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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei243 – 2431Acetyl-CoABy similarity
Active sitei274 – 2741Proton donor/acceptorBy similarity
Binding sitei278 – 2781Acetyl-CoABy similarity
Binding sitei287 – 2871Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri132 – 15423C2HC-typeAdd
BLAST

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 H3-K14 acetylation Source: GOC
  • negative regulation of chromatin silencing at telomere 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

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
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

  • 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Histone acetyltransferase mst2PRO_0000051565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ10325.

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 interactions.
MINTiMINT-4698771.
STRINGi4896.SPAC17G8.13c.1.

Structurei

3D structure databases

ProteinModelPortaliQ10325.
SMRiQ10325. Positions 102-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 372275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni241 – 2433Acetyl-CoA bindingBy similarity
Regioni248 – 2547Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri132 – 15423C2HC-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
InParanoidiQ10325.
KOiK11378.
OrthoDBiEOG7RFTRR.
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.
SMRiQ10325. Positions 102-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278645. 98 interactions.
MINTiMINT-4698771.
STRINGi4896.SPAC17G8.13c.1.

Proteomic databases

MaxQBiQ10325.

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

eggNOGiCOG5027.
InParanoidiQ10325.
KOiK11378.
OrthoDBiEOG7RFTRR.
PhylomeDBiQ10325.

Miscellaneous databases

NextBioi20803241.
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...

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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  3. "Histone H3 lysine 14 acetylation is required for activation of a DNA damage checkpoint in fission yeast."
    Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J., Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J., Jia S.
    J. Biol. Chem. 287:4386-4393(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX, FUNCTION.
  4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

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: June 24, 2015
This is version 103 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.