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Entry version 170 (25 May 2022)
Sequence version 2 (28 Nov 2003)
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Protein

Histone acetyltransferase KAT5

Gene

Kat5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4 (PubMed:28694333, PubMed:30297459, PubMed:32542325).

Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription (By similarity).

The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:17728759).

The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks (PubMed:30297459).

Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage (By similarity).

The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes (PubMed:32542325).

The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (PubMed:28694333).

Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (By similarity).

Also acetylates non-histone proteins, such as ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer (PubMed:22539723, PubMed:24835996, PubMed:31294688).

Directly acetylates and activates ATM (By similarity).

Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex (By similarity).

Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (By similarity).

Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity (PubMed:24835996).

Involved in skeletal myoblast differentiation by mediating acetylation of SOX4 (PubMed:26291311).

Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity (By similarity).

Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of ARNTL/BMAL1, promoting elongation of circadian transcripts (PubMed:31294688).

Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:22539723).

Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation (By similarity).

Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1 (PubMed:29765047).

Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase (By similarity).

Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol (PubMed:29765047).

In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation and 2-hydroxyisobutyrylation, respectively (By similarity).

Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins (By similarity).

Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis (By similarity).

Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes (By similarity).

Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore-microtubule attachment (By similarity).

Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis (By similarity).

By similarity9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Acyltransferase and acetyltransferase activities are activated by phosphorylation and autoacetylation (PubMed:22539723). Autoacetylation activates the histone acetyltransferase activity (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei403Proton donor/acceptorBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei407Acetyl-CoABy similarity1
Binding sitei416Acetyl-CoABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri260 – 285C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Acyltransferase, Chromatin regulator, Transferase
Biological processDNA damage, DNA repair, Growth regulation, Immunity, Innate immunity, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-201722, Formation of the beta-catenin:TCF transactivating complex
R-MMU-2559586, DNA Damage/Telomere Stress Induced Senescence
R-MMU-5685938, HDR through Single Strand Annealing (SSA)
R-MMU-5685942, HDR through Homologous Recombination (HRR)
R-MMU-5693548, Sensing of DNA Double Strand Breaks
R-MMU-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693568, Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693571, Nonhomologous End-Joining (NHEJ)
R-MMU-5693579, Homologous DNA Pairing and Strand Exchange
R-MMU-5693607, Processing of DNA double-strand break ends
R-MMU-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756, Regulation of TP53 Activity through Phosphorylation
R-MMU-69473, G2/M DNA damage checkpoint
R-MMU-9018519, Estrogen-dependent gene expression

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone acetyltransferase KAT5Curated (EC:2.3.1.481 Publication)
Alternative name(s):
60 kDa Tat-interactive protein1 Publication
Short name:
Tip601 Publication
Histone acetyltransferase HTATIP
Lysine acetyltransferase 5
Protein 2-hydroxyisobutyryltransferase KAT5Curated (EC:2.3.1.-By similarity)
Protein acetyltransferase KAT5Curated (EC:2.3.1.-3 Publications)
Protein crotonyltransferase KAT5Curated (EC:2.3.1.-By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Kat51 PublicationImported
Synonyms:Htatip, Tip601 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:1932051, Kat5

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSMUSG00000024926

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic lethality before implantation (PubMed:17728759). Conditional deletion leads to rapid hematopoietic stem cell loss in both fetal and adult stages (PubMed:32542325). Conditional deletion at postnatal day 15 leads to impaired spermatid development: testes are smaller and show defects in the transition from the transition from round to elongating spermatids (PubMed:28694333). Defects in spermatid development is probably caused by impaired acetylation of histones that affects histone replacement (PubMed:28694333). Conditional deletion in response to DNA damage leads to impaired homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs), associated with increased non-homologous end joining (NHEJ)-mediated repair mediated by TP53BP1 (PubMed:30297459).4 Publications
Mice lacking isoform 5 die during mid-gestation (around embryonic day 11.5) (PubMed:30297694). Prior to developmental arrest, embryos display defects in heart and neural tube (PubMed:30297694). Specification of cardiac and neural cell fates is first normal; however, cell division and survival are impaired in heart and neural tube, respectively (PubMed:30297694).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi86S → A: Abolished phosphorylation by GSK3 and decreased acetyltransferase activity. Impaired ability to activate the cGAS-STING antiviral response in knockin mice. Lean phenotype caused by impaired ability to promote the synthesis of diacylglycerol in knockin mice. Decreased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs). 4 Publications1
Mutagenesisi86S → D: Mimics phosphorylation; constitutively active mutant that shows constitutive protein acetyltransferase activity. Increased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs). 1 Publication1
Mutagenesisi90S → A: Impaired phosphorylation and decreased acetyltransferase activity, leading to decreased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs). 1 Publication1
Mutagenesisi90S → D: Mimics phosphorylation; constitutively active mutant that shows constitutive protein acetyltransferase and acyltransferase activities in knockin mice. Increased ability to promote homologous recombination (HR)repair in response to DNA double-strand breaks (DSBs). 2 Publications1
Mutagenesisi377 – 380QRRG → ERRE: Abolished acetyltransferase activity. 1 Publication4

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000515811 – 513Histone acetyltransferase KAT5Add BLAST513

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei52N6-acetyllysineBy similarity1
Modified residuei86Phosphoserine3 Publications1
Modified residuei90Phosphoserine; by CDK1 and CDK92 Publications1
Modified residuei104N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei120N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei148N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei150N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei187N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei189N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei199PhosphoserineCombined sources1
Modified residuei327N6-acetyllysine; by autocatalysisBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase (PubMed:22539723, PubMed:30297459, PubMed:34608293). The phosphorylated form has a higher activity (PubMed:30297459, PubMed:34608293). Phosphorylation at Ser-90 by CDK1 or CDK9 is a prerequisite for phosphorylation at Ser-86 by GSK3 (PubMed:34608293). Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates acetyltransferase and acyltransferase activity (PubMed:22539723, PubMed:30297459). Phosphorylation at Ser-90 by CDK9 promotes KAT5 recruitment to chromatin (By similarity). Phosphorylation by VRK1 following DNA damage promotes KAT5 association with chromatin and histone acetyltransferase activity (PubMed:33076429).By similarity4 Publications
Autoacetylated (By similarity). Autoacetylation is required for histone acetyltransferase activity (By similarity). Autoacetylation at Lys-327 is facilitated by interaction with EP300/p300: it prevents ubiquitination and subsequent degradation by the proteasome and promotes acetylation of target proteins (By similarity). Deacetylated by HDAC3 and SIRT1 (By similarity). Deacetylation by HDAC3 promotes its ubiquitination and cytoplasmic localization (By similarity).By similarity
Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies (By similarity). Sumoylation with SUMO2 by PIAS4 at Lys-430 promotes repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (By similarity). Sumoylation by PIAS4 impairs interaction with PRKDC, inhibiting non-homologous end joining (NHEJ)-mediated repair of DSBs, thereby facilitating HR (By similarity). Desumoylated by SENP3 (By similarity).By similarity
Ubiquitinated by MDM2, leading to its proteasome-dependent degradation (By similarity). Ubiquitination is prevented by autoacetylation at Lys-327 (By similarity). Ubiquitinated following deacetylation by HDAC3, leading to cytoplasmic localization (By similarity). Deubiquitinated by USP7 following interaction with ATF3, promoting its stabilization (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8CHK4

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8CHK4

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8CHK4

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q8CHK4

PeptideAtlas

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PeptideAtlasi
Q8CHK4

PRoteomics IDEntifications database

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PRIDEi
Q8CHK4

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
301733 [Q8CHK4-1]
301734 [Q8CHK4-2]
301735 [Q8CHK4-3]
301736 [Q8CHK4-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8CHK4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q8CHK4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in testis, heart, brain, kidney and liver. Weakly expressed in lung.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000024926, Expressed in cerebellum and 280 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8CHK4, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8CHK4, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6 (PubMed:32542325). KAT5/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4 (By similarity). The NuA4 complex interacts with MYC (By similarity).

Interacts with ATM (By similarity).

Interacts with JADE1 (By similarity).

Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7 (By similarity).

Interacts with the cytoplasmic tail of APP and APBB1/FE65 (By similarity).

