Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone acetyltransferase ESA1  

UniProtKB / Swiss-Prot ID :  ESA1_YEAST

Gene Name (Synonyms) : 
ESA1 YOR244W O5257  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :   

Protein 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. 

Protein Sequence MSHDGKEEPGIAKKINSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTD...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCHHHCCCCCEEEEEECCCCCCCEEEEEECCCCCCEEEEEECCCCCCCCCCCCHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
17PhosphoserineKKINSVDDI
CCCCCHHHC
30.32SysPTM
Link-
17Phosphoserine.KKINSVDDI
CCCCCHHHC
30.32UniProtKB
Link-
262N6-acetyllysine; by autocatalysis.FLDHKTLYY
HHCCCEEEE
39.63UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"MYST protein acetyltransferase activity requires active site lysineautoacetylation.";
Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J.,Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J.,Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A.,Johnson F.B., Berger S.L., Sternglanz R., McMahon S.B., Cote J.,Marmorstein R.;
EMBO J. 31:58-70(2012).
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-435, ACTIVE SITE, ANDACETYLATION AT LYS-262.
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures