PARP_DROME - dbPTM
PARP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARP_DROME
UniProt AC P35875
Protein Name Poly [ADP-ribose] polymerase
Gene Name Parp
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 994
Subcellular Localization Nucleus . Nucleus, nucleolus . Highly enriched in nucleoli, heterochromatic chromosomal regions, and diverse euchromatic sites in the cells of most embryonic and adult tissues.
Protein Description Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. Plays a fundamental role in organizing chromatin on a global scale; isoform e autoregulates Parp transcription by influencing the chromatin structure of its heterochromatic environment..
Protein Sequence MDIELPYLAEYARTGRATCKGCKSTISKDTLRIAVMVQSAFHDAKVPNWFHKTCFFKNQRPSSVGDIQNIGNLRFADQKELTDLVENIQEVISAQLGKKRSKAFNLALKDFGIEYAKSSRSTCRGCEQKINKDLVRLRKTVYDTEVGMKYGGQPLWHHLECFAQLRSELGWFASGEDMPGFQSLADDDQAKVKNAIPPIKSEELPDTKRAKMELSDTNEEGEKKQRLKDQNDAYFRFRDDIKNKMKKKDIDILLKFNNQQPVTGDTEKLFDQTADLLTFGAIESCSECNSCQFIVNKSGYICNGNHSEWTKCNKLLKEPTRSACIVPKELKALYNFLNTVKEIPSTRIFNNFPPNKSTFSRSLLKTNKNNDVLVRPTIPRISPPLYNLKFSIIGLKNQHKELRKRIENLGGKFEVKISENTIAIISTELEIQKKSTRMKFAEELGIHIVPIEFLDFVEADTEGAIKYINSTCICSWGTDPKSRIPKETTKSLNSNSIYTKSMPVSRTFKVKDGLAVDPDSGLEDIAHVYVDSNNKYSVVLGLTDIQRNKNSYYKVQLLKADKKEKYWIFRSWGRIGTNIGNSKLEEFDTSESAKRNFKEIYADKTGNEYEQRDNFVKRTGRMYPIEIQYDDDQKLVKHESHFFTSKLEISVQNLIKLIFDIDSMNKTLMEFHIDMDKMPLGKLSAHQIQSAYRVVKEIYNVLECGSNTAKLIDATNRFYTLIPHNFGVQLPTLIETHQQIEDLRQMLDSLAEIEVAYSIIKSEDVSDACNPLDNHYAQIKTQLVALDKNSEEFSILSQYVKNTHASTHKSYDLKIVDVFKVSRQGEARRFKPFKKLHNRKLLWHGSRLTNFVGILSHGLRIAPPEAPPTGYMFGKGIYFADMVSKSANYCCTSQQNSTGLMLLSEVALGDMMECTSAKYINKLSNNKHSCFGRGRTMPDPTKSYIRSDGVEIPYGETITDEHLKSSLLYNEYIVYDVAQVNIQYLFRMEFKYSY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster

Oops, there are no PTM records of PARP_DROME !!

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PARP_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARP_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PARP_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SQD_DROMEsqdphysical
19346337
ROA1_DROMEHrb98DEphysical
19346337
FBP1_DROMEFbp1physical
17827147
PARP_DROMEParpphysical
17827147
PARG_DROMEPargphysical
17827147
KARG_DROMEArgkphysical
17827147
ROA1_DROMEHrb98DEphysical
17827147
G3P1_DROMEGapdh1physical
17827147
RL22_DROMERpL22physical
17827147
RS4_DROMERpS4physical
17827147
RS6_DROMERpS6physical
17827147
RL18A_DROMERpL18Aphysical
17827147
RL14_DROMERpL14physical
17827147
RS13_DROMERpS13physical
17827147
H2AV_DROMEHis2Avphysical
17827147
KU70_DROMEIrbpphysical
22036573
RFC2_DROMERfC4physical
22036573
PARG_DROMEParggenetic
20371698

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PARP_DROME

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Related Literatures of Post-Translational Modification

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