Interacts with TRIM24 and TRIM68 (By similarity).

Forms a complex with SENP6 and UBE2I in response to UV irradiation (By similarity).

Identified in a complex with HINT1 (By similarity).

Interacts with ATF2 and CUL3 (By similarity).

Interacts with NR1D2 (via N-terminus) (By similarity).

Component of a SWR1-like complex (By similarity).

Interacts with FOXP3 (PubMed:19696312).

Interacts with ZBTB49 (By similarity).

Interacts with SRF (PubMed:16597624).

Interacts with ATF3; promoting autoacetylation and deubiquitination by USP7 (By similarity).

Interacts with EP300/p300; interaction promotes KAT5 autoacetylation (By similarity).

Interacts with PRKDC; interaction is impaired following KAT5 sumoylation (By similarity).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
219884, 59 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-747, Piccolo NuA4 histone acetyltransferase complex
CPX-990, NuA4 histone acetyltransferase complex

Protein interaction database and analysis system

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IntActi
Q8CHK4, 29 interactors

Molecular INTeraction database

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MINTi
Q8CHK4

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000109271

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q8CHK4, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

AlphaFold Protein Structure Database

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AlphaFoldDBi
Q8CHK4

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q8CHK4

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 65Tudor-knotSequence analysisAdd BLAST58
Domaini227 – 504MYST-type HATPROSITE-ProRule annotationAdd BLAST278

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni69 – 106DisorderedSequence analysisAdd BLAST38
Regioni122 – 217DisorderedSequence analysisAdd BLAST96
Regioni368 – 513Interaction with ATF2By similarityAdd BLAST146
Regioni370 – 372Acetyl-CoA bindingBy similarity3
Regioni377 – 383Acetyl-CoA bindingBy similarity7

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri260 – 285C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2747, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000162343

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_011815_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8CHK4

Identification of Orthologs from Complete Genome Data

More...
OMAi
SMTQNQT

Database of Orthologous Groups

More...
OrthoDBi
629545at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8CHK4

TreeFam database of animal gene trees

More...
TreeFami
TF317619

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016181, Acyl_CoA_acyltransferase
IPR016197, Chromo-like_dom_sf
IPR000953, Chromo/chromo_shadow_dom
IPR002717, HAT_MYST-type
IPR037995, KAT5/Tip60
IPR025995, Tudor-knot
IPR036388, WH-like_DNA-bd_sf
IPR040706, Zf-MYST

The PANTHER Classification System

More...
PANTHERi
PTHR10615:SF183, PTHR10615:SF183, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01853, MOZ_SAS, 1 hit
PF11717, Tudor-knot, 1 hit
PF17772, zf-MYST, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00298, CHROMO, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54160, SSF54160, 1 hit
SSF55729, SSF55729, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51726, MYST_HAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8CHK4-1) [UniParc]FASTAAdd to basket
Also known as: Tip60alpha1 Publication

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF
60 70 80 90 100
NKRLDEWVTH ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ
110 120 130 140 150
ASGKTLPIPV QITLRFNLPK EREAIPGGEP DQPLSSSSCL QPNHRSTKRK
160 170 180 190 200
VEVVSPATPV PSETAPASVF PQNGSARRAV AAQPGRKRKS NCLGTDEDSQ
210 220 230 240 250
DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH RLKPWYFSPY
260 270 280 290 300
PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS
310 320 330 340 350
FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH
360 370 380 390 400
IVGYFSKEKE STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG
410 420 430 440 450
TPEKPLSDLG LLSYRSYWSQ TILEILMGLK SESGERPQIT INEISEITSI
460 470 480 490 500
KKEDVISTLQ YLNLINYYKG QYILTLSEDI VDGHERAMLK RLLRIDSKCL
510
HFTPKDWSKR GKW
Length:513
Mass (Da):58,598
Last modified:November 28, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEACEE4D544C0DB60
GO
Isoform 2 (identifier: Q8CHK4-2) [UniParc]FASTAAdd to basket
Also known as: Tip60beta1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     96-147: Missing.

