ID A0A8L2QED5_RAT Unreviewed; 523 AA. AC A0A8L2QED5; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 27-NOV-2024, entry version 14. DE RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211}; DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211}; GN Name=Bckdk {ECO:0000313|RGD:2198}; GN Synonyms=Kat8 {ECO:0000313|Ensembl:ENSRNOP00000026527.4, GN ECO:0000313|RGD:1311512}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000026527.4, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000026527.4, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026527.4, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000026527.4} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026527.4}; RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] CC + CoA + H(+); Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA- CC COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000256|ARBA:ARBA00024456}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000256|ARBA:ARBA00024456}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000256|RuleBase:RU361211}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|RuleBase:RU361211}. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}. 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 Ensembl; ENSRNOT00000026527.5; ENSRNOP00000026527.4; ENSRNOG00000019485.7. DR RGD; 2198; Bckdk. DR RGD; 1311512; Kat8. DR GeneTree; ENSGT00940000159512; -. DR Proteomes; UP000002494; Chromosome 1. DR GO; GO:0000776; C:kinetochore; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0071339; C:MLL1 complex; IEA:Ensembl. DR GO; GO:0072487; C:MSL complex; IEA:Ensembl. DR GO; GO:0044545; C:NSL complex; IEA:Ensembl. DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IEA:Ensembl. DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IEA:Ensembl. DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl. DR GO; GO:0061920; F:protein propionyltransferase activity; IEA:Ensembl. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl. DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl. DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IEA:Ensembl. DR GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0032480; P:negative regulation of type I interferon production; IEA:Ensembl. DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl. DR GO; GO:0048477; P:oogenesis; IEA:Ensembl. DR GO; GO:1902726; P:positive regulation of skeletal muscle satellite cell differentiation; IEA:Ensembl. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IEA:Ensembl. DR GO; GO:0035166; P:post-embryonic hemopoiesis; IEA:Ensembl. DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl. DR GO; GO:1903108; P:regulation of mitochondrial transcription; IEA:Ensembl. DR GO; GO:0050684; P:regulation of mRNA processing; IEA:Ensembl. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl. DR CDD; cd18984; CBD_MOF_like; 1. DR CDD; cd04301; NAT_SF; 1. DR FunFam; 1.10.10.10:FF:000022; Histone acetyltransferase; 1. DR FunFam; 2.30.30.140:FF:000039; Histone acetyltransferase; 1. DR FunFam; 3.30.60.60:FF:000001; Histone acetyltransferase; 1. DR FunFam; 3.40.630.30:FF:000002; Histone acetyltransferase; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR050603; MYST_HAT. DR InterPro; IPR025995; Tudor-knot. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF82; HISTONE ACETYLTRANSFERASE KAT8; 1. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF11717; Tudor-knot; 1. DR Pfam; PF17772; zf-MYST; 1. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR PROSITE; PS51726; MYST_HAT; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361211}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 239..512 FT /note="MYST-type HAT" FT /evidence="ECO:0000259|PROSITE:PS51726" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 81..116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..47 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 415 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51" SQ SEQUENCE 523 AA; 59679 MW; BA675E84F663A50F CRC64; MSSKRKRNQI GPISSNNSPT EYALLNKTLP RHNLPTSNTQ TMPAPTDPEL KTSLCLIARI TSGTAMAAQG ATAAVAATTS GIVGEGEPGP GENTSVEGPA RSPGRVSPPT PARGEPEVTV EIGETYLCRR PDSTWHSAEV IQSRVNDQEG REEFYVHYVG FNRRLDEWVD KNRLALTKTV KDAVQKNSEK YLSELAEQPE RKITRNQKRK HDEINHVQKT YAEMDPTTAA LEKEHEAITK VKYVDKIHIG NYEIDAWYFS PFPEDYGKQP KLWLCEYCLK YMKFEKSYRF HLGQCQWRQP PGKEIYRKSN ISVYEVDGKD HKIYCQNLCL LAKLFLDHKT LYFDVEPFVF YILTEVDRQG AHIVGYFSKE KESPDGNNVA CILTLPPYQR RGYGKFLIAF SYELSKLEST VGSPEKPLSD LGKLSYRSYW SWVLLEILRD FRGTLSIKDL SQMTSITQND IISTLQSLNM VKYWKGQHVI CVTPKLVEEH LKSAQYKKPP ITVDSVCLKW APPKHKQVKL SKK //