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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi259 – 2591I → A: Decreases histone-binding. 1 Publication
Mutagenesisi261 – 2611Y → A: Impairs histone-binding. 1 Publication
Mutagenesisi269 – 2691F → A: Impairs histone-binding. 1 Publication
Mutagenesisi288 – 2881Q → A: Decreases histone-binding. 1 Publication
Mutagenesisi291 – 2911Y → A: Impairs histone-binding.
Mutagenesisi294 – 2941I → A: Impairs histone-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 455454Histone chaperone RTT106PRO_0000203392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei408 – 4081PhosphoserineCombined sources
Modified residuei411 – 4111PhosphoserineCombined sources
Modified residuei450 – 4501PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP40161.
PeptideAtlasiP40161.

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 interactions.
DIPiDIP-4292N.
IntActiP40161. 56 interactions.
MINTiMINT-521994.

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Helixi11 – 2111Combined sources
Helixi27 – 4115Combined sources
Beta strandi60 – 634Combined sources
Beta strandi71 – 8515Combined sources
Beta strandi87 – 959Combined sources
Turni97 – 993Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi111 – 1166Combined sources
Helixi119 – 1224Combined sources
Beta strandi123 – 1308Combined sources
Beta strandi137 – 1459Combined sources
Helixi148 – 1503Combined sources
Beta strandi156 – 1616Combined sources
Helixi162 – 17110Combined sources
Helixi183 – 19513Combined sources
Beta strandi220 – 23516Combined sources
Beta strandi237 – 24711Combined sources
Beta strandi249 – 2524Combined sources
Helixi253 – 2553Combined sources
Beta strandi256 – 2638Combined sources
Beta strandi266 – 27510Combined sources
Beta strandi280 – 2878Combined sources
Helixi288 – 2903Combined sources
Helixi291 – 2999Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-67, 70-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40161.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 200133PH 1Add
BLAST
Domaini217 – 30185PH 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 6766Dimeric regionAdd
BLAST
Regioni68 – 301234Double PH domainAdd
BLAST
Regioni315 – 455141Disordered acidic regionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi351 – 44898Asp/Glu-richAdd
BLAST

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.
OrthoDBiEOG7TBCC0.

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
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. Positions 1-67, 70-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP40161.

Proteomic databases

MaxQBiP40161.
PeptideAtlasiP40161.

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.
OrthoDBiEOG7TBCC0.

Enzyme and pathway databases

BioCyciYEAST:G3O-33212-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40161.
NextBioi979541.
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...

Publicationsi

« Hide 'large scale' publications
  1. "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8 new open reading frames of unknown function."
    Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.
    Yeast 10:1639-1645(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance."
    Scholes D.T., Banerjee M., Bowen B., Curcio M.J.
    Genetics 159:1449-1465(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing."
    Huang S., Zhou H., Katzmann D., Hochstrasser M., Atanasova E., Zhang Z.
    Proc. Natl. Acad. Sci. U.S.A. 102:13410-13415(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H3; HISTONE H4 AND RLF2.
  8. "A novel role for histone chaperones CAF-1 and Rtt106p in heterochromatin silencing."
    Huang S., Zhou H., Tarara J., Zhang Z.
    EMBO J. 26:2274-2283(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SIR4.
  9. "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-408 AND SER-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Two-color cell array screen reveals interdependent roles for histone chaperones and a chromatin boundary regulator in histone gene repression."
    Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K., Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J., Andrews B.J.
    Mol. Cell 35:340-351(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "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-408; SER-411 AND SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "A role for Gcn5 in replication-coupled nucleosome assembly."
    Burgess R.J., Zhou H., Han J., Zhang Z.
    Mol. Cell 37:469-480(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H3.
  13. "Transcriptome profiling reveals a novel role for trichostatin A in antagonizing histone chaperone Chz1 mediated telomere anti-silencing."
    Wan Y., Chen W., Xing J., Tan J., Li B., Chen H., Lin Z., Chiang J.H., Saleem R.A.
    FEBS Lett. 585:2519-2525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Restriction of histone gene transcription to S phase by phosphorylation of a chromatin boundary protein."
    Kurat C.F., Lambert J.P., van Dyk D., Tsui K., van Bakel H., Kaluarachchi S., Friesen H., Kainth P., Nislow C., Figeys D., Fillingham J., Andrews B.J.
    Genes Dev. 25:2489-2501(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH YTA7.
  15. "A conserved patch near the C terminus of histone H4 is required for genome stability in budding yeast."
    Yu Y., Srinivasan M., Nakanishi S., Leatherwood J., Shilatifard A., Sternglanz R.
    Mol. Cell. Biol. 31:2311-2325(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONES H3 AND H4.
  16. "The Saccharomyces cerevisiae histone chaperone Rtt106 mediates the cell cycle recruitment of SWI/SNF and RSC to the HIR-dependent histone genes."
    Ferreira M.E., Flaherty K., Prochasson P.
    PLoS ONE 6:E21113-E21113(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SWI/SNF; RSC AND HIR COMPLEXES.
  17. "The mitotic Clb cyclins are required to alleviate HIR-mediated repression of the yeast histone genes at the G1/S transition."
    Amin A.D., Dimova D.K., Ferreira M.E., Vishnoi N., Hancock L.C., Osley M.A., Prochasson P.
    Biochim. Biophys. Acta 1819:16-27(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106 co-operate to maintain promoter fidelity."
    Silva A.C., Xu X., Kim H.S., Fillingham J., Kislinger T., Mennella T.A., Keogh M.C.
    J. Biol. Chem. 287:1709-1718(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing."
    Liu Y., Huang H., Zhou B.O., Wang S.S., Hu Y., Li X., Liu J., Zang J., Niu L., Wu J., Zhou J.Q., Teng M., Shi Y.
    J. Biol. Chem. 285:4251-4262(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 65-320, DNA-BINDING, INTERACTION WITH HISTONES H3 AND H4, FUNCTION.
  21. "Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106."
    Su D., Hu Q., Li Q., Thompson J.R., Cui G., Fazly A., Davies B.A., Botuyan M.V., Zhang Z., Mer G.
    Nature 483:104-107(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 68-301, DOMAIN, SUBUNIT, INTERACTION WITH HISTONES H3 AND H4, MUTAGENESIS OF ILE-259; TYR-261; PHE-269; GLN-288 AND ILE-294.
  22. "Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing."
    Zunder R.M., Antczak A.J., Berger J.M., Rine J.
    Proc. Natl. Acad. Sci. U.S.A. 109:E144-E153(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 69-300.

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: May 11, 2016
This is version 125 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.