MYST1_ARATH
ID MYST1_ARATH Reviewed; 445 AA.
AC Q9FLF7; C0SVV9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Histone acetyltransferase of the MYST family 1 {ECO:0000303|PubMed:17877703};
DE EC=2.3.1.48 {ECO:0000255|RuleBase:RU361211};
DE AltName: Full=Histone acetyltransferase of the GNAT/MYST superfamily 4 {ECO:0000303|PubMed:12466527};
DE AltName: Full=MYST-like histone acetyltransferase 1 {ECO:0000303|PubMed:17877703};
GN Name=HAM1 {ECO:0000303|PubMed:17877703};
GN Synonyms=HAG4 {ECO:0000303|PubMed:12466527};
GN OrderedLocusNames=At5g64610 {ECO:0000312|Araport:AT5G64610};
GN ORFNames=MUB3.13 {ECO:0000312|EMBL:BAB11428.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17877703; DOI=10.1111/j.1365-313x.2007.03264.x;
RA Earley K.W., Shook M.S., Brower-Toland B., Hicks L., Pikaard C.S.;
RT "In vitro specificities of Arabidopsis co-activator histone
RT acetyltransferases: implications for histone hyperacetylation in gene
RT activation.";
RL Plant J. 52:615-626(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19040736; DOI=10.1186/1471-2229-8-121;
RA Latrasse D., Benhamed M., Henry Y., Domenichini S., Kim W., Zhou D.X.,
RA Delarue M.;
RT "The MYST histone acetyltransferases are essential for gametophyte
RT development in Arabidopsis.";
RL BMC Plant Biol. 8:121-121(2008).
RN [8]
RP FUNCTION, AND INDUCTION BY UV.
RX PubMed=22170978; DOI=10.1104/pp.111.191452;
RA Campi M., D'Andrea L., Emiliani J., Casati P.;
RT "Participation of chromatin-remodeling proteins in the repair of
RT ultraviolet-B-damaged DNA.";
RL Plant Physiol. 158:981-995(2012).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23273925; DOI=10.1016/j.jplph.2012.11.007;
RA Xiao J., Zhang H., Xing L., Xu S., Liu H., Chong K., Xu Y.;
RT "Requirement of histone acetyltransferases HAM1 and HAM2 for epigenetic
RT modification of FLC in regulating flowering in Arabidopsis.";
RL J. Plant Physiol. 170:444-451(2013).
RN [10]
RP INTERACTION WITH MRG1 AND MRG2.
RC STRAIN=cv. Columbia;
RX PubMed=25183522; DOI=10.1093/nar/gku781;
RA Xu Y., Gan E.S., Zhou J., Wee W.Y., Zhang X., Ito T.;
RT "Arabidopsis MRG domain proteins bridge two histone modifications to
RT elevate expression of flowering genes.";
RL Nucleic Acids Res. 42:10960-10974(2014).
RN [11]
RP IDENTIFICATION IN THE NUA4 COMPLEX.
RX DOI=10.1186/s12870-015-0461-1;
RA Bieluszewski T., Galganski L., Sura W., Bieluszewska A., Abram M.,
RA Ludwikow A., Ziolkowski P., Sadowski J.;
RT "AtEAF1 is a potential platform protein for Arabidopsis NuA4
RT acetyltransferase complex.";
RL BMC Plant Biol. 15:0-0(2015).
CC -!- FUNCTION: Histone acetyltransferase which may be involved in
CC transcriptional activation. Acetylates 'Lys-5' of histone H4 (H4K5ac)
CC (PubMed:17877703, PubMed:19040736, PubMed:22170978, PubMed:23273925).
CC Essential for gametophyte development (PubMed:19040736). Involved in
CC DNA repair after UV-B exposure (PubMed:22170978). Negative regulator of
CC flowering controlling the H4K5ac levels in the FLC chromatin
CC (PubMed:23273925). {ECO:0000269|PubMed:17877703,
CC ECO:0000269|PubMed:19040736, ECO:0000269|PubMed:22170978,
CC ECO:0000269|PubMed:23273925}.
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:0000250|UniProtKB:Q9LXD7};
CC -!- SUBUNIT: Interacts with MRG1 and MRG2 (PubMed:25183522). Component of
CC the NuA4 histone acetyltransferase complex (Ref.11).
