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Q10325 (MST2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone acetyltransferase mst2

EC=2.3.1.48
Gene names
Name:mst2
ORF Names:SPAC17G8.13c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3

Catalytic activity

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

Subunit structure

Component of the mst2 complex composed of at least eaf6, mst2, nto1, pdp3, ptf1, ptf2 and tfg3. Ref.3

Subcellular location

Cytoplasm. Nucleus Ref.2 Ref.4.

Post-translational modification

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

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407Histone acetyltransferase mst2
PRO_0000051565

Regions

Zinc finger132 – 15423C2HC-type
Region248 – 2547Acetyl-CoA binding By similarity

Sites

Active site1981 By similarity
Active site2401Nucleophile By similarity
Binding site2431Acetyl-CoA By similarity
Binding site2781Acetyl-CoA By similarity

Amino acid modifications

Modified residue1981N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q10325 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 27B70EB7AB947102

FASTA40747,275
        10         20         30         40         50         60 
MPATILKSTA SSKTLLIIKF DTNSSRYPFY KKHLLELNSE STFLGLLTKG QADTSITRLN 

        70         80         90        100        110        120 
QDDVRLFEKA KTVADRTKDV AYSFSDPILS TQLRTPPPQP TSIRYLYFGT YRIKPWYTSP 

       130        140        150        160        170        180 
YPEEYSCAKN LYICESCLKY MNSDHVLQRH KMKCSWSYPP GDEIYRDKNI SIFEVDGQRQ 

       190        200        210        220        230        240 
PIYCQNLCLL AKMFLHSKML YYDVEPFLFY VLTEFDGQEC KVIGYFSKEK RSASDYNVSC 

       250        260        270        280        290        300 
ILTLPIYQRR GYGVFLIDFS YLLTQVEGKL GSPEKPLSDL GLVTYRSYWK MRVAKALLEI 

       310        320        330        340        350        360 
TTPISINAIA KSTSMVCDDV ISTLESLSVF KYDPLKKKYV LQLKRDELEN VYKAWNIKHP 

       370        380        390        400 
QRVNPKLLRW TPYLGEEQIS NLLLKENILI PLPQKRLLDN SHHLDSV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA93696.1.
PIRT37865.
RefSeqNP_593736.1. NM_001019167.2.

3D structure databases

ProteinModelPortalQ10325.
SMRQ10325. Positions 102-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278645. 96 interactions.
MINTMINT-4698771.
STRING4896.SPAC17G8.13c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC17G8.13c.1; SPAC17G8.13c.1:pep; SPAC17G8.13c.
GeneID2542170.
KEGGspo:SPAC17G8.13c.

Organism-specific databases

PomBaseSPAC17G8.13c.

Phylogenomic databases

eggNOGCOG5027.
KOK11378.
OMAICEHTHT.
OrthoDBEOG7RFTRR.
PhylomeDBQ10325.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR002717. MOZ_SAS.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

NextBio20803241.

Entry information

Entry nameMST2_SCHPO
AccessionPrimary (citable) accession number: Q10325
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names