KAT5_RAT
ID KAT5_RAT Reviewed; 513 AA.
AC Q99MK2; Q5XI16;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Histone acetyltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92993};
DE AltName: Full=60 kDa Tat-interactive protein {ECO:0000303|PubMed:11441186};
DE Short=Tip60 {ECO:0000303|PubMed:11441186};
DE AltName: Full=Histone acetyltransferase HTATIP;
DE AltName: Full=Lysine acetyltransferase 5;
DE AltName: Full=Protein 2-hydroxyisobutyryltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92993};
DE AltName: Full=Protein acetyltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92993};
DE AltName: Full=Protein crotonyltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92993};
GN Name=Kat5 {ECO:0000312|RGD:621061};
GN Synonyms=Htatip, Tip60 {ECO:0000303|PubMed:11441186}, Tip60b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-506 (ISOFORM 2), AND INTERACTION WITH APP.
RX PubMed=11441186; DOI=10.1126/science.1058783;
RA Cao X., Suedhof T.C.;
RT "A transcriptionally active complex of APP with Fe65 and histone
RT acetyltransferase Tip60.";
RL Science 293:115-120(2001).
RN [3]
RP INTERACTION WITH APBB1.
RX PubMed=19282473; DOI=10.1073/pnas.0810869106;
RA Stante M., Minopoli G., Passaro F., Raia M., Vecchio L.D., Russo T.;
RT "Fe65 is required for Tip60-directed histone H4 acetylation at DNA strand
RT breaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5093-5098(2009).
CC -!- FUNCTION: Catalytic subunit of the NuA4 histone acetyltransferase
CC complex, a multiprotein complex involved in transcriptional activation
CC of select genes principally by acetylation of nucleosomal histones H2A
CC and H4. Histone acetylation alters nucleosome-DNA interactions and
CC promotes interaction of the modified histones with other proteins which
CC positively regulate transcription. The NuA4 histone acetyltransferase
CC complex is required for the activation of transcriptional programs
CC associated with proto-oncogene mediated growth induction, tumor
CC suppressor mediated growth arrest and replicative senescence,
CC apoptosis, and DNA repair. The NuA4 complex plays a direct role in
CC repair of DNA double-strand breaks (DSBs) by promoting homologous
CC recombination (HR): the complex inhibits TP53BP1 binding to chromatin
CC via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-
CC 20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of
CC histone H2A (H2AK15ac), thereby blocking the ubiquitination mark
CC required for TP53BP1 localization at DNA breaks. Also involved in DSB
CC repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac),
CC promoting NBN/NBS1 assembly at the sites of DNA damage (By similarity).
CC The NuA4 complex plays a key role in hematopoietic stem cell
CC maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC
CC target genes. The NuA4 complex is also required for spermatid
CC development by promoting acetylation of histones: histone
CC hyperacetylation is required for histone replacement during the
CC transition from round to elongating spermatids (By similarity).
CC Component of a SWR1-like complex that specifically mediates the removal
CC of histone H2A.Z/H2AZ1 from the nucleosome. Also acetylates non-histone
CC proteins, such as ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF,
CC LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer.
CC Directly acetylates and activates ATM. Promotes nucleotide excision
CC repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting
CC formation of the ERCC4-ERCC1 complex. Relieves NR1D2-mediated
CC inhibition of APOC3 expression by acetylating NR1D2. Acts as a
CC regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation,
CC thereby promoting FOXP3 transcriptional repressor activity. Involved in
CC skeletal myoblast differentiation by mediating acetylation of SOX4.
CC Catalyzes acetylation of APBB1/FE65, increasing its transcription
CC activator activity (By similarity). Promotes transcription elongation
CC during the activation phase of the circadian cycle by catalyzing
CC acetylation of ARNTL/BMAL1, promoting elongation of circadian
CC transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts
CC as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under
CC starvation conditions, leading to activate acetyltransferase activity
CC and promote acetylation of key autophagy regulators, such as ULK1 and
CC RUBCNL/Pacer. Acts as a regulator of the cGAS-STING innate antiviral
CC response by catalyzing acetylation the N-terminus of CGAS, thereby
CC promoting CGAS DNA-binding and activation. Also regulates lipid
CC metabolism by mediating acetylation of CHKA or LPIN1. Promotes
CC lipolysis of lipid droplets following glucose deprivation by mediating
CC acetylation of isoform 1 of CHKA, thereby promoting monomerization of
CC CHKA and its conversion into a tyrosine-protein kinase. Acts as a
CC regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing
CC acetylation of LPIN1, thereby promoting the synthesis of
CC diacylglycerol. In addition to protein acetyltransferase, can use
CC different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA)
CC and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to
CC mediate protein crotonylation and 2-hydroxyisobutyrylation,
CC respectively. Acts as a key regulator of chromosome segregation and
CC kinetochore-microtubule attachment during mitosis by mediating
CC acetylation or crotonylation of target proteins. Catalyzes acetylation
CC of AURKB at kinetochores, increasing AURKB activity and promoting
CC accurate chromosome segregation in mitosis. Acetylates RAN during
CC mitosis, promoting microtubule assembly at mitotic chromosomes.
