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Q07794 (RT109_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase RTT109

EC=2.3.1.48
Alternative name(s):
Regulator of Ty1 transposition protein 109
Gene names
Name:RTT109
Synonyms:KIM2, REM50
Ordered Locus Names:YLL002W
ORF Names:L1377
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G2/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition. Ref.4 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Subunit structure

Interacts with ASF1 and VPS75. Ref.9 Ref.10 Ref.11 Ref.13 Ref.15

Subcellular location

Nucleus Ref.5 Ref.7.

Induction

Expression peaks in cell cycle G1. Ref.7

Miscellaneous

Present with 1140 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the RTT109 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Histone acetyltransferase RTT109
PRO_0000268738

Experimental info

Mutagenesis891D → A or N: Losses histone acetylase activity. Ref.13
Mutagenesis287 – 2882DD → AA or NN: Reduces histone acetylase activity.

Secondary structure

.............................................................................. 436
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07794 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 17825D6EF97C4BB5

FASTA43650,096
        10         20         30         40         50         60 
MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ HFFSLFHQGK 

        70         80         90        100        110        120 
VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV RDITKIILEF ILSIDPNYYL 

       130        140        150        160        170        180 
QKVKPAIRSY KKISPELISA ASTPARTLRI LARRLKQSGS TVLKEIESPR FQQDLYLSFT 

       190        200        210        220        230        240 
CPREILTKIC LFTRPASQYL FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA 

       250        260        270        280        290        300 
KLRIPGEDPA RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE 

       310        320        330        340        350        360 
DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI VPKSRKQFRA 

       370        380        390        400        410        420 
IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG KREHRERNQP VPASNINTLA 

       430 
ITMLKPRKKA KALPKT 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a 43.7 kb fragment of chromosome XII including an open reading frame homologous to the human cystic fibrosis transmembrane conductance regulator protein CFTR."
Miosga T., Zimmermann F.K.
Yeast 12:693-708(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"Localization of proteins that are coordinately expressed with Cln2 during the cell cycle."
Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.
Yeast 21:793-800(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION.
[8]"Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II."
Schneider J., Bajwa P., Johnson F.C., Bhaumik S.R., Shilatifard A.
J. Biol. Chem. 281:37270-37274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3."
Han J., Zhou H., Li Z., Xu R.-M., Zhang Z.
J. Biol. Chem. 282:14158-14164(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VPS75.
[10]"Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity."
Han J., Zhou H., Li Z., Xu R.-M., Zhang Z.
J. Biol. Chem. 282:28587-28596(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ASF1 AND VPS75.
[11]"Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes."
Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A., Denu J.M., Kaufman P.D.
Mol. Cell 25:703-712(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ASF1 AND VPS75.
[12]"Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56."
Driscoll R., Hudson A., Jackson S.P.
Science 315:649-652(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication."
Han J., Zhou H., Horazdovsky B., Zhang K., Xu R.-M., Zhang Z.
Science 315:653-655(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-89 AND 287-ASP-ASP-288, INTERACTION WITH VPS75.
[14]"Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation."
Williams S.K., Truong D., Tyler J.K.
Proc. Natl. Acad. Sci. U.S.A. 105:9000-9005(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Structure of Vps75 and implications for histone chaperone function."
Tang Y., Meeth K., Jiang E., Luo C., Marmorstein R.
Proc. Natl. Acad. Sci. U.S.A. 105:12206-12211(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VPS75.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91488 Genomic DNA. Translation: CAA62768.1.
Z73107 Genomic DNA. Translation: CAA97445.1.
BK006945 Genomic DNA. Translation: DAA09317.1.
PIRS64744.
RefSeqNP_013099.1. NM_001181822.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RIMX-ray2.20A1-436[»]
2ZFNX-ray1.90A1-436[»]
3CZ7X-ray2.00A1-127[»]
A171-403[»]
3Q33X-ray2.80A1-436[»]
3Q35X-ray3.30A1-436[»]
3Q66X-ray2.70C1-436[»]
3Q68X-ray2.70C1-436[»]
3QM0X-ray3.10A1-436[»]
ProteinModelPortalQ07794.
SMRQ07794. Positions 1-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31249. 355 interactions.
DIPDIP-8842N.
IntActQ07794. 1 interaction.
MINTMINT-2781350.
STRING4932.YLL002W.

Proteomic databases

PaxDbQ07794.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLL002W; YLL002W; YLL002W.
GeneID850658.
KEGGsce:YLL002W.

Organism-specific databases

CYGDYLL002w.
SGDS000003925. RTT109.

Phylogenomic databases

eggNOGCOG5087.
HOGENOMHOG000001105.
KOK11309.
OMAFTSKENS.
OrthoDBEOG79PJZ1.

Enzyme and pathway databases

BioCycYEAST:G3O-32107-MONOMER.

Gene expression databases

GenevestigatorQ07794.

Family and domain databases

InterProIPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR016849. Histone_H3-K56_AcTrfase_yeast.
[Graphical view]
PfamPF08214. KAT11. 1 hit.
[Graphical view]
PIRSFPIRSF027124. Histone_acetylase_Rtt109. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ07794.
NextBio966623.

Entry information

Entry nameRT109_YEAST
AccessionPrimary (citable) accession number: Q07794
Secondary accession number(s): D6VY01
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references