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P34218 (SAS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:YBL0507, YBL0515
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length831 AA.
Sequence statusComplete.
Protein existenceEvidence 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 Ref.11

Subcellular location

Nucleus Ref.9.

Post-translational modification

Autoacetylation at Lys-367 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TAF14P351892EBI-16484,EBI-18920
YNG1Q084654EBI-16484,EBI-31890

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 831831Histone acetyltransferase SAS3
PRO_0000051579

Regions

Zinc finger301 – 32323C2HC-type
Region426 – 4327Acetyl-CoA binding By similarity
Compositional bias736 – 83196Asp/Glu-rich (acidic)

Sites

Active site3671 By similarity
Active site4181Nucleophile By similarity
Binding site4211Acetyl-CoA By similarity
Binding site4561Acetyl-CoA By similarity

Amino acid modifications

Modified residue3671N6-acetyllysine; by autocatalysis By similarity

Experimental info

Mutagenesis3031C → A: Greatly diminishes HAT activity. Ref.7
Mutagenesis3061C → A: Greatly diminishes HAT activity. Ref.7
Mutagenesis3191H → A: Greatly diminishes HAT activity. Ref.7
Mutagenesis3231C → A: Abolishes HAT activity. Ref.7
Mutagenesis426 – 4272QR → AA: Loss of function.
Mutagenesis429 – 4313GYG → AAA: Loss of function. Ref.4
Mutagenesis434 – 4352LM → AA: No effect.

Sequences

Sequence LengthMass (Da)Tools
P34218 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: ACF5B1B225CB4A71

FASTA83197,582
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]Erratum
Reifsnyder C., Lowell J., Clarke A., Pillus L.
Nat. Genet. 16:109-109(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, IDENTIFICATION BY 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.
PIRS39835.
RefSeqNP_009501.1. NM_001178292.1.

3D structure databases

ProteinModelPortalP34218.
SMRP34218. Positions 275-573.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32646. 93 interactions.
DIPDIP-4277N.
IntActP34218. 20 interactions.
MINTMINT-509916.
STRING4932.YBL052C.

Proteomic databases

MaxQBP34218.
PaxDbP34218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL052C; YBL052C; YBL052C.
GeneID852228.
KEGGsce:YBL052C.

Organism-specific databases

CYGDYBL052c.
SGDS000000148. SAS3.

Phylogenomic databases

eggNOGCOG5027.
GeneTreeENSGT00730000114398.
KOK11378.
OrthoDBEOG7RFTRR.

Enzyme and pathway databases

BioCycYEAST:G3O-28951-MONOMER.

Gene expression databases

GenevestigatorP34218.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR002717. MOZ_SAS.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

NextBio970757.

Entry information

Entry nameSAS3_YEAST
AccessionPrimary (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: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families