCCCCCCCCCCCCCE
34.2125159151
870PhosphorylationSSEESRPYTNKVITL
CCCCCCCCCCCEEEE
23.1023927012
871PhosphorylationSEESRPYTNKVITLW
CCCCCCCCCCEEEEE
31.1125159151
927PhosphorylationLAQLELISRICGSPC
HHHHHHHHHHHCCCC
28.3724719451
943UbiquitinationAVWPDVIKLPYFNTM
CCCCCCCCCCCCCCC
43.17-
951AcetylationLPYFNTMKPKKQYRR
CCCCCCCCCHHHHHH
52.2023954790
951MalonylationLPYFNTMKPKKQYRR
CCCCCCCCCHHHHHH
52.2032601280
1022PhosphorylationQDCHELWSKKRRRQK
HHHHHHHHHHHHHHH
40.7125159151
1034PhosphorylationRQKQMGMTDDVSTIK
HHHHHCCCCCHHHCC
24.2629457462
1045AcetylationSTIKAPRKDLSLGLD
HHCCCCCCCCCCCCC
63.0626051181
1045UbiquitinationSTIKAPRKDLSLGLD
HHCCCCCCCCCCCCC
63.06-
1048PhosphorylationKAPRKDLSLGLDDSR
CCCCCCCCCCCCCCC
30.4423401153
1054PhosphorylationLSLGLDDSRTNTPQG
CCCCCCCCCCCCCCC
40.4429255136
1054 (in isoform 2)Phosphorylation-40.4418220336
1056PhosphorylationLGLDDSRTNTPQGVL
CCCCCCCCCCCCCCC
47.6023401153
1058PhosphorylationLDDSRTNTPQGVLPS
CCCCCCCCCCCCCCH
19.1722167270
1065PhosphorylationTPQGVLPSSQLKSQG
CCCCCCCHHHHHCCC
26.9323927012
1065 (in isoform 2)Phosphorylation-26.9330131370
1066PhosphorylationPQGVLPSSQLKSQGS
CCCCCCHHHHHCCCC
37.2817525332
1074 (in isoform 2)Phosphorylation-41.9922210691
1083 (in isoform 2)Phosphorylation-44.4918669648
1086 (in isoform 2)Phosphorylation-34.2225849741
1087 (in isoform 2)Phosphorylation-4.7925849741
1092 (in isoform 2)Phosphorylation-3.9421552520
1093 (in isoform 2)Phosphorylation-6.0722210691
1138PhosphorylationLPAGILATGEKQTDP
CCCCCCCCCCCCCCC
42.2923401153
1143PhosphorylationLATGEKQTDPSTPQQ
CCCCCCCCCCCCCCC
62.0330278072
1146PhosphorylationGEKQTDPSTPQQESS
CCCCCCCCCCCCCCC
56.3729255136
1147PhosphorylationEKQTDPSTPQQESSK
CCCCCCCCCCCCCCC
30.4229255136
1152PhosphorylationPSTPQQESSKPLGGI
CCCCCCCCCCCCCCC
39.0529255136
1153PhosphorylationSTPQQESSKPLGGIQ
CCCCCCCCCCCCCCC
37.2223927012
1154AcetylationTPQQESSKPLGGIQP
CCCCCCCCCCCCCCC
54.2426051181
1162PhosphorylationPLGGIQPSSQTIQPK
CCCCCCCCCCCCCCC
20.7825159151
1163PhosphorylationLGGIQPSSQTIQPKV
CCCCCCCCCCCCCCC
37.7225159151
1165PhosphorylationGIQPSSQTIQPKVET
CCCCCCCCCCCCCCC
24.4325159151
1199UbiquitinationKAQQSKQKDVLLEER
HHHHHHCCCCEEEEC
54.24-
1210PhosphorylationLEERENGSGHEASLQ
EEECCCCCCCCCEEE
48.8625850435
1215PhosphorylationNGSGHEASLQLRPPP
CCCCCCCEEEECCCC
17.4225850435
1225PhosphorylationLRPPPEPSTPVSGQD
ECCCCCCCCCCCCCC
43.6223401153
1226PhosphorylationRPPPEPSTPVSGQDD
CCCCCCCCCCCCCCC
38.1221082442
1229PhosphorylationPEPSTPVSGQDDLIQ
CCCCCCCCCCCCCHH
31.7525850435
1246PhosphorylationDMRILELTPEPDRPR
CCEEEECCCCCCCCC
19.0729255136
1271PhosphorylationPPEPPPVTEEDLDYR
CCCCCCCCHHHCCCC
39.1620068231
1277PhosphorylationVTEEDLDYRTENQHV
CCHHHCCCCCCCCCC
27.0820068231
1286O-linked_GlycosylationTENQHVPTTSSSLTD
CCCCCCCCCCCCCCC
37.9230059200
1287O-linked_GlycosylationENQHVPTTSSSLTDP
CCCCCCCCCCCCCCC
22.1230059200
1288O-linked_GlycosylationNQHVPTTSSSLTDPH
CCCCCCCCCCCCCCC
22.0230059200
1289O-linked_GlycosylationQHVPTTSSSLTDPHA
CCCCCCCCCCCCCCH
27.5530059200
1290O-linked_GlycosylationHVPTTSSSLTDPHAG
CCCCCCCCCCCCCHH
34.7530059200
1292O-linked_GlycosylationPTTSSSLTDPHAGVK
CCCCCCCCCCCHHHH
49.8130059200
1316UbiquitinationHQPQDDPKREGGIDY
CCCCCCCCCCCCCCC
70.81-
1335PhosphorylationTYVSTSDYKDNFGSS
EEEECCCCCCCCCCC
21.7330576142
1342PhosphorylationYKDNFGSSSFSSAPY
CCCCCCCCCCCCCCC
35.4625159151
1343PhosphorylationKDNFGSSSFSSAPYV
CCCCCCCCCCCCCCC
30.7425627689
1345PhosphorylationNFGSSSFSSAPYVSN
CCCCCCCCCCCCCCC
27.7730576142
1346PhosphorylationFGSSSFSSAPYVSND
CCCCCCCCCCCCCCC
31.1125159151
1471PhosphorylationGNLQENPSGPSLMHG
CCCCCCCCCCCCCCC
74.9518691976
1474PhosphorylationQENPSGPSLMHGQTW
CCCCCCCCCCCCCEE
41.6828348404
1480PhosphorylationPSLMHGQTWTSPAQG
CCCCCCCEECCCCCC
34.9928348404
1482PhosphorylationLMHGQTWTSPAQGPG
CCCCCEECCCCCCCC
28.3726074081
1483PhosphorylationMHGQTWTSPAQGPGY
CCCCEECCCCCCCCC
15.1426074081

