EAF6_SCHPO
ID EAF6_SCHPO Reviewed; 138 AA.
AC O14240;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Chromatin modification-related protein eaf6;
GN Name=eaf6; ORFNames=SPAC6F6.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX,
RP AND FUNCTION.
RX PubMed=22184112; DOI=10.1074/jbc.m111.329417;
RA Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J.,
RA Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J.,
RA Jia S.;
RT "Histone H3 lysine 14 acetylation is required for activation of a DNA
RT damage checkpoint in fission yeast.";
RL J. Biol. Chem. 287:4386-4393(2012).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair (By similarity). Component of the mst2
CC complex which is a highly specific H3 lysine 14 (H3K14)
CC acetyltransferase that functions together with gcn5 to regulate global
CC levels of H3K14 acetylation (H3K14ac), critical for DNA damage
CC checkpoint activation. {ECO:0000250, ECO:0000269|PubMed:22184112}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex (By
CC similarity). Component of the mst2 complex composed of at least eaf6,
CC mst2, nto1, pdp3, ptf1, ptf2 and tfg3. {ECO:0000250,
CC ECO:0000269|PubMed:22184112}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11732.1; -; Genomic_DNA.
DR PIR; T39043; T39043.
DR RefSeq; NP_593902.1; NM_001019332.2.
DR AlphaFoldDB; O14240; -.
DR SMR; O14240; -.
DR BioGRID; 278633; 7.
DR IntAct; O14240; 1.
DR MINT; O14240; -.
DR STRING; 4896.SPAC6F6.09.1; -.
DR iPTMnet; O14240; -.
DR MaxQB; O14240; -.
DR PaxDb; O14240; -.
DR PRIDE; O14240; -.
DR EnsemblFungi; SPAC6F6.09.1; SPAC6F6.09.1:pep; SPAC6F6.09.
DR GeneID; 2542157; -.
DR KEGG; spo:SPAC6F6.09; -.
DR PomBase; SPAC6F6.09; eaf6.
DR VEuPathDB; FungiDB:SPAC6F6.09; -.
DR eggNOG; KOG3856; Eukaryota.
DR HOGENOM; CLU_1741639_0_0_1; -.
DR InParanoid; O14240; -.
DR OMA; CKKELHE; -.
DR PhylomeDB; O14240; -.
DR Reactome; R-SPO-6804758; Regulation of TP53 Activity through Acetylation.
DR PRO; PR:O14240; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0036410; C:Mst2 histone acetyltransferase complex; TAS:PomBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
DR GO; GO:0006281; P:DNA repair; NAS:PomBase.
DR GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR InterPro; IPR015418; Eaf6.
DR PANTHER; PTHR13476; PTHR13476; 1.
DR Pfam; PF09340; NuA4; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..138
FT /note="Chromatin modification-related protein eaf6"
FT /id="PRO_0000086899"
FT REGION 93..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 18..44
FT /evidence="ECO:0000255"
FT COMPBIAS 106..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 138 AA; 15878 MW; 236E39FC7CB2BDAB CRC64;
MSTPNSTPSE PPVNVSYYEQ CKKELHEMIE KRQLLETSLI GLEDSIYRLE GSYLEKTSGT
GNIIRGFEGL LKNNASNLRR RADYSESDRL FSLSSLSSPH TRSPAYDLDD STETSRRRKR
KNESDSHEGR RRSSFREL
