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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
24 | Phosphorylation | EPENLANSLDDSWRG CHHHHHHHCCCCCCC | 38.02 | 22817900 | |
28 | Phosphorylation | LANSLDDSWRGVSME HHHHCCCCCCCCCHH | 11.59 | 22817900 | |
69 | Phosphorylation | YQLPIRETPPRPYKS EECCCCCCCCCCCCC | 27.80 | 18327897 | |
73 | Phosphorylation | IRETPPRPYKSPGKW CCCCCCCCCCCCCCC | 20.52 | 18327897 | |
579 | Phosphorylation | GEGKSETSAKSSPEL CCCCCCCCCCCCCCH | 49.65 | 22817900 | |
582 | Phosphorylation | KSETSAKSSPELNKQ CCCCCCCCCCCHHCC | 59.80 | 22817900 | |
583 | Phosphorylation | SETSAKSSPELNKQP CCCCCCCCCCHHCCC | 45.58 | 22817900 | |
624 | Phosphorylation | SEDQALLMLSDDEEA CHHHEEEECCCHHHH | 29.64 | 18327897 | |
627 | Phosphorylation | QALLMLSDDEEANAM HEEEECCCHHHHHHH | 51.33 | 18327897 | |
628 | Phosphorylation | ALLMLSDDEEANAMM EEEECCCHHHHHHHH | 22.99 | 18327897 | |
673 | Phosphorylation | GSGGRQLSLLEMLDT CCCCHHHHHHHHHHH | 52.86 | 19429919 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PARG_DROME !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CADE_DROME | shg | genetic | 22453833 | |
PARP_DROME | Parp | genetic | 16219773 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |