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P43609 (RSC8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 RSC8
Alternative name(s):
Remodel the structure of chromatin complex subunit 8
SWI3 homolog
Gene names
Name:RSC8
Synonyms:SWH3
Ordered Locus Names:YFR037C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length557 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 for repression of CHA1 expression. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Dimerizes via the C-terminal coiled coil. Interacts directly with HTL1, NPL6, RSC6 and the N-terminus of STH1. 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.6 Ref.11 Ref.14 Ref.16 Ref.17

Subcellular location

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

Miscellaneous

Present with 3380 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 SANT domain.

Contains 1 SWIRM domain.

Contains 1 ZZ-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Chromatin structure-remodeling complex protein RSC8
PRO_0000197114

Regions

Domain80 – 17798SWIRM
Domain310 – 36253SANT
Zinc finger254 – 29845ZZ-type
Coiled coil38 – 7740 Potential
Coiled coil462 – 49433 Potential

Amino acid modifications

Modified residue4851Phosphoserine Ref.18

Experimental info

Mutagenesis347 – 3515Missing: Loss of function. Ref.15
Sequence conflict1921D → G in AAT92860. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P43609 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D3D3120397CF0058

FASTA55763,168
        10         20         30         40         50         60 
MSDTEKDKDV PMVDSHEATE EPPTTSTNTP SFPHLAQEQA KEESATLGAE VAHKKINYEQ 

        70         80         90        100        110        120 
EAQKLEEKAL RFLAKQTHPV IIPSFASWFD ISKIHEIEKR SNPDFFNDSS RFKTPKAYKD 

       130        140        150        160        170        180 
TRNFIINTYR LSPYEYLTIT AVRRNVAMDV ASIVKIHAFL EKWGLINYQI DPRTKPSLIG 

       190        200        210        220        230        240 
PSFTGHFQVV LDTPQGLKPF LPENVIKQEV EGGDGAEPQV KKEFPVNLTI KKNVYDSAQD 

       250        260        270        280        290        300 
FNALQDESRN SRQIHKVYIC HTCGNESINV RYHNLRARDT NLCSRCFQEG HFGANFQSSD 

       310        320        330        340        350        360 
FIRLENNGNS VKKNWSDQEM LLLLEGIEMY EDQWEKIADH VGGHKRVEDC IEKFLSLPIE 

       370        380        390        400        410        420 
DNYIREVVGS TLNGKGGDSR DGSVSGSKLM ECVNDAVQTL LQGDDKLGKV SDKSREISEK 

       430        440        450        460        470        480 
YIEESQAIIQ ELVKLTMEKL ESKFTKLCDL ETQLEMEKLK YVKESEKMLN DRLSLSKQIL 

       490        500        510        520        530        540 
DLNKSLEELN VSKKLVLISE QVDSGIQLVE KDQEGDDEDG NTATGHGVKR VGKEGEEVGE 

       550 
GDSIAKLQPQ VYKPWSL 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [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]"Fifteen open reading frames in a 30.8 kb region of the right arm of chromosome VI from Saccharomyces cerevisiae."
Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H., Hanaoka F., Murakami Y.
Yeast 12:177-190(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"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.
[5]"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 233-249, FUNCTION OF THE RSC COMPLEX, COMPOSITION OF THE RSC COMPLEX.
[6]"Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-related complex with an essential function in Saccharomyces cerevisiae."
Treich I., Carlson M.
Mol. Cell. Biol. 17:1768-1775(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH STH1.
[7]"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.
[8]"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.
[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]"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.
[14]"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: INTERACTION WITH RSC6.
[15]"Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes."
Boyer L.A., Langer M.R., Crowley K.A., Tan S., Denu J.M., Peterson C.L.
Mol. Cell 10:935-942(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 347-VAL--ILE-351.
[16]"Dissecting the pet18 mutation in Saccharomyces cerevisiae: HTL1 encodes a 7-kDa polypeptide that interacts with components of the RSC complex."
Lu Y.-M., Lin Y.-R., Tsai A., Hsao Y.-S., Li C.-C., Cheng M.Y.
Mol. Genet. Genomics 269:321-330(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTL1.
[17]"The RSC chromatin remodeling complex bears an essential fungal-specific protein module with broad functional roles."
Wilson B., Erdjument-Bromage H., Tempst P., Cairns B.R.
Genetics 172:795-809(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPL6.
[18]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50617 Genomic DNA. Translation: BAA09276.1.
AY692841 Genomic DNA. Translation: AAT92860.1.
BK006940 Genomic DNA. Translation: DAA12480.1.
PIRS56292.
RefSeqNP_116695.3. NM_001180002.3.

3D structure databases

ProteinModelPortalP43609.
SMRP43609. Positions 86-170, 309-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31195. 158 interactions.
DIPDIP-1478N.
IntActP43609. 93 interactions.
MINTMINT-401637.
STRING4932.YFR037C.

Proteomic databases

PaxDbP43609.
PeptideAtlasP43609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFR037C; YFR037C; YFR037C.
GeneID850598.
KEGGsce:YFR037C.

Organism-specific databases

CYGDYFR037c.
SGDS000001933. RSC8.

Phylogenomic databases

eggNOGCOG5259.
HOGENOMHOG000246692.
KOK11762.
OMAKTPKAYK.
OrthoDBEOG7ZWDBR.

Enzyme and pathway databases

BioCycYEAST:G3O-30484-MONOMER.

Gene expression databases

GenevestigatorP43609.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
IPR000433. Znf_ZZ.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966460.

Entry information

Entry nameRSC8_YEAST
AccessionPrimary (citable) accession number: P43609
Secondary accession number(s): D6VTS0, Q6B289
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 136 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 VI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families