RTT109/YLL002W Protein Information

Standard Name	Rtt109p 1
Systematic Name	Yll002wp
Alias	Kim2p , Rem50p
ORF Classification	Verified
Description	Histone acetyltransferase critical for cell survival in the presence of DNA damage during S phase; acetylates H3-K56 and H3-K9; involved in non-homologous end joining and in regulation of Ty1 transposition; interacts physically with Vps75p (1, 2, 3, 4, 5)
Name Description	Regulator of Ty1 Transposition 1
Gene Product	KAT11 6

Experimental Data
Molecules/cell	1140 7

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	436
Molecular Weight (Da)	50,095
Isoelectric Point (pI)	10.18

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Rtt109p (InterPro)
Physical Interactions	There are 52 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000006C568 \| Q07794 MIPS: YLL002W NCBI: 1360159 \| 1495223 \| 197724939 \| 198443237 \| 206581854 \| 321160030 \| 321160033 \| 323463198 \| 326634486 \| 326634489 \| 6323027 \| 74644996 \| NP_013099.1 GenBank/EMBL/DDBJ: DAA09317.1 \| X91488 \| Z73107
External Classifications	EC: 2.3.1.48 [Histone acetyltransferase]

Amino Acid Sequence (or in FASTA format)
1 MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ 51 HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV 101 RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI 151 LARRLKQSGS TVLKEIESPR FQQDLYLSFT CPREILTKIC LFTRPASQYL 201 FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA KLRIPGEDPA 251 RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE 301 DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI 351 VPKSRKQFRA IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG 401 KREHRERNQP VPASNINTLA ITMLKPRKKA KALPKT*

Amino Acid Sequence (or in FASTA format)

       1  MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ
      51  HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV
     101  RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI
     151  LARRLKQSGS TVLKEIESPR FQQDLYLSFT CPREILTKIC LFTRPASQYL
     201  FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA KLRIPGEDPA
     251  RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE
     301  DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI
     351  VPKSRKQFRA IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG
     401  KREHRERNQP VPASNINTLA ITMLKPRKKA KALPKT*

external links for Rtt109p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastGFP
Candida (CGD)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Rtt109p

1)	Scholes DT, et al. (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159(4):1449-65
2)	Driscoll R, et al. (2007) Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315(5812):649-52
3)	Han J, et al. (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315(5812):653-5
4)	Jessulat M, et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys 469(2):157-64
5)	Fillingham J, et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol Cell Biol 28(13):4342-53
6)	Allis CD, et al. (2007) New nomenclature for chromatin-modifying enzymes. Cell 131(4):633-6
7)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41