CC {ECO:0000269|PubMed:25183522, ECO:0000269|Ref.11}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17877703}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves, stems, roots and,
CC at higher levels in developing flowers, particularly in the anthers and
CC gynoecia (PubMed:19040736). Constitutively expressed in all tissues,
CC predominantly in shoot apical meristem (PubMed:23273925).
CC {ECO:0000269|PubMed:19040736, ECO:0000269|PubMed:23273925}.
CC -!- INDUCTION: Up-regulated upon UV-B exposure.
CC {ECO:0000269|PubMed:22170978}.
CC -!- PTM: Autoacetylation at Lys-269 is required for proper function.
CC {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC HAM2. Ham1 and ham2 double mutants are lethal.
CC {ECO:0000269|PubMed:19040736}.
CC -!- MISCELLANEOUS: Knockdown expression of both HAM1 and HAM2 results in
CC earlier flowering. {ECO:0000269|PubMed:23273925}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; AB010076; BAB11428.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97926.1; -; Genomic_DNA.
DR EMBL; AY099684; AAM20535.1; -; mRNA.
DR EMBL; BT000277; AAN15596.1; -; mRNA.
DR EMBL; AB493812; BAH30650.1; -; mRNA.
DR RefSeq; NP_201266.1; NM_125857.3.
DR AlphaFoldDB; Q9FLF7; -.
DR SMR; Q9FLF7; -.
DR BioGRID; 21824; 10.
DR IntAct; Q9FLF7; 8.
DR STRING; 3702.AT5G64610.1; -.
DR PaxDb; Q9FLF7; -.
DR PRIDE; Q9FLF7; -.
DR ProteomicsDB; 251379; -.
DR EnsemblPlants; AT5G64610.1; AT5G64610.1; AT5G64610.
DR GeneID; 836582; -.
DR Gramene; AT5G64610.1; AT5G64610.1; AT5G64610.
DR KEGG; ath:AT5G64610; -.
DR Araport; AT5G64610; -.
DR TAIR; locus:2174764; AT5G64610.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_011815_2_1_1; -.
DR InParanoid; Q9FLF7; -.
DR OMA; RIRNVEC; -.
DR OrthoDB; 629545at2759; -.
DR PhylomeDB; Q9FLF7; -.
DR BRENDA; 2.3.1.48; 399.
DR PRO; PR:Q9FLF7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLF7; baseline and differential.
DR Genevisible; Q9FLF7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:TAIR.
DR GO; GO:0043995; F:histone acetyltransferase activity (H4-K5 specific); IMP:CACAO.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:CACAO.
DR GO; GO:0010224; P:response to UV-B; IEP:TAIR.
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; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
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; Chromatin regulator;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..445
FT /note="Histone acetyltransferase of the MYST family 1"
FT /id="PRO_0000238464"
FT DOMAIN 60..118
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 169..440
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 202..227
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ACT_SITE 345
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 312..314
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 319..325
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 349
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 269
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
SQ SEQUENCE 445 AA; 51438 MW; F2243F5808ADE207 CRC64;
MGSSADTETA MIIATPASNH NNPATNGGDA NQNHTSGAIL ALTNSESDAS KKRRMGVLPL
EVGTRVMCQW RDGKYHPVKV IERRKNYNGG HNDYEYYVHY TEFNRRLDEW IKLEQLDLDS
VECALDEKVE DKVTSLKMTR HQKRKIDETH VEGHEELDAA SLREHEEFTK VKNIATIELG
KYEIETWYFS PFPPEYNDCV KLFFCEFCLS FMKRKEQLQR HMRKCDLKHP PGDEIYRSST
LSMFEVDGKK NKVYAQNLCY LAKLFLDHKT LYYDVDLFLF YILCECDDRG CHMVGYFSKE
KHSEEAYNLA CILTLPPYQR KGYGKFLIAF SYELSKKEGK VGTPERPLSD LGLVSYRGYW
TRILLDILKK HKGNISIKEL SDMTAIKAED ILSTLQSLEL IQYRKGQHVI CADPKVLDRH
LKAAGRGGLD VDVSKMIWTP YKEQS
