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Q6CKE9 (ESA1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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 namesRecommended name:
Histone acetyltransferase ESA1

EC=2.3.1.48
Gene names
Name:ESA1
Ordered Locus Names:KLLA0F11209g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length439 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, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. 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-256 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 – 439439Histone acetyltransferase ESA1
PRO_0000051558

Regions

Region306 – 3127Acetyl-CoA binding By similarity
Motif239 – 26022ESA1-RPD3 motif By similarity

Sites

Active site2561 By similarity
Active site2981Nucleophile By similarity
Binding site3011Acetyl-CoA By similarity
Binding site3361Acetyl-CoA By similarity

Amino acid modifications

Modified residue2561N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CKE9 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 20E81CA743A33F81

FASTA43951,474
        10         20         30         40         50         60 
MSHGEEKEPG IPQKVDSIDE IFVGCKSWVL KDGQDRLAEI LSINSRRDPP KFYVHYEDFN 

        70         80         90        100        110        120 
KRLDEWITAD RLQIDKEVIF PRPKELEEKK DSKKKKQQQN KSATPQAASA TPDGGDVMDL 

       130        140        150        160        170        180 
DNLNVQGIPN EDISREDEIK KLRTSGSMTQ NQNEVARVRN LNKVIMGKYE IEPWYFSPYP 

       190        200        210        220        230        240 
IELTDEDVVY IDDFSLQYFG SKKQYERYRK KCTLRHPPGN EIYRDDYVSF FEIDGRKQRT 

       250        260        270        280        290        300 
WCRNLCLLSK LFLDHKTLYY DVDPFLFYCM TRRDELGHHI VGYFSKEKES ADAYNVACIL 

       310        320        330        340        350        360 
TLPQYQRMGY GRLLIEFSYE LSKKEGKVGS PEKPLSDLGL LSYRAYWADT LIKLLVEHGQ 

       370        380        390        400        410        420 
EITIDEVSSI SSMTTTDILH TAKALEILRF YRGQHVLYLN SDVMKRYKKL KNNKRRSIDP 

       430 
QKLIWTPPVF TASQLRFAW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382126 Genomic DNA. Translation: CAG98298.1.
RefSeqXP_455590.1. XM_455590.1.

3D structure databases

ProteinModelPortalQ6CKE9.
SMRQ6CKE9. Positions 16-88, 156-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.Q6CKE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2895129.
KEGGkla:KLLA0F11209g.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
KOK11304.
OMASQLRFAW.
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. 1 hit.
ProtoNetSearch...

Entry information

Entry nameESA1_KLULA
AccessionPrimary (citable) accession number: Q6CKE9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 68 of the entry and version 1 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