RSC3_YEAST - dbPTM
RSC3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSC3_YEAST
UniProt AC Q06639
Protein Name Chromatin structure-remodeling complex protein RSC3
Gene Name RSC3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 885
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, and also for proper metaphase progression. Together with HTL1, LDB7, NPL6, 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..
Protein Sequence MDIRGRKMKKPPACVQCRKRKIGCDRVKPICGNCMKHNKMDCFYPDVPGQYVPSSSSSSNTRQVANGPYLNSYYASRRVSKETAALLQKNPELASLEQIREYNTRLQLLNAQNQLNNRSSAANATLNQQHTQYIPKSVPSLESKPVTSANESSTPLNWVQGPAIFHMLTSPYTQDEIINHEMNFLKGRLLELQEITGKKITGVNLDLKQDSSAQMQSSHSNRNQEEFLTIKKRKLSEDGVTDGDGKPIPESERRPHLNEFKDLDPQFLDTNKVFNVFNSAISEEGRNRLWLLPKNINKSSIFQIQYLIERDPFLFKFFNDLNILIETQFNGPLHDLVASRNSIERNSGISQILKFPSQSITQTLINKYLSTITETNSILPILKPKRLLPIVEQLFPSNTINKPNSKDFETIFQVFSVTNDQLLNLGFITLCLLILFESLNSTVLIPLRDDEHLQLFNVLFNYLPLLKSNLTTLRFEIEKRSMCNIETLRFISLWKYYQFVMDTSSSSSFVIDYDEDMHMACLLSLNHETQNQSHILTWNFIFKNYCWRHLFLGQLPLLMSEPFTNSTPIIDPLLNNDFELIDFEVNLMKYLQSKDQQLSIDKIIQLIKLLKNKNIEVSQGCLTTPSIINNIMDSLIYRNSMLYLNFYLLLQFETLKNYAKFNEILEDFLELSRETLFFVFSNLANIKFAGHEFTFINKSIVVLQTLVLMLLALYQRSFDSSKRTNDANEISEQTDIHSNNDNSKRIKNKNVIHLIINKIAMLLSDYTKNCKKQNKLIENLIIKIKTISKYIKNLEENKVTTSADSNYSINNGFSGISAEQLIKLNHELSKISESLIKTDFYEQRKNSTVSNGVLGAAAPVDSDANSDTFGLTKENFNEVFEAIRS
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
72PhosphorylationANGPYLNSYYASRRV
CCCHHHHHHHHHCCC		19.5421551504
76PhosphorylationYLNSYYASRRVSKET
HHHHHHHHCCCCHHH		12.4230377154
80PhosphorylationYYASRRVSKETAALL
HHHHCCCCHHHHHHH		23.9827214570
81AcetylationYASRRVSKETAALLQ
HHHCCCCHHHHHHHH		57.1124489116
89AcetylationETAALLQKNPELASL
HHHHHHHHCHHHHCH		74.5524489116
95PhosphorylationQKNPELASLEQIREY
HHCHHHHCHHHHHHH		45.0927214570
136UbiquitinationQHTQYIPKSVPSLES
HHHHCCCCCCCCCCC		55.3017644757
211PhosphorylationNLDLKQDSSAQMQSS
ECCCCCCCCHHHHHC		25.6928889911
212PhosphorylationLDLKQDSSAQMQSSH
CCCCCCCCHHHHHCC		30.7028889911
218PhosphorylationSSAQMQSSHSNRNQE
CCHHHHHCCCCCCHH		17.6528889911
220PhosphorylationAQMQSSHSNRNQEEF
HHHHHCCCCCCHHHH		39.1628889911
236PhosphorylationTIKKRKLSEDGVTDG
HEECEECCCCCCCCC		36.3517330950
241PhosphorylationKLSEDGVTDGDGKPI
ECCCCCCCCCCCCCC		39.5329136822
251PhosphorylationDGKPIPESERRPHLN
CCCCCCHHHCCCCHH		30.9228889911
261AcetylationRPHLNEFKDLDPQFL
CCCHHHCCCCCHHHC		51.7224489116
282PhosphorylationNVFNSAISEEGRNRL
HHHHHHCCHHHHCCE		29.3428889911
294AcetylationNRLWLLPKNINKSSI
CCEEECCCCCCHHHH		71.1224489116
354AcetylationSGISQILKFPSQSIT
CCHHHHHHCCCHHHH		57.7824489116
