ID B1ASC8_MOUSE Unreviewed; 173 AA. AC B1ASC8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 2. DT 27-MAR-2024, entry version 89. DE RecName: Full=Chromatin modification-related protein MEAF6 {ECO:0000256|ARBA:ARBA00019141, ECO:0000256|RuleBase:RU368022}; DE Flags: Fragment; GN Name=Meaf6 {ECO:0000313|Ensembl:ENSMUSP00000101777.4, GN ECO:0000313|MGI:MGI:1917338}; 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 {ECO:0000313|Ensembl:ENSMUSP00000101777.4, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000101777.4, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101777.4, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0007829|PubMed:23806337} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [4] {ECO:0000313|Ensembl:ENSMUSP00000101777.4} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000101777.4}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which CC is involved in transcriptional activation of select genes principally CC by acetylation of nucleosomal histone H4 and H2A. This modification may CC both alter nucleosome - DNA interactions and promote interaction of the CC modified histones with other proteins which positively regulate CC transcription. Component of HBO1 complexes, which specifically mediate CC acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced CC activity toward histone H4. Component of the MOZ/MORF complex which has CC a histone H3 acetyltransferase activity. CC {ECO:0000256|RuleBase:RU368022}. CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex. CC Component of the hbo1 complex. Component of the moz/morf complex. CC {ECO:0000256|RuleBase:RU368022}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000256|RuleBase:RU368022}. Chromosome, centromere, kinetochore CC {ECO:0000256|RuleBase:RU368022}. CC -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000256|ARBA:ARBA00010916, CC ECO:0000256|RuleBase:RU368022}. 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 AlphaFoldDB; B1ASC8; -. DR SMR; B1ASC8; -. DR MaxQB; B1ASC8; -. DR PeptideAtlas; B1ASC8; -. DR ProteomicsDB; 307876; -. DR Antibodypedia; 31724; 125 antibodies from 20 providers. DR Ensembl; ENSMUST00000106171.9; ENSMUSP00000101777.4; ENSMUSG00000028863.14. DR AGR; MGI:1917338; -. DR MGI; MGI:1917338; Meaf6. DR VEuPathDB; HostDB:ENSMUSG00000028863; -. DR GeneTree; ENSGT00390000015257; -. DR HOGENOM; CLU_092163_1_0_1; -. DR ChiTaRS; Meaf6; mouse. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; ENSMUSG00000028863; Expressed in superior cervical ganglion and 224 other cell types or tissues. DR ExpressionAtlas; B1ASC8; baseline and differential. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-UniRule. DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:UniProtKB-UniRule. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:UniProtKB-UniRule. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR InterPro; IPR015418; Eaf6. DR PANTHER; PTHR13476:SF0; CHROMATIN MODIFICATION-RELATED PROTEIN MEAF6; 1. DR PANTHER; PTHR13476; UNCHARACTERIZED; 1. DR Pfam; PF09340; NuA4; 1. PE 1: Evidence at protein level; KW Activator {ECO:0000256|RuleBase:RU368022}; KW Centromere {ECO:0000256|RuleBase:RU368022}; KW Chromatin regulator {ECO:0000256|RuleBase:RU368022}; KW Chromosome {ECO:0000256|RuleBase:RU368022}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054}; KW Kinetochore {ECO:0000256|RuleBase:RU368022}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368022}; KW Proteomics identification {ECO:0007829|EPD:B1ASC8, KW ECO:0007829|MaxQB:B1ASC8}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, KW ECO:0000256|RuleBase:RU368022}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, KW ECO:0000256|RuleBase:RU368022}. FT REGION 76..173 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..173 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000101777.4" SQ SEQUENCE 173 AA; 19498 MW; 55163F993B0CB39E CRC64; LAETLANLER QIYAFEGSYL EDTQMYGNII RGWDRYLTNQ KNSNSKNDRR NRKFKEAERL FSKSSVTSAA AVSALAGVQD QLIEKREPGS GTESDTSPDF HNQENEPAQE DPEDLDGSVQ GVKPQKAASS TSSGSHHSSH KKRKNKNRHS PSGMFDYDFE IDLKLNKKPR ADY //