PARP, PARP-1, dParp1, Poly-(ADP-ribose) polymerase, poly(ADP-ribose) polymerase
enzyme that attaches ADP-ribose moiety to histone - promotes chromatin silencing by regulating the localization and function of SIR2
Please see the JBrowse view of Dmel\Parp1 for information on other features
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AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.54
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.40
Gene model reviewed during 6.01
3.2 (northern blot)
There is only one protein coding transcript and one polypeptide associated with this gene
994 (aa)
994 (aa); 113 (kD)
A smaller Parp1 protein which is generated from an alternatively spliced mRNA lacks the auto-modification domain.
Interacts with coil/coilin and fib/fibrillarin, components of Cajal bodies and histone locus bodies; this interaction may be involved in recruitment of Cajal body components and maintaining Cajal body integrity (PubMed:19229318). Interacts with Iswi; the interaction is disrupted upon Parp1 activation, possibly due to Parp1-mediated ADP-ribosylation of Iswi and Parp1 (PubMed:18922045). Interacts with the kinase JIL-1; Parp1 is activated by JIL-1-mediated phosphorylation of histone H2Av on 'ser-138' and is required for JIL-1 mediated phosphorylation of histone H3 on 'Ser-11' (PubMed:24508391).
ADP-ribosylated at multiple sites, by autocatalysis (PubMed:31028139, PubMed:37268618). Some sites may only become modified in response to DNA damage (Probable). This modification is removed by Parg/Poly(ADP-ribose) glycohydrolase (PubMed:37268618). The poly(ADP-ribose) chains generated by Parp1 on itself and on other proteins may form a matrix for protein binding involved in formation of the nucleolus and other nuclear bodies (Probable). ADP-ribosylation interferes with DNA binding but not association with histones (PubMed:31028139).
Possesses an N-terminal domain consisting of 3 zinc-fingers (Probable). This domain is required for activation by DNA but not by nucleosomes (PubMed:21444826). The N-terminal PARP-Type zinc-finger domain is not required for the response to heat shock or to genotoxic stress-induced DNA damage (PubMed:20371698). This zinc-finger is not required for enzymatic activity (PubMed:20371698). This zinc-finger is not involved in general interaction with chromatin but is involved in determining the chromatin domain binding specificity; required for targeting to heterochromatin and repressing transcription of retrotransposable elements (PubMed:20371698). The 2 N-terminal PARP-type Zn-fingers associate non-site-specifically with DNA but are not required for specific localization to active chromatin (PubMed:31028139).
The automodification domain, containing several serines that are ADP-ribosylated by autocatalysis, is involved in localization to Cajal bodies (PubMed:31028139). ADP-ribosylation of the automodification domain interferes with DNA binding but not association with histones (PubMed:31028139).
The C-terminus comprising the WGR, PARP alpha-helical and PARP catalytic domains mediates association with histones (PubMed:31028139). The C-terminal PARP alpha-helical and PARP catalytic domains are sufficient for DNA-independent Parp1 catalytic activity (PubMed:31028139). Together with the WGR domain they are also sufficient for transcriptional activation and chromosome remodeling at the Hsp70 locus in response to heat shock (at reduced efficiency) (PubMed:31028139).
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Parp1 using the Feature Mapper tool.
The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).
Comment: maternally deposited
JBrowse - Visual display of RNA-Seq signals
View Dmel\Parp1 in JBrowsePlease Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see JBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Sequence of transcript(s) changed in r6 genomic release relative to r5 release.
Parp is required to produce normal-sized polytene chromosome puffs and normal amounts of Hsp70 protein after heat exposure.
Overexpression of Parp disrupts the organisation of the F-actin cytoskeleton, resulting in aberrant cell and tissue morphology.
The genomic organisation of the Parp locus and its expression pattern during development have been analysed.
PARP protein is processed in S2 cells treated with etoposide to induce apoptosis.
Amino acid sequence of Parp cDNA has been compared between different species with an emphasis on conservation of functional elements and expression during development.
Full length cDNA clones for Drosophila poly(ADP-ribose) polymerase isolated using a probe made by PCR with primers deduced from sequence in mammal, chicken, fish and amphibian species.
Source for merge of: Parp BEST:LD21673
Source for merge of: Parp CG17696 CG17685
Source for merge of: Parp CG17696
Source for merge of: CG17718, CG17696, CG17685
Annotations CG17718, CG17696 and CG17685 merged as CG40411 in release 3 of the genome annotation.
Source for identity of: Parp1 Parp
Changed symbol from 'Parp' to 'Parp1' to: acknowledge there is at least one other Parp gene in the genome (Parp16); reflect the nomenclature of the vertebrate ortholog; and reflect usage in many publications on the gene.