HATB_ARATH
ID HATB_ARATH Reviewed; 467 AA.
AC Q9FJT8; Q8LKJ6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE Short=HAT B;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:O14929};
GN Name=HAG2; Synonyms=HAT1; OrderedLocusNames=At5g56740; ORFNames=MIK19.19;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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 [MRNA] OF 22-251, 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 [4]
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).
CC -!- FUNCTION: Acetylates soluble but not nucleosomal H4 (By similarity).
CC Acetylates 'Lys-12' of histone H4. {ECO:0000250|UniProtKB:O14929,
CC ECO:0000269|PubMed:16648464}.
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:O14929};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR EMBL; AB013392; BAB09892.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96802.1; -; Genomic_DNA.
DR EMBL; AF512724; AAM70417.1; -; mRNA.
DR RefSeq; NP_200485.1; NM_125057.4.
DR AlphaFoldDB; Q9FJT8; -.
DR SMR; Q9FJT8; -.
DR BioGRID; 21019; 3.
DR STRING; 3702.AT5G56740.1; -.
DR iPTMnet; Q9FJT8; -.
DR MetOSite; Q9FJT8; -.
DR PaxDb; Q9FJT8; -.
DR PRIDE; Q9FJT8; -.
DR ProteomicsDB; 230297; -.
DR EnsemblPlants; AT5G56740.1; AT5G56740.1; AT5G56740.
DR GeneID; 835775; -.
DR Gramene; AT5G56740.1; AT5G56740.1; AT5G56740.
DR KEGG; ath:AT5G56740; -.
DR Araport; AT5G56740; -.
DR TAIR; locus:2165091; AT5G56740.
DR eggNOG; KOG2696; Eukaryota.
DR HOGENOM; CLU_046617_0_0_1; -.
DR InParanoid; Q9FJT8; -.
DR OMA; YFINLDE; -.
DR OrthoDB; 708105at2759; -.
DR PhylomeDB; Q9FJT8; -.
DR PRO; PR:Q9FJT8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJT8; baseline and differential.
DR Genevisible; Q9FJT8; AT.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:TAIR.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:InterPro.
DR Gene3D; 3.90.360.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR019467; Hat1_N.
DR InterPro; IPR037113; Hat1_N_sf.
DR InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR PANTHER; PTHR12046; PTHR12046; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF10394; Hat1_N; 1.
DR PIRSF; PIRSF038084; HAT-B_cat; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..467
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000232125"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 249..251
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 256..262
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT SITE 207
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
SQ SEQUENCE 467 AA; 52738 MW; 2B8A0465D6451662 CRC64;
MVQKQQASAG PGTEPKKRRR VGFSPADTGV EANECIKIYL VSSKEEVDSS DISSVKPVDL
NDFFDGDGKI YGYQGLKINV WINSISLHSY ADITYQSTIN GDKGITDLKS ALQNIFAETI
VDTKDEFLQT FSTQRDFIRN MVSNGEVMHA GATDGSSKNA EVVPSDPQVI RMEIGSPNAG
LLYSRLVPLV LLFVDGSNPI DVTDPDWHLY LLIQKKEEKE DPLYRIVGFT AIYKFYRYPD
RLRMRLSQIL VLPSFQGKGL GSYLMEVVNN VAITENVYDL TVEEPSEKFQ HIRTCIDINR
LRSFDPIKPD IDSAVQTLTK GKLSKKAQIP RFTPPLNAIE KVRESLKINK KQFLKCWEIL
IYLALDPIDK YMEDYTSVIT NHVRTDILGK DIETPKKQVV DVPSSFEPEA SFVVFKSVNG
EEANTNVQVD ENKPDQEQQL KQLVEERIRE IKLVAEKVSK SGQTLKV
