Transcriptional regulatory protein ASH1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P34233 (ASH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 99. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Transcriptional regulatory protein ASH1

Alternative name(s):
Daughter cells HO repressor protein

Gene names

Name:	ASH1
Ordered Locus Names:	YKL185W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the RPD3C(L) histone deacetylase complex (HDAC). Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. ASH1 is necessary to repress HO in daughter cells to block mating-type switching through its binding to HO promoter 5'-YTGAT-3' sites. Also involved in pseudohyphal growth. Ref.5 Ref.6 Ref.10 Ref.11
Subunit structure	Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
Subcellular location	Nucleus. Note: Preferentially accumulates in daughter cell nuclei at the end of anaphase. Ref.5 Ref.6 Ref.9 Ref.10 Ref.12
Miscellaneous	The ASH1 mRNA is transported to the daughter cell before cytokinesis where translation produces the protein to block mating-type switching. The ASH1 mRNA 3'-UTR and the mRNA localization machinery that are essential to restrict accumulation to the bud. Present with 1800 molecules/cell in log phase SD medium. Ref.13
Sequence similarities	Contains 1 GATA-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of G1/S transition of mitotic cell cycle Inferred from direct assay. Source: SGD negative regulation of mating type switching Inferred from mutant phenotype Ref.5 Ref.6. Source: SGD positive regulation of pseudohyphal growth Inferred from mutant phenotype. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD
Cellular component	Rpd3L complex Inferred from direct assay Ref.14. Source: SGD Rpd3L-Expanded complex Inferred from direct assay. Source: SGD cellular bud Inferred from direct assay Ref.5 Ref.6. Source: SGD
Molecular function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from direct assay. Source: SGD core promoter proximal region sequence-specific DNA binding Inferred from direct assay Ref.11. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 588

588

Transcriptional regulatory protein ASH1

PRO_0000083492

Regions

Zinc finger

499 – 526

GATA-type; atypical

Amino acid modifications

Modified residue

Phosphoserine Ref.16

Modified residue

452

Phosphoserine Ref.15

Modified residue

465

Phosphoserine Ref.16

Sequences

Sequence

Length

Mass (Da)

Tools

P34233 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 7DFFD1B9392DAC08
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FASTA

588

65,685

        10         20         30         40         50         60 
MSSLYIKTPL HALSAGPDSH ANSSYYDNLL LPSFSNLSSN ISRNNITTDN NINSASPRKY 

        70         80         90        100        110        120 
SFHSLNVSPI LSPISLANEI LGKKSNTAPA SPHHMDYNPI SSLTPGNSPE FNKASLSQIS 

       130        140        150        160        170        180 
FTNPLNYGSG LGFSSNSQPR LPLLDRLSSV SLSKRPERPQ QSLPSLRHLQ LLPSPLLQEN 

       190        200        210        220        230        240 
AARFPDTSKR TSNWKTDLTH WCKDTNYQDY VKIREEVAHF KPLSIPNLTN NQNNDSFNYG 

       250        260        270        280        290        300 
KELESTRSSK FHSPSKESFD RTKLIPSILE AKDQFKDLSN NAWSITPPVT PPMSPPTNRT 

       310        320        330        340        350        360 
MERTTLRGVE ASFFEGKSSN NDSIFNPIIS EKLVQEVKHQ RQLRGNSFPM PNASHKKTNS 

       370        380        390        400        410        420 
FKALQIKKLL ANRDILSNNS KSNVRKPSKN KISKQASNVF GNTARQLVMK LDNASYSSVS 

       430        440        450        460        470        480 
ASSSPSPSTP TKSGKMRSRS SSPVRPKAYT PSPRSPNYHR FALDSPPQSP RRSSNSSITK 

       490        500        510        520        530        540 
KGSRRSSGSS PTRHTTRVCV SCHSSDSPCW RPSWSPRKQD QLCNSCGLRY KKTHTRCLND 

