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Database: UniProt
Entry: Q02078
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Original site: Q02078 
ID   MEF2A_HUMAN             Reviewed;         507 AA.
AC   Q02078; B4DFQ7; F6XG23; O43814; Q14223; Q14224; Q59GX4; Q7Z6C9; Q96D14;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   29-SEP-2021, entry version 209.
DE   RecName: Full=Myocyte-specific enhancer factor 2A;
DE   AltName: Full=Serum response factor-like protein 1;
GN   Name=MEF2A; Synonyms=MEF2;
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 [MRNA] (ISOFORMS MEF2; RSRFC4 AND RSRFC9), DNA-BINDING,
RP   TISSUE SPECIFICITY, AND DIMERIZATION.
RC   TISSUE=Placenta;
RX   PubMed=1748287; DOI=10.1101/gad.5.12a.2327;
RA   Pollock R., Treisman R.;
RT   "Human SRF-related proteins: DNA-binding properties and potential
RT   regulatory targets.";
RL   Genes Dev. 5:2327-2341(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RSRFC9), AND SEQUENCE REVISION.
RA   Treisman R.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2 AND RSRFC9), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Heart, and Skeletal muscle;
RX   PubMed=1516833; DOI=10.1101/gad.6.9.1783;
RA   Yu Y.-T., Breitbart R.E., Smoot L.B., Lee Y., Mahdavi V., Nadal-Ginard B.;
RT   "Human myocyte-specific enhancer factor 2 comprises a group of tissue-
RT   restricted MADS box transcription factors.";
RL   Genes Dev. 6:1783-1798(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS RSRFC4 AND RSRFC9).
RA   Suzuki E., Lowry J., Sonoda G., Testa J.R., Walsh K.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   TISSUE=Amygdala;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno F.R.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
RC   TISSUE=Pancreas, 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   [9]
RP   INTERACTION WITH MAPK7, AND PHOSPHORYLATION.
RX   PubMed=9753748; DOI=10.1093/nar/26.20.4771;
RA   Yang C.-C., Ornatsky O.I., McDermott J.C., Cruz T.F., Prody C.A.;
RT   "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated
RT   protein kinase, ERK5/BMK1.";
RL   Nucleic Acids Res. 26:4771-4777(1998).
RN   [10]
RP   INTERACTION WITH HDAC4 AND HDAC9.
RX   PubMed=10487761; DOI=10.1093/emboj/18.18.5099;
RA   Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.;
RT   "HDAC4 deacetylase associates with and represses the MEF2 transcription
RT   factor.";
RL   EMBO J. 18:5099-5107(1999).
RN   [11]
RP   PHOSPHORYLATION AT THR-312; THR-319 AND SER-453, FUNCTION,
RP   HETERODIMERIZATION, AND MUTAGENESIS OF THR-312; THR-319; SER-355; SER-453
RP   AND SER-479.
RX   PubMed=9858528; DOI=10.1128/mcb.19.1.21;
RA   Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F.,
RA   Olson E.N., Ulevitch R.J., Han J.-D.;
RT   "Regulation of the MEF2 family of transcription factors by p38.";
RL   Mol. Cell. Biol. 19:21-30(1999).
RN   [12]
RP   INTERACTION WITH MAPK14, PHOSPHORYLATION AT THR-312 AND THR-319, AND
RP   MUTAGENESIS OF ARG-269; LYS-270; LEU-273; VAL-275; ILE-277 AND PRO-278.
RX   PubMed=10330143; DOI=10.1128/mcb.19.6.4028;
RA   Yang S.-H., Galanis A., Sharrocks A.D.;
RT   "Targeting of p38 mitogen-activated protein kinases to MEF2 transcription
RT   factors.";
RL   Mol. Cell. Biol. 19:4028-4038(1999).
RN   [13]
RP   PHOSPHORYLATION AT THR-312; THR-319 AND SER-355, AND MUTAGENESIS OF
RP   THR-312; THR-319 AND SER-355.
RX   PubMed=10849446; DOI=10.1074/jbc.m001573200;
RA   Kato Y., Zhao M., Morikawa A., Sugiyama T., Chakravortty D., Koide N.,
RA   Yoshida T., Tapping R.I., Yang Y., Yokochi T., Lee J.D.;
RT   "Big mitogen-activated kinase regulates multiple members of the MEF2
RT   protein family.";
RL   J. Biol. Chem. 275:18534-18540(2000).
RN   [14]
RP   PROTEOLYTIC PROCESSING AT ASP-176; ASP-213 AND ASP-466, FUNCTION, AND
RP   MUTAGENESIS OF ASP-176 AND ASP-213.
RX   PubMed=11904443; DOI=10.1073/pnas.022036399;
RA   Okamoto S., Li Z., Ju C., Scholzke M.N., Mathews E., Cui J., Salvesen G.S.,
RA   Bossy-Wetzel E., Lipton S.A.;
RT   "Dominant-interfering forms of MEF2 generated by caspase cleavage
RT   contribute to NMDA-induced neuronal apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:3974-3979(2002).
RN   [15]
RP   PHOSPHORYLATION AT SER-255; THR-312; THR-319 AND SER-408, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND MUTAGENESIS OF SER-255.
RX   PubMed=12586839; DOI=10.1074/jbc.m211312200;
RA   Cox D.M., Du M., Marback M., Yang E.C.C., Chan J., Siu K.W.M.,
RA   McDermott J.C.;
RT   "Phosphorylation motifs regulating the stability and function of myocyte
RT   enhancer factor 2A.";
RL   J. Biol. Chem. 278:15297-15303(2003).
RN   [16]
RP   PHOSPHORYLATION AT SER-408, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF SER-408.
RX   PubMed=12691662; DOI=10.1016/s0896-6273(03)00191-0;
RA   Gong X., Tang X., Wiedmann M., Wang X., Peng J., Zheng D., Blair L.A.C.,
RA   Marshall J., Mao Z.;
RT   "Cdk5-mediated inhibition of the protective effects of transcription factor
RT   MEF2 in neurotoxicity-induced apoptosis.";
RL   Neuron 38:33-46(2003).
RN   [17]
RP   INTERACTION WITH SLC2A4RG.
RX   PubMed=14630949; DOI=10.1073/pnas.2432756100;
RA   Knight J.B., Eyster C.A., Griesel B.A., Olson A.L.;
RT   "Regulation of the human GLUT4 gene promoter: interaction between a
RT   transcriptional activator and myocyte enhancer factor 2A.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:14725-14730(2003).
RN   [18]
RP   FUNCTION OF BETA DOMAIN.
RX   PubMed=15834131; DOI=10.1074/jbc.m502491200;
RA   Zhu B., Ramachandran B., Gulick T.;
RT   "Alternative pre-mRNA splicing governs expression of a conserved acidic
RT   transactivation domain in myocyte enhancer factor 2 factors of striated
RT   muscle and brain.";
RL   J. Biol. Chem. 280:28749-28760(2005).
RN   [19]
RP   PROTEOLYTIC PROCESSING, AND PHOSPHORYLATION.
RX   PubMed=15888658; DOI=10.1523/jneurosci.1331-05.2005;
RA   Tang X., Wang X., Gong X., Tong M., Park D., Xia Z., Mao Z.;
RT   "Cyclin-dependent kinase 5 mediates neurotoxin-induced degradation of the
RT   transcription factor myocyte enhancer factor 2.";
RL   J. Neurosci. 25:4823-4834(2005).
RN   [20]
RP   SUMOYLATION AT LYS-403, INTERACTION WITH PIAS1, FUNCTION, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF LYS-403.
RX   PubMed=16563226; DOI=10.1111/j.1582-4934.2006.tb00295.x;
RA   Riquelme C., Barthel K.K., Liu X.;
RT   "SUMO-1 modification of MEF2A regulates its transcriptional activity.";
RL   J. Cell. Mol. Med. 10:132-144(2006).
RN   [21]
RP   SUMOYLATION AT LYS-403, PHOSPHORYLATION AT SER-408, FUNCTION, AND
RP   MUTAGENESIS OF LYS-403 AND SER-408.
RX   PubMed=16371476; DOI=10.1073/pnas.0503698102;
RA   Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,
RA   Nakai A., Sistonen L.;
RT   "PDSM, a motif for phosphorylation-dependent SUMO modification.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006).
RN   [22]
RP   PHOSPHORYLATION AT SER-408, AND FUNCTION.
RX   PubMed=16484498; DOI=10.1126/science.1122513;
RA   Shalizi A., Gaudilliere B., Yuan Z., Stegmueller J., Shirogane T., Ge Q.,
RA   Tan Y., Schulman B., Harper J.W., Bonni A.;
RT   "A calcium-regulated MEF2 sumoylation switch controls postsynaptic
RT   differentiation.";
RL   Science 311:1012-1017(2006).
RN   [23]
RP   PHOSPHORYLATION AT THR-312 BY NLK.
RX   PubMed=17785444; DOI=10.1128/mcb.01481-07;
RA   Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T.,
RA   Shibuya H.;
RT   "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates anterior
RT   formation in Xenopus development.";
RL   Mol. Cell. Biol. 27:7623-7630(2007).
RN   [24]
RP   ACETYLATION, AND INVOLVEMENT IN CARDIAC HYPERTROPHY.
RX   PubMed=18697823; DOI=10.1161/circulationaha.107.760488;
RA   Wei J.Q., Shehadeh L.A., Mitrani J.M., Pessanha M., Slepak T.I.,
RA   Webster K.A., Bishopric N.H.;
RT   "Quantitative control of adaptive cardiac hypertrophy by acetyltransferase
RT   p300.";
RL   Circulation 118:934-946(2008).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-235 AND SER-255,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 (ISOFORMS 6; MEFA AND
RP   RSRFC9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORMS 7 AND
RP   8), AND 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   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP   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   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [28]
RP   FUNCTION, AND CHROMATIN BINDING.
RX   PubMed=21468593; DOI=10.3892/mmr.2011.465;
RA   Liu X., Jin E.Z., Zhi J.X., Li X.Q.;
RT   "Identification of HZF1 as a novel target gene of the MEF2 transcription
RT   factor.";
RL   Mol. Med. Report. 4:465-469(2011).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-255, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [30]
RP   VARIANTS SER-263; LEU-279 AND ASP-283, AND CHARACTERIZATION OF VARIANTS
RP   SER-263; LEU-279 AND ASP-283.
RX   PubMed=15496429; DOI=10.1093/hmg/ddh329;
RA   Bhagavatula M.R.K., Fan C., Shen G.-Q., Cassano J., Plow E.F., Topol E.J.,
RA   Wang Q.;
RT   "Transcription factor MEF2A mutations in patients with coronary artery
RT   disease.";
RL   Hum. Mol. Genet. 13:3181-3188(2004).
RN   [31]
RP   VARIANT LEU-279, AND ASSOCIATION WITH SUSCEPTIBILITY TO MYOCARDIAL
RP   INFARCTION.
RX   PubMed=15958500; DOI=10.1136/jmg.2005.035071;
RA   Gonzalez P., Garcia-Castro M., Reguero J.R., Batalla A., Ordonez A.G.,
RA   Palop R.L., Lozano I., Montes M., Alvarez V., Coto E.;
RT   "The Pro279Leu variant in the transcription factor MEF2A is associated with
RT   myocardial infarction.";
RL   J. Med. Genet. 43:167-169(2006).
RN   [32]
RP   VARIANT LEU-279, AND LACK OF ASSOCIATION WITH MYOCARDIAL INFARCTION.
RX   PubMed=18086930; DOI=10.1161/circulationaha.107.728485;
RA   Lieb W., Mayer B., Koenig I.R., Borwitzky I., Goetz A., Kain S.,
RA   Hengstenberg C., Linsel-Nitschke P., Fischer M., Doering A., Wichmann H.E.,
RA   Meitinger T., Kreutz R., Ziegler A., Schunkert H., Erdmann J.;
RT   "Lack of association between the MEF2A gene and myocardial infarction.";
RL   Circulation 117:185-191(2008).
RN   [33]
RP   STRUCTURE BY NMR OF 2-86 IN COMPLEX WITH DNA.
RX   PubMed=10835359; DOI=10.1093/emboj/19.11.2615;
RA   Huang K., Louis J.M., Donaldson L., Lim F.L., Sharrocks A.D., Clore G.M.;
RT   "Solution structure of the MEF2A-DNA complex: structural basis for the
RT   modulation of DNA bending and specificity by MADS-box transcription
RT   factors.";
RL   EMBO J. 19:2615-2628(2000).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-78 IN COMPLEX WITH DNA, AND
RP   DIMERIZATION.
RX   PubMed=10715212; DOI=10.1006/jmbi.2000.3568;
RA   Santelli E., Richmond T.J.;
RT   "Crystal structure of MEF2A core bound to DNA at 1.5 A resolution.";
RL   J. Mol. Biol. 297:437-449(2000).
CC   -!- FUNCTION: Transcriptional activator which binds specifically to the
CC       MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific
CC       genes. Also involved in the activation of numerous growth factor- and
CC       stress-induced genes. Mediates cellular functions not only in skeletal
CC       and cardiac muscle development, but also in neuronal differentiation
CC       and survival. Plays diverse roles in the control of cell growth,
CC       survival and apoptosis via p38 MAPK signaling in muscle-specific and/or
CC       growth factor-related transcription. In cerebellar granule neurons,
CC       phosphorylated and sumoylated MEF2A represses transcription of NUR77
CC       promoting synaptic differentiation. Associates with chromatin to the
CC       ZNF16 promoter. {ECO:0000269|PubMed:11904443,
CC       ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15834131,
CC       ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:16484498,
CC       ECO:0000269|PubMed:16563226, ECO:0000269|PubMed:21468593,
CC       ECO:0000269|PubMed:9858528}.
