Histone acetyltransferase SAS2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40963 (SAS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Histone acetyltransferase SAS2
EC=2.3.1.48

Alternative name(s):
Something about silencing protein 2

Gene names

Name:	SAS2
Synonyms:	ESO1
Ordered Locus Names:	YMR127C
ORF Names:	YM9553.03C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone acetyltransferase (HAT) subunit of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing and G0 control. Ref.8
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with CAC1. Component of the SAS complex, at least composed of SAS2, SAS4 and SAS5. These three proteins constitute the core of the complex and are sufficient to acetylate histones. SAS4 is essential for HAT activity of the complex, while SAS5 is required for maxiaml HAT activity. Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.9.
Post-translational modification	Autoacetylation at Lys-168 is required for proper function By similarity.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Chromatin regulator Repressor Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin silencing at telomere Inferred from direct assay Ref.6. Source: SGD histone exchange Inferred from mutant phenotype PubMed 18158898. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SAS acetyltransferase complex Inferred from direct assay Ref.8. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear chromatin Inferred from direct assay Ref.6. Source: SGD nuclear chromosome, telomeric region Inferred by curator Ref.6. Source: SGD
Molecular_function	histone acetyltransferase activity Inferred from direct assay Ref.8. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ASF1	P32447	4	EBI-16476,EBI-3003
RLF2	Q12495	4	EBI-16476,EBI-3913
SAS4	Q04003	7	EBI-16476,EBI-38500

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 338

338

Histone acetyltransferase SAS2

PRO_0000051578

Regions

Zinc finger

101 – 123

C2HC-type

Region

216 – 222

Acetyl-CoA binding By similarity

Sites

Active site

168

By similarity

Active site

208

Nucleophile By similarity

Binding site

246

Acetyl-CoA By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.10

Modified residue

168

N6-acetyllysine; by autocatalysis By similarity

Experimental info

Mutagenesis

106

C → L: Loss of function. Ref.7

Mutagenesis

213 – 214

PP → AV: Loss of function.

Mutagenesis

216 – 217

QR → AA: Abolishes silencing activity.

Mutagenesis

219 – 221

GLG → AAA: Does not affect silencing activity. Ref.6

Mutagenesis

224 – 225

LI → AA: Does not affect silencing activity.

Sequences

Sequence

Length

Mass (Da)

Tools

P40963 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 22CBDC0D1B62A947
Show »

FASTA

338

39,206

        10         20         30         40         50         60 
MARSLSQSLT ATTQKLKGKK NGGKGKNKPS AKIKKTQKEM LYGILNERNI RQIQFGLNKK 

        70         80         90        100        110        120 
FSTWYGSAVY FDPETKRLGC SETKGQLSSV SNSQYWLDTL FVCEYCFKYT DDQTRFVGHV 

       130        140        150        160        170        180 
ASCPFQYRVP GKIKYKSPEY TIRRVKGSKY QLFCQCLCLF TKLYLDNKSM YFKVDHYEFY 

       190        200        210        220        230        240 
IVYETGSTKP MGFFSKDLVS YQQNNLACIL IFPPYQRRGL GLLLIEFSYK LSQLEGVISG 

       250        260        270        280        290        300 
PEVPLSPFGL IGYLKYWSQI LCWHLIEGDL AHYDKVTLED LSIVTGMRVN DVILTLKHLN 

       310        320        330 
CIGENNQIYL QSLNSWLKLH GTKRNWFKLK DEYLLIDD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function." Ehrenhofer-Murray A.E., Rivier D.H., Rine J. Genetics 145:923-934(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	Erratum Reifsnyder C., Lowell J., Clarke A., Pillus L. Nat. Genet. 16:109-109(1997) [PubMed] [Europe PMC] [Abstract]
[6]	"The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1." Osada S., Sutton A., Muster N., Brown C.E., Yates J.R. III, Sternglanz R., Workman J.L. Genes Dev. 15:3155-3168(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE SAS COMPLEX WITH SAS2 AND SAS5, MUTAGENESIS OF 216-GLN-ARG-217; 219-GLY--GLY-221 AND 224-LEU-ILE-225.
[7]	"The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae." Meijsing S.H., Ehrenhofer-Murray A.E. Genes Dev. 15:3169-3182(2001) [PubMed] [Europe PMC] [Abstract] Cited for: COMPONENT OF THE SAS COMPLEX WITH SAS2 AND SAS5, INTERACTION WITH CAC1, MUTAGENESIS OF CYS-106 AND 213-PRO-PRO-214.
[8]	"Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex." Sutton A., Shia W.-J., Band D., Kaufman P.D., Osada S., Workman J.L., Sternglanz R. J. Biol. Chem. 278:16887-16892(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE SAS COMPLEX.
[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]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14548 Genomic DNA. Translation: AAA21555.1. Z48622 Genomic DNA. Translation: CAA88552.1. BK006946 Genomic DNA. Translation: DAA10024.1.
PIR	S48299.
RefSeq	NP_013846.1. NM_001182628.1.
3D structure databases
ProteinModelPortal	P40963.
SMR	P40963. Positions 100-302.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4601N.
IntAct	P40963. 6 interactions.
MINT	MINT-497812.
STRING	4932.YMR127C.
Proteomic databases
PaxDb	P40963.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR127C; YMR127C; YMR127C.
GeneID	855157.
KEGG	sce:YMR127C.
Organism-specific databases
CYGD	YMR127c.
SGD	S000004734. SAS2.
Phylogenomic databases
eggNOG	COG5027.
GeneTree	ENSGT00650000094487.
HOGENOM	HOG000066050.
KO	K11401.
OMA	DNNLACI.
OrthoDB	EOG4PVS7R.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32820-MONOMER.
Gene expression databases
Genevestigator	P40963.
GermOnline	YMR127C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR002717. MOZ_SAS. [Graphical view]
Pfam	PF01853. MOZ_SAS. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNet	Search...
Other
NextBio	978572.

Entry information

Entry name

SAS2_YEAST

Accession

Primary (citable) accession number: P40963
Secondary accession number(s): D6VZV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents