MYST2_ARATH
ID MYST2_ARATH Reviewed; 445 AA.
AC Q9LXD7; C0SVP1; F4KE11; Q8GZ97; Q8LCD4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Histone acetyltransferase of the MYST family 2 {ECO:0000303|PubMed:17877703};
DE EC=2.3.1.48 {ECO:0000269|PubMed:16648464};
DE AltName: Full=Histone acetyltransferase of the GNAT/MYST superfamily 5 {ECO:0000303|PubMed:12466527};
DE AltName: Full=MYST-like histone acetyltransferase 2 {ECO:0000303|PubMed:17877703};
GN Name=HAM2 {ECO:0000303|PubMed:17877703};
GN Synonyms=HAG5 {ECO:0000303|PubMed:12466527};
GN OrderedLocusNames=At5g09740 {ECO:0000312|Araport:AT5G09740};
GN ORFNames=F17I14.70 {ECO:0000312|EMBL:CAB89356.1},
GN MTH16.20 {ECO:0000312|EMBL:BAB09532.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=16648464; DOI=10.1101/gad.1417706;
RA Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J., Silva M.,
RA Neves N., Gross M., Viegas W., Pikaard C.S.;
RT "Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale
RT gene silencing in nucleolar dominance.";
RL Genes Dev. 20:1283-1293(2006).
RN [9]
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 [10]
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 [11]
RP 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 [12]
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 [13]
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).
CC -!- FUNCTION: Histone acetyltransferase which may be involved in
CC transcriptional activation. Acetylates 'Lys-5' of histone H4 (H4K5ac)
CC (PubMed:16648464, PubMed:17877703). Essential for gametophyte
CC development (PubMed:19040736). Negative regulator of flowering
CC controlling the H4K5ac levels in the FLC chromatin (PubMed:23273925).
CC {ECO:0000269|PubMed:16648464, ECO:0000269|PubMed:17877703,
CC ECO:0000269|PubMed:19040736, 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:0000269|PubMed:16648464};
CC -!- SUBUNIT: Interacts with MRG1 and MRG2. {ECO:0000269|PubMed:25183522}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17877703}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LXD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LXD7-2; Sequence=VSP_018609, VSP_018610;
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 HAM1. 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; AL353994; CAB89356.1; -; Genomic_DNA.
DR EMBL; AB020752; BAB09532.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91440.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91441.1; -; Genomic_DNA.
DR EMBL; AK117126; BAC41804.1; -; mRNA.
DR EMBL; AY086663; AAM63720.1; -; mRNA.
DR EMBL; AB493744; BAH30582.1; -; mRNA.
DR PIR; T49924; T49924.
DR RefSeq; NP_001078558.1; NM_001085089.1.
DR RefSeq; NP_196536.1; NM_121011.4. [Q9LXD7-1]
DR AlphaFoldDB; Q9LXD7; -.
DR SMR; Q9LXD7; -.
DR BioGRID; 16112; 2.
DR STRING; 3702.AT5G09740.1; -.
DR PaxDb; Q9LXD7; -.
DR PRIDE; Q9LXD7; -.
DR ProteomicsDB; 251309; -. [Q9LXD7-1]
DR EnsemblPlants; AT5G09740.1; AT5G09740.1; AT5G09740. [Q9LXD7-1]
DR GeneID; 830834; -.
DR Gramene; AT5G09740.1; AT5G09740.1; AT5G09740. [Q9LXD7-1]
DR KEGG; ath:AT5G09740; -.
DR Araport; AT5G09740; -.
DR TAIR; locus:2144776; AT5G09740.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_011815_2_1_1; -.
DR InParanoid; Q9LXD7; -.
DR OMA; MNMVKYW; -.
DR PhylomeDB; Q9LXD7; -.
DR BRENDA; 2.3.1.48; 399.
DR PRO; PR:Q9LXD7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXD7; baseline and differential.
DR Genevisible; Q9LXD7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:TAIR.
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: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; Alternative splicing;
KW Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..445
FT /note="Histone acetyltransferase of the MYST family 2"
FT /id="PRO_0000238465"
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 REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT VAR_SEQ 135
FT /note="S -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_018609"
FT VAR_SEQ 172..249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_018610"
FT CONFLICT 129
FT /note="V -> L (in Ref. 5; AAM63720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 51367 MW; 3BA39F07E2E47C33 CRC64;
MGSSANTETN GNAPPPSSNQ KPPATNGVDG SHPPPPPLTP DQAIIESDPS KKRKMGMLPL
EVGTRVMCRW RDGKHHPVKV IERRRIHNGG QNDYEYYVHY TEFNRRLDEW TQLDQLDLDS
VECAVDEKVE DKVTSLKMTR HQKRKIDETH IEGHEELDAA SLREHEEFTK VKNISTIELG
KYEIETWYFS PFPPEYNDCV KLFFCEFCLN FMKRKEQLQR HMRKCDLKHP PGDEIYRSGT
LSMFEVDGKK NKVYAQNLCY LAKLFLDHKT LYYDVDLFLF YVLCECDDRG CHMVGYFSKE
KHSEEAYNLA CILTLPSYQR KGYGKFLIAF SYELSKKEGK VGTPERPLSD LGLLSYRGYW
TRVLLEILKK HKGNISIKEL SDVTAIKAED ILSTLQSLEL IQYRKGQHVI CADPKVLDRH
LKAAGRGGLD VDASKLIWTP YKDQS
