Q10325 (MST2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase mst2
EC=2.3.1.48

Gene names

Name:	mst2
ORF Names:	SPAC17G8.13c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of chromatin silencing at telomere Inferred from mutant phenotype Ref.2. Source: PomBase regulation of meiotic cell cycle Inferred from mutant phenotype Ref.2. Source: PomBase
Cellular_component	cytosol Inferred from direct assay Ref.4. Source: PomBase histone acetyltransferase complex Inferred from sequence orthology. Source: PomBase nuclear chromatin Inferred from direct assay Ref.2. Source: PomBase
Molecular_function	histone acetyltransferase activity Non-traceable author statement. Source: PomBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 407	407	Histone acetyltransferase mst2		PRO_0000051565
Regions
	Zinc finger	132 – 154	23	C2HC-type
	Region	248 – 254	7	Acetyl-CoA binding By similarity
Sites
	Active site	198	1	By similarity
	Active site	240	1	Nucleophile By similarity
	Binding site	243	1	Acetyl-CoA By similarity
	Binding site	278	1	Acetyl-CoA By similarity
Amino acid modifications
	Modified residue	198	1	N6-acetyllysine; by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10325 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 27B70EB7AB947102	FASTA	407	47,275
	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

References

	« Hide 'large scale' referencesShow '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. , 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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA93696.1.
PIR	T37865.
RefSeq	NP_593736.1. NM_001019167.2.
3D structure databases
ProteinModelPortal	Q10325.
SMR	Q10325. Positions 102-372.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC17G8.13c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC17G8.13c.1; SPAC17G8.13c.1:pep; SPAC17G8.13c.
GeneID	2542170.
KEGG	spo:SPAC17G8.13c.
Organism-specific databases
PomBase	SPAC17G8.13c.
Phylogenomic databases
eggNOG	COG5027.
KO	K11378.
OMA	NICLVAR.
OrthoDB	EOG4F21C3.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR002717. MOZ_SAS. [Graphical view]
Pfam	PF01853. MOZ_SAS. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNet	Search...
Other
NextBio	20803241.

Entry information

Entry name

MST2_SCHPO

Accession

Primary (citable) accession number: Q10325

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program