Table 2. ADP-ribosylation sites identified by mass spectrometry analysis of automodified PARPs.
For the peptides highlighted in grey the MS/MS spectra do not contain enough information to distinguish between ADP-ribosylation on the internal residue from the modification on the peptide N-terminus
| Protein | Amino acid | Position | Peptide sequence |
|---|---|---|---|
| PARP3 (540 aa) | Glu | 19 | _PKPWVQTE(ad)GPEK_ |
| Glu | 22 | _PKPWVQTEGPE(ad)K_ | |
| Glu | 33 | _QAGREE(ad)DPFR_ | |
| Glu | 41 | _STAE(ad)ALK_ | |
| Glu | 170 | _YTLIEVQAEDEAQE(ad)AVVK_ | |
| Glu | 238 | _GFE(ad)ALEALEEALK_ | |
| Glu | 316 | _TVE(ad)EVPHPLDR_ | |
| Glu | 317 | _TVEE(ad)VPHPLDR_ | |
| Glu | 351 | _VIQTYLE(ad)QTGSNHR_ | |
| Glu | 456 | _E(ad)HHINTDNPSLK_ | |
| Asp | 148 | _D(ad)HFVSHPGK_ | |
| Asp | 217 | _NTMALMD(ad)LDVK_ | |
| Lys | 13 | _PK(ad)PWVQTEGPEK_ | |
| Lys | 44 | _STAEALK(ad)AIPAEK_ | |
| PARP6 (630 aa) | Asp | 600 | _FFFVYED(ad)GQVGDANINTQDPK_ |
| Cys | 237 | _VEVFGYPPSPQAGLLC(ad)PQHVGLPPPAR_ | |
| PARP8 (854 aa) | Cys | 332 | _TDDVC(ad)VTK_ |
| Cys | 367 | _LLNRPC(ad)PAAVK_ | |
| Cys | 376 | _SEEC(ad)LTLK_ | |
| Cys | 395 | _C(ad)EHNTNLKPHK_ | |
| PARP10 (1025 aa) | Glu | 106 | _LE(ad)QHVQALLR_ |
| Lys | 140 | _ALVQLPK(ad)PLSEADVR_ | |
| Lys | 916 | _NATVYGK(ad)_ | |
| PARP11 (331 aa) | Glu | 6 | _AE(ad)ELFSK_ |
| Asp | 80 | _ID(ad)FAEMK_ | |
| Cys | 49 | _WHMFQPDTNSQC(ad)SVSSEDIEK_ | |
| Cys | 65 | _TNPC(ad)GSISFTTSK_ | |
| Lys | 11 | _AEELFSK(ad)_ | |
| PARP12 (701 aa) | Asp | 600 | _D(ad)AAYSHHYSK_ |
| Asp | 611 | _SD(ad)TQTHTMFLAR_ | |
| Cys | 474 | _YVSPQDVTTMQTC(ad)NTK_ | |
| Cys | 584 | _VC(ad)GVHGTSYGK_ | |
| PARP16 (322 aa) | Glu | 77 | _E(ad)LLQSSGDNHKR_ |
| Asp | 37 | _D(ad)SVLRPFPASYAR_ | |
| Lys | 110 | _IQK(ad)LTGAPHTPVPAPDFLFEIEYFDPANAK | |
| Lys | 137 | _LTGAPHTPVPAPDFLFEIEYFDPANAK(ad)_ |