WDR33_HUMAN - dbPTM
WDR33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR33_HUMAN
UniProt AC Q9C0J8
Protein Name pre-mRNA 3' end processing protein WDR33
Gene Name WDR33
Organism Homo sapiens (Human).
Sequence Length 1336
Subcellular Localization Nucleus .
Protein Description Essential for both cleavage and polyadenylation of pre-mRNA 3' ends..
Protein Sequence MATEIGSPPRFFHMPRFQHQAPRQLFYKRPDFAQQQAMQQLTFDGKRMRKAVNRKTIDYNPSVIKYLENRIWQRDQRDMRAIQPDAGYYNDLVPPIGMLNNPMNAVTTKFVRTSTNKVKCPVFVVRWTPEGRRLVTGASSGEFTLWNGLTFNFETILQAHDSPVRAMTWSHNDMWMLTADHGGYVKYWQSNMNNVKMFQAHKEAIREASFSPTDNKFATCSDDGTVRIWDFLRCHEERILRGHGADVKCVDWHPTKGLVVSGSKDSQQPIKFWDPKTGQSLATLHAHKNTVMEVKLNLNGNWLLTASRDHLCKLFDIRNLKEELQVFRGHKKEATAVAWHPVHEGLFASGGSDGSLLFWHVGVEKEVGGMEMAHEGMIWSLAWHPLGHILCSGSNDHTSKFWTRNRPGDKMRDRYNLNLLPGMSEDGVEYDDLEPNSLAVIPGMGIPEQLKLAMEQEQMGKDESNEIEMTIPGLDWGMEEVMQKDQKKVPQKKVPYAKPIPAQFQQAWMQNKVPIPAPNEVLNDRKEDIKLEEKKKTQAEIEQEMATLQYTNPQLLEQLKIERLAQKQVEQIQPPPSSGTPLLGPQPFPGQGPMSQIPQGFQQPHPSQQMPMNMAQMGPPGPQGQFRPPGPQGQMGPQGPPLHQGGGGPQGFMGPQGPQGPPQGLPRPQDMHGPQGMQRHPGPHGPLGPQGPPGPQGSSGPQGHMGPQGPPGPQGHIGPQGPPGPQGHLGPQGPPGTQGMQGPPGPRGMQGPPHPHGIQGGPGSQGIQGPVSQGPLMGLNPRGMQGPPGPRENQGPAPQGMIMGHPPQEMRGPHPPGGLLGHGPQEMRGPQEIRGMQGPPPQGSMLGPPQELRGPPGSQSQQGPPQGSLGPPPQGGMQGPPGPQGQQNPARGPHPSQGPIPFQQQKTPLLGDGPRAPFNQEGQSTGPPPLIPGLGQQGAQGRIPPLNPGQGPGPNKGDSRGPPNHHMGPMSERRHEQSGGPEHGPERGPFRGGQDCRGPPDRRGPHPDFPDDFSRPDDFHPDKRFGHRLREFEGRGGPLPQEEKWRRGGPGPPFPPDHREFSEGDGRGAARGPPGAWEGRRPGDERFPRDPEDPRFRGRREESFRRGAPPRHEGRAPPRGRDGFPGPEDFGPEENFDASEEAARGRDLRGRGRGTPRGGRKGLLPTPDEFPRFEGGRKPDSWDGNREPGPGHEHFRDTPRPDHPPHDGHSPASRERSSSLQGMDMASLPPRKRPWHDGPGTSEHREMEAPGGPSEDRGGKGRGGPGPAQRVPKSGRSSSLDGEHHDGYHRDEPFGGPPGSGTPSRGGRSGSNWGRGSNMNSGPPRRGASRGGGRGR
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------MATEIGSPP
------CCCCCCCCC
25.8321406692
3Phosphorylation-----MATEIGSPPR
-----CCCCCCCCCC
39.7428464451
7Phosphorylation-MATEIGSPPRFFHM
-CCCCCCCCCCCCCC
37.0729255136
10DimethylationTEIGSPPRFFHMPRF
CCCCCCCCCCCCCCC
50.69-
10MethylationTEIGSPPRFFHMPRF
CCCCCCCCCCCCCCC
50.6930763443
16DimethylationPRFFHMPRFQHQAPR
CCCCCCCCCCCCCCH
35.96-
16MethylationPRFFHMPRFQHQAPR
CCCCCCCCCCCCCCH
35.9630763437
23DimethylationRFQHQAPRQLFYKRP
CCCCCCCHHHHHCCC
49.18-
23MethylationRFQHQAPRQLFYKRP
