| UniProt ID | RCOR_DROME | |
|---|---|---|
| UniProt AC | Q59E36 | |
| Protein Name | REST corepressor | |
| Gene Name | CoRest | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 590 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Essential component of a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited by Ttk88 and probably acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. May serve as a molecular beacon for the recruitment of molecular machinery that imposes silencing across a chromosomal interval.. | |
| Protein Sequence | MVLAERNTTDVVRNGRRSRGPSPNTHTTGGVTNSASLVGSGNNSGHSGNANANEKTTTAVPGAGTPESSDDDNSTKRNGKSKAKQSEYEEKIRVGRDYQAVCPPLVPEAERRPEQMNERALLVWSPTKEIPDLKLEEYISVAKEKYGYNGEQALGMLFWHKHDLERAVMDLANFTPFPDEWTIEDKVLFEQAFQFHGKSFHRIRQMLPDKSIASLVKYYYSWKKTRHRSSAMDRQEKAIKAVVKDGSENGSEVGSNEESDNDDKIQKNRQVMEQLDKECETINVDDVLSKPAAANTESAQPRISARWLPDEIQVALLAIREYGKNFPTIAKVVATKTEAHVRTFYLNNRRRYNLDQIVKEYEAGKSEESGAEEQTEPAVDAAAAGAATASAPSAADSTSAASATADRKQSTENSNNGVETMQESLPKKEDPKKPELAAAVLKIGVAEAADAVATVASSTASGVIGAATSASKPSTSATITIIDESDTATNSSSDVVTTGLATSTGSSALSSTTSAPASKTQTSSEELSAQKSNPASGIAAIGAATGGGQTANSSGSKRDSSVLPVAEQPPAKKIALSTGGGSSVAEFLAN | |
| 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 |
|---|---|---|---|---|---|
| 18 | Phosphorylation | VVRNGRRSRGPSPNT HHHCCCCCCCCCCCC | 39.98 | 19429919 | |
| 22 | Phosphorylation | GRRSRGPSPNTHTTG CCCCCCCCCCCCCCC | 33.34 | 19429919 | |
| 25 | Phosphorylation | SRGPSPNTHTTGGVT CCCCCCCCCCCCCCC | 24.80 | 19429919 | |
| 27 | Phosphorylation | GPSPNTHTTGGVTNS CCCCCCCCCCCCCCC | 25.71 | 19429919 | |
| 28 | Phosphorylation | PSPNTHTTGGVTNSA CCCCCCCCCCCCCCC | 25.08 | 19429919 | |
| 32 | Phosphorylation | THTTGGVTNSASLVG CCCCCCCCCCCEECC | 27.08 | 19429919 | |
| 34 | Phosphorylation | TTGGVTNSASLVGSG CCCCCCCCCEECCCC | 15.18 | 23607784 | |
| 36 | Phosphorylation | GGVTNSASLVGSGNN CCCCCCCEECCCCCC | 24.33 | 23607784 | |
| 65 | Phosphorylation | TAVPGAGTPESSDDD CCCCCCCCCCCCCCC | 24.29 | 19429919 | |
| 68 | Phosphorylation | PGAGTPESSDDDNST CCCCCCCCCCCCCCC | 40.03 | 19429919 | |
| 69 | Phosphorylation | GAGTPESSDDDNSTK CCCCCCCCCCCCCCC | 43.31 | 19429919 | |
| 74 | Phosphorylation | ESSDDDNSTKRNGKS CCCCCCCCCCCCCCH | 42.15 | 19429919 | |
| 75 | Phosphorylation | SSDDDNSTKRNGKSK CCCCCCCCCCCCCHH | 40.03 | 19429919 | |
| 125 | Phosphorylation | ERALLVWSPTKEIPD CCEEEEECCCCCCCC | 18.40 | 21082442 | |
| 255 | Phosphorylation | ENGSEVGSNEESDND CCCCCCCCCCCCCCH | 46.36 | 29892262 | |
| 259 | Phosphorylation | EVGSNEESDNDDKIQ CCCCCCCCCCHHHHH | 35.22 | 29892262 | |
| 375 | Phosphorylation | ESGAEEQTEPAVDAA CCCCHHCCHHHHHHH | 2.97 | 18327897 | |
| 410 | Phosphorylation | ATADRKQSTENSNNG HCCCHHHHCCCCCCH | 18.62 | 19429919 | |
| 411 | Phosphorylation | TADRKQSTENSNNGV CCCHHHHCCCCCCHH | 4.59 | 19429919 | |
| 414 | Phosphorylation | RKQSTENSNNGVETM HHHHCCCCCCHHHHH | 28.69 | 19429919 | |
| 442 | Phosphorylation | ELAAAVLKIGVAEAA HHHHHHHHHHHHHHH | 47.41 | 18327897 | |
| 478 | Phosphorylation | SKPSTSATITIIDES CCCCCCEEEEEECCC | 36.37 | 18327897 | |
| 481 | Phosphorylation | STSATITIIDESDTA CCCEEEEEECCCCCC | 25.99 | 18327897 | |
| 560 | Phosphorylation | SSGSKRDSSVLPVAE CCCCCCCCCCCCCCC | 33.96 | 19429919 | |
| 561 | Phosphorylation | SGSKRDSSVLPVAEQ CCCCCCCCCCCCCCC | 40.63 | 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 RCOR_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RCOR_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 RCOR_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-18; SER-22; THR-25;THR-65; SER-68; SER-69; THR-442; THR-478 AND SER-481, 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-22; SER-34; SER-36 ANDSER-627, AND MASS SPECTROMETRY. | |