357PhosphorylationSQILKFPSQSITQTL
HHHHHCCCHHHHHHH		39.4329688323
359PhosphorylationILKFPSQSITQTLIN
HHHCCCHHHHHHHHH		31.7629688323
361PhosphorylationKFPSQSITQTLINKY
HCCCHHHHHHHHHHH		22.2829688323
363PhosphorylationPSQSITQTLINKYLS
CCHHHHHHHHHHHHH		22.4329688323
367UbiquitinationITQTLINKYLSTITE
HHHHHHHHHHHHHHC		40.3417644757
383AcetylationNSILPILKPKRLLPI
CCCHHHCCHHHHHHH		49.5724489116
383UbiquitinationNSILPILKPKRLLPI
CCCHHHCCHHHHHHH		49.5717644757
385UbiquitinationILPILKPKRLLPIVE
CHHHCCHHHHHHHHH		54.8317644757
468PhosphorylationNYLPLLKSNLTTLRF
HHHHHHHCCCEEECC		36.7227017623
602AcetylationDQQLSIDKIIQLIKL
CCCCCHHHHHHHHHH		39.7924489116
608AcetylationDKIIQLIKLLKNKNI
HHHHHHHHHHHCCCC		57.2524489116
830AcetylationKLNHELSKISESLIK
HHHHHHHHHHHHHHH		63.9824489116
847PhosphorylationFYEQRKNSTVSNGVL
HHHHHCCCCCCCCCC		32.9721440633
848PhosphorylationYEQRKNSTVSNGVLG
HHHHCCCCCCCCCCC		37.0319779198
850PhosphorylationQRKNSTVSNGVLGAA
HHCCCCCCCCCCCCC		28.1419779198
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 RSC3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSC3_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 RSC3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSC7_YEASTNPL6physical
14759368
ARP7_YEASTARP7physical
14759368
ARP9_YEASTARP9physical
14759368
RSC2_YEASTRSC2physical
14759368
RSC3_YEASTRSC3physical
14759368
RSC4_YEASTRSC4physical
14759368
RSC58_YEASTRSC58physical
14759368
RSC6_YEASTRSC6physical
14759368
RSC8_YEASTRSC8physical
14759368
RSC9_YEASTRSC9physical
14759368
STH1_YEASTSTH1physical
14759368
RSC2_YEASTRSC2physical
14729968
ARP7_YEASTARP7physical
14729968
ARP9_YEASTARP9physical
14729968
COG6_YEASTCOG6physical
14729968
HSC82_YEASTHSC82physical
14729968
HS104_YEASTHSP104physical
14729968
SIZ2_YEASTNFI1physical
14729968
RSC7_YEASTNPL6physical
14729968
RSC4_YEASTRSC4physical
14729968
RSC58_YEASTRSC58physical
14729968
RSC6_YEASTRSC6physical
14729968
RSC8_YEASTRSC8physical
14729968
RSC9_YEASTRSC9physical
14729968
RT102_YEASTRTT102physical
14729968
HSP71_YEASTSSA1physical
14729968
HSP72_YEASTSSA2physical
14729968
HSP7F_YEASTSSE1physical
14729968
STH1_YEASTSTH1physical
14729968
SFH1_YEASTSFH1physical
14729968
RSC30_YEASTRSC30genetic
11336698
RSC6_YEASTRSC6physical
16554755
NAT1_YEASTNAT1physical
16554755
RSC8_YEASTRSC8physical
16554755
EIF2A_YEASTYGR054Wphysical
16554755
ARD1_YEASTARD1physical
16554755
STH1_YEASTSTH1physical
16554755
RSC58_YEASTRSC58physical
16554755
SFH1_YEASTSFH1physical
16554755
RSC2_YEASTRSC2physical
16554755
ARP9_YEASTARP9physical
16554755
RSC7_YEASTNPL6physical
16554755
NAT5_YEASTNAT5physical
16554755
ARP7_YEASTARP7physical
16554755
RSC4_YEASTRSC4physical
16554755
H4_YEASTHHF1physical
16429126
ISW1_YEASTISW1physical
16429126
MOT1_YEASTMOT1physical
16429126
VPS1_YEASTVPS1physical
16429126
H2A2_YEASTHTA2physical
16429126
RSC1_YEASTRSC1physical
16429126
RSC2_YEASTRSC2physical
16429126
STH1_YEASTSTH1physical
16429126
RSC7_YEASTNPL6physical
16429126
H2B1_YEASTHTB1physical
16429126
RSC30_YEASTRSC30physical
16429126
ARP9_YEASTARP9physical
16429126
H2A1_YEASTHTA1physical
16429126
RSC4_YEASTRSC4physical
16429126
RSC58_YEASTRSC58physical
16429126
RSC6_YEASTRSC6physical
16429126
RSC8_YEASTRSC8physical
16429126
RSC9_YEASTRSC9physical
16429126
SFH1_YEASTSFH1physical
16429126
ARP7_YEASTARP7physical
16429126
TRA1_YEASTTRA1physical
16429126
RSC30_YEASTRSC30physical
16204215
CGS5_YEASTCLB5genetic
17542652
HSP7F_YEASTSSE1physical
19536198
HOG1_YEASTHOG1physical
19153600
MAD1_YEASTMAD1genetic
11336698
ICE2_YEASTICE2genetic
23891562
ISW1_YEASTISW1genetic
25821983
GAS1_YEASTGAS1genetic
27708008
CALM_YEASTCMD1genetic
27708008
NSE4_YEASTNSE4genetic
27708008
TIM22_YEASTTIM22genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ESP1_YEASTESP1genetic
27708008
HSP77_YEASTSSC1genetic
27708008
KTHY_YEASTCDC8genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
SSL1_YEASTSSL1genetic
27708008
SED5_YEASTSED5genetic
27708008
BOS1_YEASTBOS1genetic
27708008
POB3_YEASTPOB3genetic
27708008
RSC9_YEASTRSC9genetic
27708008
ARP9_YEASTARP9genetic
27708008
MCM1_YEASTMCM1genetic
27708008
PDS5_YEASTPDS5genetic
27708008
TYSY_YEASTCDC21genetic
27708008
TFC8_YEASTTFC8genetic
27708008
ARP7_YEASTARP7genetic
27708008
ELO2_YEASTELO2genetic
27708008
GPR1_YEASTGPR1genetic
27708008
VAM6_YEASTVAM6genetic
27708008
UGA4_YEASTUGA4genetic
27708008
CEM1_YEASTCEM1genetic
27708008
AP2B_YEASTAPL1genetic
27708008
RL43A_YEASTRPL43Bgenetic
27708008
RL43B_YEASTRPL43Bgenetic
27708008
MDM35_YEASTMDM35genetic
27708008
FABG_YEASTOAR1genetic
27708008
CSF1_YEASTCSF1genetic
27708008
ALAM_YEASTALT1genetic
27708008
MMR1_YEASTMMR1genetic
27708008
YL297_YEASTYLR297Wgenetic
27708008
OCA2_YEASTOCA2genetic
27708008
ATG3_YEASTATG3genetic
27708008
VAM10_YEASTVAM10genetic
27708008
YP022_YEASTYPR022Cgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RSC3_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-95; SER-236 AND SER-282,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-236, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND MASSSPECTROMETRY.

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