UniProt ID | Y7065_DROME | |
---|---|---|
UniProt AC | Q7YZA2 | |
Protein Name | Uncharacterized protein CG7065 | |
Gene Name | CG7065 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 1231 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MSFLPGEPVPPGFEEDVSRTAVIQKQIESYTAGPLIGTEYTIELHEPAQLRPNYFCVLCQTCSDGRNVFVHWTSQAHRTKYLQTHFQKAYKELQKLKRTPNSSGDLVTATGNLVKCIEKHFGRSRNLITATGDDFRRYRSKMCSQVRDSFHFDECAGSDFSEEAQRVIRELKPDESIKSSMKKNVDGTGDSNKQHDDGNIIALDAISSDDESFGGSTASVVPVPKGRQKNNLSEDAGGRSKNQSPPPAGGVNKTQHLPTPKELAIQASKISQERYKWEKFRCMLEIQLKQLRSDTEMYESNPEKHPDYPDEWKQFWNRRYKQLQEEKKCDPNQYDYKPEWISYWKDRRIVLFDIAVNKIKKDLKEKFKLGDEDEEKTLELMERYKIRVASPRRAPATTNSDNCRKTKPNFRNNRPIVATSKLPDAVIDISDDDVDSPPSRSRHSHKRRSISRSLSPKRGGRRAVRRSRSRSPRRSYNRGSTRSRSRSMRHRSRSPAHYRGRGRGREPASKERGSSSRDFGGRHSLQRERERSSEYYHRNEGYARSSRGYESVETFRVLDSRVYPEYKVTKTSSISPTASSNKEKEKEASEPIEEGPLTVVSVLRMLSAVEEHLGSLGPKALNLLSKALAMELVKPNAAEDLLRNEDNCVFLETTKEKLKGILIAEVLDDPQKVRVIKKLITNIAEIIYQATFKGTNDAVDVKVKANANPAPIQLPFDRNLVAPKLANALVLNGYNNVSTGDMNNLLHMLTLLMKTDKQRRQLDNNNGLKFEEIKVKLGLQNNPSPDDMGIDLDELMKEVEHQLHKESVDIVNKPTGAPAKVQAADTVGGSTGLESLTDSDLQTLLQNFKFLSNEEQVHLIGHLRKLEVQDPSRVDRLRKYVNLVELRGDGESCSDFLARVVKIGGASKAKPATKFKASVMGGRTSSAMAASSASATAPKVGHSMLSAQRPNLDRDMSSMPINKQRRGRNTPSIMLDDDDEEDDDYNFDDLVMKACDSNGSASAGGGGGVVGAGVHNKPGVPPIIGVESSPNALTFKPAAATKISLKDTENIIANLMGTLSKNGTSGGSPVGGNRNYMMNQQHGAPNAQNAPNLGQNPGQNLGQKQPGAGYSNAGYPGQQQQQQQQQQHGRNFGQEAQPLMSGLSGGPNANHYPNQQGYGGYHPFAGNGVQQNYGGMVPPGPGGYVGPPPNPWASNVPPQPPFNQMPQNFMGAQQQQQQQQPHFNNMFGGRH | |
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 |
---|---|---|---|---|---|
207 | Phosphorylation | IIALDAISSDDESFG EEEEECCCCCCCCCC | 29.45 | 22817900 | |
208 | Phosphorylation | IALDAISSDDESFGG EEEECCCCCCCCCCC | 42.86 | 22817900 | |
212 | Phosphorylation | AISSDDESFGGSTAS CCCCCCCCCCCCCCE | 35.86 | 20450229 | |
244 | Phosphorylation | GGRSKNQSPPPAGGV CCCCCCCCCCCCCCC | 49.09 | 19429919 | |
430 | Phosphorylation | PDAVIDISDDDVDSP CCCEEECCCCCCCCC | 31.10 | 28490779 | |
436 | Phosphorylation | ISDDDVDSPPSRSRH CCCCCCCCCCCCCCC | 38.26 | 28490779 | |
449 | Phosphorylation | RHSHKRRSISRSLSP CCCHHCHHHHHCCCC | 29.02 | 19429919 | |
451 | Phosphorylation | SHKRRSISRSLSPKR CHHCHHHHHCCCCCC | 19.64 | 19429919 | |
453 | Phosphorylation | KRRSISRSLSPKRGG HCHHHHHCCCCCCCC | 26.80 | 19429919 | |
455 | Phosphorylation | RSISRSLSPKRGGRR HHHHHCCCCCCCCHH | 29.62 | 19429919 | |
467 | Phosphorylation | GRRAVRRSRSRSPRR CHHHHHHCCCCCCCC | 24.84 | 19429919 | |
469 | Phosphorylation | RAVRRSRSRSPRRSY HHHHHCCCCCCCCCC | 38.05 | 19429919 | |
471 | Phosphorylation | VRRSRSRSPRRSYNR HHHCCCCCCCCCCCC | 24.81 | 19429919 | |
492 | Phosphorylation | SRSMRHRSRSPAHYR CHHHHHHCCCCCHHC | 30.87 | 19429919 | |
494 | Phosphorylation | SMRHRSRSPAHYRGR HHHHHCCCCCHHCCC | 27.90 | 19429919 | |
509 | Phosphorylation | GRGREPASKERGSSS CCCCCCCCCCCCCCC | 45.85 | 21082442 | |
514 | Phosphorylation | PASKERGSSSRDFGG CCCCCCCCCCCCCCC | 31.21 | 19429919 | |
515 | Phosphorylation | ASKERGSSSRDFGGR CCCCCCCCCCCCCCC | 32.01 | 19429919 | |
516 | Phosphorylation | SKERGSSSRDFGGRH CCCCCCCCCCCCCCH | 37.25 | 19429919 | |
524 | Phosphorylation | RDFGGRHSLQRERER CCCCCCHHHHHHHHH | 25.49 | 19429919 | |
549 | Phosphorylation | YARSSRGYESVETFR CCCCCCCCCCEEEEE | 12.15 | 18327897 | |
551 | Phosphorylation | RSSRGYESVETFRVL CCCCCCCCEEEEEEC | 19.44 | 19429919 | |
571 | Phosphorylation | PEYKVTKTSSISPTA CEEEEEECCCCCCCC | 20.52 | 19429919 | |
572 | Phosphorylation | EYKVTKTSSISPTAS EEEEEECCCCCCCCC | 27.51 | 19429919 | |
573 | Phosphorylation | YKVTKTSSISPTASS EEEEECCCCCCCCCC | 32.11 | 19429919 | |
575 | Phosphorylation | VTKTSSISPTASSNK EEECCCCCCCCCCCH | 20.39 | 19429919 | |
577 | Phosphorylation | KTSSISPTASSNKEK ECCCCCCCCCCCHHH | 32.17 | 19429919 | |
579 | Phosphorylation | SSISPTASSNKEKEK CCCCCCCCCCHHHHH | 36.60 | 19429919 | |
589 | Phosphorylation | KEKEKEASEPIEEGP HHHHHHCCCCCCCCC | 45.02 | 23607784 | |
934 | Phosphorylation | AMAASSASATAPKVG HHHHHHCCCCCCCHH | 28.27 | 22817900 | |
936 | Phosphorylation | AASSASATAPKVGHS HHHHCCCCCCCHHHH | 40.78 | 22817900 | |
970 | Phosphorylation | KQRRGRNTPSIMLDD HHCCCCCCCCCCCCC | 19.63 | 19429919 | |
972 | Phosphorylation | RRGRNTPSIMLDDDD CCCCCCCCCCCCCCC | 20.70 | 19429919 | |
1068 | Phosphorylation | KNGTSGGSPVGGNRN CCCCCCCCCCCCHHH | 21.67 | 25749252 |
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 Y7065_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of Y7065_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 Y7065_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of Y7065_DROME !! |
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-449; SER-451; SER-453;SER-455; TYR-549; SER-573; THR-970 AND SER-972, AND MASS SPECTROMETRY. | |
"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-589, AND MASSSPECTROMETRY. |