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Protein

Histone acetyltransferase gcn5

Gene

gcn5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, and with a lower preference histone H4 to form H4K8ac and H4K16ac. Acetylation of histones gives a specific tag for epigenetic transcription activation (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei191 – 1911Proton donor/acceptorBy similarity
Sitei191 – 1911Important for catalytic activityBy similarity

GO - Molecular functioni

  1. H3 histone acetyltransferase activity Source: PomBase

GO - Biological processi

  1. chromatin remodeling Source: PomBase
  2. histone H3 acetylation Source: PomBase
  3. negative regulation of leucine import Source: PomBase
  4. negative regulation of transcription from RNA polymerase II promoter Source: PomBase
  5. reciprocal meiotic recombination Source: PomBase
  6. regulation of transcription from RNA polymerase II promoter Source: PomBase
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase gcn5 (EC:2.3.1.48)
Gene namesi
Name:gcn5
ORF Names:SPAC1952.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1952.05.
PomBaseiSPAC1952.05.

Subcellular locationi

  1. Nucleus By similarity

GO - Cellular componenti

  1. nuclear chromatin Source: PomBase
  2. nucleus Source: PomBase
  3. SAGA complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Histone acetyltransferase gcn5PRO_0000211199Add
BLAST

Proteomic databases

MaxQBiQ9UUK2.

Interactioni

Subunit structurei

Interacts with taf72.1 Publication

Protein-protein interaction databases

BioGridi278971. 268 interactions.
IntActiQ9UUK2. 3 interactions.
MINTiMINT-8210502.
STRINGi4896.SPAC1952.05-1.

Structurei

3D structure databases

ProteinModelPortaliQ9UUK2.
SMRiQ9UUK2. Positions 118-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini118 – 273156N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST
Domaini360 – 43071BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni195 – 1973Acetyl-CoA bindingBy similarity
Regioni202 – 2087Acetyl-CoA bindingBy similarity
Regioni234 – 2374Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000192257.
InParanoidiQ9UUK2.
KOiK06062.
OMAiLLKQKEC.
OrthoDBiEOG7XM37B.
PhylomeDBiQ9UUK2.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UUK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSLNDQTR PPDSSVVDST SSNFPNASND SVHDKPVKQD EQSNPNVREA
60 70 80 90 100
IANSDGQESL AVKENKDTES SSSHFVPNGV SNSKKRKLVA TDLDVDFDIS
110 120 130 140 150
SVRVTEKPSV LEEKSGVIQF RVVSNDDTAD SMIMLTGLKN IFMKQLPKMP
160 170 180 190 200
KEYITRLIYD RNHLSMTIVK DNLHVVGGIT YRPFEQRGFA EIVFCAIASN
210 220 230 240 250
EQVRGYGSHL MNHLKDYVRG TTTIQHFLTY ADNYAIGYFK KQGFTKEITL
260 270 280 290 300
DKSIWVGYIK DYEGGTLMQC TMIPKIKYLE ANLILAIQKA AVVSKINRIT
310 320 330 340 350
RSNVVYPGLD VFKDGPAHIE PSQVPGLMEV GWCKEMEELS KKPRPKPFFA
360 370 380 390 400
VLEMLFTEMQ NHPSSWPFMQ PVSKEDVPDY YEVIEHPMDL STMEFRLRNN
410 420 430 440 450
QYESVEEFIR DAKYIFDNCR SYNDSNTTYY KNADRLEKFF QKKLRETEYS

HLAD
Length:454
Mass (Da):51,976
Last modified:May 1, 2000 - v1
Checksum:iFF99039B00E8ECB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB162439 Genomic DNA. Translation: BAD11106.1.
CU329670 Genomic DNA. Translation: CAB52569.1.
PIRiT37933.
RefSeqiNP_594807.1. NM_001020236.2.

Genome annotation databases

EnsemblFungiiSPAC1952.05.1; SPAC1952.05.1:pep; SPAC1952.05.
GeneIDi2542513.
KEGGispo:SPAC1952.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB162439 Genomic DNA. Translation: BAD11106.1.
CU329670 Genomic DNA. Translation: CAB52569.1.
PIRiT37933.
RefSeqiNP_594807.1. NM_001020236.2.

3D structure databases

ProteinModelPortaliQ9UUK2.
SMRiQ9UUK2. Positions 118-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278971. 268 interactions.
IntActiQ9UUK2. 3 interactions.
MINTiMINT-8210502.
STRINGi4896.SPAC1952.05-1.

Proteomic databases

MaxQBiQ9UUK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1952.05.1; SPAC1952.05.1:pep; SPAC1952.05.
GeneIDi2542513.
KEGGispo:SPAC1952.05.

Organism-specific databases

EuPathDBiFungiDB:SPAC1952.05.
PomBaseiSPAC1952.05.

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000192257.
InParanoidiQ9UUK2.
KOiK06062.
OMAiLLKQKEC.
OrthoDBiEOG7XM37B.
PhylomeDBiQ9UUK2.

Miscellaneous databases

NextBioi20803566.
PROiQ9UUK2.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Roles of histone acetylation and chromatin remodeling factor in a meiotic recombination hotspot."
    Yamada T., Mizuno K., Hirota K., Kon N., Wahls W.P., Hartsuiker E., Murofushi H., Shibata T., Ohta K.
    EMBO J. 23:1792-1803(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "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.
  3. "Two WD repeat-containing TATA-binding protein-associated factors in fission yeast that suppress defects in the anaphase-promoting complex."
    Mitsuzawa H., Seino H., Yamao F., Ishihama A.
    J. Biol. Chem. 276:17117-17124(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF72.

Entry informationi

Entry nameiGCN5_SCHPO
AccessioniPrimary (citable) accession number: Q9UUK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.