PARP1_HUMAN - dbPTM
PARP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARP1_HUMAN
UniProt AC P09874
Protein Name Poly [ADP-ribose] polymerase 1
Gene Name PARP1
Organism Homo sapiens (Human).
Sequence Length 1014
Subcellular Localization Nucleus . Nucleus, nucleolus . Localizes at sites of DNA damage.
Protein Description Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. [PubMed: 17177976]
Protein Sequence MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW
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------MAESSDKLY
------CCCCCCCEE
36.3622814378
4Phosphorylation----MAESSDKLYRV
----CCCCCCCEEEH
51.3930108239
5Phosphorylation---MAESSDKLYRVE
---CCCCCCCEEEHH
30.2130108239
72-Hydroxyisobutyrylation-MAESSDKLYRVEYA
-CCCCCCCEEEHHHH
49.74-
7Acetylation-MAESSDKLYRVEYA
-CCCCCCCEEEHHHH
49.7425953088
7Ubiquitination-MAESSDKLYRVEYA
-CCCCCCCEEEHHHH
49.74-
9PhosphorylationAESSDKLYRVEYAKS
CCCCCCEEEHHHHHC
20.5321406692
15AcetylationLYRVEYAKSGRASCK
EEEHHHHHCCCCCHH
53.1725953088
15UbiquitinationLYRVEYAKSGRASCK
EEEHHHHHCCCCCHH
53.17-
16PhosphorylationYRVEYAKSGRASCKK
EEHHHHHCCCCCHHH
25.9124719451
25PhosphorylationRASCKKCSESIPKDS
CCCHHHCCCCCCHHH
43.17-
27PhosphorylationSCKKCSESIPKDSLR
CHHHCCCCCCHHHHE
28.09-
30AcetylationKCSESIPKDSLRMAI
HCCCCCCHHHHEEEE
59.2726051181
32PhosphorylationSESIPKDSLRMAIMV
CCCCCHHHHEEEEEE
24.81-
35SulfoxidationIPKDSLRMAIMVQSP
CCHHHHEEEEEECCC
3.4321406390
41PhosphorylationRMAIMVQSPMFDGKV
EEEEEECCCCCCCCC
13.6125159151
63PhosphorylationCFWKVGHSIRHPDVE
EEEECCCCCCCCCCE
18.5227080861
65MethylationWKVGHSIRHPDVEVD
EECCCCCCCCCCEEC
38.00115486469
75PhosphorylationDVEVDGFSELRWDDQ
CCEECCCCCCCCCCH
41.0530108239
78MethylationVDGFSELRWDDQQKV
ECCCCCCCCCCHHHH
30.63115486477
84AcetylationLRWDDQQKVKKTAEA
CCCCCHHHHHHHHHH
50.8423749302
84UbiquitinationLRWDDQQKVKKTAEA
CCCCCHHHHHHHHHH
50.84-
87UbiquitinationDDQQKVKKTAEAGGV
CCHHHHHHHHHHCCC
56.82-
88PhosphorylationDQQKVKKTAEAGGVT
CHHHHHHHHHHCCCC
24.8223663014
95PhosphorylationTAEAGGVTGKGQDGI
HHHHCCCCCCCCCCC
36.1323663014
97SumoylationEAGGVTGKGQDGIGS
HHCCCCCCCCCCCCC
43.99-
97AcetylationEAGGVTGKGQDGIGS
HHCCCCCCCCCCCCC
43.9919608861
97SumoylationEAGGVTGKGQDGIGS
HHCCCCCCCCCCCCC
43.9919608861
97UbiquitinationEAGGVTGKGQDGIGS
HHCCCCCCCCCCCCC
43.9919608861
104PhosphorylationKGQDGIGSKAEKTLG
CCCCCCCCHHHHHHH
27.1123663014
105SumoylationGQDGIGSKAEKTLGD
CCCCCCCHHHHHHHH
56.18-
105AcetylationGQDGIGSKAEKTLGD
CCCCCCCHHHHHHHH
56.1819608861
105SumoylationGQDGIGSKAEKTLGD
CCCCCCCHHHHHHHH
56.1819608861
108AcetylationGIGSKAEKTLGDFAA
CCCCHHHHHHHHHHH
54.6423954790
108UbiquitinationGIGSKAEKTLGDFAA
CCCCHHHHHHHHHHH
54.6421890473
109PhosphorylationIGSKAEKTLGDFAAE
CCCHHHHHHHHHHHH
27.7228555341
117PhosphorylationLGDFAAEYAKSNRST
HHHHHHHHHHHCCCC
18.0128152594
119AcetylationDFAAEYAKSNRSTCK
HHHHHHHHHCCCCCH
47.5725953088
119UbiquitinationDFAAEYAKSNRSTCK
HHHHHHHHHCCCCCH
47.5721906983
120PhosphorylationFAAEYAKSNRSTCKG
HHHHHHHHCCCCCHH
29.3327080861
131AcetylationTCKGCMEKIEKGQVR
CCHHHHHHHHHCCCE
29.3119608861
131UbiquitinationTCKGCMEKIEKGQVR
CCHHHHHHHHHCCCE
29.3119608861
134AcetylationGCMEKIEKGQVRLSK
HHHHHHHHCCCEEEC
59.1025953088
142AcetylationGQVRLSKKMVDPEKP
CCCEEECCCCCCCCC
40.5626051181
148SumoylationKKMVDPEKPQLGMID
CCCCCCCCCCCCCCC
43.37-
148AcetylationKKMVDPEKPQLGMID
CCCCCCCCCCCCCCC
43.3723954790
148SumoylationKKMVDPEKPQLGMID
CCCCCCCCCCCCCCC
43.37-
148UbiquitinationKKMVDPEKPQLGMID
CCCCCCCCCCCCCCC
43.37-
156MethylationPQLGMIDRWYHPGCF
CCCCCCCCCCCCCCC
25.57115486437
158PhosphorylationLGMIDRWYHPGCFVK
CCCCCCCCCCCCCCC
10.0728152594
165AcetylationYHPGCFVKNREELGF
CCCCCCCCCHHHHCC
29.9925953088
165UbiquitinationYHPGCFVKNREELGF
