HAT1_RAT
ID HAT1_RAT Reviewed; 419 AA.
AC Q5M939;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:O14929};
DE AltName: Full=Histone acetyltransferase 1;
GN Name=Hat1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Histone acetyltransferase that plays a role in different
CC biological processes including cell cycle progression, glucose
CC metabolism, histone production or DNA damage repair. Coordinates
CC histone production and acetylation via H4 promoter binding. Acetylates
CC histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser
CC extent, histone H2A at 'Lys-5' (H2AK5ac). Drives H4 production by
CC chromatin binding to support chromatin replication and acetylation.
CC Since transcription of H4 genes is tightly coupled to S-phase, plays an
CC important role in S-phase entry and progression. Promotes homologous
CC recombination in DNA repair by facilitating histone turnover and
CC incorporation of acetylated H3.3 at sites of double-strand breaks. In
CC addition, acetylates other substrates such as chromatin-related
CC proteins. Acetylates also RSAD2 which mediates the interaction of
CC ubiquitin ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and
CC subsequent degradation. {ECO:0000250|UniProtKB:O14929}.
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 -!- SUBUNIT: Catalytic subunit of the type B histone acetyltransferase
CC (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4
CC and H2A. The interaction is dependent of the ability of RBBP7 to bind
CC to the N-terminus of histones. Component of the histone H3.1 and H3.3
CC complexes. {ECO:0000250|UniProtKB:O14929}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:O14929}.
CC Mitochondrion {ECO:0000250|UniProtKB:O14929}.
CC -!- PTM: Phosphorylated by AMPK at Ser-190; phosphorylation increases HAT1
CC activity. {ECO:0000250|UniProtKB:O14929}.
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR EMBL; BC087663; AAH87663.1; -; mRNA.
DR RefSeq; NP_001009657.1; NM_001009657.1.
DR AlphaFoldDB; Q5M939; -.
DR SMR; Q5M939; -.
DR STRING; 10116.ENSRNOP00000002085; -.
DR iPTMnet; Q5M939; -.
DR PhosphoSitePlus; Q5M939; -.
DR jPOST; Q5M939; -.
DR PaxDb; Q5M939; -.
DR PRIDE; Q5M939; -.
DR Ensembl; ENSRNOT00000002085; ENSRNOP00000002085; ENSRNOG00000001524.
DR GeneID; 296501; -.
DR KEGG; rno:296501; -.
DR UCSC; RGD:1305716; rat.
DR CTD; 8520; -.
DR RGD; 1305716; Hat1.
DR eggNOG; KOG2696; Eukaryota.
DR GeneTree; ENSGT00390000007069; -.
DR HOGENOM; CLU_036024_0_0_1; -.
DR InParanoid; Q5M939; -.
DR OMA; YFINLDE; -.
DR OrthoDB; 708105at2759; -.
DR Reactome; R-RNO-3214847; HATs acetylate histones.
DR PRO; PR:Q5M939; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000001524; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5M939; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:RGD.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:RGD.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:InterPro.
DR Gene3D; 1.10.10.390; -; 1.
DR Gene3D; 3.90.360.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR019467; Hat1_N.
DR InterPro; IPR037113; Hat1_N_sf.
DR InterPro; IPR017380; Hist_AcTrfase_B-typ_cat-su.
DR InterPro; IPR013523; Hist_AcTrfase_HAT1_C.
DR PANTHER; PTHR12046; PTHR12046; 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 Acetylation; Acyltransferase; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT CHAIN 2..419
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000227730"
FT REGION 62..64
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT REGION 225..227
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT ACT_SITE 276
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 241..243
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT BINDING 248..254
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT SITE 199
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BY71"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BY71"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14929"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14929"
SQ SEQUENCE 419 AA; 49241 MW; AF111B82A7370238 CRC64;
MAGFGAMEKF LVEYKSAVEK KLAEYKCNTN TAIELKLVRF PEDLENDIRT FFPEYTHQLF
GDDETAFGYK GLKILLYYIA GSLSTMFRVE YASKVDENFD CVEADDVEGK IRQIIPPGFC
TNTNDFLSLL EKEADFKPFG TLLHTYSVPS PTGGENFTFQ IYKADMTCRG FREYHERLQT
FLMWFIETAS FIDVDDERWH YFLVFEKYNK DGATLFATVG YMTVYNYYVY PDKTRPRVSQ
MLILTPFQGQ GHGAQLLETV HRYYIASSSV LDITAEDPSK SYVKLRDFVL VKLCQDLPCF
SRERLLQGFN EDMAIQAQQK FKINKQHARR VYEILRLLVT DMSDAEQCRS YRLDIKRRLI
SPYKKKQTDL AKMRKCLRPE ELTNQMNQIE ISVQHEQLEE QFQELVEDYR RVIERLAQE
