HAT1_MOUSE
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 03-AUG-2022, entry version 130.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.ENSMUSP00000107750; -.
DR iPTMnet; Q8BY71; -.
DR PhosphoSitePlus; Q8BY71; -.
DR EPD; Q8BY71; -.
DR MaxQB; Q8BY71; -.
DR PaxDb; Q8BY71; -.
DR PeptideAtlas; Q8BY71; -.
DR PRIDE; Q8BY71; -.
DR ProteomicsDB; 269715; -.
DR Antibodypedia; 19385; 406 antibodies from 32 providers.
DR DNASU; 107435; -.
DR Ensembl; ENSMUST00000028408; ENSMUSP00000028408; ENSMUSG00000027018.
DR GeneID; 107435; -.
DR KEGG; mmu:107435; -.
DR UCSC; uc008kap.1; mouse.
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; 708105at2759; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 107435; 6 hits in 78 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 260 other tissues.
DR ExpressionAtlas; Q8BY71; baseline and differential.
DR Genevisible; Q8BY71; MM.
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:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:MGI.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
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 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
