EAF6_MOUSE
ID EAF6_MOUSE Reviewed; 191 AA.
AC Q2VPQ9; B1ASC6; Q9D7J5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Jaw, and Limb;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND THR-120,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-6; LYS-69 AND LYS-74,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS 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).
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=Q2VPQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2VPQ9-2; Sequence=VSP_022452;
CC -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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DR EMBL; AK009177; BAB26123.1; -; mRNA.
DR EMBL; AL626775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108404; AAI08405.1; -; mRNA.
DR CCDS; CCDS18637.1; -. [Q2VPQ9-2]
DR CCDS; CCDS71467.1; -. [Q2VPQ9-1]
DR RefSeq; NP_001277630.1; NM_001290701.1. [Q2VPQ9-1]
DR RefSeq; NP_081586.1; NM_027310.4. [Q2VPQ9-2]
DR AlphaFoldDB; Q2VPQ9; -.
DR SMR; Q2VPQ9; -.
DR BioGRID; 213858; 12.
DR ComplexPortal; CPX-794; HBO1-4.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-795; HBO1-4.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-796; HBO1-4.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-797; HBO1-5.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-798; HBO1-5.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-799; HBO1-5.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-800; MOZ1 histone acetyltransferase complex.
DR ComplexPortal; CPX-801; MOZ2 histone acetyltransferase complex.
DR ComplexPortal; CPX-802; MOZ3 histone acetyltransferase complex.
DR ComplexPortal; CPX-803; MORF1 histone acetyltransferase complex.
DR ComplexPortal; CPX-804; MORF3 histone acetyltransferase complex.
DR ComplexPortal; CPX-805; MORF2 histone acetyltransferase complex.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q2VPQ9; 1.
DR MINT; Q2VPQ9; -.
DR STRING; 10090.ENSMUSP00000053543; -.
DR iPTMnet; Q2VPQ9; -.
DR PhosphoSitePlus; Q2VPQ9; -.
DR EPD; Q2VPQ9; -.
DR jPOST; Q2VPQ9; -.
DR MaxQB; Q2VPQ9; -.
DR PaxDb; Q2VPQ9; -.
DR PeptideAtlas; Q2VPQ9; -.
DR PRIDE; Q2VPQ9; -.
DR ProteomicsDB; 277751; -. [Q2VPQ9-1]
DR ProteomicsDB; 277752; -. [Q2VPQ9-2]
DR Antibodypedia; 31724; 119 antibodies from 20 providers.
DR Ensembl; ENSMUST00000055213; ENSMUSP00000053543; ENSMUSG00000028863. [Q2VPQ9-2]
DR Ensembl; ENSMUST00000154689; ENSMUSP00000122288; ENSMUSG00000028863. [Q2VPQ9-1]
DR GeneID; 70088; -.
DR KEGG; mmu:70088; -.
DR UCSC; uc008urs.2; mouse. [Q2VPQ9-2]
DR UCSC; uc008uru.2; mouse. [Q2VPQ9-1]
DR CTD; 64769; -.
DR MGI; MGI:1917338; Meaf6.
DR VEuPathDB; HostDB:ENSMUSG00000028863; -.
DR eggNOG; KOG3856; Eukaryota.
DR GeneTree; ENSGT00390000015257; -.
DR InParanoid; Q2VPQ9; -.
DR OMA; HPSAMFD; -.
DR OrthoDB; 1629629at2759; -.
DR TreeFam; TF324130; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 70088; 14 hits in 76 CRISPR screens.
DR ChiTaRS; Meaf6; mouse.
DR PRO; PR:Q2VPQ9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q2VPQ9; protein.
DR Bgee; ENSMUSG00000028863; Expressed in superior cervical ganglion and 221 other tissues.
DR ExpressionAtlas; Q2VPQ9; baseline and differential.
DR Genevisible; Q2VPQ9; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISO:MGI.
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:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISO:MGI.
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 GO; GO:0016570; P:histone modification; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR InterPro; IPR015418; Eaf6.
DR PANTHER; PTHR13476; PTHR13476; 1.
DR Pfam; PF09340; NuA4; 1.
PE 1: Evidence at protein 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:0007744|PubMed:23806337"
FT CHAIN 2..191
FT /note="Chromatin modification-related protein MEAF6"
FT /id="PRO_0000272610"
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:0007744|PubMed:23806337"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 69
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 179..191
FT /note="IDLKLNKKPRADY -> MNVSPQTGWHQLHL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022452"
FT MOD_RES Q2VPQ9-2:182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 191 AA; 21649 MW; 4B9EDC2812CFF1FD CRC64;
MAMHNKTAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG
WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT
ESDTSPDFHN QENEPAQEDP EDLDGSVQGV KPQKAASSTS SGSHHSSHKK RKNKNRHRID
LKLNKKPRAD Y
