Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q07794

- RT109_YEAST

UniProt

Q07794 - RT109_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone acetyltransferase RTT109

Gene

RTT109

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.9 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. H3 histone acetyltransferase activity Source: SGD

GO - Biological processi

  1. double-strand break repair via nonhomologous end joining Source: SGD
  2. histone acetylation Source: SGD
  3. histone H3 acetylation Source: GOC
  4. maintenance of rDNA Source: SGD
  5. negative regulation of transposition, RNA-mediated Source: SGD
  6. regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

DNA damage, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32107-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase RTT109 (EC:2.3.1.48)
Alternative name(s):
Regulator of Ty1 transposition protein 109
Gene namesi
Name:RTT109
Synonyms:KIM2, REM50
Ordered Locus Names:YLL002W
ORF Names:L1377
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLL002w.
SGDiS000003925. RTT109.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891D → A or N: Losses histone acetylase activity. 1 Publication
Mutagenesisi287 – 2882DD → AA or NN: Reduces histone acetylase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Histone acetyltransferase RTT109PRO_0000268738Add
BLAST

Proteomic databases

PaxDbiQ07794.

Expressioni

Inductioni

Expression peaks in cell cycle G1.1 Publication

Gene expression databases

GenevestigatoriQ07794.

Interactioni

Subunit structurei

Interacts with ASF1 and VPS75.5 Publications

Protein-protein interaction databases

BioGridi31249. 357 interactions.
DIPiDIP-8842N.
IntActiQ07794. 1 interaction.
MINTiMINT-2781350.
STRINGi4932.YLL002W.

Structurei

Secondary structure

1
436
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 108Combined sources
Beta strandi16 – 238Combined sources
Beta strandi27 – 293Combined sources
Beta strandi37 – 404Combined sources
Beta strandi44 – 5714Combined sources
Beta strandi60 – 7718Combined sources
Beta strandi79 – 9012Combined sources
Helixi100 – 11213Combined sources
Helixi117 – 1204Combined sources
Beta strandi121 – 1244Combined sources
Helixi135 – 1373Combined sources
Helixi144 – 15815Combined sources
Beta strandi159 – 1613Combined sources
Helixi164 – 1674Combined sources
Helixi169 – 1746Combined sources
Beta strandi175 – 1773Combined sources
Helixi182 – 1843Combined sources
Beta strandi186 – 1938Combined sources
Helixi195 – 1973Combined sources
Beta strandi199 – 2013Combined sources
Helixi204 – 2063Combined sources
Beta strandi207 – 2093Combined sources
Helixi215 – 23319Combined sources
Beta strandi239 – 2435Combined sources
Helixi249 – 2568Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi264 – 2674Combined sources
Helixi273 – 2764Combined sources
Helixi278 – 2803Combined sources
Helixi289 – 29911Combined sources
Turni303 – 3053Combined sources
Helixi308 – 31811Combined sources
Helixi320 – 3234Combined sources
Turni324 – 3263Combined sources
Beta strandi328 – 3347Combined sources
Beta strandi336 – 3383Combined sources
Turni346 – 3483Combined sources
Helixi355 – 36612Combined sources
Helixi373 – 39119Combined sources
Beta strandi396 – 3994Combined sources
Helixi411 – 42313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ07794.
SMRiQ07794. Positions 1-426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 404403Rtt109-type HATPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RTT109 family.Curated
Contains 1 Rtt109-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5087.
HOGENOMiHOG000001105.
InParanoidiQ07794.
KOiK11309.
OMAiFTSKENS.
OrthoDBiEOG79PJZ1.

Family and domain databases

InterProiIPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR016849. Histone_H3-K56_AcTrfase_yeast.
[Graphical view]
PfamiPF08214. KAT11. 1 hit.
[Graphical view]
PIRSFiPIRSF027124. Histone_acetylase_Rtt109. 1 hit.
PROSITEiPS51728. RTT109_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07794-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ
60 70 80 90 100
HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV
110 120 130 140 150
RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI
160 170 180 190 200
LARRLKQSGS TVLKEIESPR FQQDLYLSFT CPREILTKIC LFTRPASQYL
210 220 230 240 250
FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA KLRIPGEDPA
260 270 280 290 300
RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE
310 320 330 340 350
DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI
360 370 380 390 400
VPKSRKQFRA IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG
410 420 430
KREHRERNQP VPASNINTLA ITMLKPRKKA KALPKT
Length:436
Mass (Da):50,096
Last modified:November 1, 1996 - v1
Checksum:i17825D6EF97C4BB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91488 Genomic DNA. Translation: CAA62768.1.
Z73107 Genomic DNA. Translation: CAA97445.1.
BK006945 Genomic DNA. Translation: DAA09317.1.
PIRiS64744.
RefSeqiNP_013099.1. NM_001181822.1.

Genome annotation databases

EnsemblFungiiYLL002W; YLL002W; YLL002W.
GeneIDi850658.
KEGGisce:YLL002W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91488 Genomic DNA. Translation: CAA62768.1 .
Z73107 Genomic DNA. Translation: CAA97445.1 .
BK006945 Genomic DNA. Translation: DAA09317.1 .
PIRi S64744.
RefSeqi NP_013099.1. NM_001181822.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RIM X-ray 2.20 A 1-436 [» ]
2ZFN X-ray 1.90 A 1-436 [» ]
3CZ7 X-ray 2.00 A 1-127 [» ]
A 171-403 [» ]
3Q33 X-ray 2.80 A 1-436 [» ]
3Q35 X-ray 3.30 A 1-436 [» ]
3Q66 X-ray 2.70 C 1-436 [» ]
3Q68 X-ray 2.70 C 1-436 [» ]
3QM0 X-ray 3.10 A 1-436 [» ]
ProteinModelPortali Q07794.
SMRi Q07794. Positions 1-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31249. 357 interactions.
DIPi DIP-8842N.
IntActi Q07794. 1 interaction.
MINTi MINT-2781350.
STRINGi 4932.YLL002W.

Proteomic databases

PaxDbi Q07794.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLL002W ; YLL002W ; YLL002W .
GeneIDi 850658.
KEGGi sce:YLL002W.

Organism-specific databases

CYGDi YLL002w.
SGDi S000003925. RTT109.

Phylogenomic databases

eggNOGi COG5087.
HOGENOMi HOG000001105.
InParanoidi Q07794.
KOi K11309.
OMAi FTSKENS.
OrthoDBi EOG79PJZ1.

Enzyme and pathway databases

BioCyci YEAST:G3O-32107-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q07794.
NextBioi 966623.

Gene expression databases

Genevestigatori Q07794.

Family and domain databases

InterProi IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR016849. Histone_H3-K56_AcTrfase_yeast.
[Graphical view ]
Pfami PF08214. KAT11. 1 hit.
[Graphical view ]
PIRSFi PIRSF027124. Histone_acetylase_Rtt109. 1 hit.
PROSITEi PS51728. RTT109_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. "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.

Entry informationi

Entry nameiRT109_YEAST
AccessioniPrimary (citable) accession number: Q07794
Secondary accession number(s): D6VY01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 107 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 1140 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3