HAT1_HUMAN
ID HAT1_HUMAN Reviewed; 419 AA.
AC O14929; Q49A44; Q53QF0; Q53SU4; Q6P594; Q8WWB9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE EC=2.3.1.48 {ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:9427644};
DE AltName: Full=Histone acetyltransferase 1;
GN Name=HAT1; Synonyms=KAT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, ENZYME ACTIVITY, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Teratocarcinoma;
RX PubMed=9427644; DOI=10.1016/s0960-9822(98)70040-5;
RA Verreault A., Kaufman P.D., Kobayashi R., Stillman B.;
RT "Nucleosomal DNA regulates the core-histone-binding subunit of the human
RT Hat1 acetyltransferase.";
RL Curr. Biol. 8:96-108(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-419 (ISOFORM A).
RC TISSUE=Brain, Lung, and Testis;
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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11585814; DOI=10.1074/jbc.c100549200;
RA Makowski A.M., Dutnall R.N., Annunziato A.T.;
RT "Effects of acetylation of histone H4 at lysines 8 and 16 on activity of
RT the Hat1 histone acetyltransferase.";
RL J. Biol. Chem. 276:43499-43502(2001).
RN [6]
RP INDUCTION BY ESTROGEN.
RX PubMed=12841681; DOI=10.5301/jbm.2008.1705;
RA Sorbello V., Fuso L., Sfiligoi C., Scafoglio C., Ponzone R., Biglia N.,
RA Weisz A., Sismondi P., De Bortoli M.;
RT "Quantitative real-time RT-PCR analysis of eight novel estrogen-regulated
RT genes in breast cancer.";
RL Int. J. Biol. Markers 18:123-129(2003).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20148353; DOI=10.1007/s11010-010-0390-0;
RA Lebel E.A., Boukamp P., Tafrov S.T.;
RT "Irradiation with heavy-ion particles changes the cellular distribution of
RT human histone acetyltransferase HAT1.";
RL Mol. Cell. Biochem. 339:271-284(2010).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20953179; DOI=10.1038/nsmb.1911;
RA Campos E.I., Fillingham J., Li G., Zheng H., Voigt P., Kuo W.H.,
RA Seepany H., Gao Z., Day L.A., Greenblatt J.F., Reinberg D.;
RT "The program for processing newly synthesized histones H3.1 and H4.";
RL Nat. Struct. Mol. Biol. 17:1343-1351(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23653357; DOI=10.1074/jbc.m113.473199;
RA Yang X., Li L., Liang J., Shi L., Yang J., Yi X., Zhang D., Han X., Yu N.,
RA Shang Y.;
RT "Histone acetyltransferase 1 promotes homologous recombination in DNA
RT repair by facilitating histone turnover.";
RL J. Biol. Chem. 288:18271-18282(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION AT SER-190, AND MUTAGENESIS OF SER-190.
RX PubMed=28143904; DOI=10.1126/scisignal.aaf7478;
RA Marin T.L., Gongol B., Zhang F., Martin M., Johnson D.A., Xiao H., Wang Y.,
RA Subramaniam S., Chien S., Shyy J.Y.;
RT "AMPK promotes mitochondrial biogenesis and function by phosphorylating the
RT epigenetic factors DNMT1, RBBP7, and HAT1.";
RL Sci. Signal. 10:0-0(2017).
RN [15]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=31695772; DOI=10.7150/thno.37173;
RA Yang G., Feng J., Liu Y., Zhao M., Yuan Y., Yuan H., Yun H., Sun M., Bu Y.,
RA Liu L., Liu Z., Niu J.Q., Yin M., Song X., Miao Z., Lin Z., Zhang X.;
RT "HAT1 signaling confers to assembly and epigenetic regulation of HBV cccDNA
RT minichromosome.";
RL Theranostics 9:7345-7358(2019).
RN [16]
RP FUNCTION.
RX PubMed=31278053; DOI=10.1016/j.molcel.2019.05.034;
RA Gruber J.J., Geller B., Lipchik A.M., Chen J., Salahudeen A.A., Ram A.N.,
RA Ford J.M., Kuo C.J., Snyder M.P.;
RT "HAT1 Coordinates Histone Production and Acetylation via H4 Promoter
RT Binding.";
RL Mol. Cell 75:711-724.e5(2019).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32081014; DOI=10.1021/acs.jproteome.9b00843;
RA Agudelo Garcia P.A., Nagarajan P., Parthun M.R.;
RT "Hat1-Dependent Lysine Acetylation Targets Diverse Cellular Functions.";
RL J. Proteome Res. 19:1663-1673(2020).
RN [18]
RP FUNCTION, AND INDUCTION BY VIRUSES AND INTERFERONS.
RX PubMed=31812350; DOI=10.1016/j.molcel.2019.11.003;
RA Yuan Y., Miao Y., Qian L., Zhang Y., Liu C., Liu J., Zuo Y., Feng Q.,
RA Guo T., Zhang L., Chen X., Jin L., Huang F., Zhang H., Zhang W., Li W.,
RA Xu G., Zheng H.;
RT "Targeting UBE4A Revives Viperin Protein in Epithelium to Enhance Host
RT Antiviral Defense.";
RL Mol. Cell 77:734-747(2020).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 20-341 IN COMPLEX WITH ACETYL-COA
RP AND HISTONE H4 PEPTIDE, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF ASP-62; GLU-64; GLU-187; TRP-199; GLU-276 AND
RP ASP-277, ACTIVE SITE, AND INTERACTION WITH HISTONE H4.
RX PubMed=22615379; DOI=10.1073/pnas.1114117109;
RA Wu H., Moshkina N., Min J., Zeng H., Joshua J., Zhou M.M., Plotnikov A.N.;
RT "Structural basis for substrate specificity and catalysis of human histone
RT acetyltransferase 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:8925-8930(2012).
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-317.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (PubMed:31278053,
CC PubMed:20953179, PubMed:23653357, PubMed:32081014). Coordinates histone
CC production and acetylation via H4 promoter binding (PubMed:31278053).
CC Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and,
CC to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac) (PubMed:22615379,
CC PubMed:11585814). Drives H4 production by chromatin binding to support
CC chromatin replication and acetylation. Since transcription of H4 genes
CC is tightly coupled to S-phase, plays an important role in S-phase entry
CC and progression (PubMed:31278053). Promotes homologous recombination in
CC DNA repair by facilitating histone turnover and incorporation of
CC acetylated H3.3 at sites of double-strand breaks (PubMed:23653357). In
CC addition, acetylates other substrates such as chromatin-related
CC proteins (PubMed:32081014). Acetylates also RSAD2 which mediates the
CC interaction of ubiquitin ligase UBE4A with RSAD2 leading to RSAD2
CC ubiquitination and subsequent degradation (PubMed:31812350).
CC {ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:20953179,
CC ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:23653357,
CC ECO:0000269|PubMed:31278053, ECO:0000269|PubMed:31812350,
CC ECO:0000269|PubMed:32081014}.
CC -!- FUNCTION: (Microbial infection) Contributes to hepatitis B virus (HBV)
CC replication by acetylating histone H4 at the sites of 'Lys-5' and 'Lys-
CC 12' on the covalently closed circular DNA (cccDNA) minichromosome
CC leading to its accumulation within the host cell.
CC {ECO:0000269|PubMed:31695772}.
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:11585814, ECO:0000269|PubMed:22615379,
CC ECO:0000269|PubMed:9427644};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.68 uM for acetyl-CoA {ECO:0000269|PubMed:22615379};
CC Note=kcat is 4.14 (sec-1) for acetyl-CoA.
CC {ECO:0000269|PubMed:22615379};
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:0000269|PubMed:20953179, ECO:0000269|PubMed:22615379,
CC ECO:0000269|PubMed:9427644}.
CC -!- INTERACTION:
CC O14929; P62805: H4C9; NbExp=7; IntAct=EBI-2339359, EBI-302023;
CC O14929; Q5T7N3: KANK4; NbExp=3; IntAct=EBI-2339359, EBI-9355810;
CC O14929; P50222: MEOX2; NbExp=3; IntAct=EBI-2339359, EBI-748397;
CC O14929; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2339359, EBI-16439278;
CC O14929; Q5VZ52: MORN5; NbExp=5; IntAct=EBI-2339359, EBI-12835568;
CC O14929; Q09028: RBBP4; NbExp=4; IntAct=EBI-2339359, EBI-620823;
CC O14929; Q04864: REL; NbExp=3; IntAct=EBI-2339359, EBI-307352;
CC O14929; Q04864-2: REL; NbExp=3; IntAct=EBI-2339359, EBI-10829018;
CC O14929; Q16533: SNAPC1; NbExp=3; IntAct=EBI-2339359, EBI-11915024;
CC O14929; Q9H5V9: STEEP1; NbExp=3; IntAct=EBI-2339359, EBI-1053419;
CC O14929; P15884: TCF4; NbExp=3; IntAct=EBI-2339359, EBI-533224;
CC O14929; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-2339359, EBI-11139477;
CC O14929; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-2339359, EBI-2505861;
CC O14929; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-2339359, EBI-492476;
CC O14929; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-2339359, EBI-7252920;
CC O14929; P12520: vpr; Xeno; NbExp=3; IntAct=EBI-2339359, EBI-6164519;
CC O14929-2; P50222: MEOX2; NbExp=3; IntAct=EBI-10181798, EBI-748397;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Nucleus matrix
CC {ECO:0000269|PubMed:20148353, ECO:0000269|PubMed:23653357}.
CC Mitochondrion {ECO:0000269|PubMed:32081014}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm
CC {ECO:0000269|PubMed:20148353}. Nucleus {ECO:0000269|PubMed:20148353}.
CC Nucleus matrix {ECO:0000269|PubMed:20148353}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:20148353}. Note=Localization is predominantly
CC nuclear in normal cells. Treatment with hydrogen peroxide or ionizing
CC radiation enhances nuclear localization through redistribution of
CC existing protein. {ECO:0000269|PubMed:20148353}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=a, Nuclear;
CC IsoId=O14929-1; Sequence=Displayed;
CC Name=B; Synonyms=b;
CC IsoId=O14929-2; Sequence=VSP_041129;
CC -!- DEVELOPMENTAL STAGE: Highly expressed in mitotic cells (at protein
CC level). {ECO:0000269|PubMed:20148353}.
CC -!- INDUCTION: By viruses and interferons (PubMed:31812350). Up-regulated
CC also by estrogen (PubMed:12841681). {ECO:0000269|PubMed:12841681,
CC ECO:0000269|PubMed:31812350}.
CC -!- PTM: Phosphorylated by AMPK at Ser-190; phosphorylation increases HAT1
CC activity. {ECO:0000269|PubMed:28143904}.
CC -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18682.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Histone acetyltransferase entry;
CC URL="https://en.wikipedia.org/wiki/Histone_acetyltransferase";
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DR EMBL; AF030424; AAC02425.1; -; mRNA.
DR EMBL; AC015976; AAY14731.1; -; Genomic_DNA.
DR EMBL; AC114745; AAX93247.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11195.1; -; Genomic_DNA.
DR EMBL; BC018682; AAH18682.1; ALT_INIT; mRNA.
DR EMBL; BC045673; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC063003; AAH63003.1; -; mRNA.
DR CCDS; CCDS2245.1; -. [O14929-1]
DR RefSeq; NP_003633.1; NM_003642.3.
DR PDB; 2P0W; X-ray; 1.90 A; A/B=20-341.
DR PDB; 6VO5; X-ray; 1.60 A; A/B=20-341.
DR PDBsum; 2P0W; -.
DR PDBsum; 6VO5; -.
DR AlphaFoldDB; O14929; -.
DR BioGRID; 114092; 157.
DR CORUM; O14929; -.
DR DIP; DIP-52811N; -.
DR IntAct; O14929; 59.
DR MINT; O14929; -.
DR STRING; 9606.ENSP00000264108; -.
DR BindingDB; O14929; -.
DR ChEMBL; CHEMBL4523128; -.
DR GlyGen; O14929; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14929; -.
DR MetOSite; O14929; -.
DR PhosphoSitePlus; O14929; -.
DR SwissPalm; O14929; -.
DR BioMuta; HAT1; -.
DR EPD; O14929; -.
DR jPOST; O14929; -.
DR MassIVE; O14929; -.
DR MaxQB; O14929; -.
DR PaxDb; O14929; -.
DR PeptideAtlas; O14929; -.
DR PRIDE; O14929; -.
DR ProteomicsDB; 48308; -. [O14929-1]
DR ProteomicsDB; 48309; -. [O14929-2]
DR Antibodypedia; 19385; 406 antibodies from 32 providers.
DR DNASU; 8520; -.
DR Ensembl; ENST00000264108.5; ENSP00000264108.4; ENSG00000128708.13. [O14929-1]
DR GeneID; 8520; -.
DR KEGG; hsa:8520; -.
DR MANE-Select; ENST00000264108.5; ENSP00000264108.4; NM_003642.4; NP_003633.2.
DR UCSC; uc002uhi.4; human. [O14929-1]
DR CTD; 8520; -.
DR DisGeNET; 8520; -.
DR GeneCards; HAT1; -.
DR HGNC; HGNC:4821; HAT1.
DR HPA; ENSG00000128708; Low tissue specificity.
DR MIM; 603053; gene.
DR neXtProt; NX_O14929; -.
DR OpenTargets; ENSG00000128708; -.
DR PharmGKB; PA29197; -.
DR VEuPathDB; HostDB:ENSG00000128708; -.
DR eggNOG; KOG2696; Eukaryota.
DR GeneTree; ENSGT00390000007069; -.
DR HOGENOM; CLU_036024_0_0_1; -.
DR InParanoid; O14929; -.
DR OrthoDB; 708105at2759; -.
DR PhylomeDB; O14929; -.
DR TreeFam; TF314995; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; O14929; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; O14929; -.
DR SIGNOR; O14929; -.
DR BioGRID-ORCS; 8520; 16 hits in 1089 CRISPR screens.
DR ChiTaRS; HAT1; human.
DR EvolutionaryTrace; O14929; -.
DR GeneWiki; HAT1; -.
DR GenomeRNAi; 8520; -.
DR Pharos; O14929; Tbio.
DR PRO; PR:O14929; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O14929; protein.
DR Bgee; ENSG00000128708; Expressed in ventricular zone and 213 other tissues.
DR ExpressionAtlas; O14929; baseline and differential.
DR Genevisible; O14929; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; TAS:ProtInc.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0051276; P:chromosome organization; TAS:ProtInc.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0006475; P:internal protein amino acid acetylation; TAS:ProtInc.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW Cytoplasm; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..419
FT /note="Histone acetyltransferase type B catalytic subunit"
FT /id="PRO_0000083902"
FT REGION 62..64
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000269|PubMed:22615379"
FT REGION 225..227
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000305"
FT ACT_SITE 276
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000303|PubMed:22615379"
FT BINDING 241..243
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:22615379"
FT BINDING 248..254
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:22615379"
FT SITE 199
FT /note="Interaction with histone H4 N-terminus"
FT /evidence="ECO:0000269|PubMed:22615379"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
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; by AMPK"
FT /evidence="ECO:0000269|PubMed:28143904"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041129"
FT VARIANT 317
FT /note="A -> P (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035997"
FT MUTAGEN 62
FT /note="D->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:22615379"
FT MUTAGEN 64
FT /note="E->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:22615379"
FT MUTAGEN 187
FT /note="E->Q: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:22615379"
FT MUTAGEN 190
FT /note="S->A: Complete loss of activity after pulsatile
FT shear stress."
FT /evidence="ECO:0000269|PubMed:28143904"
FT MUTAGEN 190
FT /note="S->D: No loss of activity after pulsatile shear
FT stress."
FT /evidence="ECO:0000269|PubMed:28143904"
FT MUTAGEN 199
FT /note="W->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:22615379"
FT MUTAGEN 276
FT /note="E->Q: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:22615379"
FT MUTAGEN 277
FT /note="D->N: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:22615379"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6VO5"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6VO5"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 213..229
FT /evidence="ECO:0007829|PDB:6VO5"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 233..243
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:6VO5"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:6VO5"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:6VO5"
SQ SEQUENCE 419 AA; 49541 MW; 72DE4146ACC40EF6 CRC64;
MAGFGAMEKF LVEYKSAVEK KLAEYKCNTN TAIELKLVRF PEDLENDIRT FFPEYTHQLF
GDDETAFGYK GLKILLYYIA GSLSTMFRVE YASKVDENFD CVEADDVEGK IRQIIPPGFC
TNTNDFLSLL EKEVDFKPFG TLLHTYSVLS PTGGENFTFQ IYKADMTCRG FREYHERLQT
FLMWFIETAS FIDVDDERWH YFLVFEKYNK DGATLFATVG YMTVYNYYVY PDKTRPRVSQ
MLILTPFQGQ GHGAQLLETV HRYYTEFPTV LDITAEDPSK SYVKLRDFVL VKLCQDLPCF
SREKLMQGFN EDMVIEAQQK FKINKQHARR VYEILRLLVT DMSDAEQYRS YRLDIKRRLI
SPYKKKQRDL AKMRKCLRPE ELTNQMNQIE ISMQHEQLEE SFQELVEDYR RVIERLAQE
