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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
  • chromatin modification Source: UniProtKB-KW
  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00002112131 – 625Chromatin structure-remodeling complex subunit RSC4Add BLAST625

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei199PhosphoserineCombined sources1
Modified residuei545PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02206.
PRIDEiQ02206.

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. 140 interactors.
DIPiDIP-6639N.
IntActiQ02206. 124 interactors.
MINTiMINT-656919.

Structurei

Secondary structure

1625
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi47 – 50Combined sources4
Helixi58 – 72Combined sources15
Helixi74 – 77Combined sources4
Helixi78 – 80Combined sources3
Turni86 – 88Combined sources3
Helixi90 – 95Combined sources6
Helixi102 – 107Combined sources6
Helixi115 – 133Combined sources19
Beta strandi136 – 138Combined sources3
Helixi139 – 159Combined sources21
Helixi160 – 163Combined sources4
Helixi169 – 184Combined sources16
Helixi187 – 195Combined sources9
Helixi196 – 198Combined sources3
Beta strandi205 – 207Combined sources3
Helixi211 – 213Combined sources3
Turni219 – 221Combined sources3
Helixi223 – 228Combined sources6
Helixi235 – 244Combined sources10
Helixi250 – 267Combined sources18
Helixi273 – 291Combined sources19
Helixi293 – 302Combined sources10
Turni313 – 318Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ02206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 141Bromo 1PROSITE-ProRule annotationAdd BLAST70
Domaini205 – 275Bromo 2PROSITE-ProRule annotationAdd BLAST71

Sequence similaritiesi

Contains 2 bromo domains.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

HOGENOMiHOG000142075.
InParanoidiQ02206.
KOiK11759.
OMAiLPSRKFH.
OrthoDBiEOG092C3W5G.

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)DescriptionActionsGraphical viewLength
Sequence conflicti390K → I in CAA46244 (PubMed:1441752).Curated1
Sequence conflicti390K → I in CAA82078 (PubMed:8196765).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R0SX-ray1.80A36-320[»]
2R0VX-ray2.35A/B/C1-340[»]
2R0YX-ray1.75A36-340[»]
2R10X-ray2.20A/B1-340[»]
ProteinModelPortaliQ02206.
SMRiQ02206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34140. 140 interactors.
DIPiDIP-6639N.
IntActiQ02206. 124 interactors.
MINTiMINT-656919.

PTM databases

iPTMnetiQ02206.

Proteomic databases

MaxQBiQ02206.
PRIDEiQ02206.

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.
OrthoDBiEOG092C3W5G.

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...

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: November 2, 2016
This is version 156 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.