PIWI_DROME - dbPTM
PIWI_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIWI_DROME
UniProt AC Q9VKM1
Protein Name Protein piwi
Gene Name piwi
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 843
Subcellular Localization Cytoplasm. Nucleus, nucleoplasm. Component of polar granules. Present in the cytoplasm of the developing oocyte. At the mitotic cycle 11 translocates to the nucleus where it remains localized throughout germ-cell development and gonadogenesis. Locali
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. In ovarian somatic cells, mediates silencing of transposable elements at the transcriptional level in a mael-dependent manner. In germ cells, mediates silencing at both transcriptional and post-transcriptional levels and is involved in the maintenance of populations of primary and secondary piRNAs. Piwi-mediated transcriptional silencing is accompanied by the formation of His3 'Lys-9' trimethylated (H3K9me3) euchromatin and heterochromatin. In ovary, associates predominantly with antisense piRNAs that contain uridine at their 5' end. Association with sense piRNAs is also observed but to a lesser extent. Involved in silencing of long terminal repeat (LTR) retrotransposons in male germline. Mediates a somatic signaling mechanism required for the maintenance of germline stem cells to produce and maintain a daughter germline stem cell. It is not essential for the further differentiation of the committed daughter cell. Acts cell autonomously to promote germline stem cell division. Its role in stem cell maintenance does not seem to require nuclear localization. Required maternally for the posterior localization of osk and vas and for pole cell formation during oogenesis and early embryogenesis. Together with Hop and Hsp83, mediates canalization, also known as developmental robustness, likely via epigenetic silencing of existing genetic variants and suppression of transposon-induced new genetic variation. Shows RNA cleavage activity, although is not required for any of its known functions..
Protein Sequence MADDQGRGRRRPLNEDDSSTSRGSGDGPRVKVFRGSSSGDPRADPRIEASRERRALEEAPRREGGPTERKPWGDQYDYLNTRPAELVSKKGTDGVPVMLQTNFFRLKTKPEWRIVHYHVEFEPSIENPRVRMGVLSNHANLLGSGYLFDGLQLFTTRKFEQEITVLSGKSKLDIEYKISIKFVGFISCAEPRFLQVLNLILRRSMKGLNLELVGRNLFDPRAKIEIREFKMELWPGYETSIRQHEKDILLGTEITHKVMRTETIYDIMRRCSHNPARHQDEVRVNVLDLIVLTDYNNRTYRINDVDFGQTPKSTFSCKGRDISFVEYYLTKYNIRIRDHNQPLLISKNRDKALKTNASELVVLIPELCRVTGLNAEMRSNFQLMRAMSSYTRMNPKQRTDRLRAFNHRLQNTPESVKVLRDWNMELDKNVTEVQGRIIGQQNIVFHNGKVPAGENADWQRHFRDQRMLTTPSDGLDRWAVIAPQRNSHELRTLLDSLYRAASGMGLRIRSPQEFIIYDDRTGTYVRAMDDCVRSDPKLILCLVPNDNAERYSSIKKRGYVDRAVPTQVVTLKTTKNRSLMSIATKIAIQLNCKLGYTPWMIELPLSGLMTIGFDIAKSTRDRKRAYGALIASMDLQQNSTYFSTVTECSAFDVLANTLWPMIAKALRQYQHEHRKLPSRIVFYRDGVSSGSLKQLFEFEVKDIIEKLKTEYARVQLSPPQLAYIVVTRSMNTRFFLNGQNPPPGTIVDDVITLPERYDFYLVSQQVRQGTVSPTSYNVLYSSMGLSPEKMQKLTYKMCHLYYNWSGTTRVPAVCQYAKKLATLVGTNLHSIPQNALEKKFYYL
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
7Methylation-MADDQGRGRRRPLN
-CCCCCCCCCCCCCC
29.7929531043
9MethylationADDQGRGRRRPLNED
CCCCCCCCCCCCCCC
30.0329531043
10MethylationDDQGRGRRRPLNEDD
CCCCCCCCCCCCCCC
47.6029531043
11MethylationDQGRGRRRPLNEDDS
CCCCCCCCCCCCCCC
38.4029531043
67PhosphorylationPRREGGPTERKPWGD
CCCCCCCCCCCCCCC
52.2619429919
510PhosphorylationGMGLRIRSPQEFIIY
CCCCEECCCCEEEEE
28.6718511481
517PhosphorylationSPQEFIIYDDRTGTY
CCCEEEEEECCCCCE
13.6318511481

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 PIWI_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIWI_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 PIWI_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARNT_DROMEtgogenetic
14704180
HH_DROMEhhgenetic
11463375
RS3_DROMERpS3genetic
14704180
S39AD_DROMEZip99Cgenetic
14704180
SRYD_DROMESry-deltagenetic
14704180
SIMA_DROMEsimagenetic
14704180
HP1_DROMESu(var)205physical
17875665
ESC_DROMEescphysical
26780607
MUT7_DROMENbrphysical
26718004
FMR1_DROMEFmr1physical
16949822
FMR1_DROMEFmr1physical
26842990
FOSLD_DROMEkayphysical
27622269
FOSLA_DROMEkayphysical
27622269
ARMI_DROMEarmiphysical
20818334
ARMI_DROMEarmiphysical
20966047
EZ_DROMEE(z)physical
26780607
CORTO_DROMEcortophysical
26780607
DCR1_DROMEDcr-1physical
16949822
SUZ12_DROMESu(z)12physical
26780607

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

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Related Literatures of Post-Translational Modification

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