Show »
Length:461
Mass (Da):53,093
Checksum:iD3B238AF01737EF3
GO
Isoform 3 (identifier: Q8CHK4-3) [UniParc]FASTAAdd to basket
Also known as: Ltip601 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ

Show »
Length:546
Mass (Da):61,814
Checksum:i8557B105D8F4B291
GO
Isoform 4 (identifier: Q8CHK4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-211: Missing.

Show »
Length:302
Mass (Da):35,396
Checksum:iD96A7FCCB49FA85D
GO
Isoform 5 (identifier: Q8CHK4-5) [UniParc]FASTAAdd to basket
Also known as: Tip551 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     390-492: YELSKVEGKT...GHERAMLKRL → EYVLPDQELA...STPRAMNSRK
     493-513: Missing.

Show »
Length:492
Mass (Da):55,402
Checksum:i45A121DF361A753D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A494BAP7A0A494BAP7_MOUSE
Histone acetyltransferase
Kat5
494Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A494B979A0A494B979_MOUSE
Histone acetyltransferase
Kat5
90Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A494BA96A0A494BA96_MOUSE
Histone acetyltransferase KAT5
Kat5
157Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A494BA68A0A494BA68_MOUSE
Histone acetyltransferase KAT5
Kat5
114Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 5 (identifier: Q8CHK4-5)
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti465R → G AAZ67923.1 (PubMed:16597624).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0091051 – 211Missing in isoform 4. 1 PublicationAdd BLAST211
Alternative sequenceiVSP_0091064V → VVSPVPGAGRREPGEVGRAR GPPVADPGVALSPQ in isoform 3. Curated1
Alternative sequenceiVSP_00910796 – 147Missing in isoform 2. 2 PublicationsAdd BLAST52
Alternative sequenceiVSP_061400390 – 492YELSK…MLKRL → EYVLPDQELAGQACVGPILL RAAGVPRIAAKLMTLKRFPC PQTTKGSLITAIHPDTGWQG SDPSWQPSLADKYPTRAALL AFGPQHCRQGSCWSTPRAMN SRK in isoform 5. Add BLAST103
Alternative sequenceiVSP_061401493 – 513Missing in isoform 5. Add BLAST21

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY061983 Genomic DNA Translation: AAL34981.1
AF528194 mRNA Translation: AAN77140.1
AF528195 mRNA Translation: AAN77141.1
AF528196 mRNA Translation: AAN77142.1
DQ139980 mRNA Translation: AAZ67923.1
AB055409 mRNA Translation: BAC53807.1
BC129968 mRNA Translation: AAI29969.1
BC110675 mRNA Translation: AAI10676.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS29472.1 [Q8CHK4-1]
CCDS89314.1 [Q8CHK4-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001186176.1, NM_001199247.1 [Q8CHK4-2]
NP_001186177.1, NM_001199248.1
NP_848752.1, NM_178637.2 [Q8CHK4-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000113641; ENSMUSP00000109271; ENSMUSG00000024926 [Q8CHK4-1]
ENSMUST00000236229; ENSMUSP00000158391; ENSMUSG00000024926 [Q8CHK4-2]
ENSMUST00000236883; ENSMUSP00000157766; ENSMUSG00000024926 [Q8CHK4-5]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
81601

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:81601

UCSC genome browser

More...
UCSCi
uc008gdy.2, mouse [Q8CHK4-1]
uc008geb.2, mouse [Q8CHK4-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061983 Genomic DNA Translation: AAL34981.1
AF528194 mRNA Translation: AAN77140.1
AF528195 mRNA Translation: AAN77141.1
AF528196 mRNA Translation: AAN77142.1
DQ139980 mRNA Translation: AAZ67923.1
AB055409 mRNA Translation: BAC53807.1
BC129968 mRNA Translation: AAI29969.1
BC110675 mRNA Translation: AAI10676.1
CCDSiCCDS29472.1 [Q8CHK4-1]
CCDS89314.1 [Q8CHK4-2]
RefSeqiNP_001186176.1, NM_001199247.1 [Q8CHK4-2]
NP_001186177.1, NM_001199248.1
NP_848752.1, NM_178637.2 [Q8CHK4-1]

