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Protein

Chromatin structure-remodeling complex protein RSC3

Gene

RSC3

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 is required for transcription of ribosomal protein genes and genes involved in the integrity of the cell wall, and also for proper metaphase progression. Together with HTL1, LDB7, NPL6, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi14 – 4229Zn(2)-C6 fungal-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29863-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin structure-remodeling complex protein RSC3
Alternative name(s):
Remodel the structure of chromatin complex subunit 3
Gene namesi
Name:RSC3
Ordered Locus Names:YDR303C
ORF Names:D9740.13
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR303C.
SGDiS000002711. RSC3.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141C → G: Complete inactivation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 885885Chromatin structure-remodeling complex protein RSC3PRO_0000114973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951PhosphoserineCombined sources
Modified residuei236 – 2361PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06639.
PRIDEiQ06639.

PTM databases

iPTMnetiQ06639.

Interactioni

Subunit structurei

Forms a heteromer with RSC30. Interacts with LDB7 and NPL6. 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. Component of a fungal-specific module (HTL1-LDB7-NPL6-RSC3-RSC30) within the RSC complex.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RSC30P387815EBI-22058,EBI-24549

Protein-protein interaction databases

BioGridi32355. 64 interactions.
DIPiDIP-5867N.
IntActiQ06639. 69 interactions.
MINTiMINT-648493.

Structurei

3D structure databases

ProteinModelPortaliQ06639.
SMRiQ06639. Positions 13-44.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000074705.
InParanoidiQ06639.
KOiK11758.
OMAiDIRGRKM.
OrthoDBiEOG74TX72.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06639-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIRGRKMKK PPACVQCRKR KIGCDRVKPI CGNCMKHNKM DCFYPDVPGQ
60 70 80 90 100
YVPSSSSSSN TRQVANGPYL NSYYASRRVS KETAALLQKN PELASLEQIR
110 120 130 140 150
EYNTRLQLLN AQNQLNNRSS AANATLNQQH TQYIPKSVPS LESKPVTSAN
160 170 180 190 200
ESSTPLNWVQ GPAIFHMLTS PYTQDEIINH EMNFLKGRLL ELQEITGKKI
210 220 230 240 250
TGVNLDLKQD SSAQMQSSHS NRNQEEFLTI KKRKLSEDGV TDGDGKPIPE
260 270 280 290 300
SERRPHLNEF KDLDPQFLDT NKVFNVFNSA ISEEGRNRLW LLPKNINKSS
310 320 330 340 350
IFQIQYLIER DPFLFKFFND LNILIETQFN GPLHDLVASR NSIERNSGIS
360 370 380 390 400
QILKFPSQSI TQTLINKYLS TITETNSILP ILKPKRLLPI VEQLFPSNTI
410 420 430 440 450
NKPNSKDFET IFQVFSVTND QLLNLGFITL CLLILFESLN STVLIPLRDD
460 470 480 490 500
EHLQLFNVLF NYLPLLKSNL TTLRFEIEKR SMCNIETLRF ISLWKYYQFV
510 520 530 540 550
MDTSSSSSFV IDYDEDMHMA CLLSLNHETQ NQSHILTWNF IFKNYCWRHL
560 570 580 590 600
FLGQLPLLMS EPFTNSTPII DPLLNNDFEL IDFEVNLMKY LQSKDQQLSI
610 620 630 640 650
DKIIQLIKLL KNKNIEVSQG CLTTPSIINN IMDSLIYRNS MLYLNFYLLL
660 670 680 690 700
QFETLKNYAK FNEILEDFLE LSRETLFFVF SNLANIKFAG HEFTFINKSI
710 720 730 740 750
VVLQTLVLML LALYQRSFDS SKRTNDANEI SEQTDIHSNN DNSKRIKNKN
760 770 780 790 800
VIHLIINKIA MLLSDYTKNC KKQNKLIENL IIKIKTISKY IKNLEENKVT
810 820 830 840 850
TSADSNYSIN NGFSGISAEQ LIKLNHELSK ISESLIKTDF YEQRKNSTVS
860 870 880
NGVLGAAAPV DSDANSDTFG LTKENFNEVF EAIRS
Length:885
Mass (Da):101,720
Last modified:November 1, 1996 - v1
Checksum:i2DB1D529E2686A0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64739.1.
BK006938 Genomic DNA. Translation: DAA12142.1.
PIRiS61189.
RefSeqiNP_010589.3. NM_001180611.3.

Genome annotation databases

EnsemblFungiiYDR303C; YDR303C; YDR303C.
GeneIDi851897.
KEGGisce:YDR303C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28374 Genomic DNA. Translation: AAB64739.1.
BK006938 Genomic DNA. Translation: DAA12142.1.
PIRiS61189.
RefSeqiNP_010589.3. NM_001180611.3.

3D structure databases

ProteinModelPortaliQ06639.
SMRiQ06639. Positions 13-44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32355. 64 interactions.
DIPiDIP-5867N.
IntActiQ06639. 69 interactions.
MINTiMINT-648493.

PTM databases

iPTMnetiQ06639.

Proteomic databases

MaxQBiQ06639.
PRIDEiQ06639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR303C; YDR303C; YDR303C.
GeneIDi851897.
KEGGisce:YDR303C.

Organism-specific databases

EuPathDBiFungiDB:YDR303C.
SGDiS000002711. RSC3.

Phylogenomic databases

HOGENOMiHOG000074705.
InParanoidiQ06639.
KOiK11758.
OMAiDIRGRKM.
OrthoDBiEOG74TX72.

Enzyme and pathway databases

BioCyciYEAST:G3O-29863-MONOMER.

Miscellaneous databases

PROiQ06639.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [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. "A Rsc3/Rsc30 zinc cluster dimer reveals novel roles for the chromatin remodeler RSC in gene expression and cell cycle control."
    Angus-Hill M.L., Schlichter A., Roberts D., Erdjument-Bromage H., Tempst P., Cairns B.R.
    Mol. Cell 7:741-751(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 137-151, IDENTIFICATION IN THE RSC COMPLEX, FUNCTION OF THE RSC COMPLEX, HETEROMERIC COMPLEX FORMATION WITH RSC30, MUTAGENESIS OF CYS-14.
  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. "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: FUNCTION, INTERACTION WITH LDB7 AND NPL6.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  14. "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-95 AND SER-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRSC3_YEAST
AccessioniPrimary (citable) accession number: Q06639
Secondary accession number(s): D6VST2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 148 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 1750 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.