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

Histone acetyltransferase mst1

Gene

mst1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me (By similarity).By similarity1 Publication

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei321Important for catalytic activityBy similarity1
Active sitei355Proton donor/acceptorBy similarity1
Binding sitei359Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri212 – 237C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

GO - Biological processi

  • centromere complex assembly Source: PomBase
  • double-strand break repair Source: PomBase
  • histone H3-K4 acetylation Source: PomBase
  • histone H4 acetylation Source: PomBase
  • negative regulation of heterochromatin assembly Source: PomBase
  • positive regulation of heterochromatin assembly Source: PomBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • replication fork protection Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionActivator, Chromatin regulator, Transferase
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-SPO-5693548. Sensing of DNA Double Strand Breaks.
R-SPO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase mst1 (EC:2.3.1.48By similarity)
Gene namesi
Name:mst1
Synonyms:esa1
ORF Names:SPAC637.12c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC637.12c.
PomBaseiSPAC637.12c. mst1.

Subcellular locationi

GO - Cellular componenti

  • NuA4 histone acetyltransferase complex Source: PomBase
  • nuclear chromatin Source: PomBase
  • nuclear pericentric heterochromatin Source: PomBase
  • nucleus Source: PomBase

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515641 – 463Histone acetyltransferase mst1Add BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei279N6-acetyllysine; by autocatalysisBy similarity1

Post-translational modificationi

Autoacetylation at Lys-279 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO94446.
PRIDEiO94446.

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex (By similarity). Interacts with arp4.By similarity1 Publication

Protein-protein interaction databases

BioGridi279924. 29 interactors.
IntActiO94446. 1 interactor.
MINTiMINT-8210884.
STRINGi4896.SPAC637.12c.1.

Structurei

3D structure databases

ProteinModelPortaliO94446.
SMRiO94446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 89ChromoAdd BLAST57
Domaini179 – 451MYST-type HATPROSITE-ProRule annotationAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni320 – 324Acetyl-CoA bindingBy similarity5
Regioni329 – 335Acetyl-CoA bindingBy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi262 – 283ESA1-RPD3 motifAdd BLAST22

Domaini

The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri212 – 237C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000182457.
InParanoidiO94446.
KOiK11304.
OMAiMNMVKYW.
OrthoDBiEOG092C043Q.
PhylomeDBiO94446.

Family and domain databases

InterProiView protein in InterPro
IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
IPR025995. Tudor-knot.
PfamiView protein in Pfam
PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
SMARTiView protein in SMART
SM00298. CHROMO. 1 hit.
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiView protein in PROSITE
PS51726. MYST_HAT. 1 hit.

Sequencei

Sequence statusi: Complete.

O94446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNDVDDESK IETKSYEAKD IVYKSKVFAF KDGEYRKAEI LMIQKRTRGV
60 70 80 90 100
VYYVHYNDYN KRLDEWITID NIDLSKGIEY PPPEKPKKAH GKGKSSKRPK
110 120 130 140 150
AVDRRRSITA PSKTEPSTPS TEKPEPSTPS GESDHGSNAG NESLPLLEED
160 170 180 190 200
HKPESLSKEQ EVERLRFSGS MVQNPHEIAR IRNINKICIG DHEIEPWYFS
210 220 230 240 250
PYPKEFSEVD IVYICSFCFC YYGSERQFQR HREKCTLQHP PGNEIYRDDY
260 270 280 290 300
ISFFEIDGRK QRTWCRNICL LSKLFLDHKM LYYDVDPFLF YCMCRRDEYG
310 320 330 340 350
CHLVGYFSKE KESSENYNLA CILTLPQYQR HGYGKLLIQF SYELTKREHK
360 370 380 390 400
HGSPEKPLSD LGLISYRAYW AEQIINLVLG MRTETTIDEL ANKTSMTTND
410 420 430 440 450
VLHTLQALNM LKYYKGQFII CISDGIEQQY ERLKNKKRRR INGDLLADWQ
460
PPVFHPSQLR FGW
Length:463
Mass (Da):54,390
Last modified:May 1, 1999 - v1
Checksum:iA5C6A4AEA1207902
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA22591.1.
AB027858 Genomic DNA. Translation: BAA87162.1.
PIRiT39004.
RefSeqiNP_594630.1. NM_001020058.2.

Genome annotation databases

EnsemblFungiiSPAC637.12c.1; SPAC637.12c.1:pep; SPAC637.12c.
GeneIDi2543506.
KEGGispo:SPAC637.12c.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiESA1_SCHPO
AccessioniPrimary (citable) accession number: O94446
Secondary accession number(s): Q9USC8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: May 1, 1999
Last modified: July 5, 2017
This is version 118 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families