| General Information |
| MoonProt ID | 483 |
| First appeared in release | 3.0 |
| Name(s) | Poly [ADP-ribose] polymerase 1; PARP1 |
| UniProt ID | P11103 (PARP1_MOUSE) |
| GO terms | GO:0005730 nucleolus
GO:1990404 protein ADP-ribosylase activity
GO:0003950 NAD+ ADP-ribosyltransferase activity
GO:0005634 nucleus
GO:0006302 double-strand break repair
GO:0070213 protein auto-ADP-ribosylation
GO:0010613 positive regulation of cardiac muscle hypertrophy
GO:1905168 positive regulation of double-strand break repair via homologous recombination P
GO:0030592 DNA ADP-ribosylation
GO:0018424 peptidyl-glutamic acid poly-ADP-ribosylation
GO:0006974 cellular response to DNA damage stimulus
GO:1990966 ATP generation from poly-ADP-D-ribose
GO:0006302 double-strand break repair
GO:0018312 peptidyl-serine ADP-ribosylation
GO:0006471 protein ADP-ribosylation
GO:0008270 zinc ion binding
GO:0003677 DNA binding |
| Organisms for which functions have been demonstrated | Mus musculus |
| Sequence length | 1013 amino acids |
| FASTA sequence | >sp|P11103|PARP1_MOUSE Poly [ADP-ribose] polymerase 1 OS=Mus musculus OX=10090 GN=Parp1 PE=1 SV=3
MAEASERLYRVQYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGQSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQDGSGGKAEKTLGDFAAEYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQLGMIDRWYHPTCFVKKRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAIKNEGKRKGDEVDGTDEVAKKKSRKETDKYSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKEWVTPKEFREISYLKKLKVKKQDRIFPPESSAPITVHWPLSVTSAPTAVNSSAPADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCISIKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQDLLSAHSLSPWGAEVKAEPGEVVAPRGKSAAPSKKSKGCFKEEGVNKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRLGTVIGSNKLEQMPSKEEAVEQFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVKPGTKSKLPKPVQELVGMIFDVDSMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQPVSQGSSESQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLIMLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSASITLEGVEVPLGTGIPSGVNDTALLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices
# sp|P11103|PARP1_MOUSE Number of predicted TMHs: 0
# sp|P11103|PARP1_MOUSE Exp number of AAs in TMHs: 0.00921999999999999999
# sp|P11103|PARP1_MOUSE Exp number, first 60 AAs: 0.00023
# sp|P11103|PARP1_MOUSE Total prob of N-in: 0.00002
sp|P11103|PARP1_MOUSE TMHMM2.0 outside 1 1013 |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
sp_P11103_PARP1_MOUSE_Po is 999 residues long, with 161 residues (16.12 %) predicted as disordered. The protein has 4 short (< 30 residues) disorder segments and 2 long (>= 30 residues) disorder segments.
Segment 1 - Short (< 30 residues) disordered segment
Segment is located between positions 1 and 9 in the sequence.
The segment is 9 residues long (0.90 % of the total sequence length).
Segment 2 - Short (< 30 residues) disordered segment
Segment is located between positions 92 and 108 in the sequence.
The segment is 17 residues long (1.70 % of the total sequence length).
Segment 3 - Long (>= 30 residues) disordered segment
Segment is located between positions 197 and 240 in the sequence.
The segment is 44 residues long (4.40 % of the total sequence length).
Segment 4 - Short (< 30 residues) disordered segment
Segment is located between positions 363 and 385 in the sequence.
The segment is 23 residues long (2.30 % of the total sequence length).
Segment 5 - Long (>= 30 residues) disordered segment
Segment is located between positions 476 and 532 in the sequence.
The segment is 57 residues long (5.71 % of the total sequence length).
Segment 6 - Short (< 30 residues) disordered segment
Segment is located between positions 651 and 661 in the sequence.
The segment is 11 residues long (1.10 % 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 | 2.4.2.30 |
| 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 |