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P34233 (ASH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional regulatory protein ASH1
Alternative name(s):
Daughter cells HO repressor protein
Gene names
Name:ASH1
Ordered Locus Names:YKL185W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.14

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.

Sequence similarities

Contains 1 GATA-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of G1/S transition of mitotic cell cycle by negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19841732. Source: SGD

negative regulation of mating type switching by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.5Ref.6. Source: SGD

positive regulation of pseudohyphal growth by positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 11046133. Source: SGD

   Cellular_componentRpd3L complex

Inferred from direct assay PubMed 16286007Ref.14. Source: SGD

cellular bud

Inferred from direct assay Ref.5Ref.6. Source: SGD

nucleus

Inferred from direct assay Ref.5Ref.6Ref.10. Source: SGD

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay PubMed 19841732. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Transcriptional regulatory protein ASH1
PRO_0000083492

Regions

Zinc finger499 – 52628GATA-type; atypical

Amino acid modifications

Modified residue561Phosphoserine Ref.16
Modified residue4651Phosphoserine Ref.15 Ref.16

Sequences

Sequence LengthMass (Da)Tools
P34233 [UniParc].

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

FASTA58865,685
        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' 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] [Europe PMC] [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. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RPD3C(L) COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"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-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS34685.
RefSeqNP_012736.1. NM_001179751.1.

3D structure databases

ProteinModelPortalP34233.
SMRP34233. Positions 497-534.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33937. 76 interactions.
DIPDIP-8053N.
IntActP34233. 9 interactions.
MINTMINT-2783083.
STRING4932.YKL185W.

Proteomic databases

PaxDbP34233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL185W; YKL185W; YKL185W.
GeneID853650.
KEGGsce:YKL185W.

Organism-specific databases

CYGDYKL185w.
SGDS000001668. ASH1.

Phylogenomic databases

eggNOGNOG44003.
HOGENOMHOG000034095.
OMASDSPCWR.
OrthoDBEOG7M3J86.

Enzyme and pathway databases

BioCycYEAST:G3O-31948-MONOMER.

Gene expression databases

GenevestigatorP34233.

Family and domain databases

Gene3D3.30.50.10. 1 hit.
InterProIPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00320. GATA. 1 hit.
[Graphical view]
SMARTSM00401. ZnF_GATA. 1 hit.
[Graphical view]
PROSITEPS00344. GATA_ZN_FINGER_1. 1 hit.
PS50114. GATA_ZN_FINGER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974560.

Entry information

Entry nameASH1_YEAST
AccessionPrimary (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: April 16, 2014
This is version 120 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 XI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families