UniProt ID | RSC30_YEAST | |
---|---|---|
UniProt AC | P38781 | |
Protein Name | Chromatin structure-remodeling complex protein RSC30 | |
Gene Name | RSC30 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 883 | |
Subcellular Localization | Nucleus . Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1. | |
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. This subunit is required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall. Together with HTL1, LDB7, NPL6, RSC3 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.. | |
Protein Sequence | MMDMQVRKVRKPPACTQCRKRKIGCDRAKPICGNCVKYNKPDCFYPDGPGKMVAVPSASGMSTHGNGQGSNHFSQGNGVNQKNVMIQTQYPIMQTSIEAFNFSFNPSVDTAMQWTKAASYQNNNTNNNTAPRQNSSTVSSNVHGNTIVRSDSPDVPSMDQIREYNTRLQLVNAQSFDYTDNPYSFNVGINQDSAVFDLMTSPFTQEEVLIKEIDFLKNKLLDLQSLQLKSLKEKSNLNADNTTANKINKTGENSKKGKVDGKRAGFDHQTSRTSQSSQKYFTALTITDVQSLVQVKPLKDTPNYLFTKNFIIFRDHYLFKFYNILHDICHINQFKVSPPNNKNHQQYMEVCKVNFPPKAIIIETLNSESLNNLNIEEFLPIFDKTLLLEFVHNSFPNGDTCPSFSTVDLPLSQLTKLGELTVLLLLLNDSMTLFNKQAINNHVSALMNNLRLIRSQITLINLEYYDQETIKFIAITKFYESLYMHDDHKSSLDEDLSCLLSFQIKDFKLFHFLKKMYYSRHSLLGQSSFMVPAAENLSPIPASIDTNDIPLIANDLKLLETQAKLINILQGVPFYLPVNLTKIESLLETLTMGVSNTVDLYFHDNEVRKEWKDTLNFINTIVYTNFFLFVQNESSLSMAVQHSSNNNKTSNSERCAKDLMKIISNMHIFYSITFNFIFPIKSIKSFSSGNNRFHSNGKEFLFANHFIEILQNFIAITFAIFQRCEVILYDEFYKNLSNEEINVQLLLIHDKILEILKKIEIIVSFLRDEMNSNGSFKSIKGFNKVLNLIKYMLRFSKKKQNFARNSDNNNVTDYSQSAKNKNVLLKFPVSELNRIYLKFKEISDFLMEREVVQRSIIIDKDLESDNLGITTANFNDFYDAFYN | |
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 |
---|---|---|---|---|---|
119 | Phosphorylation | MQWTKAASYQNNNTN HHHHHHHHHCCCCCC | 31.92 | 28889911 | |
135 | Phosphorylation | NTAPRQNSSTVSSNV CCCCCCCCCCCCCCC | 21.03 | 22369663 | |
136 | Phosphorylation | TAPRQNSSTVSSNVH CCCCCCCCCCCCCCC | 40.14 | 23749301 | |
137 | Phosphorylation | APRQNSSTVSSNVHG CCCCCCCCCCCCCCC | 24.99 | 22369663 | |
139 | Phosphorylation | RQNSSTVSSNVHGNT CCCCCCCCCCCCCCE | 19.11 | 22369663 | |
150 | Phosphorylation | HGNTIVRSDSPDVPS CCCEEECCCCCCCCC | 31.39 | 22369663 | |
152 | Phosphorylation | NTIVRSDSPDVPSMD CEEECCCCCCCCCHH | 25.01 | 22369663 | |
157 | Phosphorylation | SDSPDVPSMDQIREY CCCCCCCCHHHHHHH | 34.54 | 22890988 | |
164 | Phosphorylation | SMDQIREYNTRLQLV CHHHHHHHHHHHEEE | 16.40 | 22369663 | |
166 | Phosphorylation | DQIREYNTRLQLVNA HHHHHHHHHHEEEEC | 31.67 | 22369663 | |
235 | Phosphorylation | LKSLKEKSNLNADNT HHHHHHHHCCCCCCC | 47.87 | 30377154 | |
806 | Phosphorylation | KQNFARNSDNNNVTD HHHCCCCCCCCCCCC | 35.84 | 30377154 | |
815 | Phosphorylation | NNNVTDYSQSAKNKN CCCCCCCCHHHCCCC | 22.07 | 25752575 | |
819 | Ubiquitination | TDYSQSAKNKNVLLK CCCCHHHCCCCEEEE | 73.94 | 23749301 |
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 RSC30_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RSC30_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 RSC30_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RSC3_YEAST | RSC3 | genetic | 11336698 | |
RAD50_YEAST | RAD50 | genetic | 20865123 | |
RPGR1_HUMAN | RPGRIP1 | physical | 27107014 | |
USH1C_HUMAN | USH1C | physical | 27107014 |
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-135; SER-150 ANDSER-152, AND MASS SPECTROMETRY. | |
"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-135, AND MASSSPECTROMETRY. |