CC   -!- SUBUNIT: Binds DNA as a homo- or heterodimer. Dimerizes with MEF2D.
CC       Interacts with HDAC7 (By similarity). Interacts with PIAS1; the
CC       interaction enhances sumoylation. Interacts with HDAC4, HDAC9 and
CC       SLC2A4RG. Interacts (via the N-terminal) with MAPK7; the interaction
CC       results in the phosphorylation and transcriptional activity of MEF2A.
CC       {ECO:0000250, ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10487761,
CC       ECO:0000269|PubMed:10715212, ECO:0000269|PubMed:10835359,
CC       ECO:0000269|PubMed:14630949, ECO:0000269|PubMed:16563226,
CC       ECO:0000269|PubMed:9753748}.
CC   -!- INTERACTION:
CC       Q02078; Q99697-3: PITX2; NbExp=2; IntAct=EBI-2656305, EBI-1175243;
CC       Q02078; P10085: Myod1; Xeno; NbExp=2; IntAct=EBI-2656305, EBI-4405734;
CC       Q02078; P70257-2: Nfix; Xeno; NbExp=2; IntAct=EBI-2656305, EBI-2639084;
CC       Q02078-1; P63165: SUMO1; NbExp=3; IntAct=EBI-15799584, EBI-80140;
CC       Q02078-2; P50221: MEOX1; NbExp=3; IntAct=EBI-16431401, EBI-2864512;
CC       Q02078-5; P56524-2: HDAC4; NbExp=3; IntAct=EBI-12232917, EBI-11953488;
CC       Q02078-5; O75031: HSF2BP; NbExp=3; IntAct=EBI-12232917, EBI-7116203;
CC       Q02078-6; Q13164: MAPK7; NbExp=3; IntAct=EBI-16437973, EBI-1213983;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251,
CC       ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:16563226}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=MEF2;
CC         IsoId=Q02078-1; Sequence=Displayed;
CC       Name=MEFA;
CC         IsoId=Q02078-2; Sequence=VSP_006240;
CC       Name=RSRFC4;
CC         IsoId=Q02078-3; Sequence=VSP_006241, VSP_006242;
CC       Name=RSRFC9;
CC         IsoId=Q02078-4; Sequence=VSP_006240, VSP_006241, VSP_006242;
CC       Name=5;
CC         IsoId=Q02078-5; Sequence=VSP_006241;
CC       Name=6;
CC         IsoId=Q02078-6; Sequence=VSP_006240, VSP_006241;
CC       Name=7;
CC         IsoId=Q02078-7; Sequence=VSP_043338, VSP_006240;
CC       Name=8;
CC         IsoId=Q02078-8; Sequence=VSP_046018, VSP_046019, VSP_006241;
CC   -!- TISSUE SPECIFICITY: Isoform MEF2 and isoform MEFA are expressed only in
CC       skeletal and cardiac muscle and in the brain. Isoform RSRFC4 and
CC       isoform RSRFC9 are expressed in all tissues examined.
CC       {ECO:0000269|PubMed:1516833, ECO:0000269|PubMed:1748287}.
CC   -!- PTM: Constitutive phosphorylation on Ser-408 promotes Lys-403
CC       sumoylation thus preventing acetylation at this site. Dephosphorylation
CC       on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from
CC       sumoylation to acetylation on residue Lys-403 leading to inhibition of
CC       dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319
CC       are the main sites involved in p38 MAPK signaling and activate
CC       transcription. Phosphorylated on these sites by MAPK14/p38alpha and
CC       MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma.
CC       Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits
CC       MEF2A transcriptional activation leading to apoptosis of cortical
CC       neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced
CC       by EGF. {ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10849446,
CC       ECO:0000269|PubMed:12586839, ECO:0000269|PubMed:12691662,
CC       ECO:0000269|PubMed:15888658, ECO:0000269|PubMed:16371476,
CC       ECO:0000269|PubMed:16484498, ECO:0000269|PubMed:16563226,
CC       ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:9753748,
CC       ECO:0000269|PubMed:9858528}.
CC   -!- PTM: Sumoylation on Lys-403 is enhanced by PIAS1 and represses
CC       transcriptional activity. Phosphorylation on Ser-408 is required for
CC       sumoylation. Has no effect on nuclear location nor on DNA binding.
CC       Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3.
CC       PIASx facilitates sumoylation in postsynaptic dendrites in the
CC       cerebellar cortex and promotes their morphogenesis (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Acetylation on Lys-403 activates transcriptional activity.
CC       Acetylated by p300 on several sites in diffentiating myocytes.
CC       Acetylation on Lys-4 increases DNA binding and transactivation (By
CC       similarity). Hyperacetylation by p300 leads to enhanced cardiac myocyte
CC       growth and heart failure. {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved in cerebellar granule neurons on several
CC       sites by caspase 3 and caspase 7 following neurotoxicity.
CC       Preferentially cleaves the CDK5-mediated hyperphosphorylated form which
CC       leads to neuron apoptosis and transcriptional inactivation.
CC       {ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:15888658}.
CC   -!- DISEASE: Coronary artery disease, autosomal dominant, 1 (ADCAD1)
CC       [MIM:608320]: A common heart disease characterized by reduced or absent
CC       blood flow in one or more of the arteries that encircle and supply the
CC       heart. Its most important complication is acute myocardial infarction.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH53871.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD92222.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y16312; CAA76175.1; -; mRNA.
DR   EMBL; X63381; CAA44979.1; -; mRNA.
DR   EMBL; X68503; CAA48516.1; -; mRNA.
DR   EMBL; X68505; CAA48517.1; -; mRNA.
DR   EMBL; U49020; AAB17195.1; -; Genomic_DNA.
DR   EMBL; U44889; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49012; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49013; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49015; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49016; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49017; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49018; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49019; AAB17195.1; JOINED; Genomic_DNA.
DR   EMBL; U49020; AAB17196.1; -; Genomic_DNA.
DR   EMBL; U44889; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; U49012; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; U49013; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; U49015; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; U49016; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; U49017; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; U49018; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; U49019; AAB17196.1; JOINED; Genomic_DNA.
DR   EMBL; AK294207; BAG57518.1; -; mRNA.
DR   EMBL; AB208985; BAD92222.1; ALT_INIT; mRNA.
DR   EMBL; AC015660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013437; AAH13437.1; -; mRNA.
DR   EMBL; BC053871; AAH53871.1; ALT_INIT; mRNA.
DR   CCDS; CCDS45362.1; -. [Q02078-5]
DR   CCDS; CCDS45363.1; -. [Q02078-7]
DR   CCDS; CCDS53978.1; -. [Q02078-6]
DR   CCDS; CCDS58401.1; -. [Q02078-8]
DR   CCDS; CCDS81920.1; -. [Q02078-2]
DR   PIR; C39481; C39481.
DR   PIR; S25831; S25831.
DR   RefSeq; NP_001124399.1; NM_001130927.2. [Q02078-7]
DR   RefSeq; NP_001124400.1; NM_001130928.2. [Q02078-8]
DR   RefSeq; NP_001165365.1; NM_001171894.2. [Q02078-6]
DR   RefSeq; NP_001306135.1; NM_001319206.1. [Q02078-2]
DR   RefSeq; NP_005578.2; NM_005587.3. [Q02078-5]
DR   RefSeq; XP_011519883.1; XM_011521581.2.
DR   RefSeq; XP_011519884.1; XM_011521582.2. [Q02078-1]
DR   RefSeq; XP_011519888.1; XM_011521586.2.
DR   RefSeq; XP_016877679.1; XM_017022190.1.
DR   RefSeq; XP_016877680.1; XM_017022191.1. [Q02078-1]
DR   RefSeq; XP_016877682.1; XM_017022193.1.
DR   RefSeq; XP_016877683.1; XM_017022194.1.
DR   PDB; 1C7U; NMR; -; A/B=2-86.
DR   PDB; 1EGW; X-ray; 1.50 A; A/B/C/D=2-78.
DR   PDB; 1LEW; X-ray; 2.30 A; B=269-280.
DR   PDB; 3KOV; X-ray; 2.90 A; A/B/I/J=2-91.
DR   PDB; 3MU6; X-ray; 2.43 A; A/B/C/D=2-70.
DR   PDB; 3P57; X-ray; 2.19 A; A/B/C/D/I/J=2-91.
DR   PDB; 6BYY; X-ray; 2.30 A; A/B/C/D=1-64, A/B/C/D=92-95.
DR   PDB; 6BZ1; X-ray; 2.97 A; A/B/C/D=1-64, A/B/C/D=92-95.
DR   PDBsum; 1C7U; -.
DR   PDBsum; 1EGW; -.
DR   PDBsum; 1LEW; -.
DR   PDBsum; 3KOV; -.
DR   PDBsum; 3MU6; -.
DR   PDBsum; 3P57; -.
DR   PDBsum; 6BYY; -.
DR   PDBsum; 6BZ1; -.
DR   SMR; Q02078; -.
DR   BioGRID; 110369; 59.
DR   CORUM; Q02078; -.
DR   DIP; DIP-40711N; -.
DR   IntAct; Q02078; 43.
DR   MINT; Q02078; -.
DR   STRING; 9606.ENSP00000346389; -.
DR   GlyGen; Q02078; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q02078; -.
DR   PhosphoSitePlus; Q02078; -.
DR   BioMuta; MEF2A; -.
DR   EPD; Q02078; -.
DR   jPOST; Q02078; -.
DR   MassIVE; Q02078; -.
DR   MaxQB; Q02078; -.
DR   PaxDb; Q02078; -.
DR   PeptideAtlas; Q02078; -.
DR   PRIDE; Q02078; -.
DR   ProteomicsDB; 28155; -.
DR   ProteomicsDB; 58035; -. [Q02078-1]
DR   ProteomicsDB; 58036; -. [Q02078-2]
DR   ProteomicsDB; 58037; -. [Q02078-3]
DR   ProteomicsDB; 58038; -. [Q02078-4]
DR   ProteomicsDB; 58039; -. [Q02078-5]
DR   ProteomicsDB; 58040; -. [Q02078-6]
DR   ProteomicsDB; 58041; -. [Q02078-7]
DR   Antibodypedia; 3854; 1065 antibodies.
DR   DNASU; 4205; -.
DR   Ensembl; ENST00000338042; ENSP00000337202; ENSG00000068305. [Q02078-6]
DR   Ensembl; ENST00000354410; ENSP00000346389; ENSG00000068305. [Q02078-5]
DR   Ensembl; ENST00000449277; ENSP00000399460; ENSG00000068305. [Q02078-8]
DR   Ensembl; ENST00000557785; ENSP00000453441; ENSG00000068305. [Q02078-6]
DR   Ensembl; ENST00000557942; ENSP00000453095; ENSG00000068305. [Q02078-2]
DR   Ensembl; ENST00000558812; ENSP00000454120; ENSG00000068305. [Q02078-7]
DR   GeneID; 4205; -.
DR   KEGG; hsa:4205; -.
DR   UCSC; uc002bve.4; human. [Q02078-1]
DR   CTD; 4205; -.
DR   DisGeNET; 4205; -.
DR   GeneCards; MEF2A; -.
DR   HGNC; HGNC:6993; MEF2A.
DR   HPA; ENSG00000068305; Low tissue specificity.
DR   MalaCards; MEF2A; -.
DR   MIM; 600660; gene.
DR   MIM; 608320; phenotype.
DR   neXtProt; NX_Q02078; -.
DR   OpenTargets; ENSG00000068305; -.
DR   Orphanet; 411969; NON RARE IN EUROPE: Metabolic syndrome.
DR   PharmGKB; PA30731; -.
DR   VEuPathDB; HostDB:ENSG00000068305; -.
DR   eggNOG; KOG0014; Eukaryota.
DR   GeneTree; ENSGT00940000156205; -.
DR   HOGENOM; CLU_022902_4_0_1; -.
DR   InParanoid; Q02078; -.
DR   OMA; MNTQRIS; -.
DR   OrthoDB; 729387at2759; -.
DR   PhylomeDB; Q02078; -.
DR   TreeFam; TF314067; -.
DR   PathwayCommons; Q02078; -.
DR   Reactome; R-HSA-198753; ERK/MAPK targets.
DR   Reactome; R-HSA-525793; Myogenesis.
DR   SignaLink; Q02078; -.
DR   SIGNOR; Q02078; -.
DR   BioGRID-ORCS; 4205; 4 hits in 1043 CRISPR screens.
DR   ChiTaRS; MEF2A; human.
DR   EvolutionaryTrace; Q02078; -.
DR   GeneWiki; Myocyte-specific_enhancer_factor_2A; -.
DR   GenomeRNAi; 4205; -.
DR   Pharos; Q02078; Tbio.
DR   PRO; PR:Q02078; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q02078; protein.
DR   Bgee; ENSG00000068305; Expressed in heart and 242 other tissues.
DR   ExpressionAtlas; Q02078; baseline and differential.
DR   Genevisible; Q02078; HS.
DR   GO; GO:0000785; C:chromatin; ISS:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0070375; P:ERK5 cascade; IMP:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEP:UniProtKB.
DR   GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
DR   GO; GO:0048311; P:mitochondrion distribution; ISS:UniProtKB.
DR   GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IDA:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0055005; P:ventricular cardiac myofibril assembly; ISS:UniProtKB.
DR   CDD; cd00265; MADS_MEF2_like; 1.
DR   DisProt; DP01925; -.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   IDEAL; IID00240; -.