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
437SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDK13_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 CDK13_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK12_HUMANCDK12physical
22939629
MK14_HUMANMAPK14physical
22939629
PRPF3_HUMANPRPF3physical
22939629
MTA3_HUMANMTA3physical
22939629
NSUN5_HUMANNSUN5physical
22939629
TCPG_HUMANCCT3physical
25852190
EF2_HUMANEEF2physical
25852190
TBB5_HUMANTUBBphysical
26186194
TBB4B_HUMANTUBB4Bphysical
26186194
TBB3_HUMANTUBB3physical
26186194
TBB8_HUMANTUBB8physical
26186194
HS90A_HUMANHSP90AA1physical
26186194
HS90B_HUMANHSP90AB1physical
26186194
FKBP5_HUMANFKBP5physical
26186194
KEAP1_HUMANKEAP1physical
26186194
CDC37_HUMANCDC37physical
26186194
PLSI_HUMANPLS1physical
26186194
SPSB3_HUMANSPSB3physical
26186194
DUSTY_HUMANDSTYKphysical
26186194
CDK12_HUMANCDK12physical
26186194
RB_HUMANRB1physical
26186194
FBX11_HUMANFBXO11physical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
TBA1C_HUMANTUBA1Cphysical
26186194
CCNK_HUMANCCNKphysical
26186194
EDRF1_HUMANEDRF1physical
26186194
NEK3_HUMANNEK3physical
26186194
WDR34_HUMANWDR34physical
26186194
GBB2_HUMANGNB2physical
26186194
FBX44_HUMANFBXO44physical
26186194
PALD_HUMANPALD1physical
26186194
TTC9C_HUMANTTC9Cphysical
26186194
PPM1B_HUMANPPM1Bphysical
26344197
CDK12_HUMANCDK12physical
28514442
NEK3_HUMANNEK3physical
28514442
SPSB3_HUMANSPSB3physical
28514442
FKBP5_HUMANFKBP5physical
28514442
HS90A_HUMANHSP90AA1physical
28514442
HS90B_HUMANHSP90AB1physical
28514442
FBX44_HUMANFBXO44physical
28514442
RB_HUMANRB1physical
28514442
CCNK_HUMANCCNKphysical
28514442
FBX11_HUMANFBXO11physical
28514442
KEAP1_HUMANKEAP1physical
28514442
DUSTY_HUMANDSTYKphysical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TBB4A_HUMANTUBB4Aphysical
28514442
TBB8_HUMANTUBB8physical
28514442
EDRF1_HUMANEDRF1physical
28514442
TBB4B_HUMANTUBB4Bphysical
28514442
TBA1A_HUMANTUBA1Aphysical
28514442
PALD_HUMANPALD1physical
28514442
PLSI_HUMANPLS1physical
28514442
TBB5_HUMANTUBBphysical
28514442

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 CDK13_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-556, 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-383 AND SER-437, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-238; SER-315;SER-317; SER-325; SER-342; SER-348; SER-358; SER-360; SER-383;SER-385; SER-395; SER-397; SER-413; SER-436; SER-437; SER-439;SER-490; THR-492; SER-525; SER-527; SER-662; SER-664; SER-863;TYR-870; THR-871; SER-1048; SER-1054; THR-1058; THR-1143; SER-1146;THR-1147 AND THR-1246, 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-383 AND THR-494, ANDMASS 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-315; SER-317; SER-325;SER-340; SER-342; SER-349; SER-383; SER-395; SER-397; SER-400;SER-437; SER-439; THR-871 AND THR-1246, 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-315; SER-317; SER-325;SER-358; SER-360; SER-383; SER-395; SER-397; SER-400; SER-437;SER-439; SER-525; SER-664; THR-871; THR-1056 AND THR-1246, 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-1054, 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 SER-1066, 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-437 AND SER-441, 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-315; SER-317; SER-325;SER-437; SER-439 AND THR-1246, AND MASS 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-317; SER-340; SER-342;SER-367 AND SER-383, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND THR-442, ANDMASS SPECTROMETRY.

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