3D structure databases

AlphaFoldDBiQ8CHK4
SMRiQ8CHK4
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi219884, 59 interactors
ComplexPortaliCPX-747, Piccolo NuA4 histone acetyltransferase complex
CPX-990, NuA4 histone acetyltransferase complex
IntActiQ8CHK4, 29 interactors
MINTiQ8CHK4
STRINGi10090.ENSMUSP00000109271

PTM databases

iPTMnetiQ8CHK4
PhosphoSitePlusiQ8CHK4

Proteomic databases

EPDiQ8CHK4
jPOSTiQ8CHK4
MaxQBiQ8CHK4
PaxDbiQ8CHK4
PeptideAtlasiQ8CHK4
PRIDEiQ8CHK4
ProteomicsDBi301733 [Q8CHK4-1]
301734 [Q8CHK4-2]
301735 [Q8CHK4-3]
301736 [Q8CHK4-4]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
1823, 732 antibodies from 38 providers

The DNASU plasmid repository

More...
DNASUi
81601

Genome annotation databases

EnsembliENSMUST00000113641; ENSMUSP00000109271; ENSMUSG00000024926 [Q8CHK4-1]
ENSMUST00000236229; ENSMUSP00000158391; ENSMUSG00000024926 [Q8CHK4-2]
ENSMUST00000236883; ENSMUSP00000157766; ENSMUSG00000024926 [Q8CHK4-5]
GeneIDi81601
KEGGimmu:81601
UCSCiuc008gdy.2, mouse [Q8CHK4-1]
uc008geb.2, mouse [Q8CHK4-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10524
MGIiMGI:1932051, Kat5
VEuPathDBiHostDB:ENSMUSG00000024926

Phylogenomic databases

eggNOGiKOG2747, Eukaryota
GeneTreeiENSGT00940000162343
HOGENOMiCLU_011815_2_0_1
InParanoidiQ8CHK4
OMAiSMTQNQT
OrthoDBi629545at2759
PhylomeDBiQ8CHK4
TreeFamiTF317619

Enzyme and pathway databases

ReactomeiR-MMU-201722, Formation of the beta-catenin:TCF transactivating complex
R-MMU-2559586, DNA Damage/Telomere Stress Induced Senescence
R-MMU-5685938, HDR through Single Strand Annealing (SSA)
R-MMU-5685942, HDR through Homologous Recombination (HRR)
R-MMU-5693548, Sensing of DNA Double Strand Breaks
R-MMU-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693568, Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693571, Nonhomologous End-Joining (NHEJ)
R-MMU-5693579, Homologous DNA Pairing and Strand Exchange
R-MMU-5693607, Processing of DNA double-strand break ends
R-MMU-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756, Regulation of TP53 Activity through Phosphorylation
R-MMU-69473, G2/M DNA damage checkpoint
R-MMU-9018519, Estrogen-dependent gene expression

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
81601, 22 hits in 114 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Kat5, mouse

Protein Ontology

More...
PROi
PR:Q8CHK4
RNActiQ8CHK4, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000024926, Expressed in cerebellum and 280 other tissues
ExpressionAtlasiQ8CHK4, baseline and differential
GenevisibleiQ8CHK4, MM

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016181, Acyl_CoA_acyltransferase
IPR016197, Chromo-like_dom_sf
IPR000953, Chromo/chromo_shadow_dom
IPR002717, HAT_MYST-type
IPR037995, KAT5/Tip60
IPR025995, Tudor-knot
IPR036388, WH-like_DNA-bd_sf
IPR040706, Zf-MYST
PANTHERiPTHR10615:SF183, PTHR10615:SF183, 1 hit
PfamiView protein in Pfam
PF01853, MOZ_SAS, 1 hit
PF11717, Tudor-knot, 1 hit
PF17772, zf-MYST, 1 hit
SMARTiView protein in SMART
SM00298, CHROMO, 1 hit
SUPFAMiSSF54160, SSF54160, 1 hit
SSF55729, SSF55729, 1 hit
PROSITEiView protein in PROSITE
PS51726, MYST_HAT, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKAT5_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8CHK4
Secondary accession number(s): A0A494B9U8
, A1L394, Q3YFI9, Q8CGZ3, Q8CGZ4, Q8VIH0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: May 25, 2022
This is version 170 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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