CCCCCCCCCHHHHCC
29.9921890473
176PhosphorylationELGFRPEYSASQLKG
HHCCCCCCCHHHHCC
16.5423403867
177PhosphorylationLGFRPEYSASQLKGF
HCCCCCCCHHHHCCC
21.5625159151
179PhosphorylationFRPEYSASQLKGFSL
CCCCCCHHHHCCCEE
30.0617525332
182UbiquitinationEYSASQLKGFSLLAT
CCCHHHHCCCEEEEC
50.72-
185PhosphorylationASQLKGFSLLATEDK
HHHHCCCEEEECCCH
31.0125159151
189PhosphorylationKGFSLLATEDKEALK
CCCEEEECCCHHHHH
44.6921815630
192SumoylationSLLATEDKEALKKQL
EEEECCCHHHHHHHC
38.36-
1922-HydroxyisobutyrylationSLLATEDKEALKKQL
EEEECCCHHHHHHHC
38.36-
192AcetylationSLLATEDKEALKKQL
EEEECCCHHHHHHHC
38.3625953088
192SumoylationSLLATEDKEALKKQL
EEEECCCHHHHHHHC
38.3628112733
192UbiquitinationSLLATEDKEALKKQL
EEEECCCHHHHHHHC
38.36-
196AcetylationTEDKEALKKQLPGVK
CCCHHHHHHHCCCCC
45.5923749302
196MalonylationTEDKEALKKQLPGVK
CCCHHHHHHHCCCCC
45.5926320211
197UbiquitinationEDKEALKKQLPGVKS
CCHHHHHHHCCCCCC
58.90-
203SumoylationKKQLPGVKSEGKRKG
HHHCCCCCCCCCCCC
49.02-
203SumoylationKKQLPGVKSEGKRKG
HHHCCCCCCCCCCCC
49.0225114211
204PhosphorylationKQLPGVKSEGKRKGD
HHCCCCCCCCCCCCC
49.5325159151
209AcetylationVKSEGKRKGDEVDGV
CCCCCCCCCCCCCCH
74.3626051181
209UbiquitinationVKSEGKRKGDEVDGV
CCCCCCCCCCCCCCH
74.3621906983
221UbiquitinationDGVDEVAKKKSKKEK
CCHHHHHHHHCHHHH
66.9521906983
224PhosphorylationDEVAKKKSKKEKDKD
HHHHHHHCHHHHCCC
58.81-
239UbiquitinationSKLEKALKAQNDLIW
HHHHHHHHHHHHHHH
53.4321890473
239UbiquitinationSKLEKALKAQNDLIW
HHHHHHHHHHHHHHH
53.4321906983
249SumoylationNDLIWNIKDELKKVC
HHHHHHHHHHHHHHC
41.77-
249AcetylationNDLIWNIKDELKKVC
HHHHHHHHHHHHHHC
41.7726822725
249SumoylationNDLIWNIKDELKKVC
HHHHHHHHHHHHHHC
41.7728112733
249UbiquitinationNDLIWNIKDELKKVC
HHHHHHHHHHHHHHC
41.77-
253AcetylationWNIKDELKKVCSTND
HHHHHHHHHHCCCCC
40.9026051181
254AcetylationNIKDELKKVCSTNDL
HHHHHHHHHCCCCCH
62.1830582485
254UbiquitinationNIKDELKKVCSTNDL
HHHHHHHHHCCCCCH
62.18-
256GlutathionylationKDELKKVCSTNDLKE
HHHHHHHCCCCCHHH
5.9622555962
257PhosphorylationDELKKVCSTNDLKEL
HHHHHHCCCCCHHHH
32.9825159151
258PhosphorylationELKKVCSTNDLKELL
HHHHHCCCCCHHHHH
27.8528464451
262SumoylationVCSTNDLKELLIFNK
HCCCCCHHHHHEEEC
49.53-
262AcetylationVCSTNDLKELLIFNK
HCCCCCHHHHHEEEC
49.5325825284
262SumoylationVCSTNDLKELLIFNK
HCCCCCHHHHHEEEC
49.53-
262UbiquitinationVCSTNDLKELLIFNK
HCCCCCHHHHHEEEC
49.53-
269UbiquitinationKELLIFNKQQVPSGE
HHHHEEECCCCCCCC
31.2121890473
2692-HydroxyisobutyrylationKELLIFNKQQVPSGE
HHHHEEECCCCCCCC
31.21-
269AcetylationKELLIFNKQQVPSGE
HHHHEEECCCCCCCC
31.2126051181
269UbiquitinationKELLIFNKQQVPSGE
HHHHEEECCCCCCCC
31.2121906983
274PhosphorylationFNKQQVPSGESAILD
EECCCCCCCCCHHHH
57.2330266825
277PhosphorylationQQVPSGESAILDRVA
CCCCCCCCHHHHHHC
24.9230266825
282MethylationGESAILDRVADGMVF
CCCHHHHHHCCCCEE
23.29115486445
298GlutathionylationALLPCEECSGQLVFK
EEEECHHHCCEEEEE
2.3022555962
299PhosphorylationLLPCEECSGQLVFKS
EEECHHHCCEEEEEC
32.6226714015
306PhosphorylationSGQLVFKSDAYYCTG
CCEEEEECCCEEECC
18.9328152594
309PhosphorylationLVFKSDAYYCTGDVT
EEEECCCEEECCCHH
12.2228152594
310PhosphorylationVFKSDAYYCTGDVTA
EEECCCEEECCCHHH
5.8128152594
311GlutathionylationFKSDAYYCTGDVTAW
EECCCEEECCCHHHE
1.9222555962
316PhosphorylationYYCTGDVTAWTKCMV
EEECCCHHHEEEEEE
22.6330576142
320UbiquitinationGDVTAWTKCMVKTQT
CCHHHEEEEEEECCC
15.0521890473
320AcetylationGDVTAWTKCMVKTQT
CCHHHEEEEEEECCC
15.0526051181
320UbiquitinationGDVTAWTKCMVKTQT
CCHHHEEEEEEECCC
15.0521906983
324AcetylationAWTKCMVKTQTPNRK
HEEEEEEECCCCCCC
14.1826051181
325PhosphorylationWTKCMVKTQTPNRKE
EEEEEEECCCCCCCC
26.6823403867
327PhosphorylationKCMVKTQTPNRKEWV
EEEEECCCCCCCCCC
27.9727174698
331AcetylationKTQTPNRKEWVTPKE
ECCCCCCCCCCCHHH
63.6726051181
331SumoylationKTQTPNRKEWVTPKE
ECCCCCCCCCCCHHH
63.67-
331UbiquitinationKTQTPNRKEWVTPKE
ECCCCCCCCCCCHHH
63.67-
335PhosphorylationPNRKEWVTPKEFREI
CCCCCCCCHHHHHHH
29.7123403867
337UbiquitinationRKEWVTPKEFREISY
CCCCCCHHHHHHHHH
61.1821890473
337SumoylationRKEWVTPKEFREISY
CCCCCCHHHHHHHHH
61.18-
337AcetylationRKEWVTPKEFREISY
CCCCCCHHHHHHHHH
61.1826822725
337SumoylationRKEWVTPKEFREISY
CCCCCCHHHHHHHHH
61.18-
337UbiquitinationRKEWVTPKEFREISY
CCCCCCHHHHHHHHH
61.1821906983
343PhosphorylationPKEFREISYLKKLKV
HHHHHHHHHHHHCCC
21.4728152594
344PhosphorylationKEFREISYLKKLKVK
HHHHHHHHHHHCCCC
28.3625367160
346AcetylationFREISYLKKLKVKKQ
HHHHHHHHHCCCCCC
48.0725953088
361PhosphorylationDRIFPPETSASVAAT
CCCCCCCCCCCCCCC
35.0530266825
362PhosphorylationRIFPPETSASVAATP
CCCCCCCCCCCCCCC
19.5130266825
364PhosphorylationFPPETSASVAATPPP
CCCCCCCCCCCCCCC
16.4430266825
368PhosphorylationTSASVAATPPPSTAS
CCCCCCCCCCCCCCC
26.9623401153
372PhosphorylationVAATPPPSTASAPAA
CCCCCCCCCCCCCCC
42.2430266825
373PhosphorylationAATPPPSTASAPAAV
CCCCCCCCCCCCCCC
30.3330266825
375PhosphorylationTPPPSTASAPAAVNS
CCCCCCCCCCCCCCC
34.5730266825
382PhosphorylationSAPAAVNSSASADKP
CCCCCCCCCCCCCCC
22.2323403867
383PhosphorylationAPAAVNSSASADKPL
CCCCCCCCCCCCCCC
22.5023403867
385PhosphorylationAAVNSSASADKPLSN
CCCCCCCCCCCCCCC
38.6623403867
387ADP-ribosylationVNSSASADKPLSNMK
CCCCCCCCCCCCCCE
51.0819764761
391PhosphorylationASADKPLSNMKILTL
CCCCCCCCCCEEEHH
43.3224732914
394UbiquitinationDKPLSNMKILTLGKL
CCCCCCCEEEHHHHH
38.5221890473
394UbiquitinationDKPLSNMKILTLGKL
CCCCCCCEEEHHHHH
38.5221906983
400UbiquitinationMKILTLGKLSRNKDE
CEEEHHHHHCCCHHH
46.5321890473
400AcetylationMKILTLGKLSRNKDE
CEEEHHHHHCCCHHH
46.5325953088
400UbiquitinationMKILTLGKLSRNKDE
CEEEHHHHHCCCHHH
46.5321906983
407PolyADP-ribosyl glutamic acidKLSRNKDEVKAMIEK
HHCCCHHHHHHHHHH
47.75-
407ADP-ribosylationKLSRNKDEVKAMIEK
HHCCCHHHHHHHHHH
47.75-
409SumoylationSRNKDEVKAMIEKLG
CCCHHHHHHHHHHHC
30.14-
409AcetylationSRNKDEVKAMIEKLG
CCCHHHHHHHHHHHC
30.1426822725
409SumoylationSRNKDEVKAMIEKLG
CCCHHHHHHHHHHHC
30.14-
413PolyADP-ribosyl glutamic acidDEVKAMIEKLGGKLT
HHHHHHHHHHCCCCC
29.19-
413ADP-ribosylationDEVKAMIEKLGGKLT
HHHHHHHHHHCCCCC
29.19-
4142-HydroxyisobutyrylationEVKAMIEKLGGKLTG
HHHHHHHHHCCCCCC
41.32-
414AcetylationEVKAMIEKLGGKLTG
HHHHHHHHHCCCCCC
41.3225953088
414UbiquitinationEVKAMIEKLGGKLTG
HHHHHHHHHCCCCCC
41.32-
418AcetylationMIEKLGGKLTGTANK
HHHHHCCCCCCCCCH
40.8723749302
418UbiquitinationMIEKLGGKLTGTANK
HHHHHCCCCCCCCCH
40.87-
420PhosphorylationEKLGGKLTGTANKAS
HHHCCCCCCCCCHHH
35.6524732914
422PhosphorylationLGGKLTGTANKASLC
HCCCCCCCCCHHHHH
23.0924732914
425UbiquitinationKLTGTANKASLCIST
CCCCCCCHHHHHHHC
36.57-
427PhosphorylationTGTANKASLCISTKK
CCCCCHHHHHHHCHH
25.9430576142
431PhosphorylationNKASLCISTKKEVEK
CHHHHHHHCHHHHHH
32.9330576142
432PhosphorylationKASLCISTKKEVEKM
HHHHHHHCHHHHHHH
26.6529083192
433SumoylationASLCISTKKEVEKMN
HHHHHHCHHHHHHHH
39.90-
433AcetylationASLCISTKKEVEKMN
HHHHHHCHHHHHHHH
39.9025953088
433SumoylationASLCISTKKEVEKMN
HHHHHHCHHHHHHHH
39.90-
434UbiquitinationSLCISTKKEVEKMNK
HHHHHCHHHHHHHHH
68.06-
435PolyADP-ribosyl glutamic acidLCISTKKEVEKMNKK
HHHHCHHHHHHHHHH
58.42-
435ADP-ribosylationLCISTKKEVEKMNKK
HHHHCHHHHHHHHHH
58.42-
437PolyADP-ribosyl glutamic acidISTKKEVEKMNKKME
HHCHHHHHHHHHHHH
47.91-
437ADP-ribosylationISTKKEVEKMNKKME
HHCHHHHHHHHHHHH
47.91-
4382-HydroxyisobutyrylationSTKKEVEKMNKKMEE
HCHHHHHHHHHHHHH
53.61-
444PolyADP-ribosyl glutamic acidEKMNKKMEEVKEANI
HHHHHHHHHHHHCCE
69.39-
444ADP-ribosylationEKMNKKMEEVKEANI
HHHHHHHHHHHHCCE
69.39-
445PolyADP-ribosyl glutamic acidKMNKKMEEVKEANIR
HHHHHHHHHHHCCEE
56.22-
445ADP-ribosylationKMNKKMEEVKEANIR
HHHHHHHHHHHCCEE
56.22-
4472-HydroxyisobutyrylationNKKMEEVKEANIRVV
HHHHHHHHHCCEEEE
55.15-
447UbiquitinationNKKMEEVKEANIRVV
HHHHHHHHHCCEEEE
55.15-
448PolyADP-ribosyl glutamic acidKKMEEVKEANIRVVS
HHHHHHHHCCEEEEC
52.72-
448ADP-ribosylationKKMEEVKEANIRVVS
HHHHHHHHCCEEEEC
52.72-
455PhosphorylationEANIRVVSEDFLQDV
HCCEEEECHHHHHHH
28.7020068231
456PolyADP-ribosyl glutamic acidANIRVVSEDFLQDVS
CCEEEECHHHHHHHC
40.97-
456ADP-ribosylationANIRVVSEDFLQDVS
CCEEEECHHHHHHHC
40.97-
463PhosphorylationEDFLQDVSASTKSLQ
HHHHHHHCCCCHHHH
25.4520068231
465PhosphorylationFLQDVSASTKSLQEL
HHHHHCCCCHHHHHH
28.9420068231
466PhosphorylationLQDVSASTKSLQELF
HHHHCCCCHHHHHHH
25.1120068231
467SumoylationQDVSASTKSLQELFL
HHHCCCCHHHHHHHH
46.83-
467SumoylationQDVSASTKSLQELFL
HHHCCCCHHHHHHHH
46.8328112733
471PolyADP-ribosyl glutamic acidASTKSLQELFLAHIL
CCCHHHHHHHHHHHH
46.94-
471ADP-ribosylationASTKSLQELFLAHIL
CCCHHHHHHHHHHHH
46.94-
479PhosphorylationLFLAHILSPWGAEVK
HHHHHHHCCCCCCCE
20.2928450419
484PolyADP-ribosyl glutamic acidILSPWGAEVKAEPVE
HHCCCCCCCEEECEE
40.38-
484ADP-ribosylationILSPWGAEVKAEPVE
HHCCCCCCCEEECEE
40.38-
486SumoylationSPWGAEVKAEPVEVV
CCCCCCCEEECEEEE
38.24-
486SumoylationSPWGAEVKAEPVEVV
CCCCCCCEEECEEEE
38.2425114211
486UbiquitinationSPWGAEVKAEPVEVV
CCCCCCCEEECEEEE
38.24-
488PolyADP-ribosyl glutamic acidWGAEVKAEPVEVVAP
CCCCCEEECEEEEEC
44.13-
488ADP-ribosylationWGAEVKAEPVEVVAP
CCCCCEEECEEEEEC
44.1319764761
491PolyADP-ribosyl glutamic acidEVKAEPVEVVAPRGK
CCEEECEEEEECCCC
41.83-
491ADP-ribosylationEVKAEPVEVVAPRGK
CCEEECEEEEECCCC
41.8319764761
498AcetylationEVVAPRGKSGAALSK
EEEECCCCCCCCCCC
47.1716204234
499ADP-ribosylationVVAPRGKSGAALSKK
EEECCCCCCCCCCCC
36.1728190768
499PhosphorylationVVAPRGKSGAALSKK
EEECCCCCCCCCCCC
36.1724719451
504ADP-ribosylationGKSGAALSKKSKGQV
CCCCCCCCCCCCCCC
33.0529954836
504PhosphorylationGKSGAALSKKSKGQV
CCCCCCCCCCCCCCC
33.0524719451
505AcetylationKSGAALSKKSKGQVK
CCCCCCCCCCCCCCC
63.0116204234
507ADP-ribosylationGAALSKKSKGQVKEE
CCCCCCCCCCCCCCC
45.8428190768
507PhosphorylationGAALSKKSKGQVKEE
CCCCCCCCCCCCCCC
45.8429496963
508AcetylationAALSKKSKGQVKEEG
CCCCCCCCCCCCCCC
63.3416204234
508MethylationAALSKKSKGQVKEEG
CCCCCCCCCCCCCCC
63.34-
512SumoylationKKSKGQVKEEGINKS
CCCCCCCCCCCCCHH
42.01-
5122-HydroxyisobutyrylationKKSKGQVKEEGINKS
CCCCCCCCCCCCCHH
42.01-
512AcetylationKKSKGQVKEEGINKS
CCCCCCCCCCCCCHH
42.0126051181
512SumoylationKKSKGQVKEEGINKS
CCCCCCCCCCCCCHH
42.0128112733
513PolyADP-ribosyl glutamic acidKSKGQVKEEGINKSE
CCCCCCCCCCCCHHH
63.70-
513ADP-ribosylationKSKGQVKEEGINKSE
CCCCCCCCCCCCHHH
63.70-
514PolyADP-ribosyl glutamic acidSKGQVKEEGINKSEK
CCCCCCCCCCCHHHH
60.71-
514ADP-ribosylationSKGQVKEEGINKSEK
CCCCCCCCCCCHHHH
60.71-
518SumoylationVKEEGINKSEKRMKL
CCCCCCCHHHHHEEE
59.06-
518AcetylationVKEEGINKSEKRMKL
CCCCCCCHHHHHEEE
59.0625953088
518SumoylationVKEEGINKSEKRMKL
CCCCCCCHHHHHEEE
59.06-
519ADP-ribosylationKEEGINKSEKRMKLT
CCCCCCHHHHHEEEE
43.8128190768
519PhosphorylationKEEGINKSEKRMKLT
CCCCCCHHHHHEEEE
43.8129496963
520PolyADP-ribosyl glutamic acidEEGINKSEKRMKLTL
CCCCCHHHHHEEEEE
46.41-
520ADP-ribosylationEEGINKSEKRMKLTL
CCCCCHHHHHEEEEE
46.41-
521AcetylationEGINKSEKRMKLTLK
CCCCHHHHHEEEEEE
65.9516204234
524AcetylationNKSEKRMKLTLKGGA
CHHHHHEEEEEECCC
42.2116204234
526PhosphorylationSEKRMKLTLKGGAAV
HHHHEEEEEECCCCC
22.3924719451
528UbiquitinationKRMKLTLKGGAAVDP
HHEEEEEECCCCCCC
50.4921890473
528SumoylationKRMKLTLKGGAAVDP
HHEEEEEECCCCCCC
50.49-
528AcetylationKRMKLTLKGGAAVDP
HHEEEEEECCCCCCC
50.4925953088
528SumoylationKRMKLTLKGGAAVDP
HHEEEEEECCCCCCC
50.4928112733
528UbiquitinationKRMKLTLKGGAAVDP
HHEEEEEECCCCCCC
50.4921906983
537PhosphorylationGAAVDPDSGLEHSAH