CCCCCCCHHHHHCCC
49.1830763449
28UbiquitinationAPRQLFYKRPDFAQQ
CCHHHHHCCCCHHHH
50.5521906983
28UbiquitinationAPRQLFYKRPDFAQQ
CCHHHHHCCCCHHHH
50.5521890473
28UbiquitinationAPRQLFYKRPDFAQQ
CCHHHHHCCCCHHHH
50.5521890473
28UbiquitinationAPRQLFYKRPDFAQQ
CCHHHHHCCCCHHHH
50.5521890473
28UbiquitinationAPRQLFYKRPDFAQQ
CCHHHHHCCCCHHHH
50.5521890473
28UbiquitinationAPRQLFYKRPDFAQQ
CCHHHHHCCCCHHHH
50.5521890473
29MethylationPRQLFYKRPDFAQQQ
CHHHHHCCCCHHHHH
25.33115919969
38SulfoxidationDFAQQQAMQQLTFDG
CHHHHHHHHHHHCCH
1.9621406390
42PhosphorylationQQAMQQLTFDGKRMR
HHHHHHHHCCHHHHH
18.4924173317
46AcetylationQQLTFDGKRMRKAVN
HHHHCCHHHHHHHHH
44.8819608861
46UbiquitinationQQLTFDGKRMRKAVN
HHHHCCHHHHHHHHH
44.8822817900
50UbiquitinationFDGKRMRKAVNRKTI
CCHHHHHHHHHCCCC
47.5522817900
55UbiquitinationMRKAVNRKTIDYNPS
HHHHHHCCCCCCCHH
44.6322505724
55MalonylationMRKAVNRKTIDYNPS
HHHHHHCCCCCCCHH
44.6332601280
65UbiquitinationDYNPSVIKYLENRIW
CCCHHHHHHHHHHHH
41.4422817900
65 (in isoform 2)Ubiquitination-41.44-
65UbiquitinationDYNPSVIKYLENRIW
CCCHHHHHHHHHHHH
41.4421890473
65UbiquitinationDYNPSVIKYLENRIW
CCCHHHHHHHHHHHH
41.4421890473
65UbiquitinationDYNPSVIKYLENRIW
CCCHHHHHHHHHHHH
41.4421890473
65UbiquitinationDYNPSVIKYLENRIW
CCCHHHHHHHHHHHH
41.4421890473
65UbiquitinationDYNPSVIKYLENRIW
CCCHHHHHHHHHHHH
41.4421890473
88PhosphorylationAIQPDAGYYNDLVPP
HHCCCCCCCCCCCCC
10.7923401153
89PhosphorylationIQPDAGYYNDLVPPI
HCCCCCCCCCCCCCC
10.9829116813
107PhosphorylationNNPMNAVTTKFVRTS
CCCCHHHHHHHHEEC
23.1223401153
108PhosphorylationNPMNAVTTKFVRTST
CCCHHHHHHHHEECC
18.8423401153
109UbiquitinationPMNAVTTKFVRTSTN
CCHHHHHHHHEECCC
32.2821963094
109 (in isoform 2)Ubiquitination-32.28-
119UbiquitinationRTSTNKVKCPVFVVR
EECCCCEECCEEEEE
34.14-
187PhosphorylationDHGGYVKYWQSNMNN
CCCCHHHEHHHCCCC
9.9125332170
190PhosphorylationGYVKYWQSNMNNVKM
CHHHEHHHCCCCHHH
24.7325332170
196UbiquitinationQSNMNNVKMFQAHKE
HHCCCCHHHHHHHHH
35.80-
196AcetylationQSNMNNVKMFQAHKE
HHCCCCHHHHHHHHH
35.8025953088
202UbiquitinationVKMFQAHKEAIREAS
HHHHHHHHHHHHHHC
52.4321906983
209PhosphorylationKEAIREASFSPTDNK
HHHHHHHCCCCCCCC
22.8521406692
211PhosphorylationAIREASFSPTDNKFA
HHHHHCCCCCCCCCE
25.1321406692
213PhosphorylationREASFSPTDNKFATC
HHHCCCCCCCCCEEC
51.5121406692
216UbiquitinationSFSPTDNKFATCSDD
CCCCCCCCCEECCCC
38.9021963094
216AcetylationSFSPTDNKFATCSDD
CCCCCCCCCEECCCC
38.9026051181
217 (in isoform 2)Phosphorylation-9.49-
221PhosphorylationDNKFATCSDDGTVRI
CCCCEECCCCCCEEH
34.0922468782
225PhosphorylationATCSDDGTVRIWDFL
EECCCCCCEEHHHHH
17.3822468782
228 (in isoform 2)Phosphorylation-3.44-
248UbiquitinationRGHGADVKCVDWHPT
CCCCCCCEEECCCCC
29.1429967540
248AcetylationRGHGADVKCVDWHPT
CCCCCCCEEECCCCC
29.1425953088
264AcetylationGLVVSGSKDSQQPIK
CEEEECCCCCCCCCC
65.9926051181
264UbiquitinationGLVVSGSKDSQQPIK
CEEEECCCCCCCCCC
65.9927667366
264MalonylationGLVVSGSKDSQQPIK
CEEEECCCCCCCCCC
65.9932601280
266PhosphorylationVVSGSKDSQQPIKFW
EEECCCCCCCCCCEE
34.1625159151
271UbiquitinationKDSQQPIKFWDPKTG
CCCCCCCCEECCCCC
47.2729967540
277PhosphorylationIKFWDPKTGQSLATL
CCEECCCCCCCHHEE
45.9320068231
280PhosphorylationWDPKTGQSLATLHAH
ECCCCCCCHHEEECC
22.7020068231
283PhosphorylationKTGQSLATLHAHKNT
CCCCCHHEEECCCCC
25.1120068231
288UbiquitinationLATLHAHKNTVMEVK
HHEEECCCCCEEEEE
55.9129967540
290PhosphorylationTLHAHKNTVMEVKLN
EEECCCCCEEEEEEE
26.4921712546
321SumoylationLFDIRNLKEELQVFR
HHHHCCHHHHHHHHH
53.33-
321UbiquitinationLFDIRNLKEELQVFR
HHHHCCHHHHHHHHH
53.3329967540
464PhosphorylationEQMGKDESNEIEMTI
HHHCCCCCCCEEEEC
50.3123403867
470PhosphorylationESNEIEMTIPGLDWG
CCCCEEEECCCCCCC
15.9523403867
493AcetylationQKKVPQKKVPYAKPI
HHCCCCCCCCCCCCC
43.1023954790
496PhosphorylationVPQKKVPYAKPIPAQ
CCCCCCCCCCCCCHH
30.19-
498AcetylationQKKVPYAKPIPAQFQ
CCCCCCCCCCCHHHH
37.3225953088
526SumoylationNEVLNDRKEDIKLEE
HHHHCCHHHHCCHHH
63.7028112733
530SumoylationNDRKEDIKLEEKKKT
CCHHHHCCHHHHHHH
63.27-
530SumoylationNDRKEDIKLEEKKKT
CCHHHHCCHHHHHHH
63.2728112733
550PhosphorylationQEMATLQYTNPQLLE
HHHHHHHCCCHHHHH
16.1727642862
560SumoylationPQLLEQLKIERLAQK
HHHHHHHHHHHHHHH
42.06-
560UbiquitinationPQLLEQLKIERLAQK
HHHHHHHHHHHHHHH
42.0629967540
560SumoylationPQLLEQLKIERLAQK
HHHHHHHHHHHHHHH
42.0628112733
764PhosphorylationGIQGGPGSQGIQGPV
CCCCCCCCCCCCCCC
28.50-
772PhosphorylationQGIQGPVSQGPLMGL
CCCCCCCCCCCCCCC
32.3325332170
782MethylationPLMGLNPRGMQGPPG
CCCCCCCCCCCCCCC
52.7424129315
791MethylationMQGPPGPRENQGPAP
CCCCCCCCCCCCCCC
62.50115919973
811MethylationGHPPQEMRGPHPPGG
CCCCHHHCCCCCCCC
55.53115919977
