AGO3_DROME - dbPTM
AGO3_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGO3_DROME
UniProt AC Q7PLK0
Protein Name Protein argonaute-3 {ECO:0000312|EMBL:EAA45981.3}
Gene Name AGO3
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 867
Subcellular Localization Cytoplasm . Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Also found in prominent but discrete foci in the germarium. Unlike other nuage components, does n
Protein Description Acts via the piwi-interacting RNA (piRNA) metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Associates predominantly with sense piRNAs that contain adenine at nucleotide 10, but shows no preference for uridine at the 5' end. In testis, however, associates with Su(Ste) and AT-chX-1 piRNAs mostly produced from antisense precursors. Shows RNA cleavage activity. In the germline, acts to amplify pools of antisense piRNAs, among others Su(Ste), AT-chX-1 and roo, and to limit sense piRNA accumulation. Forms a complex with smg, twin, aub and specific piRNAs that targets nos mRNA (and probably other maternal mRNAS) for deadenylation promoting its decay during early embryogenesis. Involved in transposon silencing in the adult brain..
Protein Sequence MSGRGNLLSLFNKNAGNMGKSISSKDHEIDSGLDFNNSESSGERLLSSHNIETDLITTLQHVNISVGRGRARLIDTLKTDDHTSNQFITSESKENITKKTKGPESEAIASENGLFFPDLIYGSKGSSVNIYCNYLKLTTDESKGVFNYEVRFFPPIDSVHLRIKYLNDHKDKLGGTKTFDGNTLYLPILLPNKMTVFISKAEDVELQIRILYKKKEEMRNCTQLYNILFDRVMKVLNYVKFDRKQFDPSRPKIIPLAKLEVWPGYVTAVDEYKGGLMLCCDVSHRILCQKTVLEMLVDLYQQNVEHYQESARKMLVGNIVLTRYNNRTYKINDICFDQNPTCQFEIKTGCTSYVEYYKQYHNINIKDVNQPLIYSIKKSRGIPAERENLQFCLIPELCYLTGLRDEVRSDNKLMREIATFTRVSPNQRQMALNKFYENVSNTPAAQEILNSWGLSLTNNSNKISGRQMDIEQIYFSKISVSAGRSAEFSKHAVTNEMLKVVHLSKWIIIHLRNYRQAATSLLDNMKQACESLGMNISNPTMISLDHDRIDAYIQALRRNITMNTQMVVCICHNRRDDRYAAIKKICCSEIPIPSQVINAKTLQNDLKIRSVVQKIVLQMNCKLGGSLWTVKIPFKNVMICGIDSYHDPSNRGNSVAAFVASINSSYSQWYSKAVVQTKREEIVNGLSASFEIALKMYRKRNGKLPTNIIIYRDGIGDGQLYTCLNYEIPQFEMVCGNRIKISYIVVQKRINTRIFSGSGIHLENPLPGTVVDQHITKSNMYDFFLVSQLVRQGTVTPTHYVVLRDDCNYGPDIIQKLSYKLCFLYYNWAGTVRIPACCMYAHKLAYLIGQSIQRDVAEALSEKLFYL
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
4Methylation----MSGRGNLLSLF
----CCCCCCHHHHH
19959991
68MethylationHVNISVGRGRARLID
ECCEEECCCCCEEEE
19959991
70MethylationNISVGRGRARLIDTL
CEEECCCCCEEEEEC
19959991

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 AGO3_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGO3_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 AGO3_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_DROMETER94physical
21447556
TUD_DROMEtudphysical
26212455
ARMI_DROMEarmiphysical
25049272

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGO3_DROME

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Related Literatures of Post-Translational Modification

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