EAF6_BOVIN
ID EAF6_BOVIN Reviewed; 191 AA.
AC Q58CU0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Chromatin modification-related protein MEAF6;
DE Short=MYST/Esa1-associated factor 6;
DE AltName: Full=Esa1-associated factor 6 homolog;
DE Short=Protein EAF6 homolog;
GN Name=MEAF6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9HAF1}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5 and the subunits EP400, TRRAP,
CC BRD8, EPC1, DMAP1, RUVBL1, RUVBL2, ING3, actin, ACTL6A, MORF4L1,
CC MORF4L2, MRGBP, YEATS4, VPS72 and MEAF6. Component of the HBO1 complex
CC composed of KAT7/HBO1, MEAF6, ING4 or ING5, and one scaffold subunit:
CC complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct
CC KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE
CC scaffold (JADE1, JADE2 and JADE3) mediate acetylation of histone H4.
CC Component of the MOZ/MORF complex composed at least of ING5, KAT6A,
CC KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.
CC {ECO:0000250|UniProtKB:Q9HAF1}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9HAF1}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9HAF1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58CU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58CU0-2; Sequence=VSP_022449, VSP_022448;
CC -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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DR EMBL; BT021857; AAX46704.1; -; mRNA.
DR EMBL; DV808321; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_005204893.1; XM_005204836.3. [Q58CU0-1]
DR AlphaFoldDB; Q58CU0; -.
DR SMR; Q58CU0; -.
DR GeneID; 540599; -.
DR CTD; 64769; -.
DR eggNOG; KOG3856; Eukaryota.
DR InParanoid; Q58CU0; -.
DR OrthoDB; 1629629at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR InterPro; IPR015418; Eaf6.
DR PANTHER; PTHR13476; PTHR13476; 1.
DR Pfam; PF09340; NuA4; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Alternative splicing; Centromere;
KW Chromatin regulator; Chromosome; Coiled coil; Isopeptide bond; Kinetochore;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q2VPQ9"
FT CHAIN 2..191
FT /note="Chromatin modification-related protein MEAF6"
FT /id="PRO_0000272608"
FT REGION 104..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..47
FT /evidence="ECO:0000255"
FT COMPBIAS 164..182
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q2VPQ9"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q2VPQ9"
FT MOD_RES 69
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAF1"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAF1"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAF1"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAF1"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAF1"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAF1"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAF1"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_022449"
FT VAR_SEQ 178
FT /note="R -> SPSGMFDYDFE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_022448"
SQ SEQUENCE 191 AA; 21676 MW; 58EBDA4B6BAAF693 CRC64;
MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG
WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT
ESDTSPDFHN QENEPNQEDP EDLDGSVQGV KPQKAASSTS TGSHHSSHKK RKNKNRHRID
LKLNKKPRAD Y
