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Protein

Histone acetyltransferase RTT109

Gene

RTT109

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

Present with 1140 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.

GO - Molecular functioni

GO - Biological processi

  • chromatin silencing at centromere Source: GO_Central
  • histone acetylation Source: SGD
  • maintenance of rDNA Source: SGD
  • negative regulation of transposition, RNA-mediated Source: SGD
  • regulation of double-strand break repair via nonhomologous end joining Source: SGD
  • regulation of gene expression Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
  • replication-born double-strand break repair via sister chromatid exchange Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionTransferase
Biological processDNA damage, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32107-MONOMER
BRENDAi2.3.1.48 984

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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLL002W
SGDiS000003925 RTT109

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi89D → A or N: Losses histone acetylase activity. 1 Publication1
Mutagenesisi287 – 288DD → AA or NN: Reduces histone acetylase activity. 1 Publication2

Chemistry databases

ChEMBLiCHEMBL3414417

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002687381 – 436Histone acetyltransferase RTT109Add BLAST436

Proteomic databases

PaxDbiQ07794
PRIDEiQ07794

Expressioni

Inductioni

Expression peaks in cell cycle G1.1 Publication

Interactioni

Subunit structurei

Interacts with ASF1 and VPS75.5 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi31249, 550 interactors
ComplexPortaliCPX-1333 RTT109-VPS75 histone acetyltransferase complex
DIPiDIP-8842N
IntActiQ07794, 4 interactors
MINTiQ07794
STRINGi4932.YLL002W

Structurei

Secondary structure

1436
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Beta strandi16 – 23Combined sources8
Beta strandi27 – 29Combined sources3
Beta strandi37 – 40Combined sources4
Beta strandi44 – 57Combined sources14
Beta strandi60 – 77Combined sources18
Beta strandi79 – 90Combined sources12
Helixi100 – 112Combined sources13
Helixi117 – 120Combined sources4
Beta strandi121 – 124Combined sources4
Helixi135 – 137Combined sources3
Helixi144 – 158Combined sources15
Beta strandi159 – 161Combined sources3
Helixi164 – 167Combined sources4
Helixi169 – 174Combined sources6
Beta strandi175 – 177Combined sources3
Helixi182 – 184Combined sources3
Beta strandi186 – 193Combined sources8
Helixi195 – 197Combined sources3
Beta strandi199 – 201Combined sources3
Helixi204 – 206Combined sources3
Beta strandi207 – 209Combined sources3
Helixi215 – 233Combined sources19
Beta strandi239 – 243Combined sources5
Helixi249 – 256Combined sources8
Beta strandi259 – 262Combined sources4
Beta strandi264 – 267Combined sources4
Helixi273 – 276Combined sources4
Helixi278 – 280Combined sources3
Helixi292 – 299Combined sources8
Turni303 – 305Combined sources3
Helixi308 – 318Combined sources11
Helixi320 – 323Combined sources4
Turni324 – 326Combined sources3
Beta strandi328 – 334Combined sources7
Beta strandi336 – 338Combined sources3
Turni346 – 348Combined sources3
Helixi355 – 366Combined sources12
Helixi373 – 391Combined sources19
Beta strandi396 – 399Combined sources4
Helixi411 – 423Combined sources13
Beta strandi427 – 429Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
6F0YNMR-B419-433[»]
ProteinModelPortaliQ07794
SMRiQ07794
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07794

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 404Rtt109-type HATPROSITE-ProRule annotationAdd BLAST403

Sequence similaritiesi

Belongs to the RTT109 family.Curated

Phylogenomic databases

HOGENOMiHOG000001105
InParanoidiQ07794
KOiK11309
OMAiVSKADTN
OrthoDBiEOG092C2EKY

Family and domain databases

InterProiView protein in InterPro
IPR013178 Histone_AcTrfase_Rtt109/CBP
IPR016849 Rtt109
PANTHERiPTHR31571:SF2 PTHR31571:SF2, 1 hit
PfamiView protein in Pfam
PF08214 HAT_KAT11, 1 hit
PIRSFiPIRSF027124 Histone_acetylase_Rtt109, 1 hit
SMARTiView protein in SMART
SM01250 KAT11, 1 hit
PROSITEiView protein in PROSITE
PS51728 RTT109_HAT, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiRT109_YEAST
AccessioniPrimary (citable) accession number: Q07794
Secondary accession number(s): D6VY01
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: June 20, 2018
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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