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Q9UTM7 (HAT1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase type B catalytic subunit

EC=2.3.1.48
Gene names
Name:hat1
ORF Names:SPAC139.06, SPAC23C4.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 + acetyl-[histone].

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Histone acetyltransferase type B catalytic subunit
PRO_0000116791

Sequences

Sequence LengthMass (Da)Tools
Q9UTM7 [UniParc].

Last modified March 29, 2004. Version 2.
Checksum: 6875CD93528FB3B9

FASTA37844,051
        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 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB59620.1.
PIRT37607.
T38257.
RefSeqNP_593173.2. NM_001018570.2.

3D structure databases

ProteinModelPortalQ9UTM7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278960. 51 interactions.
MINTMINT-4710866.
STRING4896.SPAC139.06-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC139.06.1; SPAC139.06.1:pep; SPAC139.06.
GeneID2542502.
KEGGspo:SPAC139.06.

Organism-specific databases

PomBaseSPAC139.06.

Phylogenomic databases

eggNOGNOG326277.
KOK11303.
OMAWINSKIA.
OrthoDBEOG7HTHSD.
PhylomeDBQ9UTM7.

Family and domain databases

Gene3D1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERPTHR12046. PTHR12046. 1 hit.
PfamPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

NextBio20803555.
PROQ9UTM7.

Entry information

Entry nameHAT1_SCHPO
AccessionPrimary (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: April 16, 2014
This is version 75 of the entry and version 2 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