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Q6C710 (ESA1_YARLI) 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:YALI0E04675g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia

Protein attributes

Sequence length469 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.

Post-translational modification

Autoacetylation at Lys-285 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
Reference 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 – 469469Histone acetyltransferase ESA1
PRO_0000051561

Regions

Region335 – 3417Acetyl-CoA binding By similarity
Compositional bias103 – 12826Lys-rich

Sites

Active site2851 By similarity
Active site3271Nucleophile By similarity
Binding site3301Acetyl-CoA By similarity
Binding site3651Acetyl-CoA By similarity

Amino acid modifications

Modified residue2851N6-acetyllysine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6C710 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 50ABF9A067AD9140

FASTA46953,908
        10         20         30         40         50         60 
MALAEADLPN GKTNGKASGS EETPAPVQKV DMNVAINELR VGCKVHVEKD GEDRVAEILS 

        70         80         90        100        110        120 
VQMRRGNLEF YVHYVEFNKR LDERIAATRV DLSQGVIWPE PEKPKKPLSG AAKESSKEKK 

       130        140        150        160        170        180 
KNPSKKQKLT DSAATTPGAN SEDVMDLDNL QVNGTTQDPD NFNRDEEIEK LRTGGSMTQS 

       190        200        210        220        230        240 
SHEVARVRNL QRIVLGNHVI EPWYFSPYPI ELTEEDEIYI CDFTLCYFGS KKQFERFRSK 

       250        260        270        280        290        300 
STLRHPPGNE IYRDEAVSFF EIDGRKQRTW CRNLCLLSKL FLDHKTLYYD VDPFLFYCMT 

       310        320        330        340        350        360 
RRDEKGHHLV GYFSKEKESA EGYNVACILT LPQYQRHGYG RLLIDFSYAL SKAEGKTGSP 

       370        380        390        400        410        420 
EKPLSDLGLL SYRAYWADTI IELLMEKGKQ EMTIEDIASV TAMTTTDVLH TLQTYNMLKY 

       430        440        450        460 
YKGQHIICLT DSVCEKYEKM LKKRRRKVNS ELLKWKPPVF TAAQLRFAW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382131 Genomic DNA. Translation: CAG79133.1.
RefSeqXP_503552.1. XM_503552.1.

3D structure databases

ProteinModelPortalQ6C710.
SMRQ6C710. Positions 185-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4952.Q6C710.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCAG79133; CAG79133; YALI0_E04675g.
GeneID2912208.
KEGGyli:YALI0E04675g.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
KOK11304.
OMAEVEWPAP.
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_YARLI
AccessionPrimary (citable) accession number: Q6C710
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