Histone acetyltransferase RTT109 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q07794 (RT109_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	double-strand break repair via nonhomologous end joining Inferred from mutant phenotype PubMed 18036332. Source: SGD negative regulation of transposition, RNA-mediated Inferred from mutant phenotype Ref.4. Source: SGD regulation of transcription from RNA polymerase II promoter in response to stress Inferred from mutant phenotype PubMed 19620280. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay Ref.5 Ref.7. Source: SGD
Molecular_function	H3 histone acetyltransferase activity Inferred from direct assay Ref.12 Ref.13. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 436

436

Histone acetyltransferase RTT109

PRO_0000268738

Experimental info

Mutagenesis

D → A or N: Losses histone acetylase activity. Ref.13

Mutagenesis

287 – 288

DD → AA or NN: Reduces histone acetylase activity.

Secondary structure

436

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q07794 [UniParc].

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

FASTA

436

50,096

        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' referencesShow '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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.

PIR

S64744.

RefSeq

NP_013099.1. NM_001181822.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	1-403	[»]
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	[»]

ProteinModelPortal

Q07794.

SMR

Q07794. Positions 1-426.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-8842N.

IntAct

Q07794. 1 interaction.

MINT

MINT-2781350.

STRING

4932.YLL002W.

Proteomic databases

PaxDb

Q07794.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLL002W; YLL002W; YLL002W.

GeneID

850658.

KEGG

sce:YLL002W.

Organism-specific databases

CYGD

YLL002w.

SGD

S000003925. RTT109.

Phylogenomic databases

eggNOG

COG5087.

HOGENOM

HOG000001105.

K11309.

OMA

VSKADTN.

OrthoDB

EOG40P7GZ.

Gene expression databases

Genevestigator

Q07794.

GermOnline

YLL002W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013178. Histone_H3-K56_AcTrfase_RTT109.
IPR016849. Histone_H3-K56_AcTrfase_yeast.
[Graphical view]

Pfam

PF08214. KAT11. 1 hit.
[Graphical view]

PIRSF

PIRSF027124. Histone_acetylase_Rtt109. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q07794.

NextBio

966623.

Entry information

Entry name

RT109_YEAST

Accession

Primary (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:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents