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Chromatin modification-related protein MEAF6 (MYST/Esa1-associated factor 6) (Esa1-associated factor 6 homolog) (Protein EAF6 homolog) (hEAF6) (Sarcoma antigen NY-SAR-91)

 EAF6_HUMAN              Reviewed;         191 AA.
Q9HAF1; B1AK64; Q4F967; Q7Z311; Q86WE3;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 137.
RecName: Full=Chromatin modification-related protein MEAF6;
Short=MYST/Esa1-associated factor 6;
AltName: Full=Esa1-associated factor 6 homolog;
Short=Protein EAF6 homolog;
Short=hEAF6;
AltName: Full=Sarcoma antigen NY-SAR-91;
Name=MEAF6 {ECO:0000312|HGNC:HGNC:25674};
Synonyms=C1orf149, CENP-28, EAF6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Cerebellum, and Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z.,
Liang M., Li M., Li H., Yang S.;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-191 (ISOFORM 1).
PubMed=12601173; DOI=10.1073/pnas.0437972100;
Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
"Immunomic analysis of human sarcoma.";
Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NUA4
HISTONE ACETYLTRANSFERASE COMPLEX.
PubMed=12963728; DOI=10.1074/jbc.C300389200;
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
Conaway R.C., Conaway J.W.;
"Identification of new subunits of the multiprotein mammalian
TRRAP/TIP60-containing histone acetyltransferase complex.";
J. Biol. Chem. 278:42733-42736(2003).
[8]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NUA4
HISTONE ACETYLTRANSFERASE COMPLEX.
PubMed=15647280; DOI=10.1074/jbc.M500001200;
Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B.,
Workman J.L., Washburn M.P., Conaway R.C., Conaway J.W.;
"The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60
histone acetyltransferase and SRCAP complexes.";
J. Biol. Chem. 280:13665-13670(2005).
[10]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
NUA4 HISTONE ACETYLTRANSFERASE COMPLEX, IDENTIFICATION IN THE HBO1
COMPLEX, AND IDENTIFICATION IN THE MOZ/MORF COMPLEX.
PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
Lane W.S., Tan S., Yang X.-J., Cote J.;
"ING tumor suppressor proteins are critical regulators of chromatin
acetylation required for genome expression and perpetuation.";
Mol. Cell 21:51-64(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[12]
FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH
BRPF1, AND SUBCELLULAR LOCATION.
PubMed=18794358; DOI=10.1128/MCB.01297-08;
Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C.,
Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J.,
Yang X.-J.;
"Molecular architecture of quartet MOZ/MORF histone acetyltransferase
complexes.";
Mol. Cell. Biol. 28:6828-6843(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND THR-120, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69 AND LYS-74, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
SUBCELLULAR LOCATION.
PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L.,
Wood L., Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P.,
Fukagawa T., Earnshaw W.C., Rappsilber J.;
"The protein composition of mitotic chromosomes determined using
multiclassifier combinatorial proteomics.";
Cell 142:810-821(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PHF1.
PubMed=22761769; DOI=10.1371/journal.pone.0039354;
Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M.,
Bjerkehagen B., Davidson B., Heim S.;
"Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial
stromal sarcoma.";
PLoS ONE 7:E39354-E39354(2012).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-69 AND LYS-113, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Component of the NuA4 histone acetyltransferase complex
which is involved in transcriptional activation of select genes
principally by acetylation of nucleosomal histone H4 and H2A. This
modification may both alter nucleosome - DNA interactions and
promote interaction of the modified histones with other proteins
which positively regulate transcription. Component of the HBO1
complex which has a histone H4-specific acetyltransferase
activity, a reduced activity toward histone H3 and is responsible
for the bulk of histone H4 acetylation in vivo. Component of the
MOZ/MORF complex which has a histone H3 acetyltransferase
activity. {ECO:0000269|PubMed:14966270,
ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
which contains the catalytic subunit KAT5 and the subunits EP400,
TRRAP, BRD8, EPC1, DMAP1, RUVBL1, RUVBL2, ING3, actin, ACTL6A,
MORF4L1, MORF4L2, MRGBP, YEATS4, VPS72 and MEAF6. Component of the
HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6,
and one of JADE1, JADE2 and JADE3. Component of the MOZ/MORF
complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of
BRPF1, BRD1/BRPF2 and BRPF3. {ECO:0000269|PubMed:12963728,
ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15647280,
ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358}.
-!- INTERACTION:
P51116:FXR2; NbExp=3; IntAct=EBI-399266, EBI-740459;
Q969R5:L3MBTL2; NbExp=3; IntAct=EBI-399266, EBI-739909;
O95751:LDOC1; NbExp=3; IntAct=EBI-399266, EBI-740738;
Q9H8W4:PLEKHF2; NbExp=5; IntAct=EBI-399266, EBI-742388;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-399266, EBI-2130429;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:18794358}. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:20813266}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9HAF1-1; Sequence=Displayed;
Name=2;
IsoId=Q9HAF1-2; Sequence=VSP_022450;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9HAF1-3; Sequence=VSP_022451;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9HAF1-4; Sequence=VSP_047018;
Note=Gene prediction based on EST data.;
-!- DISEASE: Note=A chromosomal aberration involving MEAF6 may be a
cause of endometrial stromal tumors. Translocation t(1;6)(p34;p21)
with PHF1. {ECO:0000269|PubMed:22761769}.
-!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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EMBL; BX538212; CAD98071.1; -; mRNA.
EMBL; BX640719; CAE45838.1; -; mRNA.
EMBL; AK021792; BAB13898.1; -; mRNA.
EMBL; DQ099384; AAZ13760.1; -; mRNA.
EMBL; AL034379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC056406; AAH56406.1; -; mRNA.
EMBL; BC016328; AAH16328.1; -; mRNA.
EMBL; AY211926; AAO65179.1; -; mRNA.
CCDS; CCDS418.1; -. [Q9HAF1-3]
CCDS; CCDS59195.1; -. [Q9HAF1-4]
CCDS; CCDS59196.1; -. [Q9HAF1-1]
RefSeq; NP_001257804.1; NM_001270875.1. [Q9HAF1-1]
RefSeq; NP_001257805.1; NM_001270876.1. [Q9HAF1-4]
RefSeq; NP_073593.2; NM_022756.5. [Q9HAF1-3]
UniGene; Hs.17118; -.
ProteinModelPortal; Q9HAF1; -.
BioGrid; 122280; 57.
ComplexPortal; CPX-718; HBO1-4.1 histone acetyltransferase complex.
ComplexPortal; CPX-719; HBO1-4.2 histone acetyltransferase complex.
ComplexPortal; CPX-720; HBO1-4.3 histone acetyltransferase complex.
ComplexPortal; CPX-721; HBO1-5.1 histone acetyltransferase complex.
ComplexPortal; CPX-722; HBO1-5.2 histone acetyltransferase complex.
ComplexPortal; CPX-723; HBO1-5.3 histone acetyltransferase complex.
ComplexPortal; CPX-727; MOZ1 histone acetyltransferase complex.
ComplexPortal; CPX-733; MOZ2 histone acetyltransferase complex.
ComplexPortal; CPX-736; MOZ3 histone acetyltransferase complex.
ComplexPortal; CPX-738; MORF1 histone acetyltransferase complex.
ComplexPortal; CPX-739; MORF2 histone acetyltransferase complex.
ComplexPortal; CPX-740; MORF3 histone acetyltransferase complex.
ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
CORUM; Q9HAF1; -.
IntAct; Q9HAF1; 17.
iPTMnet; Q9HAF1; -.
PhosphoSitePlus; Q9HAF1; -.
DMDM; 74752760; -.
EPD; Q9HAF1; -.
MaxQB; Q9HAF1; -.
PeptideAtlas; Q9HAF1; -.
PRIDE; Q9HAF1; -.
ProteomicsDB; 81400; -.
ProteomicsDB; 81401; -. [Q9HAF1-2]
ProteomicsDB; 81402; -. [Q9HAF1-3]
DNASU; 64769; -.
Ensembl; ENST00000296214; ENSP00000296214; ENSG00000163875. [Q9HAF1-1]
Ensembl; ENST00000373073; ENSP00000362164; ENSG00000163875. [Q9HAF1-4]
Ensembl; ENST00000373075; ENSP00000362166; ENSG00000163875. [Q9HAF1-3]
Ensembl; ENST00000448519; ENSP00000394966; ENSG00000163875. [Q9HAF1-2]
GeneID; 64769; -.
KEGG; hsa:64769; -.
UCSC; uc001cbe.4; human. [Q9HAF1-1]
CTD; 64769; -.
DisGeNET; 64769; -.
EuPathDB; HostDB:ENSG00000163875.15; -.
GeneCards; MEAF6; -.
HGNC; HGNC:25674; MEAF6.
MIM; 611001; gene.
neXtProt; NX_Q9HAF1; -.
OpenTargets; ENSG00000163875; -.
PharmGKB; PA165751536; -.
GeneTree; ENSGT00390000015257; -.
HOGENOM; HOG000290166; -.
InParanoid; Q9HAF1; -.
KO; K11344; -.
OMA; DMKVNKK; -.
OrthoDB; EOG091G126R; -.
PhylomeDB; Q9HAF1; -.
TreeFam; TF324130; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
ChiTaRS; MEAF6; human.
GeneWiki; C1orf149; -.
GenomeRNAi; 64769; -.
PRO; PR:Q9HAF1; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163875; Expressed in 225 organ(s), highest expression level in pituitary gland.
CleanEx; HS_C1orf149; -.
ExpressionAtlas; Q9HAF1; baseline and differential.
Genevisible; Q9HAF1; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
GO; GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR015418; Eaf6.
PANTHER; PTHR13476; PTHR13476; 1.
Pfam; PF09340; NuA4; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Centromere;
Chromatin regulator; Chromosomal rearrangement; Chromosome;
Coiled coil; Complete proteome; Isopeptide bond; Kinetochore; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q2VPQ9}.
CHAIN 2 191 Chromatin modification-related protein
MEAF6.
/FTId=PRO_0000272609.
COILED 11 47 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q2VPQ9}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q2VPQ9}.
MOD_RES 69 69 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 74 74 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 69 69 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 178 191 RIDLKLNKKPRADY -> SPSGMFDYDFEYVY (in
isoform 2). {ECO:0000303|Ref.3}.
/FTId=VSP_022450.
VAR_SEQ 178 178 R -> SPSGMFDYDFE (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_022451.
VAR_SEQ 179 191 IDLKLNKKPRADY -> MNVSPKTGWHQLHL (in
isoform 4). {ECO:0000305}.
/FTId=VSP_047018.
CONFLICT 2 3 AM -> RG (in Ref. 6; AAO65179).
{ECO:0000305}.
CONFLICT 4 4 H -> P (in Ref. 3; AAZ13760).
{ECO:0000305}.
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


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