CCCCCCCCCCCCHHH
51.1429214152
542PhosphorylationPDSGLEHSAHVLEKG
CCCCCCCHHHHHHHC
15.6425159151
548UbiquitinationHSAHVLEKGGKVFSA
CHHHHHHHCCEEEEE
69.6621890473
5482-HydroxyisobutyrylationHSAHVLEKGGKVFSA
CHHHHHHHCCEEEEE
69.66-
548AcetylationHSAHVLEKGGKVFSA
CHHHHHHHCCEEEEE
69.6623749302
548MalonylationHSAHVLEKGGKVFSA
CHHHHHHHCCEEEEE
69.6626320211
548UbiquitinationHSAHVLEKGGKVFSA
CHHHHHHHCCEEEEE
69.6621890473
551UbiquitinationHVLEKGGKVFSATLG
HHHHHCCEEEEEEEE
49.1021890473
551AcetylationHVLEKGGKVFSATLG
HHHHHCCEEEEEEEE
49.1026051181
551UbiquitinationHVLEKGGKVFSATLG
HHHHHCCEEEEEEEE
49.1021906983
554PhosphorylationEKGGKVFSATLGLVD
HHCCEEEEEEEECEE
24.2729396449
556PhosphorylationGGKVFSATLGLVDIV
CCEEEEEEEECEEEC
21.8429396449
564UbiquitinationLGLVDIVKGTNSYYK
EECEEECCCCCCEEE
61.4221890473
564UbiquitinationLGLVDIVKGTNSYYK
EECEEECCCCCCEEE
61.4221906983
571AcetylationKGTNSYYKLQLLEDD
CCCCCEEEEEEEECC
22.8626051181
571UbiquitinationKGTNSYYKLQLLEDD
CCCCCEEEEEEEECC
22.86-
579UbiquitinationLQLLEDDKENRYWIF
EEEEECCHHCCEEEE
70.0321890473
579AcetylationLQLLEDDKENRYWIF
EEEEECCHHCCEEEE
70.0323749302
579UbiquitinationLQLLEDDKENRYWIF
EEEEECCHHCCEEEE
70.0321906983
582MethylationLEDDKENRYWIFRSW
EECCHHCCEEEEECC
29.29115486429
598PhosphorylationRVGTVIGSNKLEQMP
CCEEEECCCCHHCCC
21.4826714015
600UbiquitinationGTVIGSNKLEQMPSK
EEEECCCCHHCCCCH
55.9121890473
600SumoylationGTVIGSNKLEQMPSK
EEEECCCCHHCCCCH
55.91-
600AcetylationGTVIGSNKLEQMPSK
EEEECCCCHHCCCCH
55.9119608861
600SumoylationGTVIGSNKLEQMPSK
EEEECCCCHHCCCCH
55.9119608861
600UbiquitinationGTVIGSNKLEQMPSK
EEEECCCCHHCCCCH
55.9121906983
606PhosphorylationNKLEQMPSKEDAIEH
CCHHCCCCHHHHHHH
43.2521406692
6072-HydroxyisobutyrylationKLEQMPSKEDAIEHF
CHHCCCCHHHHHHHH
54.46-
607AcetylationKLEQMPSKEDAIEHF
CHHCCCCHHHHHHHH
54.4626051181
607UbiquitinationKLEQMPSKEDAIEHF
CHHCCCCHHHHHHHH
54.46-
616AcetylationDAIEHFMKLYEEKTG
HHHHHHHHHHHHHHC
47.1526822725
621AcetylationFMKLYEEKTGNAWHS
HHHHHHHHHCCCCCC
50.2019608861
621UbiquitinationFMKLYEEKTGNAWHS
HHHHHHHHHCCCCCC
50.2019608861
629AcetylationTGNAWHSKNFTKYPK
HCCCCCCCCCCCCCC
43.1023749302
629UbiquitinationTGNAWHSKNFTKYPK
HCCCCCCCCCCCCCC
43.10-
632PhosphorylationAWHSKNFTKYPKKFY
CCCCCCCCCCCCCCC
38.7828152594
633AcetylationWHSKNFTKYPKKFYP
CCCCCCCCCCCCCCC
56.2525953088
633UbiquitinationWHSKNFTKYPKKFYP
CCCCCCCCCCCCCCC
56.25-
634PhosphorylationHSKNFTKYPKKFYPL
CCCCCCCCCCCCCCE
19.7528152594
637UbiquitinationNFTKYPKKFYPLEID
CCCCCCCCCCCEEEC
45.7021890473
637SumoylationNFTKYPKKFYPLEID
CCCCCCCCCCCEEEC
45.70-
637AcetylationNFTKYPKKFYPLEID
CCCCCCCCCCCEEEC
45.7025953088
637SumoylationNFTKYPKKFYPLEID
CCCCCCCCCCCEEEC
45.70-
637UbiquitinationNFTKYPKKFYPLEID
CCCCCCCCCCCEEEC
45.7021906983
639PhosphorylationTKYPKKFYPLEIDYG
CCCCCCCCCEEECCC
18.7828152594
645PhosphorylationFYPLEIDYGQDEEAV
CCCEEECCCCCHHHH
23.5028152594
653AcetylationGQDEEAVKKLTVNPG
CCCHHHHHHHEECCC
49.4625953088
653SumoylationGQDEEAVKKLTVNPG
CCCHHHHHHHEECCC
49.46-
653UbiquitinationGQDEEAVKKLTVNPG
CCCHHHHHHHEECCC
49.46-
654SumoylationQDEEAVKKLTVNPGT
CCHHHHHHHEECCCC
42.67-
654SumoylationQDEEAVKKLTVNPGT
CCHHHHHHHEECCCC
42.67-
654UbiquitinationQDEEAVKKLTVNPGT
CCHHHHHHHEECCCC
42.67-
661PhosphorylationKLTVNPGTKSKLPKP
HHEECCCCHHCCCHH
33.14-
662AcetylationLTVNPGTKSKLPKPV
HEECCCCHHCCCHHH
52.0525953088
662UbiquitinationLTVNPGTKSKLPKPV
HEECCCCHHCCCHHH
52.05-
664AcetylationVNPGTKSKLPKPVQD
ECCCCHHCCCHHHHH
71.0726051181
664UbiquitinationVNPGTKSKLPKPVQD
ECCCCHHCCCHHHHH
71.07-
667AcetylationGTKSKLPKPVQDLIK
CCHHCCCHHHHHHHH
69.1526051181
667UbiquitinationGTKSKLPKPVQDLIK
CCHHCCCHHHHHHHH
69.1521890473
674"N6,N6-dimethyllysine"KPVQDLIKMIFDVES
HHHHHHHHHHHCHHH
32.99-
674AcetylationKPVQDLIKMIFDVES
HHHHHHHHHHHCHHH
32.9927452117
674MethylationKPVQDLIKMIFDVES
HHHHHHHHHHHCHHH
32.99-
681PhosphorylationKMIFDVESMKKAMVE
HHHHCHHHHHHHHHE
35.43-
683AcetylationIFDVESMKKAMVEYE
HHCHHHHHHHHHEEE
46.8123749302
683MalonylationIFDVESMKKAMVEYE
HHCHHHHHHHHHEEE
46.8126320211
683UbiquitinationIFDVESMKKAMVEYE
HHCHHHHHHHHHEEE
46.8121890473
689PhosphorylationMKKAMVEYEIDLQKM
HHHHHHEEECCHHCC
13.53-
695UbiquitinationEYEIDLQKMPLGKLS
EEECCHHCCCCCCCC
50.19-
700AcetylationLQKMPLGKLSKRQIQ
HHCCCCCCCCHHHHH
58.2225953088
700UbiquitinationLQKMPLGKLSKRQIQ
HHCCCCCCCCHHHHH
58.22-
702PhosphorylationKMPLGKLSKRQIQAA
CCCCCCCCHHHHHHH
29.3125159151
714PhosphorylationQAAYSILSEVQQAVS
HHHHHHHHHHHHHHH
33.7728348404
721PhosphorylationSEVQQAVSQGSSDSQ
HHHHHHHHCCCCHHH
31.6628348404
724PhosphorylationQQAVSQGSSDSQILD
HHHHHCCCCHHHHHH
24.2828348404
725PhosphorylationQAVSQGSSDSQILDL
HHHHCCCCHHHHHHH
48.3728348404
727PhosphorylationVSQGSSDSQILDLSN
HHCCCCHHHHHHHHH
22.5228348404
733PhosphorylationDSQILDLSNRFYTLI
HHHHHHHHHCCEEEC
26.1424275569
737PhosphorylationLDLSNRFYTLIPHDF
HHHHHCCEEECCCCC
9.44-
738PhosphorylationDLSNRFYTLIPHDFG
HHHHCCEEECCCCCC
18.59-
748SumoylationPHDFGMKKPPLLNNA
CCCCCCCCCCCCCCC
42.87-
748AcetylationPHDFGMKKPPLLNNA
CCCCCCCCCCCCCCC
42.8726051181
748SumoylationPHDFGMKKPPLLNNA
CCCCCCCCCCCCCCC
42.8725114211
748UbiquitinationPHDFGMKKPPLLNNA
CCCCCCCCCCCCCCC
42.87-
757PhosphorylationPLLNNADSVQAKVEM
CCCCCCHHHHHHHHH
17.4520873877
761SumoylationNADSVQAKVEMLDNL
CCHHHHHHHHHHHHH
22.95-
775PhosphorylationLLDIEVAYSLLRGGS
HHHHHHHHHHHHCCC
12.6722817900
776PhosphorylationLDIEVAYSLLRGGSD
HHHHHHHHHHHCCCC
15.9328355574
779MethylationEVAYSLLRGGSDDSS
HHHHHHHHCCCCCCC
53.36115486461
782PhosphorylationYSLLRGGSDDSSKDP
HHHHHCCCCCCCCCC
40.8622167270
785PhosphorylationLRGGSDDSSKDPIDV
HHCCCCCCCCCCCCC
44.2530266825
786PhosphorylationRGGSDDSSKDPIDVN
HCCCCCCCCCCCCCC
48.3430266825
787AcetylationGGSDDSSKDPIDVNY
CCCCCCCCCCCCCCH
72.0423236377
787UbiquitinationGGSDDSSKDPIDVNY
CCCCCCCCCCCCCCH
72.04-
794PhosphorylationKDPIDVNYEKLKTDI
CCCCCCCHHHHCCCE
17.8123403867
796SumoylationPIDVNYEKLKTDIKV
CCCCCHHHHCCCEEE
44.94-
7962-HydroxyisobutyrylationPIDVNYEKLKTDIKV
CCCCCHHHHCCCEEE
44.94-
796AcetylationPIDVNYEKLKTDIKV
CCCCCHHHHCCCEEE
44.9426051181
796SumoylationPIDVNYEKLKTDIKV
CCCCCHHHHCCCEEE
44.94-
796UbiquitinationPIDVNYEKLKTDIKV
CCCCCHHHHCCCEEE
44.94-
798UbiquitinationDVNYEKLKTDIKVVD
CCCHHHHCCCEEEEC
56.04-
802AcetylationEKLKTDIKVVDRDSE
HHHCCCEEEECCCCH
38.7327452117
802SumoylationEKLKTDIKVVDRDSE
HHHCCCEEEECCCCH
38.73-
806MethylationTDIKVVDRDSEEAEI
CCEEEECCCCHHHHH
37.43115486485
808PhosphorylationIKVVDRDSEEAEIIR
EEEECCCCHHHHHHH
37.93-
815MethylationSEEAEIIRKYVKNTH
CHHHHHHHHHHHCCC
29.88115486493
819UbiquitinationEIIRKYVKNTHATTH
HHHHHHHHCCCCCCC
53.70-
824O-linked_GlycosylationYVKNTHATTHNAYDL
HHHCCCCCCCCCCCE
22.45OGP
824PhosphorylationYVKNTHATTHNAYDL
HHHCCCCCCCCCCCE
22.45-
838UbiquitinationLEVIDIFKIEREGEC
EEEEEEEEEEECCCC
43.95-
852AcetylationCQRYKPFKQLHNRRL
CCCCCCHHHHCCCCE
61.5523749302
852UbiquitinationCQRYKPFKQLHNRRL
CCCCCCHHHHCCCCE
61.55-
864PhosphorylationRRLLWHGSRTTNFAG
CCEEEECCCCCCHHH
17.3620068231
866PhosphorylationLLWHGSRTTNFAGIL
EEEECCCCCCHHHHH
27.9921712546
867PhosphorylationLWHGSRTTNFAGILS
EEECCCCCCHHHHHH
27.5121712546
874PhosphorylationTNFAGILSQGLRIAP
CCHHHHHHCCCEECC
21.9321712546
878MethylationGILSQGLRIAPPEAP
HHHHCCCEECCCCCC
29.82115486453
896PhosphorylationYMFGKGIYFADMVSK
EECCCCEEHHHHHHC
11.03-
900SulfoxidationKGIYFADMVSKSANY
CCEEHHHHHHCCCCC
3.0830846556
907PhosphorylationMVSKSANYCHTSQGD
HHHCCCCCCCCCCCC
5.82-
940AcetylationKHASHISKLPKGKHS
HCHHHHHCCCCCCCC
69.1125953088
940UbiquitinationKHASHISKLPKGKHS
HCHHHHHCCCCCCCC
69.11-
949UbiquitinationPKGKHSVKGLGKTTP
CCCCCCCCCCCCCCC
51.97-
1006AcetylationLKYLLKLKFNFKTSL
HHHHHHHEECCCCCC
36.3526051181
1006UbiquitinationLKYLLKLKFNFKTSL
HHHHHHHEECCCCCC
36.35-
1010MethylationLKLKFNFKTSLW---
HHHEECCCCCCC---
38.0024772241
1010UbiquitinationLKLKFNFKTSLW---
HHHEECCCCCCC---
38.00-

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
177SPhosphorylationKinaseAMPKA1Q13131
PSP
177SPhosphorylationKinasePRKAA2P54646
GPS
372SPhosphorylationKinaseMAPK1P28482
GPS
373TPhosphorylationKinaseMAPK1P28482
GPS
465SPhosphorylationKinasePKACAP17612
PSP
782SPhosphorylationKinaseCDK5Q00535
PSP
782SPhosphorylationKinasePKACAP17612
PSP
785SPhosphorylationKinaseCDK5Q00535
PSP
785SPhosphorylationKinasePKACAP17612
PSP
786SPhosphorylationKinaseCDK5Q00535
PSP
907YPhosphorylationKinaseMETP08581
PSP
-KUbiquitinationE3 ubiquitin ligaseCHFRQ96EP1
PMID:23268447
-KUbiquitinationE3 ubiquitin ligaseRNF4P78317
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseRNF146Q9NTX7
PMID:21825151

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARP1_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 PARP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
15044383
APTX_HUMANAPTXphysical
15044383
XRCC1_HUMANXRCC1physical
15044383
PCNA_HUMANPCNAphysical
12930846
CENPA_HUMANCENPAphysical
12011073
CENPB_HUMANCENPBphysical
12011073
BUB3_HUMANBUB3physical
12011073
TF65_HUMANRELAphysical
11590148
PARP2_HUMANPARP2physical
11948190
PARP2_MOUSEParp2physical
11948190
BCL2_HUMANBCL2physical
11790116
FOXO1_HUMANFOXO1physical
19281796
H11_HUMANHIST1H1Aphysical
17214964
PIAS4_HUMANPIAS4physical
19779455
MIC60_HUMANIMMTphysical
19762472
BAF_HUMANBANF1physical
19759913
HSP72_HUMANHSPA2physical
19607827
LZTR1_HUMANLZTR1physical
20211142
TRI29_HUMANTRIM29physical
20211142
ZBTB9_HUMANZBTB9physical
20211142
TOP2B_HUMANTOP2Bphysical
16794079
PRKDC_HUMANPRKDCphysical
16794079
XRCC5_HUMANXRCC5physical
16794079
XRCC6_HUMANXRCC6physical
16794079
SP16H_HUMANSUPT16Hphysical
16682447
CND1_HUMANNCAPD2physical
16543152
BUB1B_HUMANBUB1Bphysical
16449973
EP300_HUMANEP300physical
16204234
T2FA_HUMANGTF2F1physical
16204234
MED1_HUMANMED1physical
16204234
MED14_HUMANMED14physical
16204234
MED23_HUMANMED23physical
16204234
MED24_HUMANMED24physical
16204234
MED17_HUMANMED17physical
16204234
MED7_HUMANMED7physical
16204234
CDK8_HUMANCDK8physical
16204234
TR150_HUMANTHRAP3physical
16204234
MED6_HUMANMED6physical
16204234
TF65_HUMANRELAphysical
16204234
NFKB1_HUMANNFKB1physical
16204234
PARP1_HUMANPARP1physical
16204234
HDAC1_HUMANHDAC1physical
16204234
HDAC2_HUMANHDAC2physical
16204234
HDAC3_HUMANHDAC3physical
16204234
RARA_HUMANRARAphysical
15808511
THA_HUMANTHRAphysical
15808511
MED6_HUMANMED6physical
15808511
PARP1_HUMANPARP1physical
15737996
HIF1A_HUMANHIF1Aphysical
18314489
CARM1_HUMANCARM1physical
18280497
TF65_HUMANRELAphysical
18280497
EP300_HUMANEP300physical
18280497
ANM1_HUMANPRMT1physical
18280497
XRCC5_HUMANXRCC5physical
10400681
XRCC6_HUMANXRCC6physical
10400681
NFAC1_HUMANNFATC1physical
18078995
SP1_HUMANSP1physical
17961220
PARP1_HUMANPARP1physical
20388712
CDN1A_HUMANCDKN1Aphysical
20303835
PCNA_HUMANPCNAphysical
20303835
DPOLB_HUMANPOLBphysical
20303835
XRCC1_HUMANXRCC1physical
20303835
CDN1A_HUMANCDKN1Aphysical
20302655
PCNA_HUMANPCNAphysical
20302655
DPOLB_HUMANPOLBphysical
20302655
XRCC1_HUMANXRCC1physical
20302655
PARP3_HUMANPARP3physical
20064938
CTCF_HUMANCTCFphysical
20038529
KLF8_HUMANKLF8physical
21518760
APLF_HUMANAPLFphysical
17396150
XRCC1_HUMANXRCC1physical
12897160
XRCC6_HUMANXRCC6physical
