Protein: ESA1_YEAST
Sequence: MSHDGKEEPGIAKKINSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATDEDNKKQKKKKATNTSETPQDSLQDGVDGFSRENTDVMDLDNLNVQGIKDENISHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPVFTASQLRFAW
What is the function of this protein?
Catalytic component of the NuA4 histone acetyltransferase (HAT), a multiprotein complex involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A. Z (PubMed:9520405, PubMed:12379856, PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:16543223, PubMed:18245364, PubMed:9858608).  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 (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608).  Acetylation of histones gives a specific tag for epigenetic transcription initiation and elongation (PubMed:16543223, PubMed:19822662).  Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608).  Involved in cell cycle progression (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608).  Recruitment to promoters depends on H3K4me (PubMed:10082517, PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608).  Also acetylates non-histone proteins, such as ATG3 and PAH1 (PubMed:22539722, PubMed:29765047).  Regulates autophagy by acetylating ATG3, controlling interaction the interaction between ATG3 and ATG8 and ATG8 lipidation (PubMed:22539722).  Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of PAH1, thereby promoting the synthesis of diacylglycerol (PubMed:29765047).  In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (PubMed:31699900).  Catalyzes histone crotonylation (PubMed:31699900).
What are the official names of this protein?
Histone acetyltransferase ESA1, Protein 2-hydroxyisobutyryltransferase ESA1, Protein acetyltransferase ESA1, Protein crotonyltransferase ESA1.
What is the protein family that this protein belongs to?
Belongs to the MYST (SAS/MOZ) family.