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Histone acetyltransferase type B subunit 2

 HAT2_YEAST              Reviewed;         401 AA.
P39984; D3DLJ4;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
12-SEP-2018, entry version 177.
RecName: Full=Histone acetyltransferase type B subunit 2;
Name=HAT2; OrderedLocusNames=YEL056W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 83-105,
ACETYLATION OF HISTONE H4, AND INTERACTION WITH HAT1 AND HISTONE H4.
PubMed=8858151; DOI=10.1016/S0092-8674(00)81325-2;
Parthun M.R., Widom J., Gottschling D.E.;
"The major cytoplasmic histone acetyltransferase in yeast: links to
chromatin replication and histone metabolism.";
Cell 87:85-94(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
ACETYLATION OF HISTONE H4 BY THE HAT-B COMPLEX.
PubMed=9575221; DOI=10.1074/jbc.273.20.12599;
Ruiz-Garcia A.B., Sendra R., Galiana M., Pamblanco M.,
Perez-Ortin J.E., Tordera V.;
"HAT1 and HAT2 proteins are components of a yeast nuclear histone
acetyltransferase enzyme specific for free histone H4.";
J. Biol. Chem. 273:12599-12605(1998).
[5]
INDUCTION.
PubMed=10075411; DOI=10.1099/13500872-145-2-293;
Machida K., Tanaka T., Yano Y., Otani S., Taniguchi M.;
"Farnesol-induced growth inhibition in Saccharomyces cerevisiae by a
cell cycle mechanism.";
Microbiology 145:293-299(1999).
[6]
FUNCTION, AND ACETYLATION OF HISTONE H4.
PubMed=10982821; DOI=10.1128/MCB.20.19.7051-7058.2000;
Kelly T.J., Qin S., Gottschling D.E., Parthun M.R.;
"Type B histone acetyltransferase Hat1p participates in telomeric
silencing.";
Mol. Cell. Biol. 20:7051-7058(2000).
[7]
IDENTIFICATION IN THE HAT-B COMPLEX, FUNCTION OF THE HAT-B COMPLEX,
INTERACTION WITH HISTONE H4, AND SUBCELLULAR LOCATION.
PubMed=14761951; DOI=10.1074/jbc.M314228200;
Poveda A., Pamblanco M., Tafrov S., Tordera V., Sternglanz R.,
Sendra R.;
"Hif1 is a component of yeast histone acetyltransferase B, a complex
mainly localized in the nucleus.";
J. Biol. Chem. 279:16033-16043(2004).
[8]
FUNCTION, IDENTIFICATION IN THE HAT-B COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH HISTONES H3 AND H4, AND SUBCELLULAR
LOCATION.
PubMed=15099519; DOI=10.1016/S1097-2765(04)00184-4;
Ai X., Parthun M.R.;
"The nuclear Hat1p/Hat2p complex: a molecular link between type B
histone acetyltransferases and chromatin assembly.";
Mol. Cell 14:195-205(2004).
[9]
FUNCTION.
PubMed=16023114; DOI=10.1016/j.febslet.2005.06.028;
Rosaleny L.E., Antunez O., Ruiz-Garcia A.B., Perez-Ortin J.E.,
Tordera V.;
"Yeast HAT1 and HAT2 deletions have different life-span and
transcriptome phenotypes.";
FEBS Lett. 579:4063-4068(2005).
[10]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 7-390 IN COMPLEXES WITH HAT1
AND HISTONE PEPTIDES, INTERACTION WITH HAT1 AND HISTONES H3 AND H4,
SUBUNIT, FUNCTION, AND MUTAGENESIS OF LEU-266.
PubMed=24835250; DOI=10.1101/gad.240531.114;
Li Y., Zhang L., Liu T., Chai C., Fang Q., Wu H., Agudelo Garcia P.A.,
Han Z., Zong S., Yu Y., Zhang X., Parthun M.R., Chai J., Xu R.M.,
Yang M.;
"Hat2p recognizes the histone H3 tail to specify the acetylation of
the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.";
Genes Dev. 28:1217-1227(2014).
-!- FUNCTION: Regulatory subunit of the histone acetylase B (HAT-B)
complex. The complex acetylates 'Lys-12' of histone H4 which is
required for telomeric silencing. HAT2 is required for high
affinity binding of the acetyltransferase to histone H4, for the
nuclear location of HAT1 and for the HAT1-HIF1 interaction. Alone,
it is unable to bind to H4, requiring HAT1 for high affinity
interaction with the histone tail. HAT2 has also a HAT1
independent function in life-span regulation.
{ECO:0000269|PubMed:10982821, ECO:0000269|PubMed:14761951,
ECO:0000269|PubMed:15099519, ECO:0000269|PubMed:16023114,
ECO:0000269|PubMed:24835250}.
-!- SUBUNIT: Component of the HAT-B complex composed of at least HAT1
and HAT2. In the cytoplasm, this complex binds to the histone H4
tail. In the nucleus, the HAT-B complex has an additional
component, the histone H3/H4 chaperone HIF1.
{ECO:0000269|PubMed:14761951, ECO:0000269|PubMed:15099519,
ECO:0000269|PubMed:24835250, ECO:0000269|PubMed:8858151}.
-!- INTERACTION:
Q12341:HAT1; NbExp=4; IntAct=EBI-8185, EBI-8176;
Q12373:HIF1; NbExp=4; IntAct=EBI-8185, EBI-31911;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=The nuclear
location requires the presence of HAT2.
-!- INDUCTION: Repressed in presence of farnesol, probably through a
intracellular decrease of diacylglycerol.
{ECO:0000269|PubMed:10075411}.
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U18795; AAB65031.1; -; Genomic_DNA.
EMBL; BK006939; DAA07598.1; -; Genomic_DNA.
PIR; S50533; S50533.
RefSeq; NP_010858.3; NM_001178871.3.
PDB; 4PSW; X-ray; 2.10 A; B=7-390.
PDB; 4PSX; X-ray; 2.51 A; B/E=8-389.
PDBsum; 4PSW; -.
PDBsum; 4PSX; -.
ProteinModelPortal; P39984; -.
SMR; P39984; -.
BioGrid; 36673; 75.
ComplexPortal; CPX-1682; Histone acetyltransferase B.
DIP; DIP-2363N; -.
IntAct; P39984; 23.
MINT; P39984; -.
STRING; 4932.YEL056W; -.
MaxQB; P39984; -.
PaxDb; P39984; -.
PRIDE; P39984; -.
EnsemblFungi; YEL056W; YEL056W; YEL056W.
GeneID; 856654; -.
KEGG; sce:YEL056W; -.
EuPathDB; FungiDB:YEL056W; -.
SGD; S000000782; HAT2.
GeneTree; ENSGT00570000079069; -.
HOGENOM; HOG000160330; -.
InParanoid; P39984; -.
KO; K10752; -.
OMA; TNHLADF; -.
OrthoDB; EOG092C4MBO; -.
BioCyc; YEAST:G3O-30174-MONOMER; -.
Reactome; R-SCE-3214847; HATs acetylate histones.
Reactome; R-SCE-3214858; RMTs methylate histone arginines.
Reactome; R-SCE-8951664; Neddylation.
PRO; PR:P39984; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0042393; F:histone binding; IDA:SGD.
GO; GO:0006333; P:chromatin assembly or disassembly; IDA:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IGI:SGD.
GO; GO:0016573; P:histone acetylation; IDA:SGD.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR022052; Histone-bd_RBBP4_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12265; CAF1C_H4-bd; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Chromatin regulator; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Reference proteome; Repeat;
WD repeat.
CHAIN 1 401 Histone acetyltransferase type B subunit
2.
/FTId=PRO_0000051014.
REPEAT 116 147 WD 1.
REPEAT 158 189 WD 2.
REPEAT 206 237 WD 3.
REPEAT 249 280 WD 4.
REPEAT 293 324 WD 5.
REPEAT 350 381 WD 6.
REGION 335 339 Interaction with the histone H4 N-
terminus. {ECO:0000269|PubMed:24835250}.
SITE 266 266 Important for interaction with HAT1.
{ECO:0000269|PubMed:24835250}.
MUTAGEN 266 266 L->E: Abolishes interaction with HAT1.
{ECO:0000269|PubMed:24835250}.
HELIX 10 24 {ECO:0000244|PDB:4PSW}.
STRAND 25 32 {ECO:0000244|PDB:4PSW}.
STRAND 40 42 {ECO:0000244|PDB:4PSW}.
STRAND 48 50 {ECO:0000244|PDB:4PSX}.
STRAND 53 62 {ECO:0000244|PDB:4PSW}.
STRAND 71 81 {ECO:0000244|PDB:4PSW}.
HELIX 82 85 {ECO:0000244|PDB:4PSW}.
STRAND 108 119 {ECO:0000244|PDB:4PSW}.
STRAND 121 127 {ECO:0000244|PDB:4PSW}.
STRAND 130 138 {ECO:0000244|PDB:4PSW}.
STRAND 143 147 {ECO:0000244|PDB:4PSW}.
TURN 148 150 {ECO:0000244|PDB:4PSW}.
STRAND 151 156 {ECO:0000244|PDB:4PSW}.
STRAND 165 168 {ECO:0000244|PDB:4PSW}.
STRAND 170 172 {ECO:0000244|PDB:4PSW}.
STRAND 175 179 {ECO:0000244|PDB:4PSW}.
STRAND 185 189 {ECO:0000244|PDB:4PSW}.
STRAND 191 194 {ECO:0000244|PDB:4PSW}.
STRAND 200 206 {ECO:0000244|PDB:4PSW}.
STRAND 211 216 {ECO:0000244|PDB:4PSW}.
STRAND 223 228 {ECO:0000244|PDB:4PSW}.
STRAND 231 237 {ECO:0000244|PDB:4PSW}.
STRAND 244 249 {ECO:0000244|PDB:4PSW}.
STRAND 254 259 {ECO:0000244|PDB:4PSW}.
STRAND 264 271 {ECO:0000244|PDB:4PSW}.
STRAND 276 280 {ECO:0000244|PDB:4PSW}.
STRAND 288 291 {ECO:0000244|PDB:4PSW}.
STRAND 298 303 {ECO:0000244|PDB:4PSW}.
STRAND 305 307 {ECO:0000244|PDB:4PSW}.
STRAND 310 315 {ECO:0000244|PDB:4PSW}.
STRAND 320 324 {ECO:0000244|PDB:4PSW}.
HELIX 325 327 {ECO:0000244|PDB:4PSW}.
HELIX 334 337 {ECO:0000244|PDB:4PSW}.
STRAND 344 348 {ECO:0000244|PDB:4PSW}.
STRAND 355 360 {ECO:0000244|PDB:4PSW}.
STRAND 362 364 {ECO:0000244|PDB:4PSW}.
STRAND 367 372 {ECO:0000244|PDB:4PSW}.
STRAND 375 382 {ECO:0000244|PDB:4PSW}.
TURN 387 389 {ECO:0000244|PDB:4PSW}.
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


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