17283121
XRCC5_HUMANXRCC5physical
17283121
TF7L2_HUMANTCF7L2physical
17283121
PARP1_HUMANPARP1physical
17283121
HES1_HUMANHES1physical
21224467
XRCC5_HUMANXRCC5physical
14734561
XRCC6_HUMANXRCC6physical
14734561
WRN_HUMANWRNphysical
14734561
PARP1_HUMANPARP1physical
14734561
XRCC6_HUMANXRCC6physical
16490787
XRCC5_HUMANXRCC5physical
16490787
PARP1_HUMANPARP1physical
22683995
CHFR_HUMANCHFRphysical
22337872
UBC9_HUMANUBE2Iphysical
9197546
NPM_MOUSENpm1physical
15615785
NFKB1_HUMANNFKB1physical
16799643
P53_HUMANTP53physical
12898523
ZN423_HUMANZNF423physical
22863007
E2F1_HUMANE2F1physical
14627987
P53_HUMANTP53physical
14627987
ERCC6_HUMANERCC6physical
16107709
RL19_HUMANRPL19physical
24140708
OSTP_HUMANSPP1physical
24140708
MAFG_HUMANMAFGphysical
24140708
MAFK_HUMANMAFKphysical
24140708
MAFF_HUMANMAFFphysical
24140708
ABL1_HUMANABL1physical
24140708
CETN2_HUMANCETN2physical
24140708
RL35_HUMANRPL35physical
24140708
CETN1_HUMANCETN1physical
24140708
RL27A_HUMANRPL27Aphysical
24140708
PHB_HUMANPHBphysical
24140708
RL14_HUMANRPL14physical
24140708
RS8_HUMANRPS8physical
24140708
XRCC5_HUMANXRCC5physical
24140708
TBB5_HUMANTUBBphysical
24140708
ATPA_HUMANATP5A1physical
24140708
DX39A_HUMANDDX39Aphysical
24140708
TBB1_HUMANTUBB1physical
24140708
DPOG2_HUMANPOLG2physical
24140708
XRCC6_HUMANXRCC6physical
24140708
PDLI7_HUMANPDLIM7physical
24140708
RD23A_HUMANRAD23Aphysical
24140708
HNRH1_HUMANHNRNPH1physical
24140708
UHRF1_HUMANUHRF1physical
24782312
RN146_RATRnf146physical
24842055
APLF_HUMANAPLFphysical
18172500
CHFR_HUMANCHFRphysical
18172500
DDB2_HUMANDDB2physical
23319653
PARP1_HUMANPARP1physical
22362888
SIR1_HUMANSIRT1physical
19470756
EP300_HUMANEP300physical
12960163
PARP1_HUMANPARP1physical
24636898
JUN_HUMANJUNphysical
24636898
EP300_HUMANEP300physical
24636898
CBP_HUMANCREBBPphysical
25306110
H1_YEASTHHO1genetic
25779917
HUL4_YEASTHUL4genetic
25779917
PO152_YEASTPOM152genetic
25779917
OTU1_YEASTOTU1genetic
25779917
SNT1_YEASTSNT1genetic
25779917
GAL3_YEASTGAL3genetic
25779917
KLF5_HUMANKLF5physical
17283079
PO2F1_HUMANPOU2F1physical
9537509
BLID_HUMANBLIDphysical
25640309
IL24_HUMANIL24physical
25640309
MTA3_HUMANMTA3physical
25640309
RSLAB_HUMANRASL10Bphysical
25640309
THRSP_HUMANTHRSPphysical
25640309
BRCA1_HUMANBRCA1physical
25252691
UIMC1_HUMANUIMC1physical
25252691
ABRX1_HUMANFAM175Aphysical
25252691
PARP1_HUMANPARP1physical
25673562
MACD1_HUMANMACROD1physical
25735744
NEMO_HUMANIKBKGphysical
25735744
DTX3L_HUMANDTX3Lphysical
23230272
PARP9_HUMANPARP9physical
23230272
HPF1_HUMANC4orf27physical
27067600
PARP1_HUMANPARP1physical
27067600
H15_HUMANHIST1H1Bphysical
27067600
H31T_HUMANHIST3H3physical
28190768
H15_HUMANHIST1H1Bphysical
28190768
PARP1_HUMANPARP1physical
28190768
HMGA1_HUMANHMGA1physical
28190768
HMGB1_HUMANHMGB1physical
28190768
HMGN1_HUMANHMGN1physical
28190768
HMGN2_HUMANHMGN2physical
28190768
HMGN4_HUMANHMGN4physical
28190768
H31_HUMANHIST1H3Aphysical
28190768
H33_HUMANH3F3Aphysical
28190768
H12_HUMANHIST1H1Cphysical
28190768
H10_HUMANH1F0physical
28190768
HIPK2_HUMANHIPK2physical
27787517
CHIP_HUMANSTUB1physical
27787517
RIR2_HUMANRRM2genetic
28319113
BRCA2_HUMANBRCA2genetic
27453043
BRCA1_HUMANBRCA1genetic
27453043

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 PARP1_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-97; LYS-105; LYS-131;LYS-600 AND LYS-621, 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-782, 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-41; THR-368 AND SER-782,AND MASS 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-179, AND MASSSPECTROMETRY.

TOP