CC Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore-
CC microtubule attachment. Catalyzes crotonylation of MAPRE1/EB1, thereby
CC ensuring accurate spindle positioning in mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000250|UniProtKB:Q92993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- ACTIVITY REGULATION: Acyltransferase and acetyltransferase activities
CC are activated by phosphorylation and autoacetylation. Autoacetylation
CC activates the histone acetyltransferase activity.
CC {ECO:0000250|UniProtKB:Q92993}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6 (By similarity). KAT5/TIP60, EPC1,
CC and ING3 together constitute a minimal HAT complex termed Piccolo NuA4
CC (By similarity). The NuA4 complex interacts with MYC (By similarity).
CC Interacts with ATM (By similarity). Interacts with JADE1 (By
CC similarity). Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7 (By
CC similarity). Interacts with the cytoplasmic tail of APP and APBB1/FE65
CC (PubMed:11441186, PubMed:19282473). Interacts with TRIM24 and TRIM68
CC (By similarity). Forms a complex with SENP6 and UBE2I in response to UV
CC irradiation (By similarity). Identified in a complex with HINT1 (By
CC similarity). Interacts with ATF2 and CUL3 (By similarity). Interacts
CC with NR1D2 (via N-terminus) (By similarity). Component of a SWR1-like
CC complex (By similarity). Interacts with FOXP3 (By similarity).
CC Interacts with ZBTB49 (By similarity). Interacts with SRF (By
CC similarity). Interacts with ATF3; promoting autoacetylation and
CC deubiquitination by USP7 (By similarity). Interacts with EP300/p300;
CC interaction promotes KAT5 autoacetylation (By similarity). Interacts
CC with PRKDC; interaction is impaired following KAT5 sumoylation (By
CC similarity). {ECO:0000250|UniProtKB:Q8CHK4,
CC ECO:0000250|UniProtKB:Q92993, ECO:0000269|PubMed:11441186,
CC ECO:0000269|PubMed:19282473}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92993}.
CC Chromosome {ECO:0000250|UniProtKB:Q92993}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q92993}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is
CC exported from the nucleus to the perinuclear region and UV irradiation
CC induces translocation into punctuate subnuclear structures named
CC nuclear bodies. Transiently localizes to kinetochores in early mitosis.
CC Localizes to spindle poles when chromosomes align during metaphase (By
CC similarity). Localizes in the cytoplasm and nucleus of round spermatids
CC (By similarity). {ECO:0000250|UniProtKB:Q8CHK4,
CC ECO:0000250|UniProtKB:Q92993}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99MK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99MK2-2; Sequence=VSP_019781;
CC -!- PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase.
CC The phosphorylated form has a higher activity. Phosphorylation at Ser-
CC 90 by CDK1 or CDK9 is a prerequisite for phosphorylation at Ser-86 by
CC GSK3. Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates
CC acetyltransferase and acyltransferase activities. Phosphorylation at
CC Ser-90 by CDK9 promotes KAT5 recruitment to chromatin. Phosphorylation
CC by VRK1 following DNA damage promotes KAT5 association with chromatin
CC and histone acetyltransferase activity. {ECO:0000250|UniProtKB:Q92993}.
CC -!- PTM: Autoacetylated. Autoacetylation is required for histone
CC acetyltransferase activity. Autoacetylation at Lys-327 is facilitated
CC by interaction with EP300/p300: it prevents ubiquitination and
CC subsequent degradation by the proteasome and promotes acetylation of
CC target proteins. Deacetylated by HDAC3 and SIRT1. Deacetylation by
CC HDAC3 promotes its ubiquitination and cytoplasmic localization.
CC {ECO:0000250|UniProtKB:Q92993}.
