UniProt ID | DCR1_DROME | |
---|---|---|
UniProt AC | Q9VCU9 | |
Protein Name | Endoribonuclease Dcr-1 | |
Gene Name | Dcr-1 {ECO:0000312|EMBL:AAF56056.1} | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 2249 | |
Subcellular Localization | ||
Protein Description | Essential for RNA interference (RNAi); double-stranded RNA (dsRNA) induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger. May carry out the initiation step of RNAi by cleaving dsRNA to produce 22 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs. During embryogenesis, involved in germline fate determination.. | |
Protein Sequence | MAFHWCDNNLHTTVFTPRDFQVELLATAYERNTIICLGHRSSKEFIALKLLQELSRRARRHGRVSVYLSCEVGTSTEPCSIYTMLTHLTDLRVWQEQPDMQIPFDHCWTDYHVSILRPEGFLYLLETRELLLSSVELIVLEDCHDSAVYQRIRPLFENHIMPAPPADRPRILGLAGPLHSAGCELQQLSAMLATLEQSVLCQIETASDIVTVLRYCSRPHEYIVQCAPFEMDELSLVLADVLNTHKSFLLDHRYDPYEIYGTDQFMDELKDIPDPKVDPLNVINSLLVVLHEMGPWCTQRAAHHFYQCNEKLKVKTPHERHYLLYCLVSTALIQLYSLCEHAFHRHLGSGSDSRQTIERYSSPKVRRLLQTLRCFKPEEVHTQADGLRRMRHQVDQADFNRLSHTLESKCRMVDQMDQPPTETRALVATLEQILHTTEDRQTNRSAARVTPTPTPAHAKPKPSSGANTAQPRTRRRVYTRRHHRDHNDGSDTLCALIYCNQNHTARVLFELLAEISRRDPDLKFLRCQYTTDRVADPTTEPKEAELEHRRQEEVLKRFRMHDCNVLIGTSVLEEGIDVPKCNLVVRWDPPTTYRSYVQCKGRARAAPAYHVILVAPSYKSPTVGSVQLTDRSHRYICATGDTTEADSDSDDSAMPNSSGSDPYTFGTARGTVKILNPEVFSKQPPTACDIKLQEIQDELPAAAQLDTSNSSDEAVSMSNTSPSESSTEQKSRRFQCELSSLTEPEDTSDTTAEIDTAHSLASTTKDLVHQMAQYREIEQMLLSKCANTEPPEQEQSEAERFSACLAAYRPKPHLLTGASVDLGSAIALVNKYCARLPSDTFTKLTALWRCTRNERAGVTLFQYTLRLPINSPLKHDIVGLPMPTQTLARRLAALQACVELHRIGELDDQLQPIGKEGFRALEPDWECFELEPEDEQIVQLSDEPRPGTTKRRQYYYKRIASEFCDCRPVAGAPCYLYFIQLTLQCPIPEEQNTRGRKIYPPEDAQQGFGILTTKRIPKLSAFSIFTRSGEVKVSLELAKERVILTSEQIVCINGFLNYTFTNVLRLQKFLMLFDPDSTENCVFIVPTVKAPAGGKHIDWQFLELIQANGNTMPRAVPDEERQAQPFDPQRFQDAVVMPWYRNQDQPQYFYVAEICPHLSPLSCFPGDNYRTFKHYYLVKYGLTIQNTSQPLLDVDHTSARLNFLTPRYVNRKGVALPTSSEETKRAKRENLEQKQILVPELCTVHPFPASLWRTAVCLPCILYRINGLLLADDIRKQVSADLGLGRQQIEDEDFEWPMLDFGWSLSEVLKKSRESKQKESLKDDTINGKDLADVEKKPTSEETQLDKDSKDDKVEKSAIELIIEGEEKLQEADDFIEIGTWSNDMADDIASFNQEDDDEDDAFHLPVLPANVKFCDQQTRYGSPTFWDVSNGESGFKGPKSSQNKQGGKGKAKGPAKPTFNYYDSDNSLGSSYDDDDNAGPLNYMHHNYSSDDDDVADDIDAGRIAFTSKNEAETIETAQEVEKRQKQLSIIQATNANERQYQQTKNLLIGFNFKHEDQKEPATIRYEESIAKLKTEIESGGMLVPHDQQLVLKRSDAAEAQVAKVSMMELLKQLLPYVNEDVLAKKLGDRRELLLSDLVELNADWVARHEQETYNVMGCGDSFDNYNDHHRLNLDEKQLKLQYERIEIEPPTSTKAITSAILPAGFSFDRQPDLVGHPGPSPSIILQALTMSNANDGINLERLETIGDSFLKYAITTYLYITYENVHEGKLSHLRSKQVANLNLYRLGRRKRLGEYMIATKFEPHDNWLPPCYYVPKELEKALIEAKIPTHHWKLADLLDIKNLSSVQICEMVREKADALGLEQNGGAQNGQLDDSNDSCNDFSCFIPYNLVSQHSIPDKSIADCVEALIGAYLIECGPRGALLFMAWLGVRVLPITRQLDGGNQEQRIPGSTKPNAENVVTVYGAWPTPRSPLLHFAPNATEELDQLLSGFEEFEESLGYKFRDRSYLLQAMTHASYTPNRLTDCYQRLEFLGDAVLDYLITRHLYEDPRQHSPGALTDLRSALVNNTIFASLAVRHGFHKFFRHLSPGLNDVIDRFVRIQQENGHCISEEYYLLSEEECDDAEDVEVPKALGDVFESIAGAIFLDSNMSLDVVWHVYSNMMSPEIEQFSNSVPKSPIRELLELEPETAKFGKPEKLADGRRVRVTVDVFCKGTFRGIGRNYRIAKCTAAKCALRQLKKQGLIAKKD | |
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 |
---|---|---|---|---|---|
362 | Phosphorylation | QTIERYSSPKVRRLL HHHHHHCCHHHHHHH | 21.58 | 22817900 | |
405 | Phosphorylation | DFNRLSHTLESKCRM HHHHHHHHHHHHCCC | 28.92 | 21082442 | |
423 | Phosphorylation | MDQPPTETRALVATL CCCCCHHHHHHHHHH | 24.58 | 22817900 | |
1421 | Phosphorylation | FCDQQTRYGSPTFWD ECCCCCCCCCCCEEE | 25.91 | 21082442 | |
1423 | Phosphorylation | DQQTRYGSPTFWDVS CCCCCCCCCCEEECC | 16.31 | 19429919 | |
1425 | Phosphorylation | QTRYGSPTFWDVSNG CCCCCCCCEEECCCC | 38.77 | 19429919 | |
1877 | Phosphorylation | QNGQLDDSNDSCNDF CCCCCCCCCCCCCCC | 42.05 | 22817900 | |
1880 | Phosphorylation | QLDDSNDSCNDFSCF CCCCCCCCCCCCEEE | 21.04 | 22817900 |
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 DCR1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DCR1_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 DCR1_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AGO2_DROME | AGO2 | physical | 11498593 | |
MYC_DROME | dm | genetic | 20400939 | |
CCNE_DROME | CycE | genetic | 20400939 | |
ELP1_DROME | Elp1 | physical | 19805217 |
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-1423; SER-1877 ANDSER-1880, AND MASS SPECTROMETRY. |