RSC30_YEAST - dbPTM
RSC30_YEAST - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
119PhosphorylationMQWTKAASYQNNNTN
HHHHHHHHHCCCCCC
31.9228889911
135PhosphorylationNTAPRQNSSTVSSNV
CCCCCCCCCCCCCCC
21.0322369663
136PhosphorylationTAPRQNSSTVSSNVH
CCCCCCCCCCCCCCC
40.1423749301
137PhosphorylationAPRQNSSTVSSNVHG
CCCCCCCCCCCCCCC
24.9922369663
139PhosphorylationRQNSSTVSSNVHGNT
CCCCCCCCCCCCCCE
19.1122369663
150PhosphorylationHGNTIVRSDSPDVPS
CCCEEECCCCCCCCC
31.3922369663
152PhosphorylationNTIVRSDSPDVPSMD
CEEECCCCCCCCCHH
25.0122369663
157PhosphorylationSDSPDVPSMDQIREY
CCCCCCCCHHHHHHH
34.5422890988
164PhosphorylationSMDQIREYNTRLQLV
CHHHHHHHHHHHEEE
16.4022369663
166PhosphorylationDQIREYNTRLQLVNA
HHHHHHHHHHEEEEC
31.6722369663
235PhosphorylationLKSLKEKSNLNADNT
HHHHHHHHCCCCCCC
47.8730377154
806PhosphorylationKQNFARNSDNNNVTD
HHHCCCCCCCCCCCC
35.8430377154
815PhosphorylationNNNVTDYSQSAKNKN
CCCCCCCCHHHCCCC
22.0725752575
819UbiquitinationTDYSQSAKNKNVLLK
CCCCHHHCCCCEEEE
73.9423749301

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSC30_YEAST !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSC3_YEASTRSC3genetic
11336698
RAD50_YEASTRAD50genetic
20865123
RPGR1_HUMANRPGRIP1physical
27107014
USH1C_HUMANUSH1Cphysical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RSC30_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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