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P25632 (RSC6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromatin structure-remodeling complex protein RSC6
Alternative name(s):
Remodel the structure of chromatin complex subunit 6
Gene names
Name:RSC6
Ordered Locus Names:YCR052W
ORF Names:YCR52W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11

Subunit structure

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. Ref.5 Ref.11

Subcellular location

Nucleus. Note: Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1. Ref.11

Miscellaneous

Present with 2470 molecules/cell in log phase SD medium.

Sequence similarities

To yeast SNF12.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSC58Q079797EBI-21941,EBI-36549
RSC8P4360912EBI-21941,EBI-23005

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Chromatin structure-remodeling complex protein RSC6
PRO_0000097474

Sequences

Sequence LengthMass (Da)Tools
P25632 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 6A9998BDBC4D24B2

FASTA48354,165
        10         20         30         40         50         60 
MVTQTNPVPV TYPTDAYIPT YLPDDKVSNL ADLKKLIEMD SRLDLYLTRR RLDTSINLPT 

        70         80         90        100        110        120 
NTKTKDHPPN KEMLRIYVYN TTESSPRSDS GTPADSGKTT WTLRIEGKLL HESANGKHPF 

       130        140        150        160        170        180 
SEFLEGVAVD FKRLKPLGMG KKRKRDSSLS LPLNLQQPEY NDQDSTMGDN DNGEDEDSAE 

       190        200        210        220        230        240 
AESREEIVDA LEWNYDENNV VEFDGIDIKR QGKDNLRCSI TIQLRGVDGG KVQYSPNLAT 

       250        260        270        280        290        300 
LIGMQTGSVN DAVYSIYKYI LINNLFVTEQ TEAQDGSNDA EDSSNENNNK NGAGDDDGVE 

       310        320        330        340        350        360 
GSTPKDKPEL GEVKLDSLLQ KVLDTNAAHL PLMNVVQTVN KLVSPLPPII LDYTIDLSKD 

       370        380        390        400        410        420 
TTYGATTLDV DVSHILHQPQ PQPNLQKEEE TDAEDTAKLR EITKLALQLN SSAQKYQFFH 

       430        440        450        460        470        480 
ELSLHPRETL THYLWSSKQN ELVLQGDQYF NEDAARTSDI YSNNNNDRSL MGNISLLYSQ 


GRL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"RSC, an essential, abundant chromatin-remodeling complex."
Cairns B.R., Lorch Y., Li Y., Zhang M., Lacomis L., Erdjument-Bromage H., Tempst P., Du J., Laurent B.C., Kornberg R.D.
Cell 87:1249-1260(1996) [PubMed] [Europe PMC] [Abstract]
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(1998) [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(1999) [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(1999) [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(1999) [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(2002) [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(2002) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE RSC COMPLEX, SUBCELLULAR LOCATION, INTERACTION OF THE RSC COMPLEX WITH HISTONES.
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAA42283.1.
AY692985 Genomic DNA. Translation: AAT93004.1.
BK006937 Genomic DNA. Translation: DAA07529.1.
PIRS19466.
RefSeqNP_009981.1. NM_001178766.1.

3D structure databases

ProteinModelPortalP25632.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31032. 123 interactions.
DIPDIP-4999N.
IntActP25632. 48 interactions.
MINTMINT-493435.
STRING4932.YCR052W.

Proteomic databases

PaxDbP25632.
PeptideAtlasP25632.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR052W; YCR052W; YCR052W.
GeneID850419.
KEGGsce:YCR052W.

Organism-specific databases

CYGDYCR052w.
SGDS000000648. RSC6.

Phylogenomic databases

eggNOGCOG5531.
GeneTreeENSGT00730000114141.
HOGENOMHOG000000860.
KOK11760.
OMALHESANG.
OrthoDBEOG7X0VS9.

Enzyme and pathway databases

BioCycYEAST:G3O-29361-MONOMER.

Gene expression databases

GenevestigatorP25632.

Family and domain databases

Gene3D1.10.245.10. 2 hits.
InterProIPR003121. SWIB_MDM2_domain.
[Graphical view]
SUPFAMSSF47592. SSF47592. 2 hits.
ProtoNetSearch...

Other

NextBio965983.

Entry information

Entry nameRSC6_YEAST
AccessionPrimary (citable) accession number: P25632
Secondary accession number(s): D6VR60
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD