ID KAT7_MOUSE Reviewed; 613 AA.
AC Q5SVQ0; Q5SVQ1; Q5SVQ2; Q5SVQ3; Q5SVQ7; Q6PGC6; Q80Y65;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Histone acetyltransferase KAT7 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000305|PubMed:21149574};
DE AltName: Full=Histone acetyltransferase binding to ORC1 {ECO:0000303|PubMed:23319590};
DE AltName: Full=Lysine acetyltransferase 7;
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2;
DE Short=MYST-2;
GN Name=Kat7 {ECO:0000312|MGI:MGI:2182799};
GN Synonyms=Hbo1 {ECO:0000303|PubMed:23319590}, Myst2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-59; THR-87; THR-90;
RP SER-104; THR-106; SER-126 AND THR-130, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN THE HBO1 COMPLEX.
RX PubMed=21753189; DOI=10.1182/blood-2011-01-331892;
RA Mishima Y., Miyagi S., Saraya A., Negishi M., Endoh M., Endo T.A.,
RA Toyoda T., Shinga J., Katsumoto T., Chiba T., Yamaguchi N., Kitabayashi I.,
RA Koseki H., Iwama A.;
RT "The Hbo1-Brd1/Brpf2 complex is responsible for global acetylation of H3K14
RT and required for fetal liver erythropoiesis.";
RL Blood 118:2443-2453(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21149574; DOI=10.1128/mcb.00159-10;
RA Kueh A.J., Dixon M.P., Voss A.K., Thomas T.;
RT "HBO1 is required for H3K14 acetylation and normal transcriptional activity
RT during embryonic development.";
RL Mol. Cell. Biol. 31:845-860(2011).
RN [6]
RP FUNCTION, INTERACTION WITH FBXW15; MAP2K1 AND CUL1, SUBCELLULAR LOCATION,
RP AND PHOSPHORYLATION.
RX PubMed=23319590; DOI=10.1074/jbc.m112.426882;
RA Zou C., Chen Y., Smith R.M., Snavely C., Li J., Coon T.A., Chen B.B.,
RA Zhao Y., Mallampalli R.K.;
RT "SCF(Fbxw15) mediates histone acetyltransferase binding to origin
RT recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate
RT cell proliferation.";
RL J. Biol. Chem. 288:6306-6316(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-201 AND LYS-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP FUNCTION.
RX PubMed=27733580; DOI=10.1189/jlb.1ma0816-338r;
RA Newman D.M., Voss A.K., Thomas T., Allan R.S.;
RT "Essential role for the histone acetyltransferase KAT7 in T cell
RT development, fitness, and survival.";
RL J. Leukoc. Biol. 101:887-892(2017).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE HBO1 COMPLEX.
RX PubMed=31827282; DOI=10.1038/s41586-019-1835-6;
RA MacPherson L., Anokye J., Yeung M.M., Lam E.Y.N., Chan Y.C., Weng C.F.,
RA Yeh P., Knezevic K., Butler M.S., Hoegl A., Chan K.L., Burr M.L.,
RA Gearing L.J., Willson T., Liu J., Choi J., Yang Y., Bilardi R.A., Falk H.,
RA Nguyen N., Stupple P.A., Peat T.S., Zhang M., de Silva M.,
RA Carrasco-Pozo C., Avery V.M., Khoo P.S., Dolezal O., Dennis M.L.,
RA Nuttall S., Surjadi R., Newman J., Ren B., Leaver D.J., Sun Y., Baell J.B.,
RA Dovey O., Vassiliou G.S., Grebien F., Dawson S.J., Street I.P.,
RA Monahan B.J., Burns C.J., Choudhary C., Blewitt M.E., Voss A.K., Thomas T.,
RA Dawson M.A.;
RT "HBO1 is required for the maintenance of leukaemia stem cells.";
RL Nature 577:266-270(2020).
CC -!- FUNCTION: Catalytic subunit of histone acetyltransferase HBO1
CC complexes, which specifically mediate acetylation of histone H3 at
CC 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene
CC transcription, protein ubiquitination, immune regulation, stem cell
CC pluripotent and self-renewal maintenance and embryonic development
CC (PubMed:21753189, PubMed:21149574, PubMed:23319590, PubMed:27733580,
CC PubMed:31827282). Some complexes also catalyze acetylation of histone
CC H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac,
CC respectively), regulating DNA replication initiation, regulating DNA
CC replication initiation (By similarity). Specificity of the HBO1
CC complexes is determined by the scaffold subunit: complexes containing
CC BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity
CC towards H3K14ac, while complexes containing JADE (JADE1, JADE2 and
CC JADE3) scaffold direct KAT7/HBO1 specificity towards histone H4 (By
CC similarity). H3K14ac promotes transcriptional elongation by
CC facilitating the processivity of RNA polymerase II (PubMed:31827282).
CC Acts as a key regulator of hematopoiesis by forming a complex with
CC BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and
CC promoting erythroid differentiation (By similarity). H3K14ac is also
CC required for T-cell development (PubMed:27733580). KAT7/HBO1-mediated
CC acetylation facilitates two consecutive steps, licensing and
CC activation, in DNA replication initiation: H3K14ac facilitates the
CC activation of replication origins, and histone H4 acetylation (H4K5ac,
CC H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes,
CC promoting DNA replication licensing (By similarity). Acts as a positive
CC regulator of centromeric CENPA assembly: recruited to centromeres and
CC mediates histone acetylation, thereby preventing centromere
CC inactivation mediated by SUV39H1, possibly by increasing histone
CC turnover/exchange (By similarity). Involved in nucleotide excision
CC repair: phosphorylation by ATR in response to ultraviolet irradiation
CC promotes its localization to DNA damage sites, where it mediates
CC histone acetylation to facilitate recruitment of XPC at the damaged DNA
CC sites (By similarity). Acts as an inhibitor of NF-kappa-B independently
CC of its histone acetyltransferase activity (By similarity).
CC {ECO:0000250|UniProtKB:O95251, ECO:0000269|PubMed:21149574,
CC ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:23319590,
CC ECO:0000269|PubMed:27733580, ECO:0000269|PubMed:31827282}.
CC -!- FUNCTION: Plays a central role in the maintenance of leukemia stem
CC cells in acute myeloid leukemia (AML) (PubMed:31827282). Acts by
CC mediating acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby
CC facilitating the processivity of RNA polymerase II to maintain the high
CC expression of key genes, such as HOXA9 and HOXA10 that help to sustain
CC the functional properties of leukemia stem cells (PubMed:31827282).
CC {ECO:0000269|PubMed:31827282}.
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; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:31827282, ECO:0000305|PubMed:21149574};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000269|PubMed:31827282, ECO:0000305|PubMed:21149574};
CC -!- ACTIVITY REGULATION: Histone acetyltransferase activity is inhibited by
CC GMNN in the context of a complex with CDT1, inhibiting histone H4
CC acetylation and DNA replication licensing.
CC {ECO:0000250|UniProtKB:O95251}.
CC -!- SUBUNIT: Component of the HBO1 complex composed of KAT7/HBO1, MEAF6,
CC ING4 or ING5, and one scaffold subunit: complexes containing BRPF
CC scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity
CC towards H3K14ac, while complexes containing JADE scaffold (JADE1, JADE2
CC and JADE3) mediate acetylation of histone H4 (PubMed:21753189,
CC PubMed:31827282). Interacts with MCM2 and ORC1 (By similarity).
CC Interacts with the androgen receptor (AR) in the presence of
CC dihydrotestosterone (By similarity). Interacts with CDT1 (By
CC similarity). Interacts with MAP2K1 and CUL1 (PubMed:23319590).
