CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011520
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone acetyltransferase RTT109 
Protein Synonyms/Alias
 Regulator of Ty1 transposition protein 109 
Gene Name
 RTT109 
Gene Synonyms/Alias
 KIM2; REM50; YLL002W; L1377 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
260RSYLRGMKYPLWQVGacetylation[1]
290PLFPDDPKARFIHQLacetylation[1, 2, 3]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP.
 Tang Y, Holbert MA, Wurtele H, Meeth K, Rocha W, Gharib M, Jiang E, Thibault P, Verreault A, Cole PA, Marmorstein R.
 Nat Struct Mol Biol. 2008 Jul;15(7):738-45. [PMID: 18568037]
 [3] Autoacetylation of the histone acetyltransferase Rtt109.
 Albaugh BN, Arnold KM, Lee S, Denu JM.
 J Biol Chem. 2011 Jul 15;286(28):24694-701. [PMID: 21606491
Functional Description
 Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/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. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; DNA damage; DNA repair; Nucleus; Reference proteome; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 436 AA 
Protein Sequence
MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ HFFSLFHQGK 60
VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV RDITKIILEF ILSIDPNYYL 120
QKVKPAIRSY KKISPELISA ASTPARTLRI LARRLKQSGS TVLKEIESPR FQQDLYLSFT 180
CPREILTKIC LFTRPASQYL FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA 240
KLRIPGEDPA RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE 300
DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI VPKSRKQFRA 360
IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG KREHRERNQP VPASNINTLA 420
ITMLKPRKKA KALPKT 436 
Gene Ontology
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0010484; F:H3 histone acetyltransferase activity; IDA:SGD.
 GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
 GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:SGD.
 GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR013178; Histone_H3-K56_AcTrfase_RTT109.
 IPR016849; Histone_H3-K56_AcTrfase_yeast. 
Pfam
 PF08214; KAT11 
SMART
  
PROSITE
  
PRINTS