P34218 (SAS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase SAS3
EC=2.3.1.48

Alternative name(s):
Something about silencing protein 3

Gene names

Name:	SAS3
Ordered Locus Names:	YBL052C
ORF Names:	YBL0515, YBL0507

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	831 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.7 Ref.8 Ref.10 Ref.11
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6. SAS3 interacts with CDC68/SPT16. Ref.4
Subcellular location	Nucleus Ref.9.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin silencing at silent mating-type cassette Inferred from mutant phenotype. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA3 histone acetyltransferase complex Inferred from direct assay Ref.4Ref.11. Source: SGD
Molecular function	histone acetyltransferase activity Inferred from mutant phenotype Ref.4. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TAF14	P35189	2	EBI-16484,EBI-18920
YNG1	Q08465	4	EBI-16484,EBI-31890

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 831	831	Histone acetyltransferase SAS3		PRO_0000051579
Regions
	Zinc finger	301 – 323	23	C2HC-type
	Region	426 – 432	7	Acetyl-CoA binding By similarity
	Compositional bias	736 – 831	96	Asp/Glu-rich (acidic)
Sites
	Active site	418	1	Nucleophile By similarity
	Binding site	421	1	Acetyl-CoA By similarity
	Binding site	456	1	Acetyl-CoA By similarity
Experimental info
	Mutagenesis	303	1	C → A: Greatly diminishes HAT activity. Ref.7
	Mutagenesis	306	1	C → A: Greatly diminishes HAT activity. Ref.7
	Mutagenesis	319	1	H → A: Greatly diminishes HAT activity. Ref.7
	Mutagenesis	323	1	C → A: Abolishes HAT activity. Ref.7
	Mutagenesis	426 – 427	2	QR → AA: Loss of function.
	Mutagenesis	429 – 431	3	GYG → AAA: Loss of function. Ref.4
	Mutagenesis	434 – 435	2	LM → AA: No effect.

Sequences

	Sequence		Length	Mass (Da)
	P34218 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: ACF5B1B225CB4A71	FASTA	831	97,582
	10 20 30 40 50 60 MSLTANDESP KPKKNALLKN LEIDDLIHSQ FVRSDTNGHR TTRRLFNSDA SISHRIRGSV 70 80 90 100 110 120 RSDKGLNKIK KGLISQQSKL ASENSSQNIV NRDNKMGAVS FPIIEPNIEV SEELKVRIKY 130 140 150 160 170 180 DSIKFFNFER LISKSSVIAP LVNKNITSSG PLIGFQRRVN RLKQTWDLAT ENMEYPYSSD 190 200 210 220 230 240 NTPFRDNDSW QWYVPYGGTI KKMKDFSTKR TLPTWEDKIK FLTFLENSKS ATYINGNVSL 250 260 270 280 290 300 CNHNETDQEN EDRKKRKGKV PRIKNKVWFS QIEYIVLRNY EIKPWYTSPF PEHINQNKMV 310 320 330 340 350 360 FICEFCLKYM TSRYTFYRHQ LKCLTFKPPG NEIYRDGKLS VWEIDGRENV LYCQNLCLLA 370 380 390 400 410 420 KCFINSKTLY YDVEPFIFYI LTEREDTENH PYQNAAKFHF VGYFSKEKFN SNDYNLSCIL 430 440 450 460 470 480 TLPIYQRKGY GQFLMEFSYL LSRKESKFGT PEKPLSDLGL LTYRTFWKIK CAEVLLKLRD 490 500 510 520 530 540 SARRRSNNKN EDTFQQVSLN DIAKLTGMIP TDVVFGLEQL QVLYRHKTRS LSSLDDFNYI 550 560 570 580 590 600 IKIDSWNRIE NIYKTWSSKN YPRVKYDKLL WEPIILGPSF GINGMMNLEP TALADEALTN 610 620 630 640 650 660 ETMAPVISNN THIENYNNSR AHNKRRRRRR RSSEHKTSKL HVNNIIEPEV PATDFFEDTV 670 680 690 700 710 720 SSLTEYMCDY KNTNNDRLIY QAEKRVLESI HDRKGIPRSK FSTETHWELC FTIKNSETPL 730 740 750 760 770 780 GNHAARRNDT GISSLEQDEV ENDVDTELYV GENAKEDEDE DEDFTLDDDI EDEQISEEND 790 800 810 820 830 EEEDTYEEDS DDDEDGKRKG QEQDENDIES HIRKERVRKR RKITLIEDDE E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and functional analysis of a 32,560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes." Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F. Yeast 9:1355-1371(1993) [PubMed: 8154187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex." John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L. Genes Dev. 14:1196-1208(2000) [PubMed: 10817755] [Abstract] Cited for: PROTEIN SEQUENCE OF 799-813, FUNCTION, INTERACTION WITH SPT16, MUTAGENESIS OF 426-GLN-ARG-427; 429-GLY--GLY-431 AND 434-LEU-MET-435.
[5]	"Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases." Reifsnyder C., Lowell J., Clarke A., Pillus L. Nat. Genet. 14:42-49(1996) [PubMed: 8782818] [Abstract] Cited for: CHARACTERIZATION.
[6]	Erratum Reifsnyder C., Lowell J., Clarke A., Pillus L. Nat. Genet. 16:109-109(1997) [PubMed: 9140406] [Abstract]
[7]	"Sas3 is a histone acetyltransferase and requires a zinc finger motif." Takechi S., Nakayama T. Biochem. Biophys. Res. Commun. 266:405-410(1999) [PubMed: 10600516] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-303; CYS-306; HIS-319 AND CYS-323.
[8]	"Histone H3 specific acetyltransferases are essential for cell cycle progression." Howe L., Auston D., Grant P., John S., Cook R.G., Workman J.L., Pillus L. Genes Dev. 15:3144-3154(2001) [PubMed: 11731478] [Abstract] Cited for: FUNCTION.
[9]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]	"Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatin." Martin D.G., Grimes D.E., Baetz K., Howe L. Mol. Cell. Biol. 26:3018-3028(2006) [PubMed: 16581777] [Abstract] Cited for: FUNCTION OF THE NUA3 COMPLEX.
[11]	"Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs." Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H., Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J., Aitchison J.D., Tackett A.J., Allis C.D. Mol. Cell 24:785-796(2006) [PubMed: 17157260] [Abstract] Cited for: FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z23261 Genomic DNA. Translation: CAA80794.1. Z35814 Genomic DNA. Translation: CAA84873.1. BK006936 Genomic DNA. Translation: DAA07067.1.
PIR	S39835.
RefSeq	NP_009501.1. NM_001178292.1.
3D structure databases
ProteinModelPortal	P34218.
SMR	P34218. Positions 270-573.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4277N.
IntAct	P34218. 22 interactions.
MINT	MINT-509916.
STRING	P34218.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBL052C; YBL052C; YBL052C.
GeneID	852228.
KEGG	sce:YBL052C.
NMPDR	fig|4932.3.peg.191.
Organism-specific databases
CYGD	YBL052c.
SGD	S000000148. SAS3.
Phylogenomic databases
eggNOG	fuNOG07326.
GeneTree	EFGT00050000002010.
OrthoDB	EOG4F21C3.
Gene expression databases
ArrayExpress	P34218.
Genevestigator	P34218.
GermOnline	YBL052C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR002717. MOZ_SAS. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KO	K11378.
Pfam	PF01853. MOZ_SAS. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNet	Search...
Other
NextBio	970757.

Entry information

Entry name

SAS3_YEAST

Accession

Primary (citable) accession number: P34218
Secondary accession number(s): D6VPU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program