Protein Information

General Information
MoonProt ID482
First appeared in release3.0
Name(s)Poly [ADP-ribose] polymerase 1; PARP1
UniProt IDP09874 (PARP1_HUMAN)
GO termsGO: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 demonstratedHomo sapiens (Human)
Sequence length1014 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 ID1UK0, chain A/B, aa 662-1011; 1UK1, chain A/B, aa 662-1011
Quaternary structureNA
SCOP
CATH
TM Helix Predictionno TM helices
DisProt Annotation
Predicted Disorder RegionsPredicted disorder at N terminus (aa 1-7), and middle region (aa 88-100, 140-142, 198-212, 215-219, 359-382, 502-531, 946-955)
Connections to Disease
OMIM ID
Function 1
Function descriptionpoly[ADP-ribose]polymerase 1
References for functionde Murcia G, De Murcia JM. Poly (ADP-ribose) polymerase. A molecular nick sensor. Trends Biochem Sci. 1994;19:172-6.
E.C. number2.4.2.30
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 functionnucleus
Comments
Function 2
Function descriptionTranscription factor
References for functionLangelier 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 functionnucleus
CommentsWith 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