WRN_HUMAN - dbPTM
WRN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WRN_HUMAN
UniProt AC Q14191
Protein Name Werner syndrome ATP-dependent helicase
Gene Name WRN
Organism Homo sapiens (Human).
Sequence Length 1432
Subcellular Localization Nucleus, nucleolus . Nucleus . Nucleus, nucleoplasm . Gamma-irradiation leads to its translocation from nucleoli to nucleoplasm and PML regulates the irradiation-induced WRN relocation.
Protein Description Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation..
Protein Sequence MSEKKLETTAQQRKCPEWMNVQNKRCAVEERKACVRKSVFEDDLPFLEFTGSIVYSYDASDCSFLSEDISMSLSDGDVVGFDMEWPPLYNRGKLGKVALIQLCVSESKCYLFHVSSMSVFPQGLKMLLENKAVKKAGVGIEGDQWKLLRDFDIKLKNFVELTDVANKKLKCTETWSLNSLVKHLLGKQLLKDKSIRCSNWSKFPLTEDQKLYAATDAYAGFIIYRNLEILDDTVQRFAINKEEEILLSDMNKQLTSISEEVMDLAKHLPHAFSKLENPRRVSILLKDISENLYSLRRMIIGSTNIETELRPSNNLNLLSFEDSTTGGVQQKQIREHEVLIHVEDETWDPTLDHLAKHDGEDVLGNKVERKEDGFEDGVEDNKLKENMERACLMSLDITEHELQILEQQSQEEYLSDIAYKSTEHLSPNDNENDTSYVIESDEDLEMEMLKHLSPNDNENDTSYVIESDEDLEMEMLKSLENLNSGTVEPTHSKCLKMERNLGLPTKEEEEDDENEANEGEEDDDKDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWEFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKASLGIMGTEKCCDNCRSRLDHCYSMDDSEDTSWDFGPQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLADQYRRHSLFGTGKDQTESWWKAFSRQLITEGFLVEVSRYNKFMKICALTKKGRNWLHKANTESQSLILQANEELCPKKLLLPSSKTVSSGTKEHCYNQVPVELSTEKKSNLEKLYSYKPCDKISSGSNISKKSIMVQSPEKAYSSSQPVISAQEQETQIVLYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAPLLEVIKHFCQTNSVQTDLFSSTKPQEEQKTSLVAKNKICTLSQSMAITYSLFQEKKMPLKSIAESRILPLMTIGMHLSQAVKAGCPLDLERAGLTPEVQKIIADVIRNPPVNSDMSKISLIRMLVPENIDTYLIHMAIEILKHGPDSGLQPSCDVNKRRCFPGSEEICSSSKRSKEEVGINTETSSAERKRRLPVWFAKGSDTSKKLMDKTKRGGLFS
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------MSEKKLETT
------CCHHHHHHH
70.2222814378
4Ubiquitination----MSEKKLETTAQ
----CCHHHHHHHHH
72.4624816145
5Ubiquitination---MSEKKLETTAQQ
---CCHHHHHHHHHH
47.7229967540
14UbiquitinationETTAQQRKCPEWMNV
HHHHHHHCCHHHHCC
50.2129967540
32AcetylationRCAVEERKACVRKSV
CHHHHHHHHHHHHHH
49.7919826841
131UbiquitinationLKMLLENKAVKKAGV
HHHHHCCCCHHHCCC
45.2229967540
135UbiquitinationLENKAVKKAGVGIEG
HCCCCHHHCCCCCCC
43.7229967540
146UbiquitinationGIEGDQWKLLRDFDI
CCCCCCCCCHHHCCC
31.8229967540
154UbiquitinationLLRDFDIKLKNFVEL
CHHHCCCEECCEEEH
56.0829967540
154SumoylationLLRDFDIKLKNFVEL
CHHHCCCEECCEEEH
56.0828112733
167UbiquitinationELTDVANKKLKCTET
EHHHHCCCCCCCCCC
50.1529967540
168UbiquitinationLTDVANKKLKCTETW
HHHHCCCCCCCCCCC
53.65-
172PhosphorylationANKKLKCTETWSLNS
CCCCCCCCCCCCHHH
34.5626270265
174PhosphorylationKKLKCTETWSLNSLV
CCCCCCCCCCHHHHH
11.3826270265
176PhosphorylationLKCTETWSLNSLVKH
CCCCCCCCHHHHHHH
25.7026270265
179PhosphorylationTETWSLNSLVKHLLG
CCCCCHHHHHHHHHC
39.5726270265
187UbiquitinationLVKHLLGKQLLKDKS
HHHHHHCHHHHCCCC
37.4329967540
202UbiquitinationIRCSNWSKFPLTEDQ
CCCCCCCCCCCCCCH
42.4929967540
241SumoylationVQRFAINKEEEILLS
HHHHCCCHHHHHHHH
61.46-
241UbiquitinationVQRFAINKEEEILLS
HHHHCCCHHHHHHHH
61.4622817900
241SumoylationVQRFAINKEEEILLS
HHHHCCCHHHHHHHH
61.4628112733
248PhosphorylationKEEEILLSDMNKQLT
HHHHHHHHHHHHHHH
31.22-
252SumoylationILLSDMNKQLTSISE
HHHHHHHHHHHHHCH
39.7928112733
274UbiquitinationHLPHAFSKLENPRRV
HHHHHHHCCCCHHHH
54.0622505724
282PhosphorylationLENPRRVSILLKDIS
CCCHHHHEEEEHHHH
13.0023882029
286UbiquitinationRRVSILLKDISENLY
HHHEEEEHHHHHHHH
49.96-
294PhosphorylationDISENLYSLRRMIIG
HHHHHHHHHHHHHHC
20.6824719451
319PhosphorylationSNNLNLLSFEDSTTG
CCCCCEEEEECCCCC
29.7420516064
366AcetylationGEDVLGNKVERKEDG
CCCCCCCCCEECCCC
43.6120428248
366UbiquitinationGEDVLGNKVERKEDG
CCCCCCCCCEECCCC
43.6121906983
370UbiquitinationLGNKVERKEDGFEDG
CCCCCEECCCCCCCC
46.8022817900
382UbiquitinationEDGVEDNKLKENMER
CCCCCCCHHHHHHHH
73.5722817900
384UbiquitinationGVEDNKLKENMERAC
CCCCCHHHHHHHHHH
48.9622817900
409PhosphorylationLQILEQQSQEEYLSD
HHHHHHHCHHHHHHH
38.9728122231
413PhosphorylationEQQSQEEYLSDIAYK
HHHCHHHHHHHHHHH
15.6828122231
415PhosphorylationQSQEEYLSDIAYKST
HCHHHHHHHHHHHCC
26.5228122231
421PhosphorylationLSDIAYKSTEHLSPN
HHHHHHHCCCCCCCC
26.7630576142
422PhosphorylationSDIAYKSTEHLSPND
HHHHHHCCCCCCCCC
24.2319690332
426PhosphorylationYKSTEHLSPNDNEND
HHCCCCCCCCCCCCC
24.4622617229
434PhosphorylationPNDNENDTSYVIESD
CCCCCCCCCEEEECC
33.2730108239
435PhosphorylationNDNENDTSYVIESDE
CCCCCCCCEEEECCH
21.9230108239
436PhosphorylationDNENDTSYVIESDED
CCCCCCCEEEECCHH
13.9228450419
440PhosphorylationDTSYVIESDEDLEME
CCCEEEECCHHHHHH
34.8725159151
453PhosphorylationMEMLKHLSPNDNEND
HHHHHHCCCCCCCCC
22.7522617229
461PhosphorylationPNDNENDTSYVIESD
CCCCCCCCCEEECCC
33.2730108239
462PhosphorylationNDNENDTSYVIESDE
CCCCCCCCEEECCCH
21.9230108239
463PhosphorylationDNENDTSYVIESDED
CCCCCCCEEECCCHH
13.9228450419
467PhosphorylationDTSYVIESDEDLEME
CCCEEECCCHHHHHH
34.8722617229
478PhosphorylationLEMEMLKSLENLNSG
HHHHHHHHHHCCCCC
36.6330266825
484PhosphorylationKSLENLNSGTVEPTH
HHHHCCCCCCCCCCH
38.7228555341
486PhosphorylationLENLNSGTVEPTHSK
HHCCCCCCCCCCHHH
22.8623186163
490PhosphorylationNSGTVEPTHSKCLKM
CCCCCCCCHHHHHHH
25.8523917254
493AcetylationTVEPTHSKCLKMERN
CCCCCHHHHHHHHHH
35.6623749302
493UbiquitinationTVEPTHSKCLKMERN
CCCCCHHHHHHHHHH
35.6629967540
496SumoylationPTHSKCLKMERNLGL
CCHHHHHHHHHHCCC
48.46-
496SumoylationPTHSKCLKMERNLGL
CCHHHHHHHHHHCCC
48.46-
496UbiquitinationPTHSKCLKMERNLGL
CCHHHHHHHHHHCCC
48.46-
506UbiquitinationRNLGLPTKEEEEDDE
HHCCCCCCCHHCCCC
62.2829967540
543PhosphorylationQVTCLKMYFGHSSFK
HEEEEEHHHCCCCCC
12.5722798277
547PhosphorylationLKMYFGHSSFKPVQW
EEHHHCCCCCCCCHH
37.5422798277
559PhosphorylationVQWKVIHSVLEERRD
CHHHHHHHHHHHCCC
19.7822798277
612PhosphorylationQVLQLKMSNIPACFL
HHHHHHHCCCCCHHC
29.9824247654
624PhosphorylationCFLGSAQSENVLTDI
HHCCCCCCCCCCCHH
30.7524247654
629PhosphorylationAQSENVLTDIKLGKY
CCCCCCCCHHHCCCE
31.2524247654
689PhosphorylationDSFRKLGSLKTALPM
HHHHHHCCHHHHCCC
36.81-
692PhosphorylationRKLGSLKTALPMVPI
HHHCCHHHHCCCCCE
38.4324719451
707PhosphorylationVALTATASSSIREDI
EHHEECCCHHHHHHH
21.9224719451
757PhosphorylationLQPFLVKTSSHWEFE
HHHEEEECCCCCCEE
28.1623401153
758PhosphorylationQPFLVKTSSHWEFEG
HHEEEECCCCCCEEC
17.9423401153
759PhosphorylationPFLVKTSSHWEFEGP
HEEEECCCCCCEECC
37.5423401153
767PhosphorylationHWEFEGPTIIYCPSR
CCCEECCEEEECCCC
30.7523401153
770PhosphorylationFEGPTIIYCPSRKMT
EECCEEEECCCCCCH
8.4123401153
773PhosphorylationPTIIYCPSRKMTQQV
CEEEECCCCCCHHHH
40.7623401153
775UbiquitinationIIYCPSRKMTQQVTG
EEECCCCCCHHHHHH
51.11-
777PhosphorylationYCPSRKMTQQVTGEL
ECCCCCCHHHHHHHH
20.91-
790PhosphorylationELRKLNLSCGTYHAG
HHHHCCCCCCCEECC
14.93-
801PhosphorylationYHAGMSFSTRKDIHH
EECCCCCCCCCCHHH
21.72-
849PhosphorylationPKDMESYYQEIGRAG
CCCHHHHHHHHHHHC
14.67-
856UbiquitinationYQEIGRAGRDGLQSS
HHHHHHHCCCCCCCC
27.1824816145
862PhosphorylationAGRDGLQSSCHVLWA
HCCCCCCCCCEEEEE
39.7220873877
863PhosphorylationGRDGLQSSCHVLWAP
CCCCCCCCCEEEEEC
8.6920873877
887AcetylationLTEIRNEKFRLYKLK
HHHHHHHCHHHHHHH
39.0620428248
905PhosphorylationKMEKYLHSSRCRRQI
HHHHHHHCHHHHHHH
19.5128152594
906PhosphorylationMEKYLHSSRCRRQII
HHHHHHCHHHHHHHH
25.3428152594
915PhosphorylationCRRQIILSHFEDKQV
HHHHHHHHHCCCHHH
18.7424719451
924UbiquitinationFEDKQVQKASLGIMG
CCCHHHHHHHHCCCC
40.8829967540
934UbiquitinationLGIMGTEKCCDNCRS
HCCCCCHHHCHHHHH
39.75-
948PhosphorylationSRLDHCYSMDDSEDT
HHCCCCCCCCCCCCC
22.56-
968PhosphorylationPQAFKLLSAVDILGE
HHHHHHHHHHHHHHH
36.3621406692
1002PhosphorylationADQYRRHSLFGTGKD
HHHHHHHCCCCCCCC
24.4728555341
1036SumoylationVEVSRYNKFMKICAL
EEEHHHCCHHHHHHH
37.59-
1036SumoylationVEVSRYNKFMKICAL
EEEHHHCCHHHHHHH
37.59-
1058PhosphorylationLHKANTESQSLILQA
HHHCCCCCHHHHHHC
24.0317525332
1073UbiquitinationNEELCPKKLLLPSSK
CHHHCCCCEECCCCC
29.5229967540
1079PhosphorylationKKLLLPSSKTVSSGT
CCEECCCCCCCCCCC
30.33-
1080UbiquitinationKLLLPSSKTVSSGTK
CEECCCCCCCCCCCC
58.2329967540
1084PhosphorylationPSSKTVSSGTKEHCY
CCCCCCCCCCCCHHC
46.26-
1087UbiquitinationKTVSSGTKEHCYNQV
CCCCCCCCCHHCCCC
49.3229967540
1099PhosphorylationNQVPVELSTEKKSNL
CCCCCCCCCCCCCCH
22.4825627689
1100PhosphorylationQVPVELSTEKKSNLE
CCCCCCCCCCCCCHH
65.5325159151
1102UbiquitinationPVELSTEKKSNLEKL
CCCCCCCCCCCHHHH
62.6829967540
1103UbiquitinationVELSTEKKSNLEKLY
CCCCCCCCCCHHHHH
38.04-
1110PhosphorylationKSNLEKLYSYKPCDK
CCCHHHHHCCCCCCC
22.48-
1111PhosphorylationSNLEKLYSYKPCDKI
CCHHHHHCCCCCCCC
36.80-
1112PhosphorylationNLEKLYSYKPCDKIS
CHHHHHCCCCCCCCC
12.8518452278
1113AcetylationLEKLYSYKPCDKISS
HHHHHCCCCCCCCCC
32.9825953088
1117AcetylationYSYKPCDKISSGSNI
HCCCCCCCCCCCCCC
51.7220428248
1120PhosphorylationKPCDKISSGSNISKK
CCCCCCCCCCCCCCC
50.1118452278
1126AcetylationSSGSNISKKSIMVQS
CCCCCCCCCEEEECC
46.9025953088
1127AcetylationSGSNISKKSIMVQSP
CCCCCCCCEEEECCH
38.1220428248
1128PhosphorylationGSNISKKSIMVQSPE
CCCCCCCEEEECCHH
21.4728450419
1133PhosphorylationKKSIMVQSPEKAYSS
CCEEEECCHHHHCCC
24.5019664994
1138PhosphorylationVQSPEKAYSSSQPVI
ECCHHHHCCCCCCCC
21.8328464451
1139PhosphorylationQSPEKAYSSSQPVIS
CCHHHHCCCCCCCCC
28.5128122231
1140PhosphorylationSPEKAYSSSQPVISA
CHHHHCCCCCCCCCH
21.9528122231
1141PhosphorylationPEKAYSSSQPVISAQ
HHHHCCCCCCCCCHH
32.3417525332
1157PhosphorylationQETQIVLYGKLVEAR
HCCEEHHHHHHHHHH
11.0024260401
1170UbiquitinationARQKHANKMDVPPAI
HHHHHHHCCCCCHHH
36.9429967540
1189UbiquitinationKILVDMAKMRPTTVE
CCHHHHHHCCCCCHH
28.89-
1199UbiquitinationPTTVENVKRIDGVSE
CCCHHHCCCCCCCCH
56.0429967540
1205PhosphorylationVKRIDGVSEGKAAML
CCCCCCCCHHHHHHH
46.27-
1249AcetylationQKTSLVAKNKICTLS
HHHCHHHHCCCCHHH
51.8225953088
1270UbiquitinationYSLFQEKKMPLKSIA
HHHHHCCCCCHHHHH
45.02-
1274AcetylationQEKKMPLKSIAESRI
HCCCCCHHHHHHHCH
33.6712650359
1275PhosphorylationEKKMPLKSIAESRIL
CCCCCHHHHHHHCHH
34.4129083192
1279PhosphorylationPLKSIAESRILPLMT
CHHHHHHHCHHHHHH
18.6529083192
1286PhosphorylationSRILPLMTIGMHLSQ
HCHHHHHHHHHHHHH
23.2829083192
1292PhosphorylationMTIGMHLSQAVKAGC
HHHHHHHHHHHHCCC
11.0429083192
1314UbiquitinationGLTPEVQKIIADVIR
CCCHHHHHHHHHHHH
41.0529967540
1327PhosphorylationIRNPPVNSDMSKISL
HHCCCCCCCCCHHHH
34.6221406692
1330PhosphorylationPPVNSDMSKISLIRM
CCCCCCCCHHHHHHH
31.6520860994
1331UbiquitinationPVNSDMSKISLIRML
CCCCCCCHHHHHHHH
29.67-
1333PhosphorylationNSDMSKISLIRMLVP
CCCCCHHHHHHHHCC
22.8321406692
1362UbiquitinationLKHGPDSGLQPSCDV
HHHCCCCCCCCCCCC
35.3924816145
1371UbiquitinationQPSCDVNKRRCFPGS
CCCCCCCCCCCCCCC
40.8629967540
1371AcetylationQPSCDVNKRRCFPGS
CCCCCCCCCCCCCCC
40.8625953088
1378PhosphorylationKRRCFPGSEEICSSS
CCCCCCCCHHHHCCC
32.09-
1385PhosphorylationSEEICSSSKRSKEEV
CHHHHCCCCCCHHHH
18.7825627689
1386UbiquitinationEEICSSSKRSKEEVG
HHHHCCCCCCHHHHC
63.7429967540
1388PhosphorylationICSSSKRSKEEVGIN
HHCCCCCCHHHHCCC
48.4324719451
1389AcetylationCSSSKRSKEEVGINT
HCCCCCCHHHHCCCC
63.0220428248
1389UbiquitinationCSSSKRSKEEVGINT
HCCCCCCHHHHCCCC
63.0224816145
1396PhosphorylationKEEVGINTETSSAER
HHHHCCCCCCCCHHH
38.4324732914
1398PhosphorylationEVGINTETSSAERKR
HHCCCCCCCCHHHHH
26.4124732914
1399PhosphorylationVGINTETSSAERKRR
HCCCCCCCCHHHHHC
22.7124732914
1400PhosphorylationGINTETSSAERKRRL
CCCCCCCCHHHHHCC
41.3820159463
1413AcetylationRLPVWFAKGSDTSKK
CCCEEEECCCHHHHH
49.8520428248
1415PhosphorylationPVWFAKGSDTSKKLM
CEEEECCCHHHHHHH
36.6923403867
1417PhosphorylationWFAKGSDTSKKLMDK
EEECCCHHHHHHHHH
44.1123403867
1418PhosphorylationFAKGSDTSKKLMDKT
EECCCHHHHHHHHHH
32.5523403867
1427MethylationKLMDKTKRGGLFS--
HHHHHHCCCCCCC--
50.04115386503
1432PhosphorylationTKRGGLFS-------
HCCCCCCC-------
44.3427134283

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
319SPhosphorylationKinasePRKDCP78527
GPS
440SPhosphorylationKinasePRKDCP78527
GPS
467SPhosphorylationKinasePRKDCP78527
GPS
1133SPhosphorylationKinaseCDK2P24941
PSP
1141SPhosphorylationKinaseATMQ13315
PSP
1141SPhosphorylationKinaseATRQ13535
PSP
1292SPhosphorylationKinaseATMQ13315
PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WRN_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
1126Acetylation1133 (7)SArs11574358
  • Lifespan
25918517
1127Acetylation1133 (6)SArs11574358
  • Lifespan
25918517
1128Phosphorylation1133 (5)SArs11574358
  • Lifespan
25918517
1133Phosphorylation1133 (0)SArs11574358
  • Lifespan
25918517
1138Phosphorylation1133 (5)SArs11574358
  • Lifespan
25918517
1141Phosphorylation1133 (8)SArs11574358
  • Lifespan
25918517

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FEN1_HUMANFEN1physical
14688284
TERF2_HUMANTERF2physical
12181313
PCNA_HUMANPCNAphysical
12633936
PRKDC_HUMANPRKDCphysical
11889123
WRIP1_HUMANWRNIP1physical
11301316
XRCC5_HUMANXRCC5physical
12177300
XRCC6_HUMANXRCC6physical
12177300
P53_HUMANTP53physical
12080066
XRCC6_HUMANXRCC6physical
10880505
XRCC5_HUMANXRCC5physical
10880505
EXO1_YEASTEXO1physical
20447876
CAF1A_HUMANCHAF1Aphysical
17173071
POTE1_HUMANPOT1genetic
21098121
FEN1_HUMANFEN1physical
16326861
H2AX_HUMANH2AFXphysical
15733840
NBN_HUMANNBNphysical
15733840
DHX9_HUMANDHX9physical
17498979
RAD51_HUMANRAD51physical
17118963
RAD52_HUMANRAD52physical
17118963
NBN_HUMANNBNphysical
20600238
PCNA_HUMANPCNAphysical
20600238
WRN_HUMANWRNphysical
10783163
XRCC6_HUMANXRCC6physical
10783163
XRCC5_HUMANXRCC5physical
10783163
XRCC5_HUMANXRCC5physical
11328876
PARP1_HUMANPARP1physical
14734561
XRCC5_HUMANXRCC5physical
14734561
XRCC6_HUMANXRCC6physical
14734561
ATR_HUMANATRphysical
22159421
DHX9_HUMANDHX9physical
15995249
TERA_HUMANVCPphysical
12937274
XRCC5_HUMANXRCC5physical
12937274
CDN2A_HUMANCDKN2Aphysical
15355988
ARF_HUMANCDKN2Aphysical
15355988
CDC5L_HUMANCDC5Lphysical
16223718
PML_HUMANPMLphysical
21639834
TERA_HUMANVCPphysical
15037256
RAD52_HUMANRAD52physical
12750383
SIR1_HUMANSIRT1physical
18203716
CBP_HUMANCREBBPphysical
18203716

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
277700Werner syndrome (WRN)
114500Colorectal cancer (CRC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WRN_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-426; SER-467 ANDSER-1133, 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-1133, 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-453 AND SER-467, ANDMASS SPECTROMETRY.
"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-1058 AND SER-1141, ANDMASS SPECTROMETRY.

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