PARG_DROME - dbPTM
PARG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARG_DROME
UniProt AC O46043
Protein Name Poly(ADP-ribose) glycohydrolase
Gene Name Parg
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 723
Subcellular Localization
Protein Description Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism is required for maintenance of the normal function of neuronal cells..
Protein Sequence MSKSPDGGISEIETEEEPENLANSLDDSWRGVSMEAIHRNRQPFELENLPPVTAGNLHRVMYQLPIRETPPRPYKSPGKWDSEHVRLPCAPESKYPRENPDGSTTIDFRWEMIERALLQPIKTCEELQAAIISYNTTYRDQWHFRALHQLLDEELDESETRVFFEDLLPRIIRLALRLPDLIQSPVPLLKHHKNASLSLSQQQISCLLANAFLCTFPRRNTLKRKSEYSTFPDINFNRLYQSTGPAVLEKLKCIMHYFRRVCPTERDASNVPTGVVTFVRRSGLPEHLIDWSQSAAPLGDVPLHVDAEGTIEDEGIGLLQVDFANKYLGGGVLGHGCVQEEIRFVICPELLVGKLFTECLRPFEALVMLGAERYSNYTGYAGSFEWSGNFEDSTPRDSSGRRQTAIVAIDALHFAQSHHQYREDLMERELNKAYIGFVHWMVTPPPGVATGNWGCGAFGGDSYLKALLQLMVCAQLGRPLAYYTFGNVEFRDDFHEMWLLFRNDGTTVQQLWSILRSYSRLIKEKSSKEPRENKASKKKLYDFIKEELKKVRDVPGEGASAEAGSSRVAGLGEGKSETSAKSSPELNKQPARPQITITQQSTDLLPAQLSQDNSNSSEDQALLMLSDDEEANAMMEAASLEAKSSVEISNSSTTSKTSSTATKSMGSGGRQLSLLEMLDTHYEKGSASKRPRKSPNCSKAEGSAKSRKEIDVTDKDEKDDIVD
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
24PhosphorylationEPENLANSLDDSWRG
CHHHHHHHCCCCCCC
38.0222817900
28PhosphorylationLANSLDDSWRGVSME
HHHHCCCCCCCCCHH
11.5922817900
69PhosphorylationYQLPIRETPPRPYKS
EECCCCCCCCCCCCC
27.8018327897
73PhosphorylationIRETPPRPYKSPGKW
CCCCCCCCCCCCCCC
20.5218327897
579PhosphorylationGEGKSETSAKSSPEL
CCCCCCCCCCCCCCH
49.6522817900
582PhosphorylationKSETSAKSSPELNKQ
CCCCCCCCCCCHHCC
59.8022817900
583PhosphorylationSETSAKSSPELNKQP
CCCCCCCCCCHHCCC
45.5822817900
624PhosphorylationSEDQALLMLSDDEEA
CHHHEEEECCCHHHH
29.6418327897
627PhosphorylationQALLMLSDDEEANAM
HEEEECCCHHHHHHH
51.3318327897
628PhosphorylationALLMLSDDEEANAMM
EEEECCCHHHHHHHH
22.9918327897
673PhosphorylationGSGGRQLSLLEMLDT
CCCCHHHHHHHHHHH
52.8619429919

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 PARG_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARG_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 PARG_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CADE_DROMEshggenetic
22453833
PARP_DROMEParpgenetic
16219773

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-73; SER-624;SER-627 AND SER-628, AND MASS SPECTROMETRY.

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