CC Interacts with p53/TP53; leading to inhibit histone acetyltransferase
CC activity (By similarity). {ECO:0000250|UniProtKB:O95251,
CC ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:23319590,
CC ECO:0000269|PubMed:31827282}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21149574,
CC ECO:0000269|PubMed:23319590}. Chromosome
CC {ECO:0000250|UniProtKB:O95251}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O95251}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:23319590}. Note=Associates with replication origins
CC specifically during the G1 phase of the cell cycle. Localizes to
CC transcription start sites. Localizes to ultraviolet-induced DNA damage
CC sites following phosphorylation by ATR. Localizes to centromeres in G1
CC phase. {ECO:0000250|UniProtKB:O95251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5SVQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SVQ0-2; Sequence=VSP_014584;
CC Name=3;
CC IsoId=Q5SVQ0-3; Sequence=VSP_014582;
CC Name=4;
CC IsoId=Q5SVQ0-4; Sequence=VSP_014582, VSP_014584;
CC Name=5;
CC IsoId=Q5SVQ0-5; Sequence=VSP_014582, VSP_014583, VSP_014584;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues.
CC {ECO:0000269|PubMed:21149574}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously in the embryonic and
CC extraembryonic tissues (PubMed:21149574). High levels are present in
CC the chorionic plate (8.5 dpc and 9.5 dpc) as well as in and around the
CC foregut and hindgut regions (9.5 dpc) (PubMed:21149574).
CC {ECO:0000269|PubMed:21149574}.
CC -!- DOMAIN: The C2HC MYST-type zinc finger is required for interaction with
CC MCM2 and ORC1. {ECO:0000250|UniProtKB:O95251}.
CC -!- DOMAIN: The N-terminus is involved in transcriptional repression, while
CC the C-terminus mediates AR-interaction. {ECO:0000250|UniProtKB:O95251}.
CC -!- PTM: Phosphorylated at Ser-52 and Ser-55 by ATR in response to DNA
CC damage, promoting its ubiquitination by the CRL4(DDB2) complex and
CC subsequent degradation. Phosphorylation at Ser-52 and Ser-55 by ATR in
CC response to ultraviolet-induced DNA, promotes localization to DNA
CC damage sites. Phosphorylation at Ser-59 by PLK1 during mitosis seems
CC important for prereplicative complex formation and DNA replication
CC licensing, and requires prior phosphorylation at Thr-87 and Thr-90 by
CC CDK1 (By similarity). Phosphorylated by MAP2K1, which accelerates its
CC degradation (PubMed:23319590). {ECO:0000250|UniProtKB:O95251,
CC ECO:0000269|PubMed:23319590}.
CC -!- PTM: Ubiquitinated at Lys-340, leading to proteasomal degradation.
CC Ubiquitinated by the CRL4(DDB2) complex following phosphorylation by
CC ATR, leading to its subsequent degradation.
CC {ECO:0000250|UniProtKB:O95251}.
CC -!- PTM: Autoacetylation at Lys-434 is required for proper function.
CC {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality caused by a strong reduction
CC of histone H3 'Lys-14' acetylation (H3K14ac) (PubMed:21149574).
CC Development is arrested at the 10-somite stage (PubMed:21149574). Blood
CC vessels, mesenchyme, and somites are disorganized (PubMed:21149574). No
CC defects in DNA replication or cell proliferation are observed
CC (PubMed:21149574). Conditional mice lacking Kat7 in thymocytes display
CC normal alpha-beta T-cells but show impaired development of peripheral
CC CD4(+) or CD8(+) T-cells (PubMed:27733580).
CC {ECO:0000269|PubMed:21149574, ECO:0000269|PubMed:27733580}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; AL627222; CAI24800.1; -; Genomic_DNA.
DR EMBL; AL627222; CAI24801.1; -; Genomic_DNA.
DR EMBL; AL627222; CAI24802.1; -; Genomic_DNA.
DR EMBL; AL627222; CAI24803.1; -; Genomic_DNA.
DR EMBL; AL627222; CAI24804.1; -; Genomic_DNA.
DR EMBL; AL627222; CAI24805.1; -; Genomic_DNA.
DR EMBL; BC057102; AAH57102.1; -; mRNA.
DR EMBL; BC048904; AAH48904.1; -; mRNA.
DR CCDS; CCDS25275.1; -. [Q5SVQ0-5]
DR CCDS; CCDS56798.1; -. [Q5SVQ0-4]
DR CCDS; CCDS56799.1; -. [Q5SVQ0-3]
DR RefSeq; NP_001181933.1; NM_001195004.1. [Q5SVQ0-4]
DR RefSeq; NP_808287.1; NM_177619.3. [Q5SVQ0-5]
DR RefSeq; XP_006533076.1; XM_006533013.3.
DR RefSeq; XP_006533077.1; XM_006533014.3.
DR AlphaFoldDB; Q5SVQ0; -.
DR SMR; Q5SVQ0; -.
DR BioGRID; 229849; 6.
DR ComplexPortal; CPX-794; HBO1-4.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-795; HBO1-4.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-796; HBO1-4.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-797; HBO1-5.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-798; HBO1-5.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-799; HBO1-5.3 histone acetyltransferase complex.
DR IntAct; Q5SVQ0; 2.
DR MINT; Q5SVQ0; -.
DR STRING; 10090.ENSMUSP00000103362; -.
DR iPTMnet; Q5SVQ0; -.
DR PhosphoSitePlus; Q5SVQ0; -.
DR EPD; Q5SVQ0; -.
DR jPOST; Q5SVQ0; -.
DR MaxQB; Q5SVQ0; -.
DR PeptideAtlas; Q5SVQ0; -.
DR ProteomicsDB; 301737; -. [Q5SVQ0-1]
DR ProteomicsDB; 301738; -. [Q5SVQ0-2]
DR ProteomicsDB; 301739; -. [Q5SVQ0-3]
DR ProteomicsDB; 301740; -. [Q5SVQ0-4]
DR ProteomicsDB; 301741; -. [Q5SVQ0-5]
DR Pumba; Q5SVQ0; -.
DR Antibodypedia; 17983; 438 antibodies from 39 providers.
DR DNASU; 217127; -.
DR Ensembl; ENSMUST00000072621.12; ENSMUSP00000072416.6; ENSMUSG00000038909.18. [Q5SVQ0-2]
DR Ensembl; ENSMUST00000092766.12; ENSMUSP00000090441.6; ENSMUSG00000038909.18. [Q5SVQ0-1]
DR Ensembl; ENSMUST00000103159.10; ENSMUSP00000099448.4; ENSMUSG00000038909.18. [Q5SVQ0-5]
DR Ensembl; ENSMUST00000107733.10; ENSMUSP00000103361.4; ENSMUSG00000038909.18. [Q5SVQ0-4]
DR Ensembl; ENSMUST00000107734.10; ENSMUSP00000103362.4; ENSMUSG00000038909.18. [Q5SVQ0-3]
DR GeneID; 217127; -.
DR KEGG; mmu:217127; -.
DR UCSC; uc007lad.2; mouse. [Q5SVQ0-5]
DR AGR; MGI:2182799; -.
DR CTD; 11143; -.
DR MGI; MGI:2182799; Kat7.
DR VEuPathDB; HostDB:ENSMUSG00000038909; -.
DR GeneTree; ENSGT00940000157744; -.
DR HOGENOM; CLU_011815_6_1_1; -.
DR InParanoid; Q5SVQ0; -.
DR OMA; NSLXVRA; -.
DR OrthoDB; 118560at2759; -.
DR PhylomeDB; Q5SVQ0; -.
DR TreeFam; TF317619; -.
