ID B1ASC8_MOUSE Unreviewed; 173 AA.
AC B1ASC8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 2.
DT 24-JUL-2024, entry version 91.
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|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {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 (APR-2024) 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}.
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DR AlphaFoldDB; B1ASC8; -.
DR SMR; B1ASC8; -.
DR PeptideAtlas; B1ASC8; -.
DR ProteomicsDB; 307876; -.
DR Antibodypedia; 31724; 114 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|PeptideAtlas:B1ASC8,
KW ECO:0007829|ProteomicsDB: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
//