UniProt ID | EZ_DROME | |
---|---|---|
UniProt AC | P42124 | |
Protein Name | Histone-lysine N-methyltransferase E(z) | |
Gene Name | E(z) | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 760 | |
Subcellular Localization | Nucleus . | |
Protein Description | Polycomb group (PcG) protein. Catalytic subunit of the Esc/E(z) complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required.. | |
Protein Sequence | MNSTKVPPEWKRRVKSEYIKIRQQKRYKRADEIKEAWIRNWDEHNHNVQDLYCESKVWQAKPYDPPHVDCVKRAEVTSYNGIPSGPQKVPICVINAVTPIPTMYTWAPTQQNFMVEDETVLHNIPYMGDEVLDKDGKFIEELIKNYDGKVHGDKDPSFMDDAIFVELVHALMRSYSKELEEAAPGTATAIKTETLAKSKQGEDDGVVDVDADGESPMKLEKTDSKGDLTEVEKKETEEPLETEDADVKPDVEEVKDKLPFPAPIIFQAISANFPDKGTAQELKEKYIELTEHQDPERPQECTPNIDGIKAESVSRERTMHSFHTLFCRRCFKYDCFLHRLQGHAGPNLQKRRYPELKPFAEPCSNSCYMLIDGMKEKLAADSKTPPIDSCNEASSEDSNDSNSQFSNKDFNHENSKDNGLTVNSAAVAEINSIMAGMMNITSTQCVWTGADQALYRVLHKVYLKNYCAIAHNMLTKTCRQVYEFAQKEDAEFSFEDLRQDFTPPRKKKKKQRLWSLHCRKIQLKKDSSSNHVYNYTPCDHPGHPCDMNCSCIQTQNFCEKFCNCSSDCQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCQACGADQFKLTKITCKNVCVQRGLHKHLLMAPSDIAGWGIFLKEGAQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSINPNCYAKVMMVTGDHRIGIFAKRAIQPGEELFFDYRYGPTEQLKFVGIEREMEIV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
20 | Acetylation | RVKSEYIKIRQQKRY HHHHHHHHHHHHHHH | 30.82 | 21791702 | |
493 | Phosphorylation | QKEDAEFSFEDLRQD HHHCCCCCHHHHHHH | 21.16 | 22817900 | |
502 | Phosphorylation | EDLRQDFTPPRKKKK HHHHHHCCCCCHHHH | 40.44 | 12408864 | |
515 | Phosphorylation | KKKQRLWSLHCRKIQ HHHHHHHHHCCEEEE | 16.90 | 22817900 | |
727 | Acetylation | HRIGIFAKRAIQPGE CEEEEEEECCCCCCC | 31.45 | 21791702 |
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 EZ_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EZ_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 EZ_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-493 AND THR-502, ANDMASS SPECTROMETRY. |