ID MEF2C_HUMAN Reviewed; 473 AA. AC Q06413; C9JMZ0; D7F7N5; F8W7V7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=Myocyte-specific enhancer factor 2C {ECO:0000305}; DE AltName: Full=Myocyte enhancer factor 2C {ECO:0000312|HGNC:HGNC:6996}; GN Name=MEF2C {ECO:0000312|HGNC:HGNC:6996}; 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 1; 2 AND 3). RC TISSUE=Fetal brain, and Muscle; RX PubMed=7679508; DOI=10.1073/pnas.90.4.1546; RA Leifer D., Krainc D., Yu Y.-T., McDermott J., Breitbart R.E., Heng J., RA Neve R.L., Kosofsky B., Nadal-Ginard B., Lipton S.A.; RT "MEF2C, a MADS/MEF2-family transcription factor expressed in a laminar RT distribution in cerebral cortex."; RL Proc. Natl. Acad. Sci. U.S.A. 90:1546-1550(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Skeletal muscle; RX PubMed=8455629; DOI=10.1128/mcb.13.4.2564-2577.1993; RA McDermott J.C., Cardoso M.C., Yu Y.-T., Andres V., Leifer D., Krainc D., RA Lipton S.A., Nadal-Ginard B.; RT "hMEF2C gene encodes skeletal muscle- and brain-specific transcription RT factors."; RL Mol. Cell. Biol. 13:2564-2577(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Skeletal muscle; RA Infantino V., Convertini P., Palmieri F., Iacobazzi V.; RT "Identification and characterization of a new splice variant of human RT MEF2C."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6). RC TISSUE=Skeletal muscle; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP PHOSPHORYLATION AT THR-293; THR-300 AND SER-419, FUNCTION, AND MUTAGENESIS RP OF THR-293; THR-300 AND SER-419. RX PubMed=9384584; DOI=10.1093/emboj/16.23.7054; RA Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D.; RT "BMK1/ERK5 regulates serum-induced early gene expression through RT transcription factor MEF2C."; RL EMBO J. 16:7054-7066(1997). RN [7] RP PHOSPHORYLATION AT THR-293; THR-300 AND SER-419, FUNCTION, AND MUTAGENESIS RP OF THR-293; THR-300 AND SER-419. RX PubMed=9069290; DOI=10.1038/386296a0; RA Han J., Jiang Y., Li Z., Kravchenko V.V., Ulevitch R.J.; RT "Activation of the transcription factor MEF2C by the MAP kinase p38 in RT inflammation."; RL Nature 386:296-299(1997). RN [8] RP TISSUE SPECIFICITY. RX PubMed=9798649; DOI=10.1016/s0161-5890(98)00058-3; RA Swanson B.J., Jaeck H.-M., Lyons G.E.; RT "Characterization of myocyte enhancer factor 2 (MEF2) expression in B and T RT cells: MEF2C is a B cell-restricted transcription factor in lymphocytes."; RL Mol. Immunol. 35:445-458(1998). RN [9] RP INTERACTION WITH HDAC4. RX PubMed=10523670; DOI=10.1128/mcb.19.11.7816; RA Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., RA Th'ng J., Han J., Yang X.-J.; RT "HDAC4, a human histone deacetylase related to yeast HDA1, is a RT transcriptional corepressor."; RL Mol. Cell. Biol. 19:7816-7827(1999). RN [10] RP PHOSPHORYLATION BY MAPK7. 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 [11] RP INTERACTION WITH HDAC9. RX PubMed=11535832; DOI=10.1073/pnas.191375098; RA Zhou X., Marks P.A., Rifkind R.A., Richon V.M.; RT "Cloning and characterization of a histone deacetylase, HDAC9."; RL Proc. Natl. Acad. Sci. U.S.A. 98:10572-10577(2001). RN [12] RP PROTEOLYTIC PROCESSING AT ASP-432, FUNCTION, AND MUTAGENESIS OF ASP-432. 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 [13] RP PHOSPHORYLATION AT SER-396, IDENTIFICATION BY MASS SPECTROMETRY, RP MUTAGENESIS OF SER-396, AND FUNCTION OF ISOFORMS. RX PubMed=15340086; DOI=10.1128/mcb.24.18.8264-8275.2004; RA Zhu B., Gulick T.; RT "Phosphorylation and alternative pre-mRNA splicing converge to regulate RT myocyte enhancer factor 2C activity."; RL Mol. Cell. Biol. 24:8264-8275(2004). RN [14] RP INTERACTION WITH HABP4. RX PubMed=15862299; DOI=10.1016/j.febslet.2005.03.078; RA Kobarg C.B., Kobarg J., Crosara-Alberto D.P., Theizen T.H., Franchini K.G.; RT "MEF2C DNA-binding activity is inhibited through its interaction with the RT regulatory protein Ki-1/57."; RL FEBS Lett. 579:2615-2622(2005). RN [15] RP SUMOYLATION. RX PubMed=15561718; DOI=10.1074/jbc.m411718200; RA Gocke C.B., Yu H., Kang J.; RT "Systematic identification and analysis of mammalian small ubiquitin-like RT modifier substrates."; RL J. Biol. Chem. 280:5004-5012(2005). RN [16] RP FUNCTION OF BETA DOMAIN, AND MUTAGENESIS OF SER-271; GLU-272; ASP-273; RP ASP-275; SER-387 AND SER-396. 