       550        560        570        580 
LCRKIPTKGE INIMKSNGID KEFVPERNCE IEGYRCLFCN YITETVEN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene." Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W. Yeast 9:1343-1348(1993) [PubMed: 8154185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	Cusick M.E. Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-563.
[5]	"Asymmetric accumulation of Ash1p in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells." Bobola N., Jansen R.-P., Shin T.H., Nasmyth K. Cell 84:699-709(1996) [PubMed: 8625408] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"Identification of asymmetrically localized determinant, Ash1p, required for lineage-specific transcription of the yeast HO gene." Sil A., Herskowitz I. Cell 84:711-722(1996) [PubMed: 8625409] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast." Takizawa P.A., Sil A., Swedlow J.R., Herskowitz I., Vale R.D. Nature 389:90-93(1997) [PubMed: 9288973] [Abstract] Cited for: TRANSPORT AND ASYMMETRIC LOCATION OF MRNA.
[8]	"Mating type switching in yeast controlled by asymmetric localization of ASH1 mRNA." Long R.M., Singer R.H., Meng X., Gonzalez I., Nasmyth K., Jansen R.-P. Science 277:383-387(1997) [PubMed: 9219698] [Abstract] Cited for: TRANSPORT AND ASYMMETRIC LOCATION OF MRNA.
[9]	"Localization of ASH1 mRNA particles in living yeast." Bertrand E., Chartrand P., Schaefer M., Shenoy S.M., Singer R.H., Long R.M. Mol. Cell 2:437-445(1998) [PubMed: 9809065] [Abstract] Cited for: SUBCELLULAR LOCATION, MRNA TRANSPORT.
[10]	"Ash1, a daughter cell-specific protein, is required for pseudohyphal growth of Saccharomyces cerevisiae." Chandarlapaty S., Errede B. Mol. Cell. Biol. 18:2884-2891(1998) [PubMed: 9566907] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Ash1p is a site-specific DNA-binding protein that actively represses transcription." Maxon M.E., Herskowitz I. Proc. Natl. Acad. Sci. U.S.A. 98:1495-1500(2001) [PubMed: 11171979] [Abstract] Cited for: FUNCTION, DOMAIN, DNA-BINDING.
[12]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[13]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]	"Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex." Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J., Washburn M.P., Workman J.L. Biochim. Biophys. Acta 1731:77-87(2005) [PubMed: 16314178] [Abstract] Cited for: IDENTIFICATION IN THE RPD3C(L) COMPLEX, MASS SPECTROMETRY.
[15]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, MASS SPECTROMETRY.
[16]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-465, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74151 Genomic DNA. Translation: CAA52253.1. Z28185 Genomic DNA. Translation: CAA82028.1. M88605 Genomic DNA. Translation: AAA34830.1. BK006944 Genomic DNA. Translation: DAA08981.1.
PIR	S34685.
RefSeq	NP_012736.1. NM_001179751.1.
3D structure databases
ProteinModelPortal	P34233.
SMR	P34233. Positions 497-535.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-8053N.
IntAct	P34233. 11 interactions.
MINT	MINT-2783083.
STRING	P34233.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL185W; YKL185W; YKL185W.
GeneID	853650.
KEGG	sce:YKL185W.
NMPDR	fig\|4932.3.peg.3713.
Organism-specific databases
CYGD	YKL185w.
SGD	S000001668. ASH1.
Phylogenomic databases
eggNOG	fuNOG10736.
HOGENOM	HBG202400.
OMA	SDSPCWR.
OrthoDB	EOG4K3Q5R.
Gene expression databases
ArrayExpress	P34233.
Genevestigator	P34233.
GermOnline	YKL185W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000679. Znf_GATA. IPR013088. Znf_NHR/GATA. [Graphical view]
Gene3D	G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.
Pfam	PF00320. GATA. 1 hit. [Graphical view]
SMART	SM00401. ZnF_GATA. 1 hit. [Graphical view]
PROSITE	PS00344. GATA_ZN_FINGER_1. 1 hit. PS50114. GATA_ZN_FINGER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974560.

Entry information

Entry name

ASH1_YEAST

Accession

Primary (citable) accession number: P34233
Secondary accession number(s): D6VX15

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	December 14, 2011
This is version 99 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 XI

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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents