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Q6BU95 (ESA1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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, 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 activity

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

Subunit structure

Component of the NuA4 histone acetyltransferase complex By similarity.

Subcellular location

Nucleus By similarity.

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-292 is required for proper function By similarity.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionActivator
Chromatin regulator
Transferase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Histone acetyltransferase ESA1
PRO_0000051556

Regions

Region342 – 3487Acetyl-CoA binding By similarity
Motif275 – 29622ESA1-RPD3 motif By similarity
Compositional bias101 – 12929Lys-rich

Sites

Active site2921 By similarity
Active site3341Nucleophile By similarity
Binding site3371Acetyl-CoA By similarity
Binding site3721Acetyl-CoA By similarity

Amino acid modifications

Modified residue2921N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6BU95 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 0F7475FDB336E216

FASTA52159,628
        10         20         30         40         50         60 
MSVGEDKSGT ATPQHNTSIR ITDDEERSDE KKFTDDDIIT GCKLYVSKDG EYRLAEILQD 

        70         80         90        100        110        120 
HMKKGKKVFY VHYQEFNKRL DEWISADRID FTRALISPQV KVDKKDDKKE GKSKTSKKSK 

       130        140        150        160        170        180 
SKNGKTGSKS VTSTPQPNED TAPGTPRNDD EMDLDNLNVQ GLKRPGEEVS REDEIKKLRT 

       190        200        210        220        230        240 
SGSMTQNHSE VARVRNLSSV ILGEHIIEPW YFSPYPIELT EEDEIYICDF TLAYFGSLKQ 

       250        260        270        280        290        300 
FERFRTKCSM KHPPGNEIYR DSKVSFWEID GRKQRTWCRN LCLLSKLFLD HKTLYYDVDP 

       310        320        330        340        350        360 
FLFYIMTVKS SQGHHVVGYF SKEKESADGY NVACILTLPC YQKMGFGKLL IQFSYMLSNV 

       370        380        390        400        410        420 
ENKVGSPEKP LSDLGLLSYR AFWTDTLVKL LVERNNPHLF KKNNPQLLTE ASSKDSSVSP 

       430        440        450        460        470        480 
PPGGRQSANI QNGNTPSSDI TIDEISSITC MTTTDILHTL TALQILRYYK GQHIIVITDH 

       490        500        510        520 
VMAMYDKLVK KIKDKKKHEL DPSKLSWTPP AFTANQLRFG W 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382135 Genomic DNA. Translation: CAG86300.2.
RefSeqXP_458224.2. XM_458224.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4959.Q6BU95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2900534.
KEGGdha:DEHA2C12628g.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
KOK11304.
OMAENHISEI.
OrthoDBEOG7RFTRR.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 2 hits.
ProtoNetSearch...

Entry information

Entry nameESA1_DEBHA
AccessionPrimary (citable) accession number: Q6BU95
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 71 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