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Q6BU95

- ESA1_DEBHA

UniProt

Q6BU95 - ESA1_DEBHA

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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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, histone H2B to form H2BK16ac, 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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei334 – 3341Important for catalytic activityBy similarity
Active sitei368 – 3681Proton donor/acceptorBy similarity
Binding sitei372 – 3721Acetyl-CoABy similarity

GO - Molecular functioni

  1. histone acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase ESA1 (EC:2.3.1.48By similarity)
Gene namesi
Name:ESA1
Ordered Locus Names:DEHA2C12628g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
ProteomesiUP000000599: Chromosome C

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Histone acetyltransferase ESA1PRO_0000051556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei292 – 2921N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-292 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex.By similarity

Protein-protein interaction databases

STRINGi4959.Q6BU95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 509318MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni333 – 3375Acetyl-CoA bindingBy similarity
Regioni342 – 3487Acetyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi275 – 29622ESA1-RPD3 motifBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi101 – 12929Lys-richAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiQ6BU95.
KOiK11304.
OMAiENHISEI.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 2 hits.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6BU95-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVGEDKSGT ATPQHNTSIR ITDDEERSDE KKFTDDDIIT GCKLYVSKDG
60 70 80 90 100
EYRLAEILQD HMKKGKKVFY VHYQEFNKRL DEWISADRID FTRALISPQV
110 120 130 140 150
KVDKKDDKKE GKSKTSKKSK SKNGKTGSKS VTSTPQPNED TAPGTPRNDD
160 170 180 190 200
EMDLDNLNVQ GLKRPGEEVS REDEIKKLRT SGSMTQNHSE VARVRNLSSV
210 220 230 240 250
ILGEHIIEPW YFSPYPIELT EEDEIYICDF TLAYFGSLKQ FERFRTKCSM
260 270 280 290 300
KHPPGNEIYR DSKVSFWEID GRKQRTWCRN LCLLSKLFLD HKTLYYDVDP
310 320 330 340 350
FLFYIMTVKS SQGHHVVGYF SKEKESADGY NVACILTLPC YQKMGFGKLL
360 370 380 390 400
IQFSYMLSNV ENKVGSPEKP LSDLGLLSYR AFWTDTLVKL LVERNNPHLF
410 420 430 440 450
KKNNPQLLTE ASSKDSSVSP PPGGRQSANI QNGNTPSSDI TIDEISSITC
460 470 480 490 500
MTTTDILHTL TALQILRYYK GQHIIVITDH VMAMYDKLVK KIKDKKKHEL
510 520
DPSKLSWTPP AFTANQLRFG W
Length:521
Mass (Da):59,628
Last modified:December 16, 2008 - v2
Checksum:i0F7475FDB336E216
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382135 Genomic DNA. Translation: CAG86300.2.
RefSeqiXP_458224.2. XM_458224.1.

Genome annotation databases

GeneIDi2900534.
KEGGidha:DEHA2C12628g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382135 Genomic DNA. Translation: CAG86300.2 .
RefSeqi XP_458224.2. XM_458224.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4959.Q6BU95.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2900534.
KEGGi dha:DEHA2C12628g.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000182457.
InParanoidi Q6BU95.
KOi K11304.
OMAi ENHISEI.
OrthoDBi EOG7RFTRR.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 2 hits.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Entry informationi

Entry nameiESA1_DEBHA
AccessioniPrimary (citable) accession number: Q6BU95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 16, 2008
Last modified: October 29, 2014
This is version 73 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3