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Protein

Histone acetyltransferase mst2

Gene

mst2

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

Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation. Negatively regulates telomere silencing. Telomere silencing is increased due to histone hypoacetylation and/or an increase in the ratio of methylated histones to acetylated histones. Telomeric histone acetylation contributes to normal meiotic progression.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei243Acetyl-CoABy similarity1
Active sitei274Proton donor/acceptorBy similarity1
Binding sitei278Acetyl-CoABy similarity1
Binding sitei287Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri131 – 156C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

  • histone acetyltransferase activity (H3-K14 specific) Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB-KW
  • heterochromatin maintenance involved in chromatin silencing at centromere outer repeat region Source: PomBase
  • histone modification Source: PomBase
  • negative regulation of chromatin silencing at telomere Source: PomBase
  • negative regulation of extent of heterochromatin assembly Source: PomBase
  • regulation of meiotic cell cycle Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Transferase

Keywords - Biological processi

DNA damage

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-6804758. Regulation of TP53 Activity through Acetylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase mst2 (EC:2.3.1.48By similarity)
Gene namesi
Name:mst2
ORF Names:SPAC17G8.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC17G8.13c.
PomBaseiSPAC17G8.13c. mst2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric outer repeat region Source: GOC
  • cytosol Source: PomBase
  • Mst2 histone acetyltransferase complex Source: PomBase
  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515651 – 407Histone acetyltransferase mst2Add BLAST407

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198N6-acetyllysine; by autocatalysisBy similarity1

Post-translational modificationi

Autoacetylation at Lys-198 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ10325.
PRIDEiQ10325.

Interactioni

Subunit structurei

Component of the mst2 complex composed of at least eaf6, mst2, nto1, pdp3, ptf1, ptf2 and tfg3.1 Publication

Protein-protein interaction databases

BioGridi278645. 98 interactors.
MINTiMINT-4698771.

Structurei

3D structure databases

ProteinModelPortaliQ10325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 372MYST-type HATPROSITE-ProRule annotationAdd BLAST275

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni241 – 243Acetyl-CoA bindingBy similarity3
Regioni248 – 254Acetyl-CoA bindingBy similarity7

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC MYST-type zinc finger.PROSITE-ProRule annotation
Contains 1 MYST-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri131 – 156C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiQ10325.
KOiK11378.
OMAiHEVEYTR.
OrthoDBiEOG092C043Q.
PhylomeDBiQ10325.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR002717. HAT_MYST-type.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPATILKSTA SSKTLLIIKF DTNSSRYPFY KKHLLELNSE STFLGLLTKG
60 70 80 90 100
QADTSITRLN QDDVRLFEKA KTVADRTKDV AYSFSDPILS TQLRTPPPQP
110 120 130 140 150
TSIRYLYFGT YRIKPWYTSP YPEEYSCAKN LYICESCLKY MNSDHVLQRH
160 170 180 190 200
KMKCSWSYPP GDEIYRDKNI SIFEVDGQRQ PIYCQNLCLL AKMFLHSKML
210 220 230 240 250
YYDVEPFLFY VLTEFDGQEC KVIGYFSKEK RSASDYNVSC ILTLPIYQRR
260 270 280 290 300
GYGVFLIDFS YLLTQVEGKL GSPEKPLSDL GLVTYRSYWK MRVAKALLEI
310 320 330 340 350
TTPISINAIA KSTSMVCDDV ISTLESLSVF KYDPLKKKYV LQLKRDELEN
360 370 380 390 400
VYKAWNIKHP QRVNPKLLRW TPYLGEEQIS NLLLKENILI PLPQKRLLDN

SHHLDSV
Length:407
Mass (Da):47,275
Last modified:October 1, 1996 - v1
Checksum:i27B70EB7AB947102
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93696.1.
PIRiT37865.
RefSeqiNP_593736.1. NM_001019167.2.

Genome annotation databases

EnsemblFungiiSPAC17G8.13c.1; SPAC17G8.13c.1:pep; SPAC17G8.13c.
GeneIDi2542170.
KEGGispo:SPAC17G8.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93696.1.
PIRiT37865.
RefSeqiNP_593736.1. NM_001019167.2.

3D structure databases

ProteinModelPortaliQ10325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278645. 98 interactors.
MINTiMINT-4698771.

Proteomic databases

MaxQBiQ10325.
PRIDEiQ10325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC17G8.13c.1; SPAC17G8.13c.1:pep; SPAC17G8.13c.
GeneIDi2542170.
KEGGispo:SPAC17G8.13c.

Organism-specific databases

EuPathDBiFungiDB:SPAC17G8.13c.
PomBaseiSPAC17G8.13c. mst2.

Phylogenomic databases

InParanoidiQ10325.
KOiK11378.
OMAiHEVEYTR.
OrthoDBiEOG092C043Q.
PhylomeDBiQ10325.

Enzyme and pathway databases

ReactomeiR-SPO-6804758. Regulation of TP53 Activity through Acetylation.

Miscellaneous databases

PROiQ10325.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR002717. HAT_MYST-type.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMST2_SCHPO
AccessioniPrimary (citable) accession number: Q10325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 5, 2016
This is version 113 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

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.