Q07979 · RSC58_YEAST

Function

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.

Miscellaneous

Present with 4460 molecules/cell in log phase SD medium.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentnucleus
Cellular ComponentRSC-type complex
Biological Processchromatin remodeling
Biological Processnucleosome disassembly
Biological Processregulation of transcription by RNA polymerase II
Biological Processtranscription elongation by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chromatin structure-remodeling complex protein RSC58
  • Alternative names
    • Remodel the structure of chromatin complex subunit 58

Gene names

    • Name
      RSC58
    • Ordered locus names
      YLR033W

Organism names

Accessions

  • Primary accession
    Q07979
  • Secondary accessions
    • D6VY35

Proteomes

Organism-specific databases

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000974731-502Chromatin structure-remodeling complex protein RSC58

Proteomic databases

PTM databases

Interaction

Subunit

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.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q07979RSC6 P256328EBI-36549, EBI-21941
BINARY Q07979STH1 P325977EBI-36549, EBI-18410
View interactors in UniProtKB
View CPX-1888 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias336-350Basic and acidic residues
Region336-378Disordered
Compositional bias351-378Polar residues

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    502
  • Mass (Da)
    57,794
  • Last updated
    1996-11-01 v1
  • Checksum
    8F8D01184DAE1F6F
MTESVGGNKLVDFLVNVQSILNAASVKCHVVDESFPAKFFEKNPDKIYESYCKFIKNRSNSEGLIRNEDKLVLTTINKRFENGEYEPIQGGFYKLYHDIKLVCTILIHFYPQGTRNYQLVDKFYKFSSELLLRECCRIGIALTQTNNIKSRSGKLLSGNEMDEYDDDDATELDKIISYDFIKISMNYTVPISQTYQIRTKDMDLFSSIISKSNLDKRPHELPNTNFKINNVLPQTDIENEAPRLGFVGANTSNIPDPTLPPTEMMTRFLHPNWYALPTTVWLKYGNYNSWAPSFNENGTVVDSTTRGLIWLERIGYMDLYEKNEKKVKQEELLNTNEEGINRKQNDENNKNVDGKSNGVQDDGGDNDNDATIASANSESTENKEQFIIKLQNLYNWTPSNYIGDDEIENFRNGTPDKLVSDSLLKLKRLRKERILNKVLKPTTEERELYFKVKRILKEVILAKKVSKVPINNVRAFPVLQTNYNGSIPVVRAQPGRKRKHKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias336-350Basic and acidic residues
Compositional bias351-378Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z73205
EMBL· GenBank· DDBJ
CAA97557.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006945
EMBL· GenBank· DDBJ
DAA09351.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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