828MethylationGHGPQEMRGPQEIRG
CCCCCHHCCCHHHCC
53.54115919981
834MethylationMRGPQEIRGMQGPPP
HCCCHHHCCCCCCCC
33.50115919985
907PhosphorylationIPFQQQKTPLLGDGP
CCCCCCCCCCCCCCC
18.1621406692
915Asymmetric dimethylargininePLLGDGPRAPFNQEG
CCCCCCCCCCCCCCC
61.49-
915MethylationPLLGDGPRAPFNQEG
CCCCCCCCCCCCCCC
61.4924129315
942MethylationGQQGAQGRIPPLNPG
CCCCCCCCCCCCCCC
26.59115919989
971PhosphorylationNHHMGPMSERRHEQS
CCCCCCCHHCHHHHC
30.9627080861
987MethylationGPEHGPERGPFRGGQ
CCCCCCCCCCCCCCC
62.31-
991MethylationGPERGPFRGGQDCRG
CCCCCCCCCCCCCCC
52.01115388571
1030MethylationKRFGHRLREFEGRGG
CHHHHHHHHCCCCCC
46.6530989889
1035DimethylationRLREFEGRGGPLPQE
HHHHCCCCCCCCCHH
39.43-
1035MethylationRLREFEGRGGPLPQE
HHHHCCCCCCCCCHH
39.4312020187
1047MethylationPQEEKWRRGGPGPPF
CHHHHHHCCCCCCCC
53.9954560557
1067MethylationEFSEGDGRGAARGPP
CCCCCCCCCCCCCCC
36.0059080629
1071MethylationGDGRGAARGPPGAWE
CCCCCCCCCCCCCCC
58.5880702207
1106MethylationRREESFRRGAPPRHE
CCHHHHHCCCCCCCC
43.55115919933
1111MethylationFRRGAPPRHEGRAPP
HHCCCCCCCCCCCCC
39.16115919937
1121MethylationGRAPPRGRDGFPGPE
CCCCCCCCCCCCCCH
42.00115919941
1139PhosphorylationPEENFDASEEAARGR
CHHCCCHHHHHHHCC
37.5020068231
1144DimethylationDASEEAARGRDLRGR
CHHHHHHHCCCCCCC
47.96-
1144MethylationDASEEAARGRDLRGR
CHHHHHHHCCCCCCC
47.9616289359
1146MethylationSEEAARGRDLRGRGR
HHHHHHCCCCCCCCC
33.9518959317
1166PhosphorylationGRKGLLPTPDEFPRF
CCCCCCCCCCCCCCC
43.2630266825
1181PhosphorylationEGGRKPDSWDGNREP
CCCCCCCCCCCCCCC
35.2828985074
1198PhosphorylationGHEHFRDTPRPDHPP
CCCCCCCCCCCCCCC
19.5523927012
1210PhosphorylationHPPHDGHSPASRERS
CCCCCCCCHHHHHHH
27.9129255136
1213PhosphorylationHDGHSPASRERSSSL
CCCCCHHHHHHHHHC
37.7523927012
1217PhosphorylationSPASRERSSSLQGMD
CHHHHHHHHHCCCCC
21.3730631047
1218PhosphorylationPASRERSSSLQGMDM
HHHHHHHHHCCCCCH
41.0930631047
1219PhosphorylationASRERSSSLQGMDMA
HHHHHHHHCCCCCHH
26.4225159151
1227PhosphorylationLQGMDMASLPPRKRP
CCCCCHHHCCCCCCC
34.4720068231
1233MethylationASLPPRKRPWHDGPG
HHCCCCCCCCCCCCC
40.60115388563
1241PhosphorylationPWHDGPGTSEHREME
CCCCCCCCHHCCCCC
33.7929449344
1242PhosphorylationWHDGPGTSEHREMEA
CCCCCCCHHCCCCCC
37.0029449344
1247SulfoxidationGTSEHREMEAPGGPS
CCHHCCCCCCCCCCC
5.5521406390
1254PhosphorylationMEAPGGPSEDRGGKG
CCCCCCCCCCCCCCC
56.24-
1257MethylationPGGPSEDRGGKGRGG
CCCCCCCCCCCCCCC
52.2754560549
1262MethylationEDRGGKGRGGPGPAQ
CCCCCCCCCCCCCCC
50.8318583783
1270MethylationGGPGPAQRVPKSGRS
CCCCCCCCCCCCCCC
49.14115919945
1276MethylationQRVPKSGRSSSLDGE
CCCCCCCCCCCCCCC
40.22115919949
1277PhosphorylationRVPKSGRSSSLDGEH
CCCCCCCCCCCCCCC
28.0123663014
1278PhosphorylationVPKSGRSSSLDGEHH
CCCCCCCCCCCCCCC
33.2930266825
1279PhosphorylationPKSGRSSSLDGEHHD
CCCCCCCCCCCCCCC
31.5523401153
1288PhosphorylationDGEHHDGYHRDEPFG
CCCCCCCCCCCCCCC
10.3522167270
1290MethylationEHHDGYHRDEPFGGP
CCCCCCCCCCCCCCC
41.31115919953
1302PhosphorylationGGPPGSGTPSRGGRS
CCCCCCCCCCCCCCC
21.56-
1304PhosphorylationPPGSGTPSRGGRSGS
CCCCCCCCCCCCCCC
43.31-
1305MethylationPGSGTPSRGGRSGSN
CCCCCCCCCCCCCCC
53.43115919957
1308MethylationGTPSRGGRSGSNWGR
CCCCCCCCCCCCCCC
40.44115919961
1315Asymmetric dimethylarginineRSGSNWGRGSNMNSG
CCCCCCCCCCCCCCC
36.66-
1315MethylationRSGSNWGRGSNMNSG
CCCCCCCCCCCCCCC
36.6624129315
1325MethylationNMNSGPPRRGASRGG
CCCCCCCCCCCCCCC
53.45115368641

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 WDR33_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR33_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 WDR33_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAT7_HUMANKAT7physical
16169070
PROF2_HUMANPFN2physical
16169070
UT14A_HUMANUTP14Aphysical
16169070
SH3G3_HUMANSH3GL3physical
16169070
ZHX1_HUMANZHX1physical
16169070
ZBT16_HUMANZBTB16physical
16169070
GIT1_HUMANGIT1physical
16169070
ANM1_HUMANPRMT1physical
16169070
P53_HUMANTP53physical
16169070
RBM48_HUMANRBM48physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
ZN622_HUMANZNF622physical
22939629
CPSF2_HUMANCPSF2physical
26344197
PAPOA_HUMANPAPOLAphysical
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 WDR33_HUMAN

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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-7, 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-46, AND MASS SPECTROMETRY.
Phosphorylation
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-7, 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-1210, 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-7, AND MASSSPECTROMETRY.

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