O94446 (ESA1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase mst1
EC=2.3.1.48

Gene names

Name:	mst1
Synonyms:	esa1
ORF Names:	SPAC637.12c

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	463 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Component of the NuA4 histone acetyltransferase complex By similarity. Interacts with arp4. Ref.3
Subcellular location	Nucleus Ref.2 Ref.4.
Domain	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.
Post-translational modification	Autoacetylation at Lys-279 is required for proper function By similarity.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 chromo domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator Chromatin regulator Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	centromere complex assembly Inferred from genetic interaction PubMed 18505873. Source: PomBase chromatin remodeling Non-traceable author statement. Source: PomBase double-strand break repair Inferred from genetic interaction PubMed 18505873. Source: PomBase mitotic sister chromatid segregation Inferred from mutant phenotype PubMed 18505873. Source: PomBase regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW replication fork protection Inferred from genetic interaction PubMed 18505873. Source: PomBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NuA4 histone acetyltransferase complex Inferred from direct assay PubMed 19040720. Source: PomBase nuclear chromatin Inferred from direct assay Ref.4. Source: PomBase
Molecular_function	H4 histone acetyltransferase activity Inferred from sequence orthology. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 463	463	Histone acetyltransferase mst1		PRO_0000051564
Regions
	Domain	33 – 89	57	Chromo
	Region	329 – 335	7	Acetyl-CoA binding By similarity
	Motif	262 – 283	22	ESA1-RPD3 motif
Sites
	Active site	279	1	By similarity
	Active site	321	1	Nucleophile By similarity
	Binding site	324	1	Acetyl-CoA By similarity
	Binding site	359	1	Acetyl-CoA By similarity
Amino acid modifications
	Modified residue	279	1	N6-acetyllysine; by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94446 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: A5C6A4AEA1207902	FASTA	463	54,390
	10 20 30 40 50 60 MSNDVDDESK IETKSYEAKD IVYKSKVFAF KDGEYRKAEI LMIQKRTRGV VYYVHYNDYN 70 80 90 100 110 120 KRLDEWITID NIDLSKGIEY PPPEKPKKAH GKGKSSKRPK AVDRRRSITA PSKTEPSTPS 130 140 150 160 170 180 TEKPEPSTPS GESDHGSNAG NESLPLLEED HKPESLSKEQ EVERLRFSGS MVQNPHEIAR 190 200 210 220 230 240 IRNINKICIG DHEIEPWYFS PYPKEFSEVD IVYICSFCFC YYGSERQFQR HREKCTLQHP 250 260 270 280 290 300 PGNEIYRDDY ISFFEIDGRK QRTWCRNICL LSKLFLDHKM LYYDVDPFLF YCMCRRDEYG 310 320 330 340 350 360 CHLVGYFSKE KESSENYNLA CILTLPQYQR HGYGKLLIQF SYELTKREHK HGSPEKPLSD 370 380 390 400 410 420 LGLISYRAYW AEQIINLVLG MRTETTIDEL ANKTSMTTND VLHTLQALNM LKYYKGQFII 430 440 450 460 CISDGIEQQY ERLKNKKRRR INGDLLADWQ PPVFHPSQLR FGW

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]	"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(2000) [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(2005) [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(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA22591.1. AB027858 Genomic DNA. Translation: BAA87162.1.
PIR	T39004.
RefSeq	NP_594630.1. NM_001020058.2.
3D structure databases
ProteinModelPortal	O94446.
SMR	O94446. Positions 179-452.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC637.12c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC637.12c.1; SPAC637.12c.1:pep; SPAC637.12c.
GeneID	2543506.
KEGG	spo:SPAC637.12c.
Organism-specific databases
PomBase	SPAC637.12c.
Phylogenomic databases
eggNOG	COG5027.
HOGENOM	HOG000182457.
KO	K11304.
OMA	CSMKHPP.
OrthoDB	EOG4R7ZKC.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR002717. MOZ_SAS. IPR025995. Tudor-knot. [Graphical view]
Pfam	PF01853. MOZ_SAS. 1 hit. PF11717. Tudor-knot. 1 hit. [Graphical view]
SMART	SM00298. CHROMO. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF54160. Chromodomain-like. 1 hit.
PROSITE	PS00598. CHROMO_1. False negative. PS50013. CHROMO_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	20804516.

Entry information

Entry name

ESA1_SCHPO

Accession

Primary (citable) accession number: O94446
Secondary accession number(s): Q9USC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	May 1, 1999
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