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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 + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei321 – 3211Important for catalytic activityBy similarity
Active sitei355 – 3551Proton donor/acceptorBy similarity
Binding sitei359 – 3591Acetyl-CoABy similarity

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: PomBase
  2. histone acetyltransferase activity (H3-K4 specific) Source: PomBase

GO - Biological processi

  1. centromere complex assembly Source: PomBase
  2. double-strand break repair Source: PomBase
  3. histone H3-K4 acetylation Source: PomBase
  4. histone H4 acetylation Source: PomBase
  5. mitotic sister chromatid segregation Source: PomBase
  6. positive regulation of heterochromatin assembly Source: PomBase
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. replication fork protection Source: PomBase
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

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
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC637.12c.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. NuA4 histone acetyltransferase complex Source: PomBase
  2. nuclear chromatin Source: PomBase
  3. nuclear pericentric heterochromatin Source: PomBase
  4. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Histone acetyltransferase mst1PRO_0000051564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei279 – 2791N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO94446.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi279924. 29 interactions.
IntActiO94446. 1 interaction.
MINTiMINT-8210884.
STRINGi4896.SPAC637.12c-1.

Structurei

3D structure databases

ProteinModelPortaliO94446.
SMRiO94446. Positions 179-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 8957ChromoAdd
BLAST
Domaini179 – 450272MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni320 – 3245Acetyl-CoA bindingBy similarity
Regioni329 – 3357Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi262 – 28322ESA1-RPD3 motifAdd
BLAST

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
Contains 1 chromo domain.Curated

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiO94446.
KOiK11304.
OMAiNIYSICM.
OrthoDBiEOG7RFTRR.
PhylomeDBiO94446.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

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:April 30, 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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO94446.
SMRiO94446. Positions 179-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279924. 29 interactions.
IntActiO94446. 1 interaction.
MINTiMINT-8210884.
STRINGi4896.SPAC637.12c-1.

Proteomic databases

MaxQBiO94446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

PomBaseiSPAC637.12c.

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiO94446.
KOiK11304.
OMAiNIYSICM.
OrthoDBiEOG7RFTRR.
PhylomeDBiO94446.

Miscellaneous databases

NextBioi20804516.
PROiO94446.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 263-441, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  3. "BAF53/Arp4 homolog Alp5 in fission yeast is required for histone H4 acetylation, kinetochore-spindle attachment, and gene silencing at centromere."
    Minoda A., Saitoh S., Takahashi K., Toda T.
    Mol. Biol. Cell 16:316-327(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARP4.
  4. "Schizosaccharomyces pombe mst2+ encodes a MYST family histone acetyltransferase that negatively regulates telomere silencing."
    Gomez E.B., Espinosa J.M., Forsburg S.L.
    Mol. Cell. Biol. 25:8887-8903(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiESA1_SCHPO
AccessioniPrimary (citable) accession number: O94446
Secondary accession number(s): Q9USC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2004
Last sequence update: April 30, 1999
Last modified: March 31, 2015
This is version 100 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.