UniProt ID | Y3096_DROME | |
---|---|---|
UniProt AC | Q9VLK2 | |
Protein Name | Ribosomal L1 domain-containing protein CG13096 | |
Gene Name | CG13096 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 681 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MVKVQKPQPKSLNKSASIEGVVKKKGKPEKTKKLATDATLELASNKKAKNAAPVKKDAIKKEPEVSKKGAEKKQSKAAKRPLILAPPESPAAPAPAAKKSKAKPAASGAPVGKKIEAKKPLILAPPESPVPPKKQEKKTKAAPVKAKKEPAPAKKSVQDPVPSIKKVPAAKKSGQTAALTKKTAKTEKQAAPAKPAKAQPASQLQKKAKAVQKLSKPASPPKSKKALSKSKPGQAKGNAVNKEPAKSKKPVELTFELKAFDEKRFHEIVNENNVTKVCAALKSVVSEEVEKKKNTSIFSDYRYVLQVCSYKIPSCPKRMVKLNLKHSLVGKDDDVALIVPDLQRGAKFDYDPTKQHYEDMLREAGVKQRLTVVPFNQLRNEMGSFEAKRKFLNSYDYLLCDGRLSGQATAFLGKNTQKPRNVLHSLRLSKDNDKLPQEVTRALTRTAFRQLSKGDLIAVPVGNHEITAEQLAENILLVIKQLQEVYPGGLANIRSMYLKIDITGTSALPLYVSMCAPPEDVPYVVGPREQRMLKLKKQANEVLSKFAMTKDAEFIKLTSDQVKRKAQLRKEKAALLAADAAPKDNDGGDAAVPAKKARKESSSEGAKADAESDEEEEVEEAEDSAGESGDEDEEGHDGDDTDEDEDEDDDDDNEDGDDDEDEDDDEEDDDEEDDDDDDDEE | |
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 |
---|---|---|---|---|---|
15 | Phosphorylation | QPKSLNKSASIEGVV CCCCCCCCCCCCHHH | 26.61 | 25749252 | |
17 | Phosphorylation | KSLNKSASIEGVVKK CCCCCCCCCCHHHCC | 28.41 | 19429919 | |
89 | Phosphorylation | LILAPPESPAAPAPA CEECCCCCCCCCCCH | 26.13 | 19429919 | |
128 | Phosphorylation | LILAPPESPVPPKKQ EEECCCCCCCCCCCC | 36.65 | 19429919 | |
219 | Phosphorylation | QKLSKPASPPKSKKA HHHCCCCCCCCCHHH | 50.71 | 19429919 | |
299 | Phosphorylation | KKNTSIFSDYRYVLQ HCCCCCCCCHHHHHH | 31.87 | 27626673 | |
347 | Acetylation | PDLQRGAKFDYDPTK CCCCCCCCCCCCCHH | 41.41 | 21791702 | |
429 | Phosphorylation | VLHSLRLSKDNDKLP HHHHHHCCCCCCCCC | 31.37 | 19429919 | |
601 | Phosphorylation | AKKARKESSSEGAKA HHHHHHHHCCHHHHC | 42.05 | 19429919 | |
602 | Phosphorylation | KKARKESSSEGAKAD HHHHHHHCCHHHHCC | 33.24 | 19429919 | |
603 | Phosphorylation | KARKESSSEGAKADA HHHHHHCCHHHHCCC | 49.70 | 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 Y3096_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of Y3096_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 Y3096_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|
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-15 AND SER-17, AND MASSSPECTROMETRY. | |
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-128, AND MASSSPECTROMETRY. |