HAT1_YEAST
ID HAT1_YEAST Reviewed; 374 AA.
AC Q12341; D6W411; Q6Q5I5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000269|PubMed:24835250};
GN Name=HAT1; OrderedLocusNames=YPL001W; ORFNames=LPA16W, YP8132.12;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION OF
RP HISTONE H4, AND INTERACTION WITH HAT2 AND HISTONE H4.
RX PubMed=8858151; DOI=10.1016/s0092-8674(00)81325-2;
RA Parthun M.R., Widom J., Gottschling D.E.;
RT "The major cytoplasmic histone acetyltransferase in yeast: links to
RT chromatin replication and histone metabolism.";
RL Cell 87:85-94(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7559580; DOI=10.1074/jbc.270.42.24674;
RA Kleff S., Andrulis E.D., Anderson C.W., Sternglanz R.;
RT "Identification of a gene encoding a yeast histone H4 acetyltransferase.";
RL J. Biol. Chem. 270:24674-24677(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP ACETYLATION OF HISTONE H4 BY THE HAT-B COMPLEX.
RX PubMed=9575221; DOI=10.1074/jbc.273.20.12599;
RA Ruiz-Garcia A.B., Sendra R., Galiana M., Pamblanco M., Perez-Ortin J.E.,
RA Tordera V.;
RT "HAT1 and HAT2 proteins are components of a yeast nuclear histone
RT acetyltransferase enzyme specific for free histone H4.";
RL J. Biol. Chem. 273:12599-12605(1998).
RN [7]
RP FUNCTION, AND ACETYLATION OF HISTONE H4.
RX PubMed=10982821; DOI=10.1128/mcb.20.19.7051-7058.2000;
RA Kelly T.J., Qin S., Gottschling D.E., Parthun M.R.;
RT "Type B histone acetyltransferase Hat1p participates in telomeric
RT silencing.";
RL Mol. Cell. Biol. 20:7051-7058(2000).
RN [8]
RP FUNCTION.
RX PubMed=12417736; DOI=10.1128/mcb.22.23.8353-8365.2002;
RA Qin S., Parthun M.R.;
RT "Histone H3 and the histone acetyltransferase Hat1p contribute to DNA
RT double-strand break repair.";
RL Mol. Cell. Biol. 22:8353-8365(2002).
RN [9]
RP INTERACTION WITH HIF1 AND HISTONE H4, FUNCTION OF THE HAT-B COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14761951; DOI=10.1074/jbc.m314228200;
RA Poveda A., Pamblanco M., Tafrov S., Tordera V., Sternglanz R., Sendra R.;
RT "Hif1 is a component of yeast histone acetyltransferase B, a complex mainly
RT localized in the nucleus.";
RL J. Biol. Chem. 279:16033-16043(2004).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE HAT-B COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, INTERACTION WITH HISTONES H3 AND H4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15099519; DOI=10.1016/s1097-2765(04)00184-4;
RA Ai X., Parthun M.R.;
RT "The nuclear Hat1p/Hat2p complex: a molecular link between type B histone
RT acetyltransferases and chromatin assembly.";
RL Mol. Cell 14:195-205(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-320 IN COMPLEX WITH ACETYL-COA.
RX PubMed=9727486; DOI=10.1016/s0092-8674(00)81584-6;
RA Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V.;
RT "Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-
RT related N-acetyltransferase superfamily.";
RL Cell 94:427-438(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 4-320 IN COMPLEXES WITH COENZYME
RP A; HAT2 AND HISTONE PEPTIDES, CATALYTIC ACTIVITY, SUBUNIT, FUNCTION, ACTIVE
RP SITE, AND MUTAGENESIS OF TRP-197; TYR-199; ALA-202; PHE-205 AND ARG-214.
RX PubMed=24835250; DOI=10.1101/gad.240531.114;
RA Li Y., Zhang L., Liu T., Chai C., Fang Q., Wu H., Agudelo Garcia P.A.,
RA Han Z., Zong S., Yu Y., Zhang X., Parthun M.R., Chai J., Xu R.M., Yang M.;
RT "Hat2p recognizes the histone H3 tail to specify the acetylation of the
RT newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.";
RL Genes Dev. 28:1217-1227(2014).
CC -!- FUNCTION: Catalytic component of the histone acetylase B (HAT-B)
CC complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The
CC complex is also found in the nucleus, however it is not certain that it
CC modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12'
CC acetylation is required for telomeric silencing. Has intrinsic
CC substrate specificity that modifies lysine in recognition sequence
CC GXGKXG. Involved in DNA double-strand break repair.
CC {ECO:0000269|PubMed:10982821, ECO:0000269|PubMed:12417736,
CC ECO:0000269|PubMed:14761951, ECO:0000269|PubMed:15099519,
CC ECO:0000269|PubMed:24835250, ECO:0000269|PubMed:7559580}.
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:24835250};
CC -!- SUBUNIT: Component of the HAT-B complex composed of at least HAT1 and
CC HAT2. In the cytoplasm, this complex binds to the histone H4 tail. In
CC the nucleus, the HAT-B complex has an additional component, the histone
CC H3/H4 chaperone HIF1. {ECO:0000269|PubMed:14761951,
CC ECO:0000269|PubMed:15099519, ECO:0000269|PubMed:24835250,
CC ECO:0000269|PubMed:8858151, ECO:0000269|PubMed:9727486}.
CC -!- INTERACTION:
CC Q12341; P39984: HAT2; NbExp=4; IntAct=EBI-8176, EBI-8185;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR EMBL; Z48483; CAA88385.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95040.1; -; Genomic_DNA.
DR EMBL; U33335; AAB68104.1; -; Genomic_DNA.
DR EMBL; AY558042; AAS56368.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11427.1; -; Genomic_DNA.
DR PIR; A57583; A57583.
DR RefSeq; NP_015324.1; NM_001183815.1.
DR PDB; 1BOB; X-ray; 2.30 A; A=1-320.
DR PDB; 4PSW; X-ray; 2.10 A; A=4-320.
DR PDB; 4PSX; X-ray; 2.51 A; A/D=7-319.
DR PDBsum; 1BOB; -.
DR PDBsum; 4PSW; -.
DR PDBsum; 4PSX; -.
DR AlphaFoldDB; Q12341; -.
DR SMR; Q12341; -.
DR BioGRID; 36176; 170.
DR ComplexPortal; CPX-1682; Histone acetyltransferase B.
DR DIP; DIP-2362N; -.
DR IntAct; Q12341; 13.
DR MINT; Q12341; -.
DR STRING; 4932.YPL001W; -.
DR iPTMnet; Q12341; -.
DR MaxQB; Q12341; -.
DR PaxDb; Q12341; -.
DR PRIDE; Q12341; -.
DR EnsemblFungi; YPL001W_mRNA; YPL001W; YPL001W.
DR GeneID; 856106; -.
DR KEGG; sce:YPL001W; -.
DR SGD; S000005922; HAT1.
DR VEuPathDB; FungiDB:YPL001W; -.
DR eggNOG; KOG2696; Eukaryota.
DR GeneTree; ENSGT00390000007069; -.
DR HOGENOM; CLU_036024_2_1_1; -.
DR InParanoid; Q12341; -.
DR OMA; HNANECI; -.
DR BioCyc; YEAST:G3O-33920-MON; -.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR EvolutionaryTrace; Q12341; -.
DR PRO; PR:Q12341; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12341; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:SGD.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IGI:SGD.
DR Gene3D; 1.10.10.390; -; 1.
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 InterPro; IPR013523; Hist_AcTrfase_HAT1_C.
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.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Chromatin regulator; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..374
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000083903"
FT DOMAIN 135..303
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 42..44
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000269|PubMed:24835250"
FT REGION 194..196
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000269|PubMed:24835250"
FT REGION 197..205
FT /note="Interaction with HAT2"
FT /evidence="ECO:0000269|PubMed:24835250,
FT ECO:0000269|PubMed:8858151"
FT ACT_SITE 255
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000303|PubMed:24835250"
FT BINDING 220..222
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24835250,
FT ECO:0000269|PubMed:9727486"
FT BINDING 227..233
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24835250,
FT ECO:0000269|PubMed:9727486"
FT BINDING 258
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:24835250,
FT ECO:0000269|PubMed:9727486"
FT BINDING 267
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:9727486"
FT SITE 174
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000269|PubMed:24835250"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 197
FT /note="W->E: Abolishes interaction with HAT2."
FT /evidence="ECO:0000269|PubMed:24835250"
FT MUTAGEN 199
FT /note="Y->E: Abolishes interaction with HAT2."
FT /evidence="ECO:0000269|PubMed:24835250"
FT MUTAGEN 202
FT /note="A->D: Impairs interaction with HAT2."
FT /evidence="ECO:0000269|PubMed:24835250"
FT MUTAGEN 205
FT /note="F->E: Abolishes interaction with HAT2."
FT /evidence="ECO:0000269|PubMed:24835250"
FT MUTAGEN 214
FT /note="R->A: Impairs interaction with HAT2."
FT /evidence="ECO:0000269|PubMed:24835250"
FT CONFLICT 87
FT /note="L -> V (in Ref. 5; AAS56368)"
FT /evidence="ECO:0000305"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 19..31
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:4PSW"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1BOB"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4PSW"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:4PSW"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:4PSW"
SQ SEQUENCE 374 AA; 43873 MW; 8DECA134274413E6 CRC64;
MSANDFKPET WTSSANEALR VSIVGENAVQ FSPLFTYPIY GDSEKIYGYK DLIIHLAFDS
VTFKPYVNVK YSAKLGDDNI VDVEKKLLSF LPKDDVIVRD EAKWVDCFAE ERKTHNLSDV
FEKVSEYSLN GEEFVVYKSS LVDDFARRMH RRVQIFSLLF IEAANYIDET DPSWQIYWLL
NKKTKELIGF VTTYKYWHYL GAKSFDEDID KKFRAKISQF LIFPPYQNKG HGSCLYEAII
QSWLEDKSIT EITVEDPNEA FDDLRDRNDI QRLRKLGYDA VFQKHSDLSD EFLESSRKSL
KLEERQFNRL VEMLLLLNNS PSFELKVKNR LYIKNYDALD QTDPEKAREA LQNSFILVKD
DYRRIIESIN KSQG
