UniProt ID | LDB7_YEAST | |
---|---|---|
UniProt AC | P38210 | |
Protein Name | Chromatin structure-remodeling complex protein RSC14 | |
Gene Name | LDB7 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 180 | |
Subcellular Localization | Nucleus. | |
Protein Description | Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. Together with HTL1, NPL6, RSC3, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity. May be involved in the transfer of mannosylphosphate (MP) groups into N-linked oligosaccharides.. | |
Protein Sequence | MSGSNMGYYDVLAGLSALEKSSQVVFSATELQQLTQQSHATDKGIEGSENSKAKVSKPKRVAVHGYLGGKVSLADAAQVEYEVGHSLLGSYVPRQQLEALSSVDFSHHFHRTLECKAALETHDVFLAGAGQLSLPFQSHIESPRNSEAKRKRKVIICKRCQSRFIGSHRRSQLREHACVD | |
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 | Phosphorylation | ------MSGSNMGYY ------CCCCCCCHH | 51.43 | 19823750 | |
4 | Phosphorylation | ----MSGSNMGYYDV ----CCCCCCCHHHH | 19.14 | 19823750 | |
8 | Phosphorylation | MSGSNMGYYDVLAGL CCCCCCCHHHHHHHH | 5.92 | 19823750 | |
9 | Phosphorylation | SGSNMGYYDVLAGLS CCCCCCHHHHHHHHH | 8.21 | 19823750 | |
16 | Phosphorylation | YDVLAGLSALEKSSQ HHHHHHHHHHHHHHC | 29.86 | 19823750 | |
133 | Phosphorylation | LAGAGQLSLPFQSHI EECCCCCCCCCHHHC | 26.55 | 21440633 | |
138 | Phosphorylation | QLSLPFQSHIESPRN CCCCCCHHHCCCCCC | 27.15 | 22369663 | |
142 | Phosphorylation | PFQSHIESPRNSEAK CCHHHCCCCCCCHHH | 28.67 | 22369663 | |
146 | Phosphorylation | HIESPRNSEAKRKRK HCCCCCCCHHHHCCE | 39.96 | 21440633 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of LDB7_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LDB7_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of LDB7_YEAST !! |
Kegg Drug | ||||||
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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-142, AND MASSSPECTROMETRY. |