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 [17] RP SUMOYLATION AT LYS-391. RX PubMed=15743823; DOI=10.1128/mcb.25.6.2273-2287.2005; RA Gregoire S., Yang X.-J.; RT "Association with class IIa histone deacetylases upregulates the RT sumoylation of MEF2 transcription factors."; RL Mol. Cell. Biol. 25:2273-2287(2005). RN [18] RP ACETYLATION AT LYS-116; LYS-119; LYS-234; LYS-239; LYS-252 AND LYS-264, RP INTERACTION WITH EP300, FUNCTION, DNA-BINDING, AND MUTAGENESIS OF LYS-116; RP LYS-119; LYS-234; LYS-239; LYS-252 AND LYS-264. RX PubMed=15831463; DOI=10.1128/mcb.25.9.3575-3582.2005; RA Ma K., Chan J.K., Zhu G., Wu Z.; RT "Myocyte enhancer factor 2 acetylation by p300 enhances its DNA binding RT activity, transcriptional activity, and myogenic differentiation."; RL Mol. Cell. Biol. 25:3575-3582(2005). RN [19] RP SUMOYLATION AT LYS-391, AND MUTAGENESIS OF LYS-391 AND SER-396. RX PubMed=16478538; DOI=10.1186/1471-2091-7-5; RA Kang J., Gocke C.B., Yu H.; RT "Phosphorylation-facilitated sumoylation of MEF2C negatively regulates its RT transcriptional activity."; RL BMC Biochem. 7:5-5(2006). RN [20] RP INVOLVEMENT IN NEDHSIL. RX PubMed=19592390; DOI=10.1136/jmg.2009.069732; RA Le Meur N., Holder-Espinasse M., Jaillard S., Goldenberg A., Joriot S., RA Amati-Bonneau P., Guichet A., Barth M., Charollais A., Journel H., RA Auvin S., Boucher C., Kerckaert J.P., David V., Manouvrier-Hanu S., RA Saugier-Veber P., Frebourg T., Dubourg C., Andrieux J., Bonneau D.; RT "MEF2C haploinsufficiency caused by either microdeletion of the 5q14.3 RT region or mutation is responsible for severe mental retardation with RT stereotypic movements, epilepsy and/or cerebral malformations."; RL J. Med. Genet. 47:22-29(2010). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-228; SER-240 AND RP SER-445, AND 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 [22] RP VARIANT ARG-39. RX PubMed=23708187; DOI=10.1038/ng.2646; RA Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J., Cook J., RA Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S., Wallace G., RA Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S., Mackay M.T., RA Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z., Zelnick N., RA Lerman-Sagie T., Lev D., Moeller R.S., Gill D., Andrade D.M., Freeman J.L., RA Sadleir L.G., Shendure J., Berkovic S.F., Scheffer I.E., Mefford H.C.; RT "Targeted resequencing in epileptic encephalopathies identifies de novo RT mutations in CHD2 and SYNGAP1."; RL Nat. Genet. 45:825-830(2013). RN [23] RP VARIANT ARG-36. RX PubMed=27864847; DOI=10.1002/humu.23149; RG Clinical Study Group; RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D., RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S., RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.; RT "Diagnostic targeted resequencing in 349 patients with drug-resistant RT pediatric epilepsies identifies causative mutations in 30 different RT genes."; RL Hum. Mutat. 38:216-225(2017). CC -!- FUNCTION: Transcription activator which binds specifically to the MEF2 CC element present in the regulatory regions of many muscle-specific CC genes. Controls cardiac morphogenesis and myogenesis, and is also CC involved in vascular development. Enhances transcriptional activation CC mediated by SOX18. Plays an essential role in hippocampal-dependent CC learning and memory by suppressing the number of excitatory synapses CC and thus regulating basal and evoked synaptic transmission. Crucial for CC normal neuronal development, distribution, and electrical activity in CC the neocortex. Necessary for proper development of megakaryocytes and CC platelets and for bone marrow B-lymphopoiesis. Required for B-cell CC survival and proliferation in response to BCR stimulation, efficient CC IgG1 antibody responses to T-cell-dependent antigens and for normal CC induction of germinal center B-cells. May also be involved in CC neurogenesis and in the development of cortical architecture (By CC similarity). Isoforms that lack the repressor domain are more active CC than isoform 1. {ECO:0000250|UniProtKB:Q8CFN5, CC ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:15340086, CC ECO:0000269|PubMed:15831463, ECO:0000269|PubMed:15834131, CC ECO:0000269|PubMed:9069290, ECO:0000269|PubMed:9384584}. CC -!- SUBUNIT: Forms a complex with class II HDACs in undifferentiating CC cells. On myogenic differentiation, HDACs are released into the CC cytoplasm allowing MEF2s to interact with other proteins for CC activation. Interacts with EP300 in differentiating cells; the CC interaction acetylates MEF2C leading to increased DNA binding and CC activation (By similarity). Interacts with HDAC7 and CARM1 (By CC similarity). Interacts with HDAC4 and HDAC9; the interaction with HDACs CC represses transcriptional activity (PubMed:10523670, PubMed:11535832). CC Interacts with LPIN1. Interacts with MYOCD. Interacts with AKAP13 (By CC similarity). Interacts with FOXK1; the interaction inhibits MEF2C CC transactivation activity (By similarity). Interacts (via N-terminus) CC with HABP4; this interaction decreases DNA-binding activity of MEF2C in CC myocardial cells in response to mechanical stress (PubMed:15862299). CC Interacts with JPH2; interaction specifically takes place with the CC Junctophilin-2 N-terminal fragment cleavage product of JPH2 (By CC similarity). Interacts (via MADS box) with SOX18 (By similarity). CC {ECO:0000250|UniProtKB:Q8CFN5, ECO:0000269|PubMed:10523670, CC ECO:0000269|PubMed:11535832, ECO:0000269|PubMed:15862299}. CC -!- INTERACTION: CC Q06413; P56524-2: HDAC4; NbExp=5; IntAct=EBI-2684075, EBI-11953488; CC Q06413; Q9UQL6: HDAC5; NbExp=3; IntAct=EBI-2684075, EBI-715576; CC Q06413; Q9UKV0: HDAC9; NbExp=3; IntAct=EBI-2684075, EBI-765444; CC Q06413; Q9H1R3: MYLK2; NbExp=2; IntAct=EBI-2684075, EBI-356910; CC Q06413; Q05086: UBE3A; NbExp=3; IntAct=EBI-2684075, EBI-954357; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A096MJY4}. CC Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A0A096MJY4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q06413-1; Sequence=Displayed; CC Name=2; Synonyms=Muscle; CC IsoId=Q06413-2; Sequence=VSP_006248; CC Name=3; Synonyms=hMEF2C-delta32, Brain; CC IsoId=Q06413-3; Sequence=VSP_006249; CC Name=4; CC IsoId=Q06413-4; Sequence=VSP_043339, VSP_006248; CC Name=5; CC IsoId=Q06413-5; Sequence=VSP_045478, VSP_006248; CC Name=6; CC IsoId=Q06413-6; Sequence=VSP_046251, VSP_006248; CC -!- TISSUE SPECIFICITY: Expressed in brain and skeletal muscle. CC {ECO:0000269|PubMed:9798649}. CC -!- DEVELOPMENTAL STAGE: Expression is highest during the early stages of CC postnatal development, at later stages levels greatly decrease. CC -!- DOMAIN: The beta domain, missing in a number of isoforms, is required CC for enhancement of transcriptional activity. {ECO:0000250}. CC -!- PTM: Phosphorylation on Ser-59 enhances DNA binding activity (By CC similarity). Phosphorylation on Ser-396 is required for Lys-391 CC sumoylation and inhibits transcriptional activity. {ECO:0000250, CC ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:15340086, CC ECO:0000269|PubMed:15561718, ECO:0000269|PubMed:15743823, CC ECO:0000269|PubMed:16478538, ECO:0000269|PubMed:9069290, CC ECO:0000269|PubMed:9384584}. CC -!- PTM: Acetylated by p300 on several sites in diffentiating myocytes. CC Acetylation on Lys-4 increases DNA binding and transactivation (By CC similarity). {ECO:0000250}. CC -!- PTM: Sumoylated on Lys-391 with SUMO2 but not by SUMO1 represses CC transcriptional activity. {ECO:0000269|PubMed:15561718, CC ECO:0000269|PubMed:15743823, ECO:0000269|PubMed:16478538}. CC -!- PTM: Proteolytically cleaved in cerebellar granule neurons, probably by CC caspase 7, following neurotoxicity. Preferentially cleaves the CDK5- CC mediated hyperphosphorylated form which leads to neuron apoptosis and CC transcriptional inactivation. {ECO:0000269|PubMed:11904443}. CC -!- DISEASE: Neurodevelopmental disorder with hypotonia, stereotypic hand CC movements, and impaired language (NEDHSIL) [MIM:613443]: An autosomal CC dominant disorder characterized by impaired intellectual development, CC absent speech, hypotonia, poor eye contact and stereotypic movements. CC Dysmorphic features include high broad forehead with variable small CC chin, short nose with anteverted nares, large open mouth, upslanted CC palpebral fissures and prominent eyebrows. Some patients have seizures. CC {ECO:0000269|PubMed:19592390}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L08895; AAA59578.1; -; mRNA. DR EMBL; S57212; AAB25838.1; -; mRNA. DR EMBL; FM163484; CAQ57795.2; -; mRNA. DR EMBL; AL833268; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL833274; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC008525; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008835; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS47244.1; -. [Q06413-6] DR CCDS; CCDS47245.1; -. [Q06413-1] DR CCDS; CCDS54877.1; -. [Q06413-4] DR CCDS; CCDS54878.1; -. [Q06413-5] DR CCDS; CCDS78034.1; -. [Q06413-2] DR CCDS; CCDS87313.1; -. [Q06413-3] DR PIR; A47284; A47284. DR RefSeq; NP_001124477.1; NM_001131005.2. [Q06413-6] DR RefSeq; NP_001180276.1; NM_001193347.1. [Q06413-5] DR RefSeq; NP_001180277.1; NM_001193348.1. [Q06413-4] DR RefSeq; NP_001180278.1; NM_001193349.1. DR RefSeq; NP_001180279.1; NM_001193350.1. [Q06413-1] DR RefSeq; NP_001294931.1; NM_001308002.1. [Q06413-2] DR RefSeq; NP_002388.2; NM_002397.4. [Q06413-1] DR RefSeq; XP_005248568.1; XM_005248511.2. [Q06413-1] DR RefSeq; XP_006714682.1; XM_006714619.2. DR RefSeq; XP_006714688.1; XM_006714625.3. DR RefSeq; XP_011541698.1; XM_011543396.2. [Q06413-1] DR RefSeq; XP_011541702.1; XM_011543400.1. DR RefSeq; XP_016864965.1; XM_017009476.1. DR RefSeq; XP_016864966.1; XM_017009477.1. DR RefSeq; XP_016864967.1; XM_017009478.1. [Q06413-6] DR RefSeq; XP_016864968.1; XM_017009479.1. DR RefSeq; XP_016864969.1; XM_017009480.1. DR RefSeq; XP_016864970.1; XM_017009481.1. DR AlphaFoldDB; Q06413; -. DR SMR; Q06413; -. DR BioGRID; 110372; 37. DR DIP; DIP-40857N; -. DR ELM; Q06413; -. DR IntAct; Q06413; 28. DR MINT; Q06413; -. DR STRING; 9606.ENSP00000340874; -. DR GlyCosmos; Q06413; 1 site, 1 glycan. DR GlyGen; Q06413; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q06413; -. DR PhosphoSitePlus; Q06413; -. DR BioMuta; MEF2C; -. DR DMDM; 2500875; -. DR EPD; Q06413; -. DR jPOST; Q06413; -. DR MassIVE; Q06413; -. DR MaxQB; Q06413; -. DR PaxDb; 9606-ENSP00000340874; -. DR PeptideAtlas; Q06413; -. DR ProteomicsDB; 10911; -. DR ProteomicsDB; 30019; -. DR ProteomicsDB; 58439; -. [Q06413-1] DR ProteomicsDB; 58440; -. [Q06413-2] DR ProteomicsDB; 58441; -. [Q06413-3] DR ProteomicsDB; 58442; -. [Q06413-4] DR Pumba; Q06413; -. DR Antibodypedia; 755; 1469 antibodies from 36 providers. DR DNASU; 4208; -. DR Ensembl; ENST00000340208.9; ENSP00000340874.5; ENSG00000081189.17. [Q06413-5] DR Ensembl; ENST00000424173.6; ENSP00000389610.2; ENSG00000081189.17. [Q06413-6] DR Ensembl; ENST00000437473.6; ENSP00000396219.2; ENSG00000081189.17. [Q06413-1] DR Ensembl; ENST00000504921.7; ENSP00000421925.5; ENSG00000081189.17. [Q06413-1] DR Ensembl; ENST00000508569.5; ENSP00000423597.2; ENSG00000081189.17. [Q06413-2] DR Ensembl; ENST00000514015.5; ENSP00000424606.1; ENSG00000081189.17. [Q06413-3] DR Ensembl; ENST00000514028.5; ENSP00000426665.2; ENSG00000081189.17. [Q06413-3] DR Ensembl; ENST00000625674.2; ENSP00000487430.1; ENSG00000081189.17. [Q06413-6] DR Ensembl; ENST00000628656.2; ENSP00000487311.1; ENSG00000081189.17. [Q06413-4] DR Ensembl; ENST00000629612.2; ENSP00000486554.1; ENSG00000081189.17. [Q06413-2] DR Ensembl; ENST00000636294.1; ENSP00000490473.1; ENSG00000081189.17. [Q06413-1] DR Ensembl; ENST00000636998.1; ENSP00000490630.1; ENSG00000081189.17. [Q06413-3] DR Ensembl; ENST00000637732.1; ENSP00000490241.1; ENSG00000081189.17. [Q06413-3] DR GeneID; 4208; -. DR KEGG; hsa:4208; -. DR MANE-Select; ENST00000504921.7; ENSP00000421925.5; NM_002397.5; NP_002388.2. DR UCSC; uc003kjj.4; human. [Q06413-1] DR AGR; HGNC:6996; -. DR CTD; 4208; -. DR DisGeNET; 4208; -. DR GeneCards; MEF2C; -. DR HGNC; HGNC:6996; MEF2C. DR HPA; ENSG00000081189; Tissue enhanced (skeletal muscle, tongue). DR MalaCards; MEF2C; -. DR MIM; 600662; gene. DR MIM; 613443; phenotype. DR neXtProt; NX_Q06413; -. DR OpenTargets; ENSG00000081189; -. DR Orphanet; 228384; 5q14.3 microdeletion syndrome. DR Orphanet; 576227; Complete atrioventricular septal defect without ventricular hypoplasia. DR PharmGKB; PA30734; -. DR VEuPathDB; HostDB:ENSG00000081189; -. DR eggNOG; KOG0014; Eukaryota. DR GeneTree; ENSGT00940000157492; -. DR InParanoid; Q06413; -. DR OMA; MATNSYS; -. DR OrthoDB; 448298at2759; -. DR PhylomeDB; Q06413; -. DR TreeFam; TF314067; -. DR PathwayCommons; Q06413; -. DR Reactome; R-HSA-198753; ERK/MAPK targets. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR Reactome; R-HSA-400253; Circadian Clock. DR Reactome; R-HSA-525793; Myogenesis. DR Reactome; R-HSA-9022707; MECP2 regulates transcription factors. DR Reactome; R-HSA-9707616; Heme signaling. DR Reactome; R-HSA-9733709; Cardiogenesis. DR SignaLink; Q06413; -. DR SIGNOR; Q06413; -. DR BioGRID-ORCS; 4208; 42 hits in 1185 CRISPR screens. DR ChiTaRS; MEF2C; human. DR GeneWiki; MEF2C; -. DR GenomeRNAi; 4208; -. DR Pharos; Q06413; Tbio. DR PRO; PR:Q06413; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q06413; Protein. DR Bgee; ENSG00000081189; Expressed in middle temporal gyrus and 200 other cell types or tissues. DR ExpressionAtlas; Q06413; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0098794; C:postsynapse; IEA:GOC. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB. 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:0042826; F:histone deacetylase binding; IBA:GO_Central. DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. 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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:BHF-UCL. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB. DR GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB. DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0001568; P:blood vessel development; ISS:UniProtKB. DR GO; GO:0001974; P:blood vessel remodeling; ISS:UniProtKB. DR GO; GO:0003211; P:cardiac ventricle formation; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB. DR GO; GO:0071498; P:cellular response to fluid shear stress; ISS:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IDA:UniProtKB. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB. DR GO; GO:0035984; P:cellular response to trichostatin A; ISS:UniProtKB. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB. DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB. DR GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB. DR GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; ISS:UniProtKB. DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0002467; P:germinal center formation; ISS:UniProtKB. DR GO; GO:0072102; P:glomerulus morphogenesis; ISS:UniProtKB. DR GO; GO:0007507; P:heart development; IEP:UniProtKB. DR GO; GO:0001947; P:heart looping; ISS:UniProtKB. DR GO; GO:0006959; P:humoral immune response; ISS:UniProtKB. DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB. DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB. DR GO; GO:0030318; P:melanocyte differentiation; ISS:UniProtKB. DR GO; GO:0007521; P:muscle cell fate determination; ISS:UniProtKB. DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc. DR GO; GO:0014902; P:myotube differentiation; IEP:UniProtKB. DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IGI:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0030279; P:negative regulation of ossification; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IDA:BHF-UCL. DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IDA:BHF-UCL. DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IGI:BHF-UCL. DR GO; GO:0072160; P:nephron tubule epithelial cell differentiation; ISS:UniProtKB. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0014033; P:neural crest cell differentiation; ISS:UniProtKB. DR GO; GO:0048666; P:neuron development; ISS:UniProtKB. DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB. DR GO; GO:0001764; P:neuron migration; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB. DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:UniProtKB. DR GO; GO:0030220; P:platelet formation; ISS:UniProtKB. DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; ISS:UniProtKB. DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB. DR GO; GO:2000987; P:positive regulation of behavioral fear response; ISS:UniProtKB. DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB. DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IDA:UniProtKB. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:2000111; P:positive regulation of macrophage apoptotic process; ISS:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:UniProtKB. DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB. DR GO; GO:2001016; P:positive regulation of skeletal muscle cell differentiation; IDA:UniProtKB. DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0003138; P:primary heart field specification; ISS:UniProtKB. DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:Alzheimers_University_of_Toronto. DR GO; GO:0002634; P:regulation of germinal center formation; ISS:UniProtKB. DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; ISS:UniProtKB. DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:Alzheimers_University_of_Toronto. DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0051963; P:regulation of synapse assembly; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0060025; P:regulation of synaptic activity; ISS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0061333; P:renal tubule morphogenesis; ISS:UniProtKB. DR GO; GO:0002931; P:response to ischemia; ISS:Alzheimers_University_of_Toronto. DR GO; GO:0003139; P:secondary heart field specification; ISS:UniProtKB. DR GO; GO:0003185; P:sinoatrial valve morphogenesis; ISS:UniProtKB. DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB. DR GO; GO:0051145; P:smooth muscle cell differentiation; ISS:UniProtKB. DR GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; ISS:UniProtKB. DR CDD; cd00265; MADS_MEF2_like; 1. DR Gene3D; 3.40.1810.10; Transcription factor, MADS-box; 1. DR InterPro; IPR022102; HJURP_C. DR InterPro; IPR033896; MADS_MEF2-like. DR InterPro; IPR002100; TF_MADSbox. DR InterPro; IPR036879; TF_MADSbox_sf. DR PANTHER; PTHR48019:SF109; MYOCYTE-SPECIFIC ENHANCER FACTOR 2A; 1. DR PANTHER; PTHR48019; SERUM RESPONSE FACTOR HOMOLOG; 1. DR Pfam; PF12347; HJURP_C; 1. DR Pfam; PF00319; SRF-TF; 1. DR PRINTS; PR00404; MADSDOMAIN. DR SMART; SM00432; MADS; 1. DR SUPFAM; SSF55455; SRF-like; 1. DR PROSITE; PS00350; MADS_BOX_1; 1. DR PROSITE; PS50066; MADS_BOX_2; 1. DR Genevisible; Q06413; HS. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Apoptosis; Cytoplasm; KW Developmental protein; Differentiation; Disease variant; DNA-binding; KW Epilepsy; Intellectual disability; Isopeptide bond; Neurogenesis; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..473 FT /note="Myocyte-specific enhancer factor 2C" FT /id="PRO_0000199433" 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 91..116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 180..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 271..278 FT /note="Beta domain" FT REGION 368..399 FT /note="Transcription repressor" FT REGION 375..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..116 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 375..405 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 432..433 FT /note="Cleavage" FT /evidence="ECO:0000305" FT MOD_RES 4 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CFN5" FT MOD_RES 59 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250|UniProtKB:Q8CFN5" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CFN5" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CFN5" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CFN5" FT MOD_RES 116 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:15831463" FT MOD_RES 119 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:15831463" FT MOD_RES 222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 228 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 234 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:15831463" FT MOD_RES 239 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:15831463" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 252 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:15831463" FT MOD_RES 264 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:15831463" FT MOD_RES 293 FT /note="Phosphothreonine; by MAPK14" FT /evidence="ECO:0000269|PubMed:9069290, FT ECO:0000269|PubMed:9384584" FT MOD_RES 300 FT /note="Phosphothreonine; by MAPK14" FT /evidence="ECO:0000269|PubMed:9069290, FT ECO:0000269|PubMed:9384584" FT MOD_RES 396 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000269|PubMed:15340086" FT MOD_RES 419 FT /note="Phosphoserine; by MAPK7" FT /evidence="ECO:0000269|PubMed:9069290, FT ECO:0000269|PubMed:9384584" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 391 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:15743823, FT ECO:0000269|PubMed:16478538" FT VAR_SEQ 87..134 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_043339" FT VAR_SEQ 87..134 FT /note="TLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLC -> FT ALNKKENKGCESPDPDSSYALTPRTEEKYKKINEEFDNMIKSHKIP (in isoform FT 6)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_046251" FT VAR_SEQ 107..134 FT /note="VGHSPESEDKYRKINEDIDLMISRQRLC -> ALNKKENKGCESPDPDSSYA FT LTPRTEEKYKKINEEFDNMIKSHKIP (in isoform 5)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_045478" FT VAR_SEQ 271..278 FT /note="Missing (in isoform 2, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:7679508, ECO:0000303|PubMed:8455629, FT ECO:0000303|Ref.3" FT /id="VSP_006248" FT VAR_SEQ 368..399 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7679508" FT /id="VSP_006249" FT VARIANT 36 FT /note="S -> R (found in a patient with infantile onset FT epileptic encephalopathy and autism spectrum disorder; FT likely pathogenic)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078228" FT VARIANT 39 FT /note="C -> R (found in a patient with infantile onset FT epileptic encephalopathy and autism spectrum disorder; FT likely pathogenic; dbSNP:rs796052729)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078621" FT