ID   HAT1_MOUSE              Reviewed;         416 AA.
AC   Q8BY71;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Histone acetyltransferase type B catalytic subunit;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:O14929};
DE   AltName: Full=Histone acetyltransferase 1;
GN   Name=Hat1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Liver, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-6 AND LYS-12, CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23754951; DOI=10.1371/journal.pgen.1003518;
RA   Nagarajan P., Ge Z., Sirbu B., Doughty C., Agudelo Garcia P.A.,
RA   Schlederer M., Annunziato A.T., Cortez D., Kenner L., Parthun M.R.;
RT   "Histone acetyl transferase 1 is essential for mammalian development,
RT   genome stability, and the processing of newly synthesized histones H3 and
RT   H4.";
RL   PLoS Genet. 9:e1003518-e1003518(2013).
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:23754951).
CC       Coordinates histone production and acetylation via H4 promoter binding.
CC       Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and,
CC       to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac). Drives H4
CC       production by chromatin binding to support chromatin replication and
CC       acetylation (PubMed:23754951). Since transcription of H4 genes is
CC       tightly coupled to S-phase, plays an important role in S-phase entry
CC       and progression. Promotes homologous recombination in DNA repair by
CC       facilitating histone turnover and incorporation of acetylated H3.3 at
CC       sites of double-strand breaks (PubMed:23754951). In addition,
CC       acetylates other substrates such as chromatin-related proteins.
CC       Acetylates also RSAD2 which mediates the interaction of ubiquitin
CC       ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and subsequent
CC       degradation (By similarity). {ECO:0000250|UniProtKB:O14929,
CC       ECO:0000269|PubMed:23754951}.
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:0000250|UniProtKB:O14929};
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:0000250|UniProtKB:O14929}.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:O14929}.
CC       Mitochondrion {ECO:0000250|UniProtKB:O14929}.
CC   -!- PTM: Phosphorylated by AMPK at Ser-187; phosphorylation increases HAT1
CC       activity. {ECO:0000250|UniProtKB:O14929}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous deletion of HAT1 results in neonatal
CC       lethality but survival to at least late embryogenesis. The structure of
CC       the vertebrae in the neonates degenerates near the base of the spinal
CC       column. {ECO:0000269|PubMed:23754951}.
CC   -!- SIMILARITY: Belongs to the HAT1 family. {ECO:0000305}.
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DR   EMBL; AK041700; BAC31038.1; -; mRNA.
DR   EMBL; AK169315; BAE41070.1; -; mRNA.
DR   EMBL; BC055460; AAH55460.1; -; mRNA.
DR   CCDS; CCDS16114.1; -.
DR   RefSeq; NP_080391.2; NM_026115.4.
DR   AlphaFoldDB; Q8BY71; -.
DR   SMR; Q8BY71; -.
DR   BioGRID; 223283; 8.
DR   IntAct; Q8BY71; 5.
DR   STRING; 10090.ENSMUSP00000028408; -.
DR   GlyGen; Q8BY71; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BY71; -.
DR   PhosphoSitePlus; Q8BY71; -.
DR   EPD; Q8BY71; -.
DR   MaxQB; Q8BY71; -.
DR   PaxDb; 10090-ENSMUSP00000107750; -.
DR   PeptideAtlas; Q8BY71; -.
DR   ProteomicsDB; 269715; -.
DR   Pumba; Q8BY71; -.
DR   Antibodypedia; 19385; 439 antibodies from 32 providers.
DR   DNASU; 107435; -.
DR   Ensembl; ENSMUST00000028408.3; ENSMUSP00000028408.3; ENSMUSG00000027018.12.
DR   GeneID; 107435; -.
DR   KEGG; mmu:107435; -.
DR   UCSC; uc008kap.1; mouse.
DR   AGR; MGI:96013; -.
DR   CTD; 8520; -.
DR   MGI; MGI:96013; Hat1.
DR   VEuPathDB; HostDB:ENSMUSG00000027018; -.
DR   eggNOG; KOG2696; Eukaryota.
DR   GeneTree; ENSGT00390000007069; -.
DR   HOGENOM; CLU_036024_0_0_1; -.
DR   InParanoid; Q8BY71; -.
DR   OrthoDB; 180271at2759; -.
DR   Reactome; R-MMU-3214847; HATs acetylate histones.
DR   BioGRID-ORCS; 107435; 7 hits in 84 CRISPR screens.
DR   ChiTaRS; Hat1; mouse.
DR   PRO; PR:Q8BY71; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8BY71; Protein.
DR   Bgee; ENSMUSG00000027018; Expressed in spermatid and 264 other cell types or tissues.
DR   ExpressionAtlas; Q8BY71; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
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; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0043997; F:histone H4K12 acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:InterPro.
DR   Gene3D; 1.10.10.390; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.90.360.10; Histone acetyl transferase 1 (HAT1), N-terminal domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR048776; HAT1_C.
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; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR12046:SF0; HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT; 1.
DR   Pfam; PF21183; HAT1_C; 1.
DR   Pfam; PF10394; Hat1_N; 1.
DR   PIRSF; PIRSF038084; HAT-B_cat; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   Genevisible; Q8BY71; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Mitochondrion; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CHAIN           2..416
FT                   /note="Histone acetyltransferase type B catalytic subunit"
FT                   /id="PRO_0000227729"
FT   REGION          59..61
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   REGION          222..224
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   ACT_SITE        273
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   BINDING         238..240
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   BINDING         245..251
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   SITE            196
FT                   /note="Interaction with histone H4 N-terminus"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
FT   MOD_RES         340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14929"
SQ   SEQUENCE   416 AA;  49278 MW;  A20D53ABF1A7C824 CRC64;
     MAALEKFLVE YKSAVEKKLA EYKCNTNTAI ELKLVRFPED LENDIRTFFP EYTHQLFGDD
     ETAFGYKGLK ILLYYIAGSL STLFRVEYSS KVDENFDCVE ADDVEGKIRQ IIPPGFCTNT
     NDFLSLLEKE TNFKPFGTLL HTYTVPSQTG GETFTFQIHK ADMTCRGFRE YHERLQTFLM
     WFIETASFID VDDERWHYFL VFEKYNKDGA TLFATVGYMT VYNYYVYPDK TRPRVSQMLI
     LTPFQGQGHG AQLLETVHRY YISFPTVLDI TAEDPSRSYL KLRDFVLVKF CQFLPSFSRE
     RLLQGFSEDM AIQAQQMFKI NKQHARRVYE ILRLLVTDMS DAEQYRSYRL DIKRRLISPY
     KKKQRDLAKM KKCLRPEELT NQMNQIEISV QHEQLEERFQ ELVEDYRRVI ERLAQE
//