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Protein

Chromatin structure-remodeling complex protein RSC6

Gene

RSC6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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 is essential for mitotic growth and suppresses formamide sensitivity of the RSC8 mutants.7 Publications

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: UniProtKB
  2. G2/M transition of mitotic cell cycle Source: SGD
  3. nucleosome disassembly Source: SGD
  4. nucleosome positioning Source: SGD
  5. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29361-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin structure-remodeling complex protein RSC6
Alternative name(s):
Remodel the structure of chromatin complex subunit 6
Gene namesi
Name:RSC6
Ordered Locus Names:YCR052W
ORF Names:YCR52W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome III

Organism-specific databases

CYGDiYCR052w.
SGDiS000000648. RSC6.

Subcellular locationi

Nucleus 1 Publication
Note: Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.

GO - Cellular componenti

  1. RSC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Chromatin structure-remodeling complex protein RSC6PRO_0000097474Add
BLAST

Proteomic databases

MaxQBiP25632.
PaxDbiP25632.
PeptideAtlasiP25632.

Expressioni

Gene expression databases

GenevestigatoriP25632.

Interactioni

Subunit structurei

Interacts directly with RSC8. 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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RSC58Q079797EBI-21941,EBI-36549
RSC8P4360912EBI-21941,EBI-23005

Protein-protein interaction databases

BioGridi31032. 124 interactions.
DIPiDIP-4999N.
IntActiP25632. 48 interactions.
MINTiMINT-493435.
STRINGi4932.YCR052W.

Structurei

3D structure databases

ProteinModelPortaliP25632.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

To yeast SNF12.Curated

Phylogenomic databases

eggNOGiCOG5531.
GeneTreeiENSGT00730000114141.
HOGENOMiHOG000000860.
InParanoidiP25632.
KOiK11760.
OMAiLHESANG.
OrthoDBiEOG7X0VS9.

Family and domain databases

Gene3Di1.10.245.10. 2 hits.
InterProiIPR003121. SWIB_MDM2_domain.
[Graphical view]
SUPFAMiSSF47592. SSF47592. 2 hits.

Sequencei

Sequence statusi: Complete.

P25632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTQTNPVPV TYPTDAYIPT YLPDDKVSNL ADLKKLIEMD SRLDLYLTRR
60 70 80 90 100
RLDTSINLPT NTKTKDHPPN KEMLRIYVYN TTESSPRSDS GTPADSGKTT
110 120 130 140 150
WTLRIEGKLL HESANGKHPF SEFLEGVAVD FKRLKPLGMG KKRKRDSSLS
160 170 180 190 200
LPLNLQQPEY NDQDSTMGDN DNGEDEDSAE AESREEIVDA LEWNYDENNV
210 220 230 240 250
VEFDGIDIKR QGKDNLRCSI TIQLRGVDGG KVQYSPNLAT LIGMQTGSVN
260 270 280 290 300
DAVYSIYKYI LINNLFVTEQ TEAQDGSNDA EDSSNENNNK NGAGDDDGVE
310 320 330 340 350
GSTPKDKPEL GEVKLDSLLQ KVLDTNAAHL PLMNVVQTVN KLVSPLPPII
360 370 380 390 400
LDYTIDLSKD TTYGATTLDV DVSHILHQPQ PQPNLQKEEE TDAEDTAKLR
410 420 430 440 450
EITKLALQLN SSAQKYQFFH ELSLHPRETL THYLWSSKQN ELVLQGDQYF
460 470 480
NEDAARTSDI YSNNNNDRSL MGNISLLYSQ GRL
Length:483
Mass (Da):54,165
Last modified:May 1, 1992 - v1
Checksum:i6A9998BDBC4D24B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42283.1.
AY692985 Genomic DNA. Translation: AAT93004.1.
BK006937 Genomic DNA. Translation: DAA07529.1.
PIRiS19466.
RefSeqiNP_009981.1. NM_001178766.1.

Genome annotation databases

EnsemblFungiiYCR052W; YCR052W; YCR052W.
GeneIDi850419.
KEGGisce:YCR052W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42283.1.
AY692985 Genomic DNA. Translation: AAT93004.1.
BK006937 Genomic DNA. Translation: DAA07529.1.
PIRiS19466.
RefSeqiNP_009981.1. NM_001178766.1.

3D structure databases

ProteinModelPortaliP25632.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31032. 124 interactions.
DIPiDIP-4999N.
IntActiP25632. 48 interactions.
MINTiMINT-493435.
STRINGi4932.YCR052W.

Proteomic databases

MaxQBiP25632.
PaxDbiP25632.
PeptideAtlasiP25632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCR052W; YCR052W; YCR052W.
GeneIDi850419.
KEGGisce:YCR052W.

Organism-specific databases

CYGDiYCR052w.
SGDiS000000648. RSC6.

Phylogenomic databases

eggNOGiCOG5531.
GeneTreeiENSGT00730000114141.
HOGENOMiHOG000000860.
InParanoidiP25632.
KOiK11760.
OMAiLHESANG.
OrthoDBiEOG7X0VS9.

Enzyme and pathway databases

BioCyciYEAST:G3O-29361-MONOMER.

Miscellaneous databases

NextBioi965983.

Gene expression databases

GenevestigatoriP25632.

Family and domain databases

Gene3Di1.10.245.10. 2 hits.
InterProiIPR003121. SWIB_MDM2_domain.
[Graphical view]
SUPFAMiSSF47592. SSF47592. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: PROTEIN SEQUENCE OF 416-427, FUNCTION, COMPOSITION OF THE RSC COMPLEX.
  5. "Direct interaction between Rsc6 and Rsc8/Swh3, two proteins that are conserved in SWI/SNF-related complexes."
    Treich I., Ho L., Carlson M.
    Nucleic Acids Res. 26:3739-3745(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RSC8.
  6. "Histone octamer transfer by a chromatin-remodeling complex."
    Lorch Y., Zhang M., Kornberg R.D.
    Cell 96:389-392(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  7. "Transcriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC."
    Moreira J.M.A., Holmberg S.
    EMBO J. 18:2836-2844(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  8. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPOSITION OF THE RSC COMPLEX.
  9. "Chromatin remodeling by RSC involves ATP-dependent DNA translocation."
    Saha A., Wittmeyer J., Cairns B.R.
    Genes Dev. 16:2120-2134(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  10. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX.
  11. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, INTERACTION OF THE RSC COMPLEX WITH HISTONES.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRSC6_YEAST
AccessioniPrimary (citable) accession number: P25632
Secondary accession number(s): D6VR60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: March 4, 2015
This is version 107 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 2470 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

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 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.