Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcriptional regulatory protein PHO23

Gene

PHO23

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

Functioni

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.3 Publications

Miscellaneous

Present with 3250 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei282Histone H3K4me3By similarity1
Metal bindingi283Zinc 1By similarity1
Metal bindingi285Zinc 1By similarity1
Binding sitei293Histone H3K4me3By similarity1
Metal bindingi296Zinc 2By similarity1
Binding sitei297Histone H3K4me3By similarity1
Metal bindingi301Zinc 2By similarity1
Binding sitei305Histone H3K4me3By similarity1
Metal bindingi307Zinc 1; via pros nitrogenBy similarity1
Metal bindingi310Zinc 1By similarity1
Metal bindingi323Zinc 2By similarity1
Metal bindingi326Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri280 – 329PHD-typePROSITE-ProRule annotationAdd BLAST50

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB

GO - Biological processi

  • chromatin organization Source: SGD
  • covalent chromatin modification Source: UniProtKB-KW
  • negative regulation of chromatin silencing at rDNA Source: SGD
  • negative regulation of chromatin silencing at silent mating-type cassette Source: SGD
  • negative regulation of chromatin silencing at telomere Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • negative regulation of transcription from RNA polymerase I promoter Source: SGD
  • positive regulation of invasive growth in response to glucose limitation Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to heat stress Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionChromatin regulator, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33125-MONOMER.
ReactomeiR-SCE-3214847. HATs acetylate histones.
R-SCE-6804758. Regulation of TP53 Activity through Acetylation.
R-SCE-6811555. PI5P Regulates TP53 Acetylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein PHO23
Gene namesi
Name:PHO23
Ordered Locus Names:YNL097C
ORF Names:N2205
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL097C.
SGDiS000005041. PHO23.

Subcellular locationi

GO - Cellular componenti

  • histone deacetylase complex Source: SGD
  • Rpd3L complex Source: SGD

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002034401 – 330Transcriptional regulatory protein PHO23Add BLAST330

Proteomic databases

MaxQBiP50947.
PRIDEiP50947.

PTM databases

iPTMnetiP50947.

Interactioni

Subunit structurei

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.5 Publications

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi35726. 788 interactors.
DIPiDIP-4243N.
IntActiP50947. 7 interactors.
MINTiMINT-496149.
STRINGi4932.YNL097C.

Structurei

3D structure databases

ProteinModelPortaliP50947.
SMRiP50947.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.1 Publication

Sequence similaritiesi

Belongs to the ING family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri280 – 329PHD-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00890000140683.
HOGENOMiHOG000248215.
InParanoidiP50947.
OMAiCINTVPQ.
OrthoDBiEOG092C2K1R.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR028651. ING_fam.
IPR024610. ING_N_histone_binding.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
PANTHERiPTHR10333. PTHR10333. 1 hit.
PfamiView protein in Pfam
PF12998. ING. 1 hit.
SMARTiView protein in SMART
SM01408. ING. 1 hit.
SM00249. PHD. 1 hit.
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiView protein in PROSITE
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P50947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPANLFPG LNDITDVLEE FPLATSRYLT LLHEIDAKCV HSMPNLNERI
60 70 80 90 100
DKFLKKDFNK DHQTQVRLLN NINKIYEELM PSLEEKMHVS SIMLDNLDRL
110 120 130 140 150
TSRLELAYEV AIKNTEIPRG LRLGVDNHPA MHLHHELMEK IESKSNSKSS
160 170 180 190 200
QALKSESRRE AMAANRRQGE HYSASTHQQD DSKNDANYGG SRHESQDHTG
210 220 230 240 250
NNTNSRKRAN AANTNNADPE TKKRKRRVAT TAVSPSTIST ATAVNNGRIG
260 270 280 290 300
TSTASRGVSS VGNSNNSRIS RPKTNDYGEP LYCYCNQVAY GEMVGCDGAD
310 320 330
CELEWFHLPC IGLETLPKGK WYCDDCKKKL
Length:330
Mass (Da):37,024
Last modified:October 1, 1996 - v1
Checksum:i3BF7B519E77ED6EF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti8F → L in strain: SK1. 1 Publication1
Natural varianti35I → V in strain: SK1. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ115393 Genomic DNA. Translation: AAZ22511.1.
Z50161 Genomic DNA. Translation: CAA90529.1.
AY693076 Genomic DNA. Translation: AAT93095.1.
Z71373 Genomic DNA. Translation: CAA95973.1.
BK006947 Genomic DNA. Translation: DAA10449.1.
PIRiS58255.
RefSeqiNP_014302.3. NM_001182935.3.

Genome annotation databases

EnsemblFungiiYNL097C; YNL097C; YNL097C.
GeneIDi855626.
KEGGisce:YNL097C.

Similar proteinsi

Entry informationi

Entry nameiPHO23_YEAST
AccessioniPrimary (citable) accession number: P50947
Secondary accession number(s): D6W183, Q45TZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: August 30, 2017
This is version 159 of the entry and version 1 of the sequence. See 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names