DR   InterPro; IPR022102; HJURP_C.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF12347; HJURP_C; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis;
KW   Developmental protein; Differentiation; Disease variant; DNA-binding;
KW   Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..507
FT                   /note="Myocyte-specific enhancer factor 2A"
FT                   /id="PRO_0000199428"
FT   DOMAIN          3..57
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   DNA_BIND        58..86
FT                   /note="Mef2-type"
FT                   /evidence="ECO:0000255"
FT   REGION          173..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..283
FT                   /note="Required for interaction with MAPKs"
FT   REGION          289..296
FT                   /note="Beta domain"
FT   REGION          397..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..448
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            176..177
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   SITE            213..214
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   SITE            466..467
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         59
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         249
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         255
FT                   /note="Phosphoserine; by MAPK14"
FT                   /evidence="ECO:0000269|PubMed:12586839,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   MOD_RES         312
FT                   /note="Phosphothreonine; by MAPK7 and MAPK14"
FT                   /evidence="ECO:0000269|PubMed:10330143,
FT                   ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:12586839,
FT                   ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:9858528"
FT   MOD_RES         312
FT                   /note="Phosphothreonine; by NLK"
FT                   /evidence="ECO:0000269|PubMed:10330143,
FT                   ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:12586839,
FT                   ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:9858528"
FT   MOD_RES         319
FT                   /note="Phosphothreonine; by MAPK7 and MAPK14"
FT                   /evidence="ECO:0000269|PubMed:10330143,
FT                   ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:12586839,
FT                   ECO:0000269|PubMed:9858528"
FT   MOD_RES         355
FT                   /note="Phosphoserine; by MAPK7"
FT                   /evidence="ECO:0000269|PubMed:10849446"
FT   MOD_RES         403
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q2MJT0"
FT   MOD_RES         408
FT                   /note="Phosphoserine; by CDK5"
FT                   /evidence="ECO:0000269|PubMed:12586839,
FT                   ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:16371476,
FT                   ECO:0000269|PubMed:16484498"
FT   MOD_RES         415
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60929"
FT   MOD_RES         453
FT                   /note="Phosphoserine; by MAPK"
FT                   /evidence="ECO:0000269|PubMed:9858528"
FT   CROSSLNK        403
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT   VAR_SEQ         19..86
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043338"
FT   VAR_SEQ         19..62
FT                   /note="VTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDM -> TLRK
FT                   KGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046018"
FT   VAR_SEQ         63..132
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046019"
FT   VAR_SEQ         87..132
FT                   /note="ALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIA -> TL
FT                   RKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP (in isoform
FT                   MEFA, isoform RSRFC9, isoform 6 and isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:1516833, ECO:0000303|PubMed:1748287,
FT                   ECO:0000303|Ref.2, ECO:0000303|Ref.6"
FT                   /id="VSP_006240"
FT   VAR_SEQ         289..296
FT                   /note="Missing (in isoform RSRFC4, isoform RSRFC9, isoform
FT                   5, isoform 6 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:1516833,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1748287,
FT                   ECO:0000303|Ref.2, ECO:0000303|Ref.6"
FT                   /id="VSP_006241"
FT   VAR_SEQ         420..421
FT                   /note="Missing (in isoform RSRFC4 and isoform RSRFC9)"
FT                   /evidence="ECO:0000303|PubMed:1516833,
FT                   ECO:0000303|PubMed:1748287, ECO:0000303|Ref.2"
FT                   /id="VSP_006242"
FT   VARIANT         263
FT                   /note="N -> S (in dbSNP:rs121918530)"
FT                   /evidence="ECO:0000269|PubMed:15496429"
FT                   /id="VAR_038407"
FT   VARIANT         279
FT                   /note="P -> L (in dbSNP:rs121918529)"
FT                   /evidence="ECO:0000269|PubMed:15496429,
FT                   ECO:0000269|PubMed:15958500, ECO:0000269|PubMed:18086930"
FT                   /id="VAR_038408"
FT   VARIANT         283
FT                   /note="G -> D"
FT                   /evidence="ECO:0000269|PubMed:15496429"
FT                   /id="VAR_038409"
FT   VARIANT         440..446
FT                   /note="Missing (loss of nuclear localization; 66% decrease
FT                   in transcription activation; loss of synergistic activation
FT                   by MEF2A and GATA1 through a dominant-negative mechanism)"
FT                   /id="VAR_017743"
FT   MUTAGEN         176
FT                   /note="D->A: Abolishes cleavage at sites 1 and 2 by caspase
FT                   3. Increased cleavage at site 3 by caspase 3."
FT                   /evidence="ECO:0000269|PubMed:11904443"
FT   MUTAGEN         213
FT                   /note="D->A: Abolishes cleavage at sites 2 and 3 by caspase
FT                   7."
FT                   /evidence="ECO:0000269|PubMed:11904443"
FT   MUTAGEN         255
FT                   /note="S->A: Slightly increased MEF2A protein level."
FT                   /evidence="ECO:0000269|PubMed:12586839"
FT   MUTAGEN         255
FT                   /note="S->D: Decreased MEF2A protein level."
FT                   /evidence="ECO:0000269|PubMed:12586839"
FT   MUTAGEN         269
FT                   /note="R->A: Reduced p38 alpha- and beta2-mediated
FT                   transcriptional activity; when associated with A-270."
FT                   /evidence="ECO:0000269|PubMed:10330143"
FT   MUTAGEN         270
FT                   /note="K->A: Reduced p38 alpha- and beta2-mediated
FT                   transcriptional activity; when associated with A-269."
FT                   /evidence="ECO:0000269|PubMed:10330143"
FT   MUTAGEN         273
FT                   /note="L->A: Reduced p38 alpha- and beta2-mediated
FT                   transcriptional activity; when associated with A-275."
FT                   /evidence="ECO:0000269|PubMed:10330143"
FT   MUTAGEN         275
FT                   /note="V->A: Reduced p38 alpha- and beta2-mediated
FT                   transcriptional activity; when associated with A-273."
FT                   /evidence="ECO:0000269|PubMed:10330143"
FT   MUTAGEN         277
FT                   /note="I->A: Reduced p38 alpha- and beta2-mediated
FT                   transcriptional activity; when associated with A-278."
FT                   /evidence="ECO:0000269|PubMed:10330143"
FT   MUTAGEN         278
FT                   /note="P->A: Reduced p38 alpha- and beta2-mediated
FT                   transcriptional activity; when associated with A-277."
FT                   /evidence="ECO:0000269|PubMed:10330143"
FT   MUTAGEN         312
FT                   /note="T->A: Greatly reduced p38-mediated phosphorylation.
FT                   Abolishes p38-mediated transcriptional activation; when
FT                   associated with A-319."
FT                   /evidence="ECO:0000269|PubMed:10849446,
FT                   ECO:0000269|PubMed:9858528"
FT   MUTAGEN         319
FT                   /note="T->A: Greatly reduced p38-mediated phosphorylation.
FT                   Abolishes P38-mediated transcriptional activation; when
FT                   associated with A-312."
FT                   /evidence="ECO:0000269|PubMed:10849446,
FT                   ECO:0000269|PubMed:9858528"
FT   MUTAGEN         355
FT                   /note="S->A: No effect on p38-mediated transcriptional
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:10849446,
FT                   ECO:0000269|PubMed:9858528"
FT   MUTAGEN         387
FT                   /note="S->A: No effect on p38-mediated phosphorylation."
FT   MUTAGEN         403
FT                   /note="K->R: Abolishes sumoylation. No change in
FT                   subcellular location nor in DNA binding. Loss of
FT                   transcriptional repression."
FT                   /evidence="ECO:0000269|PubMed:16371476,
FT                   ECO:0000269|PubMed:16563226"
FT   MUTAGEN         408
FT                   /note="S->A: Loss of sumoylation."
FT                   /evidence="ECO:0000269|PubMed:12691662,
FT                   ECO:0000269|PubMed:16371476"
FT   MUTAGEN         408
FT                   /note="S->D: Rescues sumoylation."
FT                   /evidence="ECO:0000269|PubMed:12691662,
FT                   ECO:0000269|PubMed:16371476"
FT   MUTAGEN         453
FT                   /note="S->A: No effect on p38-mediated phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:9858528"
FT   MUTAGEN         479
FT                   /note="S->A: No effect on p38-mediated phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:9858528"
FT   CONFLICT        430
FT                   /note="Missing (in Ref. 4; AAB17195/AAB17196)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..38
FT                   /evidence="ECO:0007829|PDB:1EGW"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:1EGW"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:1C7U"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:1EGW"
FT   HELIX           62..71
FT                   /evidence="ECO:0007829|PDB:1EGW"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:3KOV"
FT   HELIX           81..90
FT                   /evidence="ECO:0007829|PDB:3P57"
FT   MOD_RES         Q02078-2:98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         Q02078-4:98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         Q02078-6:98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         Q02078-7:30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         Q02078-8:30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
SQ   SEQUENCE   507 AA;  54811 MW;  362BA4FBCC792CE2 CRC64;
     MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST
     DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD PDTSYVLTPH TEEKYKKINE
     EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS PNALSYTNPG SSLVSPSLAA SSTLTDSSML
     SPPQTTLHRN VSPGAPQRPP STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG
     ATGANSLGKV MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLSE EEELELNTQR
     ISSSQATQPL ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL QGFNSPGMLS
     LGQVSAWQQH HLGQAALSSL VAGGQLSQGS NLSINTNQNI SIKSEPISPP RDRMTPSGFQ
     QQQQQQQQQQ PPPPPQPQPQ PPQPQPRQEM GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP
     IVLGRPPNTE DRESPSVKRM RMDAWVT
//
DBGET integrated database retrieval system