UniProt Accession

 RT106_YEAST; P40161; D6W0Y4 

Genbank Protein ID

 X78898; Z71482; BK006947 

Genbank Nucleotide ID

 CAA55502.1; CAA96106.1; DAA10350.1 

Protein Name

 Histone chaperone RTT106 

Protein Synonyms/Alias

 Regulator of Ty1 transposition protein 106 

Gene Name

 RTT106 

Gene Synonyms/Alias

 YNL206C; N1346 

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
121	LSIYQLNKNIKMASF	acetylation	[1]
315	MSEELKAKSKSKGQA	acetylation	[2]

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] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591] 

Functional Description

 Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell- cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition. 

Sequence Annotation

 DOMAIN 68 200 PH 1.
 DOMAIN 217 301 PH 2.
 REGION 1 67 Dimeric region.
 REGION 68 301 Double PH domain.
 REGION 315 455 Disordered acidic region.
 MOD_RES 408 408 Phosphoserine.
 MOD_RES 411 411 Phosphoserine.
 MOD_RES 450 450 Phosphoserine.  

Keyword

 3D-structure; Chaperone; Chromosome; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Transposition. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 455 AA 

Protein Sequence

Gene Ontology

 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0003690; F:double-stranded DNA binding; IMP:SGD.
 GO:0042393; F:histone binding; IDA:SGD.
 GO:0006335; P:DNA replication-dependent nucleosome assembly; IGI:SGD.
 GO:0006336; P:DNA replication-independent nucleosome assembly; IMP:SGD.
 GO:0070869; P:heterochromatin assembly involved in chromatin silencing; IMP:SGD.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
 GO:0032196; P:transposition; IEA:UniProtKB-KW. 

Interpro

 IPR013719; DUF1747. 

Pfam

 PF08512; Rtt106 

SMART

  

PROSITE

 PS50003; PH_DOMAIN 

PRINTS