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Protein

Histone chaperone RTT106

Gene

RTT106

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

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

GO - Molecular functioni

  • double-stranded DNA binding Source: SGD
  • histone binding Source: SGD

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 from RNA polymerase II promoter Source: SGD
  • transcription elongation from RNA polymerase II promoter Source: SGD
  • transposition Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Transcription, Transcription regulation, Transposition

Keywords - Ligandi

DNA-binding

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

GO - Cellular componenti

Complete GO annotation...

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.
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

WithEntry#Exp.IntActNotes
ASF1P324475EBI-29119,EBI-3003
SIR4P119782EBI-29119,EBI-17237

GO - Molecular functioni

  • histone binding Source: SGD

Protein-protein interaction databases

BioGridi35630. 150 interactors.
DIPiDIP-4292N.
IntActiP40161. 56 interactors.
MINTiMINT-521994.

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
Contains 2 PH domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000066074.
InParanoidiP40161.
OMAiTRLTFNV.
OrthoDBiEOG092C40DW.

Family and domain databases

InterProiIPR013719. DUF1747.
IPR011993. PH_dom-like.
[Graphical view]
PfamiPF08512. Rtt106. 1 hit.
[Graphical view]
SMARTiSM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi35630. 150 interactors.
DIPiDIP-4292N.
IntActiP40161. 56 interactors.
MINTiMINT-521994.

PTM databases

iPTMnetiP40161.

Proteomic databases

MaxQBiP40161.
PRIDEiP40161.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL206C; YNL206C; YNL206C.
GeneIDi855515.
KEGGisce:YNL206C.

Organism-specific databases

EuPathDBiFungiDB:YNL206C.
SGDiS000005150. RTT106.

Phylogenomic databases

HOGENOMiHOG000066074.
InParanoidiP40161.
OMAiTRLTFNV.
OrthoDBiEOG092C40DW.

Enzyme and pathway databases

BioCyciYEAST:G3O-33212-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40161.
PROiP40161.

Family and domain databases

InterProiIPR013719. DUF1747.
IPR011993. PH_dom-like.
[Graphical view]
PfamiPF08512. Rtt106. 1 hit.
[Graphical view]
SMARTiSM01287. Rtt106. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRT106_YEAST
AccessioniPrimary (citable) accession number: P40161
Secondary accession number(s): D6W0Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 130 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 11100 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.