| UniProt ID | RT106_YEAST | |
|---|---|---|
| UniProt AC | P40161 | |
| Protein Name | Histone chaperone RTT106 | |
| Gene Name | RTT106 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 455 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.. | |
| Protein Sequence | MSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSGRHKKPRIDVSSDLLKTDEISETNTIFKLEGVSVLSPLRKKLDLVFYLSNVDGSPVITLLKGNDRELSIYQLNKNIKMASFLPVPEKPNLIYLFMTYTSCEDNKFSEPVVMTLNKENTLNQFKNLGLLDSNVTDFEKCVEYIRKQAILTGFKISNPFVNSTLVDTDAEKINSFHLQCHRGTKEGTLYFLPDHIIFGFKKPILLFDASDIESITYSSITRLTFNASLVTKDGEKYEFSMIDQTEYAKIDDYVKRKQMKDKSMSEELKAKSKSKGQATDGTADQPSILQEATRQMQDEKKAGVFSDDDEENDQNFEAESDLSDGSGQESSDGAEDGEEAEEDDEEDDEEEDKKGQSALNRDNSFASINGQPEQELQYKEFKEPLELEDIPIEIDNDDDEDDEDGSGVEYD | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSKLFLDEL ------CCCCHHHHC | 37.76 | 22814378 | |
| 43 | Phosphorylation | KYALNENSNDRSGRH HHHHHCCCCCCCCCC | 33.65 | 30377154 | |
| 47 | Phosphorylation | NENSNDRSGRHKKPR HCCCCCCCCCCCCCC | 42.94 | 30377154 | |
| 58 | Phosphorylation | KKPRIDVSSDLLKTD CCCCEECCCCCCCCC | 17.87 | 28889911 | |
| 59 | Phosphorylation | KPRIDVSSDLLKTDE CCCEECCCCCCCCCC | 31.93 | 30377154 | |
| 121 | Acetylation | LSIYQLNKNIKMASF EEEEEECCCCCCCCC | 69.51 | 22865919 | |
| 307 | Phosphorylation | RKQMKDKSMSEELKA HHHHCCHHHHHHHHH | 37.36 | 30377154 | |
| 309 | Phosphorylation | QMKDKSMSEELKAKS HHCCHHHHHHHHHHH | 34.70 | 27214570 | |
| 315 | Acetylation | MSEELKAKSKSKGQA HHHHHHHHHHCCCCC | 57.75 | 23572591 | |
| 331 | Phosphorylation | DGTADQPSILQEATR CCCCCCHHHHHHHHH | 30.23 | 23749301 | |
| 401 | Phosphorylation | EEDKKGQSALNRDNS HHHHHHHHHHHCCCC | 43.31 | 20377248 | |
| 408 | Phosphorylation | SALNRDNSFASINGQ HHHHCCCCCHHCCCC | 26.86 | 22369663 | |
| 411 | Phosphorylation | NRDNSFASINGQPEQ HCCCCCHHCCCCCHH | 17.99 | 22369663 | |
| 422 | Phosphorylation | QPEQELQYKEFKEPL CCHHHHCCCCCCCCC | 25.72 | 22369663 | |
| 450 | Phosphorylation | DEDDEDGSGVEYD-- CCCCCCCCCCCCC-- | 52.57 | 22307274 | |
| 454 | Phosphorylation | EDGSGVEYD------ CCCCCCCCC------ | 25.25 | 24961812 |
| 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 RT106_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RT106_YEAST !! | ||||||
* 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 RT106_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-408 AND SER-411,AND MASS SPECTROMETRY. | |
