| UniProt ID | CAF1_DROME | |
|---|---|---|
| UniProt AC | Q24572 | |
| Protein Name | Probable histone-binding protein Caf1 | |
| Gene Name | Caf1 | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 430 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.. | |
| Protein Sequence | MVDRSDNAAESFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTKQDGKDYSVHRLILGTHTSDEQNHLLIASVQLPSEDAQFDGSHYDNEKGEFGGFGSVCGKIEIEIKINHEGEVNRARYMPQNACVIATKTPSSDVLVFDYTKHPSKPEPSGECQPDLRLRGHQKEGYGLSWNPNLNGYLLSASDDHTICLWDINATPKEHRVIDAKNIFTGHTAVVEDVAWHLLHESLFGSVADDQKLMIWDTRNNNTSKPSHTVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLHVWDLSKIGEEQSTEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWIICSVSEDNIMQVWQMAENVYNDEEPEIPASELETNTA | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MVDRSDNAAESF ---CCCCCCCHHHHC | 30.65 | 19429919 | |
| 11 | Phosphorylation | RSDNAAESFDDAVEE CCCCHHHHCHHHHHH | 29.28 | 21082442 | |
| 58 | Phosphorylation | AQWLPDVTKQDGKDY EEECCCCCCCCCCCC | 30.30 | 30478224 | |
| 100 | Phosphorylation | EDAQFDGSHYDNEKG CCCCCCCCCCCCCCC | 22.25 | 18327897 | |
| 352 | Phosphorylation | RLHVWDLSKIGEEQS EEEEEEHHHCCCCCC | 21.54 | 18327897 | |
| 359 | Phosphorylation | SKIGEEQSTEDAEDG HHCCCCCCCCCCCCC | 36.72 | 22668510 |
| 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 CAF1_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAF1_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 CAF1_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-100, 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-11, AND MASSSPECTROMETRY. | |
