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Protein

Chromatin structure-remodeling complex subunit RSC9

Gene

RSC9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 plays a role in transcriptional response to stress. It is involved in both repression and activation of mRNAs regulated by the target of rapamycin (TOR) kinases, and in the synthesis of rRNA.7 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi395 – 47682RFX-type winged-helixPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • cellular response to hydrogen peroxide Source: SGD
  • nucleosome disassembly Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • rRNA processing Source: UniProtKB-KW
  • rRNA transcription Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: SGD
  • transfer RNA gene-mediated silencing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

rRNA processing, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32705-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin structure-remodeling complex subunit RSC9
Alternative name(s):
RSC complex subunit RSC9
Remodel the structure of chromatin complex subunit 9
Gene namesi
Name:RSC9
Ordered Locus Names:YML127W
ORF Names:YM4987.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML127W.
SGDiS000004596. RSC9.

Subcellular locationi

GO - Cellular componenti

  • RSC complex Source: UniProtKB
  • SWI/SNF complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581Chromatin structure-remodeling complex subunit RSC9PRO_0000097475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03124.

PTM databases

iPTMnetiQ03124.

Interactioni

Subunit structurei

Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RSC8P436094EBI-27977,EBI-23005

Protein-protein interaction databases

BioGridi35078. 59 interactions.
DIPiDIP-4517N.
IntActiQ03124. 35 interactions.
MINTiMINT-502885.

Structurei

3D structure databases

ProteinModelPortaliQ03124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RSC9 family.Curated
Contains 1 RFX-type winged-helix DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000000742.
InParanoidiQ03124.
KOiK11763.
OMAiWLRCCFE.
OrthoDBiEOG7D2FRW.

Family and domain databases

InterProiIPR003150. DNA-bd_RFX.
[Graphical view]
PROSITEiPS51526. RFX_DBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03124-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSLASNTPL NGTPVSEAPA TSSEPVNMFE TMVANPIKVS RLQSNGVLTG
60 70 80 90 100
PAANTKSIHY SLANFNVFQS LPKETARGVD DLTRMEMALL SGIPEEIKWS
110 120 130 140 150
LKKYLTYSNK APYMISLRTL PDLLPLFKTF ILPLERIVEG LNKSSICDSK
160 170 180 190 200
AMDSLQMGLN ALLILRNLAQ DTDSVQILVK DREIKSFILF ILKKFQCVAT
210 220 230 240 250
GDNKWQLYEG NATFFNELTH YTLDLMEAIS SYIAPAMKDD HYFQTLVSIL
260 270 280 290 300
NYTKDRYMVI SILRSLSRLL VRSKANEESA ADNLDHKTLS LIVSFLLLEC
310 320 330 340 350
DSELIIASLD FLYQYILPGS QRITELFKSK ECSLILEATL PNLLSYNIAT
360 370 380 390 400
PDYHLLQKHK IRLIKRLKPP APKEPPNLSE DLFQQLFKLN EPLRSTAWLR
410 420 430 440 450
CCFEPVQEAE FTQISLWRSY ESKFGQPVRE SGRKLLPAVE FIKNVSNAFN
460 470 480 490 500
NAAAIVITDP VTGKKRFVIK GIQPRFKALG IADGERESQV PISALKSKFL
510 520 530 540 550
NDSKEITPAR QNSIPEVKFP QELSDVSKVA CTFLCLLSND TDDGAGSAFC
560 570 580
QRIRPLVLHK LADIPPLTLA LSEYMENTSG L
Length:581
Mass (Da):65,218
Last modified:November 1, 1997 - v1
Checksum:i04EA7901486656AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601Y → T AA sequence (PubMed:11931764).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50178 Genomic DNA. Translation: CAA90556.1.
BK006946 Genomic DNA. Translation: DAA09772.1.
PIRiS58201.
RefSeqiNP_013579.1. NM_001182490.1.

Genome annotation databases

EnsemblFungiiYML127W; YML127W; YML127W.
GeneIDi854912.
KEGGisce:YML127W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50178 Genomic DNA. Translation: CAA90556.1.
BK006946 Genomic DNA. Translation: DAA09772.1.
PIRiS58201.
RefSeqiNP_013579.1. NM_001182490.1.

3D structure databases

ProteinModelPortaliQ03124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35078. 59 interactions.
DIPiDIP-4517N.
IntActiQ03124. 35 interactions.
MINTiMINT-502885.

PTM databases

iPTMnetiQ03124.

Proteomic databases

MaxQBiQ03124.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML127W; YML127W; YML127W.
GeneIDi854912.
KEGGisce:YML127W.

Organism-specific databases

EuPathDBiFungiDB:YML127W.
SGDiS000004596. RSC9.

Phylogenomic databases

HOGENOMiHOG000000742.
InParanoidiQ03124.
KOiK11763.
OMAiWLRCCFE.
OrthoDBiEOG7D2FRW.

Enzyme and pathway databases

BioCyciYEAST:G3O-32705-MONOMER.

Miscellaneous databases

PROiQ03124.

Family and domain databases

InterProiIPR003150. DNA-bd_RFX.
[Graphical view]
PROSITEiPS51526. RFX_DBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The genome-wide localization of Rsc9, a component of the RSC chromatin-remodeling complex, changes in response to stress."
    Damelin M., Simon I., Moy T.I., Wilson B., Komili S., Tempst P., Roth F.P., Young R.A., Cairns B.R., Silver P.A.
    Mol. Cell 9:563-573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-73 AND 401-418, FUNCTION, IDENTIFICATION IN THE RSC COMPLEX, SUBCELLULAR LOCATION.
  4. Cited for: FUNCTION OF THE RSC COMPLEX, COMPOSITION OF THE RSC COMPLEX.
  5. "Histone octamer transfer by a chromatin-remodeling complex."
    Lorch Y., Zhang M., Kornberg R.D.
    Cell 96:389-392(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  6. "Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC."
    Moreira J.M.A., Holmberg S.
    EMBO J. 18:2836-2844(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  7. "Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains."
    Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D., Winston F.
    Mol. Cell 4:715-723(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPOSITION OF THE RSC COMPLEX.
  8. "Chromatin remodeling by RSC involves ATP-dependent DNA translocation."
    Saha A., Wittmeyer J., Cairns B.R.
    Genes Dev. 16:2120-2134(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  9. "Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway."
    Chai B., Hsu J.-M., Du J., Laurent B.C.
    Genetics 161:575-584(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  10. "The yeast RSC chromatin-remodeling complex is required for kinetochore function in chromosome segregation."
    Hsu J.-M., Huang J., Meluh P.B., Laurent B.C.
    Mol. Cell. Biol. 23:3202-3215(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, INTERACTION OF THE RSC COMPLEX WITH HISTONES.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structural analysis of the yeast SWI/SNF chromatin remodeling complex."
    Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L., Peterson C.L.
    Nat. Struct. Biol. 10:141-145(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, ELECTRON MICROSCOPY OF THE SWI/SNF COMPLEX.

Entry informationi

Entry nameiRSC9_YEAST
AccessioniPrimary (citable) accession number: Q03124
Secondary accession number(s): D6W0F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2610 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.