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P40963

- SAS2_YEAST

UniProt

P40963 - SAS2_YEAST

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Protein

Histone acetyltransferase SAS2

Gene

SAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei242 – 2421Proton donor/acceptorBy similarity
Binding sitei246 – 2461Acetyl-CoABy similarity
Binding sitei323 – 3231Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri101 – 12323C2HC-typeAdd
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: SGD
  2. histone acetyltransferase activity Source: SGD
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. chromatin silencing at telomere Source: SGD
  2. histone acetylation Source: SGD
  3. histone exchange Source: SGD
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32820-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase SAS2 (EC:2.3.1.481 Publication)
Alternative name(s):
Something about silencing protein 2
Gene namesi
Name:SAS2
Synonyms:ESO1
Ordered Locus Names:YMR127C
ORF Names:YM9553.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR127c.
SGDiS000004734. SAS2.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nuclear chromatin Source: SGD
  3. nuclear chromosome, telomeric region Source: SGD
  4. SAS acetyltransferase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061C → L: Loss of function. 2 Publications
Mutagenesisi168 – 1681K → A, Q or R: Abolishes catalytic activity.
Mutagenesisi213 – 2142PP → AV: Loss of function. 1 Publication
Mutagenesisi216 – 2172QR → AA: Abolishes silencing activity. 1 Publication
Mutagenesisi219 – 2213GLG → AAA: Does not affect silencing activity. 1 Publication
Mutagenesisi224 – 2252LI → AA: Does not affect silencing activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Histone acetyltransferase SAS2PRO_0000051578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681N6-acetyllysine; by autocatalysis1 Publication

Post-translational modificationi

Autoacetylation at Lys-168 is required for proper function.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP40963.

Expressioni

Gene expression databases

GenevestigatoriP40963.

Interactioni

Subunit structurei

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.1 Publication1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ASF1P324474EBI-16476,EBI-3003
RLF2Q124954EBI-16476,EBI-3913
SAS4Q040037EBI-16476,EBI-38500

Protein-protein interaction databases

BioGridi35304. 85 interactions.
DIPiDIP-4601N.
IntActiP40963. 6 interactions.
MINTiMINT-497812.
STRINGi4932.YMR127C.

Structurei

3D structure databases

ProteinModelPortaliP40963.
SMRiP40963. Positions 100-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 338294MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 2113Acetyl-CoA bindingBy similarity
Regioni216 – 2227Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri101 – 12323C2HC-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00730000114398.
HOGENOMiHOG000066050.
InParanoidiP40963.
KOiK11401.
OMAiNDNNLAC.
OrthoDBiEOG74TX7K.

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.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40963-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARSLSQSLT ATTQKLKGKK NGGKGKNKPS AKIKKTQKEM LYGILNERNI
60 70 80 90 100
RQIQFGLNKK FSTWYGSAVY FDPETKRLGC SETKGQLSSV SNSQYWLDTL
110 120 130 140 150
FVCEYCFKYT DDQTRFVGHV ASCPFQYRVP GKIKYKSPEY TIRRVKGSKY
160 170 180 190 200
QLFCQCLCLF TKLYLDNKSM YFKVDHYEFY IVYETGSTKP MGFFSKDLVS
210 220 230 240 250
YQQNNLACIL IFPPYQRRGL GLLLIEFSYK LSQLEGVISG PEVPLSPFGL
260 270 280 290 300
IGYLKYWSQI LCWHLIEGDL AHYDKVTLED LSIVTGMRVN DVILTLKHLN
310 320 330
CIGENNQIYL QSLNSWLKLH GTKRNWFKLK DEYLLIDD
Length:338
Mass (Da):39,206
Last modified:February 1, 1995 - v1
Checksum:i22CBDC0D1B62A947
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14548 Genomic DNA. Translation: AAA21555.1.
Z48622 Genomic DNA. Translation: CAA88552.1.
BK006946 Genomic DNA. Translation: DAA10024.1.
PIRiS48299.
RefSeqiNP_013846.1. NM_001182628.1.

Genome annotation databases

EnsemblFungiiYMR127C; YMR127C; YMR127C.
GeneIDi855157.
KEGGisce:YMR127C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14548 Genomic DNA. Translation: AAA21555.1 .
Z48622 Genomic DNA. Translation: CAA88552.1 .
BK006946 Genomic DNA. Translation: DAA10024.1 .
PIRi S48299.
RefSeqi NP_013846.1. NM_001182628.1.

3D structure databases

ProteinModelPortali P40963.
SMRi P40963. Positions 100-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35304. 85 interactions.
DIPi DIP-4601N.
IntActi P40963. 6 interactions.
MINTi MINT-497812.
STRINGi 4932.YMR127C.

Proteomic databases

PaxDbi P40963.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YMR127C ; YMR127C ; YMR127C .
GeneIDi 855157.
KEGGi sce:YMR127C.

Organism-specific databases

CYGDi YMR127c.
SGDi S000004734. SAS2.

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00730000114398.
HOGENOMi HOG000066050.
InParanoidi P40963.
KOi K11401.
OMAi NDNNLAC.
OrthoDBi EOG74TX7K.

Enzyme and pathway databases

BioCyci YEAST:G3O-32820-MONOMER.

Miscellaneous databases

NextBioi 978572.

Gene expression databases

Genevestigatori P40963.

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.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. 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].
  11. Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-168.

Entry informationi

Entry nameiSAS2_YEAST
AccessioniPrimary (citable) accession number: P40963
Secondary accession number(s): D6VZV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 128 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, 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3