true1995-02-012024-03-27204HAT2_YEASTThe major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism.Parthun M.R.Widom J.Gottschling D.E.doi:10.1016/s0092-8674(00)81325-21996Cell8785-94NUCLEOTIDE SEQUENCE [GENOMIC DNA]PROTEIN SEQUENCE OF 83-105ACETYLATION OF HISTONE H4INTERACTION WITH HAT1 AND HISTONE H4The nucleotide sequence of Saccharomyces cerevisiae chromosome V.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.1997Nature38778-81NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]ATCC 204508 / S288cThe reference genome sequence of Saccharomyces cerevisiae: Then and now.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.doi:10.1534/g3.113.0089952014G3 (Bethesda)4389-398GENOME REANNOTATIONHAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4.Ruiz-Garcia A.B.Sendra R.Galiana M.Pamblanco M.Perez-Ortin J.E.Tordera V.doi:10.1074/jbc.273.20.125991998J. Biol. Chem.27312599-12605ACETYLATION OF HISTONE H4 BY THE HAT-B COMPLEXFarnesol-induced growth inhibition in Saccharomyces cerevisiae by a cell cycle mechanism.Machida K.Tanaka T.Yano Y.Otani S.Taniguchi M.doi:10.1099/13500872-145-2-2931999Microbiology145293-299INDUCTIONType B histone acetyltransferase Hat1p participates in telomeric silencing.Kelly T.J.Qin S.Gottschling D.E.Parthun M.R.doi:10.1128/mcb.20.19.7051-7058.20002000Mol. Cell. Biol.207051-7058FUNCTIONACETYLATION OF HISTONE H4Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus.Poveda A.Pamblanco M.Tafrov S.Tordera V.Sternglanz R.Sendra R.doi:10.1074/jbc.m3142282002004J. Biol. Chem.27916033-16043IDENTIFICATION IN THE HAT-B COMPLEXFUNCTION OF THE HAT-B COMPLEXINTERACTION WITH HISTONE H4SUBCELLULAR LOCATIONThe nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly.Ai X.Parthun M.R.doi:10.1016/s1097-2765(04)00184-42004Mol. Cell14195-205FUNCTIONIDENTIFICATION IN THE HAT-B COMPLEXIDENTIFICATION BY MASS SPECTROMETRYINTERACTION WITH HISTONES H3 AND H4SUBCELLULAR LOCATIONYeast HAT1 and HAT2 deletions have different life-span and transcriptome phenotypes.Rosaleny L.E.Antunez O.Ruiz-Garcia A.B.Perez-Ortin J.E.Tordera V.doi:10.1016/j.febslet.2005.06.0282005FEBS Lett.5794063-4068FUNCTIONHat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.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.doi:10.1101/gad.240531.1142014Genes Dev.281217-1227X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 7-390 IN COMPLEXES WITH HAT1 AND HISTONE PEPTIDESINTERACTION WITH HAT1 AND HISTONES H3 AND H4SUBUNITFUNCTIONMUTAGENESIS OF LEU-2662.10B=7-3902.51B/E=8-3893.30B=1-40182Histone acetyltransferase B23HAT2EukaryotaHDACs deacetylate histonesHATs acetylate histones0 hits in 10 CRISPR screensProteinYVTN repeat-like/Quinoprotein amine dehydrogenaseHistone-bd_RBBP4_NWD40/YVTN_repeat-like_dom_sfWD40_repeat_CSWD40_repeat_dom_sfWD40_rptCHROMATIN ASSEMBLY FACTOR 1 P55 SUBUNITWD40 REPEAT FAMILYCAF1C_H4-bdWD40WD40WD40 repeat-likeWD_REPEATS_1WD_REPEATS_2WD_REPEATS_REGIONHistone acetyltransferase type B subunit 2HAT2YEL056WRegulatory 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.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.The nuclear location requires the presence of HAT2.Repressed in presence of farnesol, probably through a intracellular decrease of diacylglycerol.Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.Histone acetyltransferase type B subunit 2450601401WD 1116147WD 2158189WD 3206237WD 4249280WD 5293324WD 6350381Interaction with the histone H4 N-terminus335339Important for interaction with HAT1266Abolishes interaction with HAT1.E1024253240424850536271818285108119121127130138143148150151156165168170172175179185191194200211216223228231244254259264271276288291298303305307310315320325327334337344348355360362364367372375382387389false4false4HAT1HIF11995-02-01145060ef345d874840bc9f99462e670564d150MENQEKPLSVDEEYDLWKSNVPLMYDFVSETRLTWPSLTVQWLPTPVQELDGGFIKQELIIGTHTSGEEENYLKFAEINLPKEILSNEDPQEEAGEEYQSSLPAPRSNIRITAKYEHEEEITRARYMPQDPNIVATINGQGTVFLYSRSEGLQSTLKFHKDNGYALSFSTLVKGRLLSGSDDHTVALWEVGSGGDPTKPVRTWNDLHSDIINDNKWHNFNKDLFGTVSEDSLLKINDVRANNTTIDTVKCPQPFNTLAFSHHSSNLLAAAGMDSYVYLYDLRNMKEPLHHMSGHEDAVNNLEFSTHVDGVVVSSGSDNRLMMWDLKQIGAEQTPDDAEDGVPELIMVHAGHRSSVNDFDLNPQIPWLVASAEEENILQVWKCSHSLPIVGGPPKVNKDIIStruetruetruetruetruetruetruetruetruetruetrue