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Protein

Histone chaperone RTT106

Gene

RTT106

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.12 Publications

Miscellaneous

Present with 11100 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • double-stranded DNA binding Source: SGD
  • histone binding Source: SGD
  • identical protein binding Source: IntAct

GO - Biological processi

  • DNA replication-dependent nucleosome assembly Source: SGD
  • DNA replication-independent nucleosome assembly Source: SGD
  • heterochromatin assembly involved in chromatin silencing Source: SGD
  • negative regulation of transcription by RNA polymerase II Source: SGD
  • transcription elongation from RNA polymerase II promoter Source: SGD
  • transposition Source: UniProtKB-KW

Keywordsi

Molecular functionChaperone, DNA-binding
Biological processTranscription, Transcription regulation, Transposition

Enzyme and pathway databases

BioCyciYEAST:G3O-33212-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Histone chaperone RTT106
Alternative name(s):
Regulator of Ty1 transposition protein 106
Gene namesi
Name:RTT106
Ordered Locus Names:YNL206C
ORF Names:N1346
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL206C
SGDiS000005150 RTT106

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi259I → A: Decreases histone-binding. 1 Publication1
Mutagenesisi261Y → A: Impairs histone-binding. 1 Publication1
Mutagenesisi269F → A: Impairs histone-binding. 1 Publication1
Mutagenesisi288Q → A: Decreases histone-binding. 1 Publication1
Mutagenesisi291Y → A: Impairs histone-binding. 1
Mutagenesisi294I → A: Impairs histone-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002033922 – 455Histone chaperone RTT106Add BLAST454

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei408PhosphoserineCombined sources1
Modified residuei411PhosphoserineCombined sources1
Modified residuei450PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP40161
PaxDbiP40161
PRIDEiP40161

PTM databases

iPTMnetiP40161

Interactioni

Subunit structurei

Homodimers (via the N-terminal domain). Interacts with the SWI/SNF, RSC and HIR complexes. Interacts with RLF2, SIR4, YTA7 and histones H3 and H4.8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • histone binding Source: SGD
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi35630, 169 interactors
DIPiDIP-4292N
IntActiP40161, 56 interactors
MINTiP40161
STRINGi4932.YNL206C

Structurei

Secondary structure

1455
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Helixi11 – 21Combined sources11
Helixi27 – 41Combined sources15
Beta strandi60 – 63Combined sources4
Beta strandi71 – 85Combined sources15
Beta strandi87 – 95Combined sources9
Turni97 – 99Combined sources3
Beta strandi102 – 108Combined sources7
Beta strandi111 – 116Combined sources6
Helixi119 – 122Combined sources4
Beta strandi123 – 130Combined sources8
Beta strandi137 – 145Combined sources9
Helixi148 – 150Combined sources3
Beta strandi156 – 161Combined sources6
Helixi162 – 171Combined sources10
Helixi183 – 195Combined sources13
Beta strandi220 – 235Combined sources16
Beta strandi237 – 247Combined sources11
Beta strandi249 – 252Combined sources4
Helixi253 – 255Combined sources3
Beta strandi256 – 263Combined sources8
Beta strandi266 – 275Combined sources10
Beta strandi280 – 287Combined sources8
Helixi288 – 290Combined sources3
Helixi291 – 299Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LH0NMR-A/B1-67[»]
3FSSX-ray1.43A68-301[»]
3GYOX-ray3.10A65-320[»]
3GYPX-ray2.41A65-320[»]
3TO1X-ray2.60A/B69-300[»]
3TVVX-ray2.59A/B68-315[»]
3TW1X-ray1.77A68-301[»]
ProteinModelPortaliP40161
SMRiP40161
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40161

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 200PH 1Add BLAST133
Domaini217 – 301PH 2Add BLAST85

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 67Dimeric regionAdd BLAST66
Regioni68 – 301Double PH domainAdd BLAST234
Regioni315 – 455Disordered acidic regionAdd BLAST141

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi351 – 448Asp/Glu-richAdd BLAST98

Domaini

The N-ter domain (residues 1-67) homodimerizes and interacts with H3-H4 independently of acetylation while the double pleckstrin-homology (PH) domain (residues 68-301) binds the 'Lys-56'-containing region of H3.1 Publication

Sequence similaritiesi

Belongs to the RTT106 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000066074
InParanoidiP40161
OMAiTRLTFNV
OrthoDBiEOG092C40DW

Family and domain databases

Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR013719 DUF1747
IPR011993 PH-like_dom_sf
PfamiView protein in Pfam
PF08512 Rtt106, 1 hit
SMARTiView protein in SMART
SM01287 Rtt106, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLFLDELP ESLSRKIGTV VRVLPSSLEI FEELYKYALN ENSNDRSGRH
60 70 80 90 100
KKPRIDVSSD LLKTDEISET NTIFKLEGVS VLSPLRKKLD LVFYLSNVDG
110 120 130 140 150
SPVITLLKGN DRELSIYQLN KNIKMASFLP VPEKPNLIYL FMTYTSCEDN
160 170 180 190 200
KFSEPVVMTL NKENTLNQFK NLGLLDSNVT DFEKCVEYIR KQAILTGFKI
210 220 230 240 250
SNPFVNSTLV DTDAEKINSF HLQCHRGTKE GTLYFLPDHI IFGFKKPILL
260 270 280 290 300
FDASDIESIT YSSITRLTFN ASLVTKDGEK YEFSMIDQTE YAKIDDYVKR
310 320 330 340 350
KQMKDKSMSE ELKAKSKSKG QATDGTADQP SILQEATRQM QDEKKAGVFS
360 370 380 390 400
DDDEENDQNF EAESDLSDGS GQESSDGAED GEEAEEDDEE DDEEEDKKGQ
410 420 430 440 450
SALNRDNSFA SINGQPEQEL QYKEFKEPLE LEDIPIEIDN DDDEDDEDGS

GVEYD
Length:455
Mass (Da):51,621
Last modified:February 1, 1995 - v1
Checksum:i79CACA659A7F4F4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78898 Genomic DNA Translation: CAA55502.1
Z71482 Genomic DNA Translation: CAA96106.1
BK006947 Genomic DNA Translation: DAA10350.1
PIRiS50725
RefSeqiNP_014193.1, NM_001183044.1

Genome annotation databases

EnsemblFungiiYNL206C; YNL206C; YNL206C
GeneIDi855515
KEGGisce:YNL206C

Similar proteinsi

Entry informationi

Entry nameiRT106_YEAST
AccessioniPrimary (citable) accession number: P40161
Secondary accession number(s): D6W0Y4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health