EAF6_HUMAN
ID EAF6_HUMAN Reviewed; 191 AA.
AC Q9HAF1; B1AK64; Q4F967; Q7Z311; Q86WE3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
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;
DE Short=hEAF6;
DE AltName: Full=Sarcoma antigen NY-SAR-91;
GN Name=MEAF6 {ECO:0000312|HGNC:HGNC:25674}; Synonyms=C1orf149, CENP-28, EAF6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Cerebellum, and Fetal brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Li M., Li H., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-191 (ISOFORM 1).
RX PubMed=12601173; DOI=10.1073/pnas.0437972100;
RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
RT "Immunomic analysis of human sarcoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NUA4 HISTONE
RP ACETYLTRANSFERASE COMPLEX.
RX PubMed=12963728; DOI=10.1074/jbc.c300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
RT containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NUA4 HISTONE
RP ACETYLTRANSFERASE COMPLEX.
RX PubMed=15647280; DOI=10.1074/jbc.m500001200;
RA Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L.,
RA Washburn M.P., Conaway R.C., Conaway J.W.;
RT "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone
RT acetyltransferase and SRCAP complexes.";
RL J. Biol. Chem. 280:13665-13670(2005).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4
RP HISTONE ACETYLTRANSFERASE COMPLEX, IDENTIFICATION IN THE HBO1 COMPLEX, AND
RP IDENTIFICATION IN THE MOZ/MORF COMPLEX.
RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
RA Lane W.S., Tan S., Yang X.-J., Cote J.;
RT "ING tumor suppressor proteins are critical regulators of chromatin
RT acetylation required for genome expression and perpetuation.";
RL Mol. Cell 21:51-64(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1,
RP AND SUBCELLULAR LOCATION.
RX PubMed=18794358; DOI=10.1128/mcb.01297-08;
RA Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C.,
RA Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J.,
RA Yang X.-J.;
RT "Molecular architecture of quartet MOZ/MORF histone acetyltransferase
RT complexes.";
RL Mol. Cell. Biol. 28:6828-6843(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND THR-120, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69 AND LYS-74, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PHF1.
RX PubMed=22761769; DOI=10.1371/journal.pone.0039354;
RA Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M.,
RA Bjerkehagen B., Davidson B., Heim S.;
RT "Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial
RT stromal sarcoma.";
RL PLoS ONE 7:E39354-E39354(2012).
RN [19]
RP FUNCTION, AND IDENTIFICATION IN THE HBO1 COMPLEX.
RX PubMed=24065767; DOI=10.1101/gad.223396.113;
RA Lalonde M.E., Avvakumov N., Glass K.C., Joncas F.H., Saksouk N.,
RA Holliday M., Paquet E., Yan K., Tong Q., Klein B.J., Tan S., Yang X.J.,
RA Kutateladze T.G., Cote J.;
RT "Exchange of associated factors directs a switch in HBO1 acetyltransferase
RT histone tail specificity.";
RL Genes Dev. 27:2009-2024(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-69 AND LYS-113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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 (PubMed:14966270).
CC This modification may both alter nucleosome - DNA interactions and
CC promote interaction of the modified histones with other proteins which
CC positively regulate transcription (PubMed:14966270). Component of HBO1
CC complexes, which specifically mediate acetylation of histone H3 at
CC 'Lys-14' (H3K14ac), and have reduced activity toward histone H4
CC (PubMed:16387653, PubMed:24065767). Component of the MOZ/MORF complex
CC which has a histone H3 acetyltransferase activity (PubMed:18794358).
CC {ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:16387653,
CC ECO:0000269|PubMed:18794358, ECO:0000269|PubMed:24065767}.
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 (PubMed:12963728,
CC PubMed:14966270, PubMed:15647280). 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 (PubMed:16387653, PubMed:24065767). Component of the MOZ/MORF complex
CC composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1,
CC BRD1/BRPF2 and BRPF3 (PubMed:18794358). {ECO:0000269|PubMed:12963728,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15647280,
CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358,
CC ECO:0000269|PubMed:24065767}.
CC -!- INTERACTION:
CC Q9HAF1; Q13895: BYSL; NbExp=3; IntAct=EBI-399266, EBI-358049;
CC Q9HAF1; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-399266, EBI-739879;
CC Q9HAF1; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-399266, EBI-21603100;
CC Q9HAF1; P22607: FGFR3; NbExp=3; IntAct=EBI-399266, EBI-348399;
CC Q9HAF1; P51116: FXR2; NbExp=3; IntAct=EBI-399266, EBI-740459;
CC Q9HAF1; P42858: HTT; NbExp=6; IntAct=EBI-399266, EBI-466029;
CC Q9HAF1; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-399266, EBI-12094820;
CC Q9HAF1; Q969R5: L3MBTL2; NbExp=4; IntAct=EBI-399266, EBI-739909;
CC Q9HAF1; O95751: LDOC1; NbExp=3; IntAct=EBI-399266, EBI-740738;
CC Q9HAF1; Q9H8W4: PLEKHF2; NbExp=5; IntAct=EBI-399266, EBI-742388;
CC Q9HAF1; P40937: RFC5; NbExp=3; IntAct=EBI-399266, EBI-712376;
CC Q9HAF1; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-399266, EBI-2130429;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18794358}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HAF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAF1-2; Sequence=VSP_022450;
CC Name=3;
CC IsoId=Q9HAF1-3; Sequence=VSP_022451;
CC Name=4;
CC IsoId=Q9HAF1-4; Sequence=VSP_047018;
CC -!- DISEASE: Note=A chromosomal aberration involving MEAF6 may be a cause
CC of endometrial stromal tumors. Translocation t(1;6)(p34;p21) with PHF1.
CC {ECO:0000269|PubMed:22761769}.
CC -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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DR EMBL; BX538212; CAD98071.1; -; mRNA.
DR EMBL; BX640719; CAE45838.1; -; mRNA.
DR EMBL; AK021792; BAB13898.1; -; mRNA.
DR EMBL; DQ099384; AAZ13760.1; -; mRNA.
DR EMBL; AL034379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056406; AAH56406.1; -; mRNA.
DR EMBL; BC016328; AAH16328.1; -; mRNA.
DR EMBL; AY211926; AAO65179.1; -; mRNA.
DR CCDS; CCDS418.1; -. [Q9HAF1-3]
DR CCDS; CCDS59195.1; -. [Q9HAF1-4]
DR CCDS; CCDS59196.1; -. [Q9HAF1-1]
DR RefSeq; NP_001257804.1; NM_001270875.1. [Q9HAF1-1]
DR RefSeq; NP_001257805.1; NM_001270876.1. [Q9HAF1-4]
DR RefSeq; NP_073593.2; NM_022756.5. [Q9HAF1-3]
DR AlphaFoldDB; Q9HAF1; -.
DR SMR; Q9HAF1; -.
DR BioGRID; 122280; 84.
DR ComplexPortal; CPX-718; HBO1-4.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-719; HBO1-4.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-720; HBO1-4.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-721; HBO1-5.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-722; HBO1-5.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-723; HBO1-5.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-727; MOZ1 histone acetyltransferase complex.
DR ComplexPortal; CPX-733; MOZ2 histone acetyltransferase complex.
DR ComplexPortal; CPX-736; MOZ3 histone acetyltransferase complex.
DR ComplexPortal; CPX-738; MORF1 histone acetyltransferase complex.
DR ComplexPortal; CPX-739; MORF2 histone acetyltransferase complex.
DR ComplexPortal; CPX-740; MORF3 histone acetyltransferase complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q9HAF1; -.
DR IntAct; Q9HAF1; 66.
DR MINT; Q9HAF1; -.
DR iPTMnet; Q9HAF1; -.
DR PhosphoSitePlus; Q9HAF1; -.
DR BioMuta; MEAF6; -.
DR DMDM; 74752760; -.
DR EPD; Q9HAF1; -.
DR jPOST; Q9HAF1; -.
DR MassIVE; Q9HAF1; -.
DR MaxQB; Q9HAF1; -.
DR PeptideAtlas; Q9HAF1; -.
DR PRIDE; Q9HAF1; -.
DR ProteomicsDB; 3023; -.
DR ProteomicsDB; 81400; -. [Q9HAF1-1]
DR ProteomicsDB; 81401; -. [Q9HAF1-2]
DR ProteomicsDB; 81402; -. [Q9HAF1-3]
DR Antibodypedia; 31724; 119 antibodies from 20 providers.
DR DNASU; 64769; -.
DR Ensembl; ENST00000296214.10; ENSP00000296214.5; ENSG00000163875.16. [Q9HAF1-1]
DR Ensembl; ENST00000373073.8; ENSP00000362164.4; ENSG00000163875.16. [Q9HAF1-4]
DR Ensembl; ENST00000373075.6; ENSP00000362166.2; ENSG00000163875.16. [Q9HAF1-3]
DR Ensembl; ENST00000448519.2; ENSP00000394966.2; ENSG00000163875.16. [Q9HAF1-2]
DR GeneID; 64769; -.
DR KEGG; hsa:64769; -.
DR MANE-Select; ENST00000296214.10; ENSP00000296214.5; NM_001270875.3; NP_001257804.1.
DR UCSC; uc001cbe.4; human. [Q9HAF1-1]
DR CTD; 64769; -.
DR DisGeNET; 64769; -.
DR GeneCards; MEAF6; -.
DR HGNC; HGNC:25674; MEAF6.
DR HPA; ENSG00000163875; Low tissue specificity.
DR MIM; 611001; gene.
DR neXtProt; NX_Q9HAF1; -.
DR OpenTargets; ENSG00000163875; -.
DR PharmGKB; PA165751536; -.
DR VEuPathDB; HostDB:ENSG00000163875; -.
DR eggNOG; KOG3856; Eukaryota.
DR GeneTree; ENSGT00390000015257; -.
DR HOGENOM; CLU_092163_1_0_1; -.
DR InParanoid; Q9HAF1; -.
DR OMA; HPSAMFD; -.
DR OrthoDB; 1629629at2759; -.
DR PhylomeDB; Q9HAF1; -.
DR TreeFam; TF324130; -.
DR PathwayCommons; Q9HAF1; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR SignaLink; Q9HAF1; -.
DR BioGRID-ORCS; 64769; 159 hits in 1087 CRISPR screens.
DR ChiTaRS; MEAF6; human.
DR GeneWiki; C1orf149; -.
DR GenomeRNAi; 64769; -.
DR Pharos; Q9HAF1; Tbio.
DR PRO; PR:Q9HAF1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HAF1; protein.
DR Bgee; ENSG00000163875; Expressed in cortical plate and 203 other tissues.
DR ExpressionAtlas; Q9HAF1; baseline and differential.
DR Genevisible; Q9HAF1; HS.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:ComplexPortal.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
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; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:ComplexPortal.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0016570; P:histone modification; IDA:ComplexPortal.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
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; IDA:ComplexPortal.
DR GO; GO:0001558; P:regulation of cell growth; IDA:ComplexPortal.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IDA:ComplexPortal.
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; IDA:ComplexPortal.
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; Chromosomal rearrangement; Chromosome; Coiled coil;
KW Isopeptide bond; Kinetochore; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; 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_0000272609"
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:0007744|PubMed:19608861"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 178..191
FT /note="RIDLKLNKKPRADY -> SPSGMFDYDFEYVY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_022450"
FT VAR_SEQ 178
FT /note="R -> SPSGMFDYDFE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_022451"
FT VAR_SEQ 179..191
FT /note="IDLKLNKKPRADY -> MNVSPKTGWHQLHL (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047018"
FT CONFLICT 2..3
FT /note="AM -> RG (in Ref. 6; AAO65179)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="H -> P (in Ref. 3; AAZ13760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21635 MW; C0FBC7566BAAF1F7 CRC64;
MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG
WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT
ESDTSPDFHN QENEPSQEDP EDLDGSVQGV KPQKAASSTS SGSHHSSHKK RKNKNRHRID
LKLNKKPRAD Y
