| UniProt ID | NHP10_YEAST | |
|---|---|---|
| UniProt AC | Q03435 | |
| Protein Name | Non-histone protein 10 | |
| Gene Name | NHP10 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 203 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex.. | |
| Protein Sequence | MSVEEKKRRLEELKDQNVVLGLAIQRSRLSVKRLKLEYGVLLERLESRIELDPELNCEDPLPTLASFKQELLTKPFRKSKTKRHKVKERDPNMPKRPTNAYLLYCEMNKERIRQNGSLDVTRDLAEGWKNLNEQDRKPYYKLYSEDRERYQMEMEIYNKKISNIDADDDKEENEQKIKNNEEGSSTKVADSKGGEDGSLVSSN | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSVEEKKRR ------CCHHHHHHH | 37.93 | 22814378 | |
| 47 | Phosphorylation | VLLERLESRIELDPE HHHHHHHHHHCCCCC | 43.05 | 17563356 | |
| 66 | Phosphorylation | DPLPTLASFKQELLT CCCCCHHHHHHHHHC | 35.77 | 30377154 | |
| 150 | Phosphorylation | YSEDRERYQMEMEIY HHHHHHHHHHHHHHH | 13.88 | 27214570 | |
| 162 | Phosphorylation | EIYNKKISNIDADDD HHHHHHHHCCCCCCC | 36.29 | 30377154 | |
| 184 | Phosphorylation | IKNNEEGSSTKVADS HHHCCCCCCCEECCC | 37.81 | 27214570 | |
| 185 | Phosphorylation | KNNEEGSSTKVADSK HHCCCCCCCEECCCC | 43.00 | 27214570 | |
| 191 | Phosphorylation | SSTKVADSKGGEDGS CCCEECCCCCCCCCC | 24.38 | 23749301 | |
| 198 | Phosphorylation | SKGGEDGSLVSSN-- CCCCCCCCCCCCC-- | 37.61 | 22369663 | |
| 201 | Phosphorylation | GEDGSLVSSN----- CCCCCCCCCC----- | 29.47 | 22369663 | |
| 202 | Phosphorylation | EDGSLVSSN------ CCCCCCCCC------ | 38.79 | 22369663 |
| 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 NHP10_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NHP10_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 NHP10_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY. | |
| "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 TYR-150, AND MASSSPECTROMETRY. | |
