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P40963 (SAS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Histone acetyltransferase SAS2
PRO_0000051578

Regions

Zinc finger101 – 12323C2HC-type
Region216 – 2227Acetyl-CoA binding By similarity

Sites

Active site1681 By similarity
Active site2081Nucleophile By similarity
Binding site2461Acetyl-CoA By similarity

Amino acid modifications

Modified residue1681N6-acetyllysine; by autocatalysis By similarity

Experimental info

Mutagenesis1061C → L: Loss of function. Ref.7
Mutagenesis213 – 2142PP → AV: Loss of function.
Mutagenesis216 – 2172QR → AA: Abolishes silencing activity.
Mutagenesis219 – 2213GLG → AAA: Does not affect silencing activity. Ref.6
Mutagenesis224 – 2252LI → AA: Does not affect silencing activity.

Sequences

Sequence LengthMass (Da)Tools
P40963 [UniParc].

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

FASTA33839,206
        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' 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. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS48299.
RefSeqNP_013846.1. NM_001182628.1.

3D structure databases

ProteinModelPortalP40963.
SMRP40963. Positions 100-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35304. 85 interactions.
DIPDIP-4601N.
IntActP40963. 6 interactions.
MINTMINT-497812.
STRING4932.YMR127C.

Proteomic databases

PaxDbP40963.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR127C; YMR127C; YMR127C.
GeneID855157.
KEGGsce:YMR127C.

Organism-specific databases

CYGDYMR127c.
SGDS000004734. SAS2.

Phylogenomic databases

eggNOGCOG5027.
GeneTreeENSGT00730000114398.
HOGENOMHOG000066050.
KOK11401.
OMANDNNLAC.
OrthoDBEOG74TX7K.

Enzyme and pathway databases

BioCycYEAST:G3O-32820-MONOMER.

Gene expression databases

GenevestigatorP40963.

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

NextBio978572.

Entry information

Entry nameSAS2_YEAST
AccessionPrimary (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: June 11, 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 XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families