Reviewed, UniProtKB/Swiss-Prot Q9UTM7 (HAT1_SCHPO)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase type B catalytic subunit
    EC=2.3.1.48

Gene names

Name:	hat1
ORF Names:	SPAC139.06, SPAC23C4.01

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair By similarity.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Component of the HAT-B complex composed of at least hat1 and hat2. The HAT-B complex binds to histone H4 tail By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the HAT1 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro histone acetylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear chromatin Non-traceable author statement. Source: GeneDB_SPombe
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 378	378	Histone acetyltransferase type B catalytic subunit		PRO_0000116791

Sequences

	Sequence		Length	Mass (Da)
	Q9UTM7-1 [UniParc]. Last modified March 29, 2004. Version 2. Checksum: 6875CD93528FB3B9	FASTA	378	44,051
	10 20 30 40 50 60 MSAVDEWVHN ANECIEIVQV NEKHEKDCQY HPSNTYAIFG DAEVIYGYKD LNVTITYECP 70 80 90 100 110 120 LMVPKLEISY SERLAPDSGV EPTDIEGTLN TYLKDRSIKV EGNSFDVHSA NSIHNYSFNG 130 140 150 160 170 180 KTFKILQATV LEASEIMQHL QIFSLFFIEG GSFIDLNDPR WMVYLLYETT EDDYCLRGYC 190 200 210 220 230 240 TVYKYYKWDK LIHDGIRARI SQFVILPPFQ HQGHGSQLYN AIVSTFLKNP KILDFTVEDA 250 260 270 280 290 300 SEAFDSLRDH CDYKRLLSMG IFSEPDFHPS LSRQWINSKI AETKLTQRQF SRCCELAFTT 310 320 330 340 350 360 KLKKLSLLER KSVRLGIKER IFRQNLDVLL QLDKSERIEK IHNAYENQFD EYKQIVKKLP 370 KLKEDSPRKR QKLAQSSS

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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB59620.1.
PIR	T37607. T38257.
RefSeq	NP_593173.2.
3D structure databases
HSSP	HSSP built from PDB template 1BOB based on UniProtKB Q12341.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UTM7.
Genome annotation databases
GeneID	2542502.
GenomeReviews	Gene locus hat1 in contig CU329670_GR.
KEGG	spo:SPAC139.06.
Organism-specific databases
GeneDB_Spombe	SPAC139.06.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001959-MON.
BRENDA	2.3.1.48. 653.
Gene expression databases
ArrayExpress	Q9UTM7.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR019467. Hat1_N. IPR017380. Hist_AcTrfase_B-typ_cat-su. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF10394. Hat1_N. 1 hit. [Graphical view]
PIRSF	PIRSF038084. HAT-B_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HAT1_SCHPO

Accession

Primary (citable) accession number: Q9UTM7
Secondary accession number(s): O13922

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 29, 2004
Last modified:	September 22, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)