HAT2_YEAST
ID HAT2_YEAST Reviewed; 401 AA.
AC P39984; D3DLJ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Histone acetyltransferase type B subunit 2;
GN Name=HAT2; OrderedLocusNames=YEL056W;
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], PROTEIN SEQUENCE OF 83-105, ACETYLATION
RP OF HISTONE H4, AND INTERACTION WITH HAT1 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RX PubMed=10075411; DOI=10.1099/13500872-145-2-293;
RA Machida K., Tanaka T., Yano Y., Otani S., Taniguchi M.;
RT "Farnesol-induced growth inhibition in Saccharomyces cerevisiae by a cell
RT cycle mechanism.";
RL Microbiology 145:293-299(1999).
RN [6]
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 [7]
RP IDENTIFICATION IN THE HAT-B COMPLEX, FUNCTION OF THE HAT-B COMPLEX,
RP INTERACTION WITH HISTONE H4, AND 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 [8]
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 [9]
RP FUNCTION.
RX PubMed=16023114; DOI=10.1016/j.febslet.2005.06.028;
RA Rosaleny L.E., Antunez O., Ruiz-Garcia A.B., Perez-Ortin J.E., Tordera V.;
RT "Yeast HAT1 and HAT2 deletions have different life-span and transcriptome
RT phenotypes.";
RL FEBS Lett. 579:4063-4068(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 7-390 IN COMPLEXES WITH HAT1 AND
RP HISTONE PEPTIDES, INTERACTION WITH HAT1 AND HISTONES H3 AND H4, SUBUNIT,
RP FUNCTION, AND MUTAGENESIS OF LEU-266.
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: Regulatory subunit of the histone acetylase B (HAT-B)
CC complex. The complex acetylates 'Lys-12' of histone H4 which is
CC required for telomeric silencing. HAT2 is required for high affinity
CC binding of the acetyltransferase to histone H4, for the nuclear
CC location of HAT1 and for the HAT1-HIF1 interaction. Alone, it is unable
CC to bind to H4, requiring HAT1 for high affinity interaction with the
CC histone tail. HAT2 has also a HAT1 independent function in life-span
CC regulation. {ECO:0000269|PubMed:10982821, ECO:0000269|PubMed:14761951,
CC ECO:0000269|PubMed:15099519, ECO:0000269|PubMed:16023114,
CC 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}.
CC -!- INTERACTION:
CC P39984; Q12341: HAT1; NbExp=4; IntAct=EBI-8185, EBI-8176;
CC P39984; Q12373: HIF1; NbExp=4; IntAct=EBI-8185, EBI-31911;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The nuclear location
CC requires the presence of HAT2.
CC -!- INDUCTION: Repressed in presence of farnesol, probably through a
CC intracellular decrease of diacylglycerol.
CC {ECO:0000269|PubMed:10075411}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; U18795; AAB65031.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07598.1; -; Genomic_DNA.
DR PIR; S50533; S50533.
DR RefSeq; NP_010858.3; NM_001178871.3.
DR PDB; 4PSW; X-ray; 2.10 A; B=7-390.
DR PDB; 4PSX; X-ray; 2.51 A; B/E=8-389.
DR PDBsum; 4PSW; -.
DR PDBsum; 4PSX; -.
DR AlphaFoldDB; P39984; -.
DR SMR; P39984; -.
DR BioGRID; 36673; 79.
DR ComplexPortal; CPX-1682; Histone acetyltransferase B.
DR DIP; DIP-2363N; -.
DR IntAct; P39984; 23.
DR MINT; P39984; -.
DR STRING; 4932.YEL056W; -.
DR MaxQB; P39984; -.
DR PaxDb; P39984; -.
DR PRIDE; P39984; -.
DR EnsemblFungi; YEL056W_mRNA; YEL056W; YEL056W.
DR GeneID; 856654; -.
DR KEGG; sce:YEL056W; -.
DR SGD; S000000782; HAT2.
DR VEuPathDB; FungiDB:YEL056W; -.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000176625; -.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; P39984; -.
DR OMA; PHEEGCL; -.
DR BioCyc; YEAST:G3O-30174-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:P39984; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39984; 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:0033698; C:Rpd3L complex; IBA:GO_Central.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IGI:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Cytoplasm; Direct protein sequencing;
KW Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..401
FT /note="Histone acetyltransferase type B subunit 2"
FT /id="PRO_0000051014"
FT REPEAT 116..147
FT /note="WD 1"
FT REPEAT 158..189
FT /note="WD 2"
FT REPEAT 206..237
FT /note="WD 3"
FT REPEAT 249..280
FT /note="WD 4"
FT REPEAT 293..324
FT /note="WD 5"
FT REPEAT 350..381
FT /note="WD 6"
FT REGION 335..339
FT /note="Interaction with the histone H4 N-terminus"
FT /evidence="ECO:0000269|PubMed:24835250"
FT SITE 266
FT /note="Important for interaction with HAT1"
FT /evidence="ECO:0000269|PubMed:24835250"
FT MUTAGEN 266
FT /note="L->E: Abolishes interaction with HAT1."
FT /evidence="ECO:0000269|PubMed:24835250"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4PSX"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4PSW"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4PSW"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:4PSW"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:4PSW"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:4PSW"
SQ SEQUENCE 401 AA; 45060 MW; C27A91C99D9FCAB7 CRC64;
MENQEKPLSV DEEYDLWKSN VPLMYDFVSE TRLTWPSLTV QWLPTPVQEL DGGFIKQELI
IGTHTSGEEE NYLKFAEINL PKEILSNEDP QEEAGEEYQS SLPAPRSNIR ITAKYEHEEE
ITRARYMPQD PNIVATINGQ GTVFLYSRSE GLQSTLKFHK DNGYALSFST LVKGRLLSGS
DDHTVALWEV GSGGDPTKPV RTWNDLHSDI INDNKWHNFN KDLFGTVSED SLLKINDVRA
NNTTIDTVKC PQPFNTLAFS HHSSNLLAAA GMDSYVYLYD LRNMKEPLHH MSGHEDAVNN
LEFSTHVDGV VVSSGSDNRL MMWDLKQIGA EQTPDDAEDG VPELIMVHAG HRSSVNDFDL
NPQIPWLVAS AEEENILQVW KCSHSLPIVG GPPKVNKDII S