DR BRENDA; 2.3.1.48; 3474.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 217127; 11 hits in 83 CRISPR screens.
DR ChiTaRS; Kat7; mouse.
DR PRO; PR:Q5SVQ0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SVQ0; Protein.
DR Bgee; ENSMUSG00000038909; Expressed in spermatocyte and 265 other cell types or tissues.
DR ExpressionAtlas; Q5SVQ0; baseline and differential.
DR Genevisible; Q5SVQ0; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0036409; C:histone H3-K14 acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; ISO:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043994; F:histone H3K23 acetyltransferase activity; ISO:MGI.
DR GO; GO:0044016; F:histone H3K4 acetyltransferase activity; ISO:MGI.
DR GO; GO:0010485; F:histone H4 acetyltransferase activity; ISO:MGI.
DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0140889; P:DNA replication-dependent chromatin disassembly; ISS:UniProtKB.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0072716; P:response to actinomycin D; ISO:MGI.
DR GO; GO:0072739; P:response to anisomycin; ISO:MGI.
DR GO; GO:0072720; P:response to dithiothreitol; ISO:MGI.
DR GO; GO:0072710; P:response to hydroxyurea; ISO:MGI.
DR GO; GO:0072708; P:response to sorbitol; ISO:MGI.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; ISO:MGI.
DR GO; GO:0030217; P:T cell differentiation; IMP:GO_Central.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IMP:UniProtKB.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 4.10.320.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103637; CCHHC domain; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Centromere;
KW Chromatin regulator; Chromosome; Cytoplasm; DNA damage; DNA repair;
KW DNA replication; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..613
FT /note="Histone acetyltransferase KAT7"
FT /id="PRO_0000051570"
FT DOMAIN 334..609
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 178..221
FT /note="CCHHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 367..392
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 510
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 477..479
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 485..490
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 514
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 523
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 90
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 201
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 434
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT VAR_SEQ 1..6
FT /note="MAIGVV -> MPRR (in isoform 3, isoform 4 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014582"
FT VAR_SEQ 57..115
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014583"
FT VAR_SEQ 224..253
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014584"
FT CONFLICT 429
FT /note="L -> P (in Ref. 2; AAH57102)"
FT /evidence="ECO:0000305"
FT CONFLICT 545..548
FT /note="EISQ -> GPDR (in Ref. 1; CAI24805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 70641 MW; 7D6F05EE90A7134E CRC64;
MAIGVVKRNA GSSSDGTEDS DFSTDLEHTD SSESDGTSRR SARVTRSSAR LSQSSQDSSP
VRNLPSFGTE EPAYSTRRVT RSQQQPTPVT PKKYPLRQTR SSGSETEQVV DFSDRETKNT
ADHDESPPRT PTGNAPSSES DIDISSPNVS HDESIAKDMS LKDSGSDLSH RPKRRRFHES
YNFNMKCPTP GCNSLGHLTG KHERHFSISG CPLYHNLSAD ECKVRAQSRD KQIEERMLSH
RQDDNNRHAT RHQAPTERQL RYKEKVAELR KKRNSGLSKE QKEKYMEHRQ TYGNTREPLL
ENLTSEYDLD LFRRAQARAS EDLEKLRLQG QITEGSNMIK TIAFGRYELD TWYHSPYPEE
YARLGRLYMC EFCLKYMKSQ TILRRHMAKC VWKHPPGDEI YRKGSISVFE VDGKKNKIYC
QNLCLLAKLF LDHKTLYYDV EPFLFYVMTE ADNTGCHLIG YFSKEKNSFL NYNVSCILTM
PQYMRQGYGK MLIDFSYLLS KVEEKVGSPE RPLSDLGLIS YRSYWKEVLL RYLHNFQGKE
ISIKEISQET AVNPVDIVST LQALQMLKYW KGKHLVLKRQ DLIDEWIAKE AKRSNSNKTM
DPSCLKWTPP KGT
//
