| General Information |
| MoonProt ID | 482 |
| First appeared in release | 3.0 |
| Name(s) | Poly [ADP-ribose] polymerase 1; PARP1 |
| UniProt ID | P09874 (PARP1_HUMAN) |
| GO terms | GO:2001170 negative regulation of ATP biosynthetic process
GO:0001228 DNA-binding transcription activator activity
GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0005730 nucleolus
GO:1990404 protein ADP-ribosylase activity
GO:0003950 NAD+ ADP-ribosyltransferase activity
GO:0006302 double-strand break repair
GO:0070212 protein poly-ADP-ribosylation
GO:0140294 NAD DNA ADP-ribosyltransferase activity
GO:0070213 protein auto-ADP-ribosylation
GO:0003950 NAD+ ADP-ribosyltransferase activity
GO:0035861 site of double-strand break
GO:0003950 NAD+ ADP-ribosyltransferase activity
GO:0035861 site of double-strand break
GO:1990966 ATP generation from poly-ADP-D-ribose
GO:0018424 peptidyl-glutamic acid poly-ADP-ribosylation
GO:1905168 positive regulation of double-strand break repair via homologous recombination |
| Organisms for which functions have been demonstrated | Homo sapiens (Human) |
| Sequence length | 1014 amino acids |
| FASTA sequence | >sp|P09874|PARP1_HUMAN Poly [ADP-ribose] polymerase 1 OS=Homo sapiens OX=9606 GN=PARP1 PE=1 SV=4
MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW |
| Structure Information |
| PDB ID | 1UK0, chain A/B, aa 662-1011; 1UK1, chain A/B, aa 662-1011 |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
sp_P09874_PARP1_HUMAN_Po is 999 residues long, with 144 residues (14.41 %) predicted as disordered. The protein has 2 short (< 30 residues) disorder segments and 3 long (>= 30 residues) disorder segments.
Segment 1 - Short (< 30 residues) disordered segment
Segment is located between positions 1 and 5 in the sequence.
The segment is 5 residues long (0.50 % of the total sequence length).
Segment 2 - Short (< 30 residues) disordered segment
Segment is located between positions 94 and 107 in the sequence.
The segment is 14 residues long (1.40 % of the total sequence length).
Segment 3 - Long (>= 30 residues) disordered segment
Segment is located between positions 196 and 241 in the sequence.
The segment is 46 residues long (4.60 % of the total sequence length).
Segment 4 - Long (>= 30 residues) disordered segment
Segment is located between positions 357 and 386 in the sequence.
The segment is 30 residues long (3.00 % of the total sequence length).
Segment 5 - Long (>= 30 residues) disordered segment
Segment is located between positions 483 and 531 in the sequence.
The segment is 49 residues long (4.90 % of the total sequence length). |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | poly[ADP-ribose]polymerase 1 |
| References for function | de Murcia G, De Murcia JM. Poly (ADP-ribose) polymerase. A molecular nick sensor. Trends Biochem Sci. 1994;19:172-6. |
| E.C. number | |
| Location of functional site(s) | Active sites: Gln763, Gly863, Tyr889, Tyr869, Lys903, Ser904, Tyr907
Skalitzky DJ, Marakovits JT, Maegley KA, Ekker A, Yu XH, Hostomsky Z, Webber SE, Eastman BW, Almassy R, Li J, Curtin NJ. Tricyclic benzimidazoles as potent poly (ADP-ribose) polymerase-1 inhibitors. Journal of medicinal chemistry. 2003 Jan 16;46(2):210-3. |
| Cellular location of function | nucleus |
| Comments | |
| Function 2 |
| Function description | Transcription factor |
| References for function | Langelier MF, Ruhl DD, Planck JL, Kraus WL, Pascal JM. The Zn3 domain of human poly (ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly (ADP-ribose) synthesis activity and chromatin compaction. Journal of biological chemistry. 2010 Jun 11;285(24):18877-87. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | nucleus |
| Comments | With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription |