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Protein

Chromatin structure-remodeling complex subunit RSC4

Gene

RSC4

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.6 Publications

GO - Molecular functioni

  • lysine-acetylated histone binding Source: SGD

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • nucleosome disassembly Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-31986-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin structure-remodeling complex subunit RSC4
Alternative name(s):
RSC complex subunit RSC4
Remodel the structure of chromatin complex subunit 4
Gene namesi
Name:RSC4
Ordered Locus Names:YKR008W
ORF Names:YK107
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR008W.
SGDiS000001716. RSC4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 625625Chromatin structure-remodeling complex subunit RSC4PRO_0000211213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991PhosphoserineCombined sources
Modified residuei545 – 5451PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02206.
PeptideAtlasiQ02206.

PTM databases

iPTMnetiQ02206.

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.

GO - Molecular functioni

  • lysine-acetylated histone binding Source: SGD

Protein-protein interaction databases

BioGridi34140. 138 interactions.
DIPiDIP-6639N.
IntActiQ02206. 124 interactions.
MINTiMINT-656919.

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 504Combined sources
Helixi58 – 7215Combined sources
Helixi74 – 774Combined sources
Helixi78 – 803Combined sources
Turni86 – 883Combined sources
Helixi90 – 956Combined sources
Helixi102 – 1076Combined sources
Helixi115 – 13319Combined sources
Beta strandi136 – 1383Combined sources
Helixi139 – 15921Combined sources
Helixi160 – 1634Combined sources
Helixi169 – 18416Combined sources
Helixi187 – 1959Combined sources
Helixi196 – 1983Combined sources
Beta strandi205 – 2073Combined sources
Helixi211 – 2133Combined sources
Turni219 – 2213Combined sources
Helixi223 – 2286Combined sources
Helixi235 – 24410Combined sources
Helixi250 – 26718Combined sources
Helixi273 – 29119Combined sources
Helixi293 – 30210Combined sources
Turni313 – 3186Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R0SX-ray1.80A36-320[»]
2R0VX-ray2.35A/B/C1-340[»]
2R0YX-ray1.75A36-340[»]
2R10X-ray2.20A/B1-340[»]
ProteinModelPortaliQ02206.
SMRiQ02206. Positions 37-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 14170Bromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini205 – 27571Bromo 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 bromo domains.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

HOGENOMiHOG000142075.
InParanoidiQ02206.
KOiK11759.
OMAiLPSRKFH.
OrthoDBiEOG7MD50F.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
[Graphical view]
PfamiPF00439. Bromodomain. 2 hits.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVKKRKLAT EAGGSDERPK YLPGKHPKNQ EKTPHVDYNA PLNPKSELFL
60 70 80 90 100
DDWHIPKFNR FISFTLDVLI DKYKDIFKDF IKLPSRKFHP QYYYKIQQPM
110 120 130 140 150
SINEIKSRDY EYEDGPSNFL LDVELLTKNC QAYNEYDSLI VKNSMQVVML
160 170 180 190 200
IEFEVLKAKN LKRNYLINSE VKAKLLHYLN KLVDATEKKI NQALLGASSP
210 220 230 240 250
KNLDDKVKLS EPFMELVDKD ELPEYYEIVH SPMALSIVKQ NLEIGQYSKI
260 270 280 290 300
YDFIIDMLLV FQNAHIFNDP SALIYKDATT LTNYFNYLIQ KEFFPELQDL
310 320 330 340 350
NERGEINLEF DKFEFENYLA IGGGGPAAAG ALAISALDND IEPESNREDL
360 370 380 390 400
IDQADYDFNH FEGLGNGYNR SLLTEDYLLN PNNFKKLIAK PETVQSEVKN
410 420 430 440 450
ERSTTSDIEK TNSLESEHLK IPKYNVIKSM QKEMQSLSEQ HTMEYKPYKL
460 470 480 490 500
IQQIYIFSSK NLYSQATKPL LGSRPSCNQN WVEYIFNGNE LSQNENAFSF
510 520 530 540 550
MLQPMQTFLT LQSHLTSSLK DTETLLTINK EPVKSRTSNV NSNLSQPQQQ
560 570 580 590 600
ENDVIGNDTK QDIENLTIGG GNNNDIVGND NDKRNNITEI FDIRLSEGLN
610 620
HLMFRCEDKI SHETEFMNFW INVLP
Length:625
Mass (Da):72,291
Last modified:September 21, 2011 - v2
Checksum:iB25614F50FA0D108
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3901K → I in CAA46244 (PubMed:1441752).Curated
Sequence conflicti390 – 3901K → I in CAA82078 (PubMed:8196765).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65124 Genomic DNA. Translation: CAA46244.1.
Z28233 Genomic DNA. Translation: CAA82078.1.
AY693123 Genomic DNA. Translation: AAT93142.1.
BK006944 Genomic DNA. Translation: DAA09164.2.
PIRiS34035.
RefSeqiNP_012933.4. NM_001179798.4.

Genome annotation databases

EnsemblFungiiYKR008W; YKR008W; YKR008W.
GeneIDi853877.
KEGGisce:YKR008W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65124 Genomic DNA. Translation: CAA46244.1.
Z28233 Genomic DNA. Translation: CAA82078.1.
AY693123 Genomic DNA. Translation: AAT93142.1.
BK006944 Genomic DNA. Translation: DAA09164.2.
PIRiS34035.
RefSeqiNP_012933.4. NM_001179798.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R0SX-ray1.80A36-320[»]
2R0VX-ray2.35A/B/C1-340[»]
2R0YX-ray1.75A36-340[»]
2R10X-ray2.20A/B1-340[»]
ProteinModelPortaliQ02206.
SMRiQ02206. Positions 37-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34140. 138 interactions.
DIPiDIP-6639N.
IntActiQ02206. 124 interactions.
MINTiMINT-656919.

PTM databases

iPTMnetiQ02206.

Proteomic databases

MaxQBiQ02206.
PeptideAtlasiQ02206.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR008W; YKR008W; YKR008W.
GeneIDi853877.
KEGGisce:YKR008W.

Organism-specific databases

EuPathDBiFungiDB:YKR008W.
SGDiS000001716. RSC4.

Phylogenomic databases

HOGENOMiHOG000142075.
InParanoidiQ02206.
KOiK11759.
OMAiLPSRKFH.
OrthoDBiEOG7MD50F.

Enzyme and pathway databases

BioCyciYEAST:G3O-31986-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ02206.
PROiQ02206.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
[Graphical view]
PfamiPF00439. Bromodomain. 2 hits.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open reading frames."
    Duesterhoeft A., Philippsen P.
    Yeast 8:749-759(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 390.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: FUNCTION OF THE RSC COMPLEX, COMPOSITION OF THE RSC COMPLEX.
  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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  14. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  15. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRSC4_YEAST
AccessioniPrimary (citable) accession number: Q02206
Secondary accession number(s): D6VX74, Q6B1F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 21, 2011
Last modified: June 8, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8570 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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