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P34218

- SAS3_YEAST

UniProt

P34218 - SAS3_YEAST

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Protein
Histone acetyltransferase SAS3
Gene
SAS3, YBL052C, YBL0507, YBL0515
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei367 – 3671 By similarity
Active sitei418 – 4181Nucleophile By similarity
Binding sitei421 – 4211Acetyl-CoA By similarity
Binding sitei456 – 4561Acetyl-CoA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri301 – 32323C2HC-type
Add
BLAST

GO - Molecular functioni

  1. histone acetyltransferase activity Source: SGD
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. chromatin modification Source: SGD
  2. chromatin silencing at silent mating-type cassette Source: SGD
  3. chromatin silencing at telomere Source: SGD
  4. histone acetylation Source: SGD
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-28951-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase SAS3 (EC:2.3.1.48)
Alternative name(s):
Something about silencing protein 3
Gene namesi
Name:SAS3
Ordered Locus Names:YBL052C
ORF Names:YBL0507, YBL0515
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBL052c.
SGDiS000000148. SAS3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. NuA3 histone acetyltransferase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi303 – 3031C → A: Greatly diminishes HAT activity. 1 Publication
Mutagenesisi306 – 3061C → A: Greatly diminishes HAT activity. 1 Publication
Mutagenesisi319 – 3191H → A: Greatly diminishes HAT activity. 1 Publication
Mutagenesisi323 – 3231C → A: Abolishes HAT activity. 1 Publication
Mutagenesisi426 – 4272QR → AA: Loss of function.
Mutagenesisi429 – 4313GYG → AAA: Loss of function. 1 Publication
Mutagenesisi434 – 4352LM → AA: No effect.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 831831Histone acetyltransferase SAS3
PRO_0000051579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei367 – 3671N6-acetyllysine; by autocatalysis By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP34218.
PaxDbiP34218.

Expressioni

Gene expression databases

GenevestigatoriP34218.

Interactioni

Subunit structurei

Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6. SAS3 interacts with CDC68/SPT16.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAF14P351892EBI-16484,EBI-18920
YNG1Q084654EBI-16484,EBI-31890

Protein-protein interaction databases

BioGridi32646. 93 interactions.
DIPiDIP-4277N.
IntActiP34218. 20 interactions.
MINTiMINT-509916.
STRINGi4932.YBL052C.

Structurei

3D structure databases

ProteinModelPortaliP34218.
SMRiP34218. Positions 275-573.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni426 – 4327Acetyl-CoA binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi736 – 83196Asp/Glu-rich (acidic)
Add
BLAST

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00730000114398.
KOiK11378.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR002717. MOZ_SAS.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.

Sequencei

Sequence statusi: Complete.

P34218-1 [UniParc]FASTAAdd to Basket

« Hide

MSLTANDESP KPKKNALLKN LEIDDLIHSQ FVRSDTNGHR TTRRLFNSDA    50
SISHRIRGSV RSDKGLNKIK KGLISQQSKL ASENSSQNIV NRDNKMGAVS 100
FPIIEPNIEV SEELKVRIKY DSIKFFNFER LISKSSVIAP LVNKNITSSG 150
PLIGFQRRVN RLKQTWDLAT ENMEYPYSSD NTPFRDNDSW QWYVPYGGTI 200
KKMKDFSTKR TLPTWEDKIK FLTFLENSKS ATYINGNVSL CNHNETDQEN 250
EDRKKRKGKV PRIKNKVWFS QIEYIVLRNY EIKPWYTSPF PEHINQNKMV 300
FICEFCLKYM TSRYTFYRHQ LKCLTFKPPG NEIYRDGKLS VWEIDGRENV 350
LYCQNLCLLA KCFINSKTLY YDVEPFIFYI LTEREDTENH PYQNAAKFHF 400
VGYFSKEKFN SNDYNLSCIL TLPIYQRKGY GQFLMEFSYL LSRKESKFGT 450
PEKPLSDLGL LTYRTFWKIK CAEVLLKLRD SARRRSNNKN EDTFQQVSLN 500
DIAKLTGMIP TDVVFGLEQL QVLYRHKTRS LSSLDDFNYI IKIDSWNRIE 550
NIYKTWSSKN YPRVKYDKLL WEPIILGPSF GINGMMNLEP TALADEALTN 600
ETMAPVISNN THIENYNNSR AHNKRRRRRR RSSEHKTSKL HVNNIIEPEV 650
PATDFFEDTV SSLTEYMCDY KNTNNDRLIY QAEKRVLESI HDRKGIPRSK 700
FSTETHWELC FTIKNSETPL GNHAARRNDT GISSLEQDEV ENDVDTELYV 750
GENAKEDEDE DEDFTLDDDI EDEQISEEND EEEDTYEEDS DDDEDGKRKG 800
QEQDENDIES HIRKERVRKR RKITLIEDDE E 831
Length:831
Mass (Da):97,582
Last modified:February 1, 1994 - v1
Checksum:iACF5B1B225CB4A71
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z23261 Genomic DNA. Translation: CAA80794.1.
Z35814 Genomic DNA. Translation: CAA84873.1.
BK006936 Genomic DNA. Translation: DAA07067.1.
PIRiS39835.
RefSeqiNP_009501.1. NM_001178292.1.

Genome annotation databases

EnsemblFungiiYBL052C; YBL052C; YBL052C.
GeneIDi852228.
KEGGisce:YBL052C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z23261 Genomic DNA. Translation: CAA80794.1 .
Z35814 Genomic DNA. Translation: CAA84873.1 .
BK006936 Genomic DNA. Translation: DAA07067.1 .
PIRi S39835.
RefSeqi NP_009501.1. NM_001178292.1.

3D structure databases

ProteinModelPortali P34218.
SMRi P34218. Positions 275-573.
ModBasei Search...

Protein-protein interaction databases

BioGridi 32646. 93 interactions.
DIPi DIP-4277N.
IntActi P34218. 20 interactions.
MINTi MINT-509916.
STRINGi 4932.YBL052C.

Proteomic databases

MaxQBi P34218.
PaxDbi P34218.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBL052C ; YBL052C ; YBL052C .
GeneIDi 852228.
KEGGi sce:YBL052C.

Organism-specific databases

CYGDi YBL052c.
SGDi S000000148. SAS3.

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00730000114398.
KOi K11378.
OrthoDBi EOG7RFTRR.

Enzyme and pathway databases

BioCyci YEAST:G3O-28951-MONOMER.

Miscellaneous databases

NextBioi 970757.

Gene expression databases

Genevestigatori P34218.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR002717. MOZ_SAS.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiSAS3_YEAST
AccessioniPrimary (citable) accession number: P34218
Secondary accession number(s): D6VPU7
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

Similar proteinsi