| Tag | Content |
|---|
| CPLM ID | CPLM-006371 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histone acetyltransferase SAS3 |
Protein Synonyms/Alias | Something about silencing protein 3 |
Gene Name | SAS3 |
Gene Synonyms/Alias | YBL052C; YBL0507; YBL0515 |
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 |
|---|
| 79 | GLISQQSKLASENSS | acetylation | [1] |
|
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] |
Functional Description | Catalytic component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. In vitro, SAS3 acetylates free histones H3 and H4. It is involved in silencing the HMR locus. |
Sequence Annotation | ZN_FING 301 323 C2HC-type.
REGION 426 432 Acetyl-CoA binding (By similarity).
ACT_SITE 367 367 By similarity.
ACT_SITE 418 418 Nucleophile (By similarity).
BINDING 421 421 Acetyl-CoA (By similarity).
BINDING 456 456 Acetyl-CoA (By similarity).
MOD_RES 367 367 N6-acetyllysine; by autocatalysis (By |
Keyword | Acetylation; Acyltransferase; Chromatin regulator; Complete proteome; Direct protein sequencing; Metal-binding; Nucleus; Reference proteome; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 831 AA |
Protein Sequence | MSLTANDESP KPKKNALLKN LEIDDLIHSQ FVRSDTNGHR TTRRLFNSDA SISHRIRGSV 60
RSDKGLNKIK KGLISQQSKL ASENSSQNIV NRDNKMGAVS FPIIEPNIEV SEELKVRIKY 120
DSIKFFNFER LISKSSVIAP LVNKNITSSG PLIGFQRRVN RLKQTWDLAT ENMEYPYSSD 180
NTPFRDNDSW QWYVPYGGTI KKMKDFSTKR TLPTWEDKIK FLTFLENSKS ATYINGNVSL 240
CNHNETDQEN EDRKKRKGKV PRIKNKVWFS QIEYIVLRNY EIKPWYTSPF PEHINQNKMV 300
FICEFCLKYM TSRYTFYRHQ LKCLTFKPPG NEIYRDGKLS VWEIDGRENV LYCQNLCLLA 360
KCFINSKTLY YDVEPFIFYI LTEREDTENH PYQNAAKFHF VGYFSKEKFN SNDYNLSCIL 420
TLPIYQRKGY GQFLMEFSYL LSRKESKFGT PEKPLSDLGL LTYRTFWKIK CAEVLLKLRD 480
SARRRSNNKN EDTFQQVSLN DIAKLTGMIP TDVVFGLEQL QVLYRHKTRS LSSLDDFNYI 540
IKIDSWNRIE NIYKTWSSKN YPRVKYDKLL WEPIILGPSF GINGMMNLEP TALADEALTN 600
ETMAPVISNN THIENYNNSR AHNKRRRRRR RSSEHKTSKL HVNNIIEPEV PATDFFEDTV 660
SSLTEYMCDY KNTNNDRLIY QAEKRVLESI HDRKGIPRSK FSTETHWELC FTIKNSETPL 720
GNHAARRNDT GISSLEQDEV ENDVDTELYV GENAKEDEDE DEDFTLDDDI EDEQISEEND 780
EEEDTYEEDS DDDEDGKRKG QEQDENDIES HIRKERVRKR RKITLIEDDE E 831 |
Gene Ontology | GO:0033100; C:NuA3 histone acetyltransferase complex; IDA:SGD. GO:0004402; F:histone acetyltransferase activity; IDA:SGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD. GO:0006348; P:chromatin silencing at telomere; IMP:SGD. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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