CC -!- PTM: Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of
CC its histone acetyltransferase activity in UV-induced DNA damage
CC response, as well as its translocation to nuclear bodies. Sumoylation
CC with SUMO2 by PIAS4 at Lys-430 promotes repair of DNA double-strand
CC breaks (DSBs) via homologous recombination (HR). Sumoylation by PIAS4
CC impairs interaction with PRKDC, inhibiting non-homologous end joining
CC (NHEJ)-mediated repair of DSBs, thereby facilitating HR. Desumoylated
CC by SENP3. {ECO:0000250|UniProtKB:Q92993}.
CC -!- PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent
CC degradation. Ubiquitination is prevented by autoacetylation at Lys-327.
CC Ubiquitinated following deacetylation by HDAC3, leading to cytoplasmic
CC localization. Deubiquitinated by USP7 following interaction with ATF3,
CC promoting its stabilization. {ECO:0000250|UniProtKB:Q92993}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; BC083879; AAH83879.1; -; mRNA.
DR EMBL; AF333984; AAK20836.1; -; mRNA.
DR RefSeq; NP_001005872.1; NM_001005872.1. [Q99MK2-1]
DR AlphaFoldDB; Q99MK2; -.
DR SMR; Q99MK2; -.
DR BioGRID; 251357; 1.
DR STRING; 10116.ENSRNOP00000039632; -.
DR ChEMBL; CHEMBL1932911; -.
DR iPTMnet; Q99MK2; -.
DR PhosphoSitePlus; Q99MK2; -.
DR PaxDb; Q99MK2; -.
DR PRIDE; Q99MK2; -.
DR Ensembl; ENSRNOT00000088799; ENSRNOP00000075290; ENSRNOG00000061012. [Q99MK2-1]
DR GeneID; 192218; -.
DR KEGG; rno:192218; -.
DR UCSC; RGD:621061; rat. [Q99MK2-1]
DR CTD; 10524; -.
DR RGD; 621061; Kat5.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000162343; -.
DR InParanoid; Q99MK2; -.
DR OrthoDB; 629545at2759; -.
DR PhylomeDB; Q99MK2; -.
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-RNO-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-RNO-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-RNO-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q99MK2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:RGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043998; F:H2A histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043999; F:histone acetyltransferase activity (H2A-K5 specific); ISO:RGD.
DR GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); ISO:RGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0140065; F:peptide butyryltransferase activity; ISS:UniProtKB.
DR GO; GO:0140064; F:peptide crotonyltransferase activity; ISS:UniProtKB.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043274; F:phospholipase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0071481; P:cellular response to X-ray; IEP:RGD.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IMP:RGD.
DR GO; GO:0043968; P:histone H2A acetylation; ISO:RGD.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1905691; P:lipid droplet disassembly; ISS:UniProtKB.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0021915; P:neural tube development; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:1900051; P:positive regulation of histone exchange; ISS:UniProtKB.
DR GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISO:RGD.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0006473; P:protein acetylation; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR037995; KAT5/Tip60.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615:SF183; PTHR10615:SF183; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Acyltransferase; Alternative splicing; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Immunity;
KW Innate immunity; Isopeptide bond; Kinetochore; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..513
FT /note="Histone acetyltransferase KAT5"
FT /id="PRO_0000051582"
FT DOMAIN 8..65
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 227..504
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 260..285
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 69..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..513
FT /note="Interaction with ATF2"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT ACT_SITE 403
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 370..372
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 377..383
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 407
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 416
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 104
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 120
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 148
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 150
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 187
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 189
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 327
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT CROSSLNK 451
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT VAR_SEQ 96..147
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11441186"
FT /id="VSP_019781"
SQ SEQUENCE 513 AA; 58598 MW; EACEE4D544C0DB60 CRC64;
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH
ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ ASGKTLPIPV QITLRFNLPK
EREAIPGGEP DQPLSSSSCL QPNHRSTKRK VEVVSPATPV PSETAPASVF PQNGSARRAV
AAQPGRKRKS NCLGTDEDSQ DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH
RLKPWYFSPY PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS
FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH IVGYFSKEKE
STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG TPEKPLSDLG LLSYRSYWSQ
TILEILMGLK SESGERPQIT INEISEITSI KKEDVISTLQ YLNLINYYKG QYILTLSEDI
VDGHERAMLK RLLRIDSKCL HFTPKDWSKR GKW