MUTAGEN 116 FT /note="K->R: Reduced acetylation. Further reduction in FT acetylation; when associated with R-119. Complete loss of FT acetylation, 15% less transactivation activity and slightly FT reduced DNA binding; when associated with R-119; R-234; FT R-239; R-252 and R-262." FT /evidence="ECO:0000269|PubMed:15831463" FT MUTAGEN 119 FT /note="K->R: Reduced acetylation. Further reduction in FT acetylation; when associated with R-119. Complete loss of FT acetylation, 15% less transactivation activity and slightly FT reduced DNA binding; when associated with R-116; R-234; FT R-239; R-252 and R-262." FT /evidence="ECO:0000269|PubMed:15831463" FT MUTAGEN 234 FT /note="K->R: Reduced acetylation. Complete loss of FT acetylation, 15% less transactivation activity and slightly FT reduced DNA binding; when associated with R-116; R-119; FT R-239; R-252 and R-264." FT /evidence="ECO:0000269|PubMed:15831463" FT MUTAGEN 239 FT /note="K->R: Reduced acetylation. Complete loss of FT acetylation, 15% less transactivation activity and slightly FT reduced DNA binding; when associated with R-116; R-119; FT R-234; R-252 and R-264." FT /evidence="ECO:0000269|PubMed:15831463" FT MUTAGEN 252 FT /note="K->R: Reduced acetylation. Complete loss of FT acetylation, 15% less transactivation activity and slightly FT reduced DNA binding; when associated with R-116; R-119; FT R-234; R-239 and R-264." FT /evidence="ECO:0000269|PubMed:15831463" FT MUTAGEN 264 FT /note="K->R: Reduced acetylation. Complete loss of FT acetylation, 15% less transactivation activity and slightly FT reduced DNA binding; when associated with R-116; R-119; FT R-234; R-239 and R-252." FT /evidence="ECO:0000269|PubMed:15831463" FT MUTAGEN 271 FT /note="S->A: No effect on transcriptional activation." FT /evidence="ECO:0000269|PubMed:15834131" FT MUTAGEN 272 FT /note="E->Q: Reduced transcriptional activation. Completely FT abolishes transcriptional activation; when associated with FT N-273 and N-275." FT /evidence="ECO:0000269|PubMed:15834131" FT MUTAGEN 273 FT /note="D->N: Reduced transcriptional activation. Completely FT abolishes transcriptional activation; when associated with FT Q-272 and N-275." FT /evidence="ECO:0000269|PubMed:15834131" FT MUTAGEN 275 FT /note="D->N: Reduced transcriptional activation. Completely FT abolishes transcriptional activation; when associated with FT Q-272 and N-273." FT /evidence="ECO:0000269|PubMed:15834131" FT MUTAGEN 293 FT /note="T->A: Abolishes MAPK14-mediated phosphorylation. No FT effect on MAPK7-mediated phosphorylation; when associated FT with A-300." FT /evidence="ECO:0000269|PubMed:9069290, FT ECO:0000269|PubMed:9384584" FT MUTAGEN 300 FT /note="T->A: Abolishes MAPK14-mediated phosphorylation. No FT effect on MAPK7-mediated phosphorylation; when associated FT with A-293." FT /evidence="ECO:0000269|PubMed:9069290, FT ECO:0000269|PubMed:9384584" FT MUTAGEN 387 FT /note="S->A: No change in transactivational activation for FT isoforms with or without the beta domain." FT /evidence="ECO:0000269|PubMed:15834131" FT MUTAGEN 391 FT /note="K->R: Abolishes sumoylation." FT /evidence="ECO:0000269|PubMed:16478538" FT MUTAGEN 396 FT /note="S->A,C: Abolishes sumoylation. Enhanced FT transcriptional activity." FT /evidence="ECO:0000269|PubMed:15340086, FT ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:16478538" FT MUTAGEN 396 FT /note="S->A: No change in transactivational activation for FT isoforms with or without the beta domain." FT /evidence="ECO:0000269|PubMed:15340086, FT ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:16478538" FT MUTAGEN 396 FT /note="S->E: No effect on sumoylation. No effect on FT transcriptional activity." FT /evidence="ECO:0000269|PubMed:15340086, FT ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:16478538" FT MUTAGEN 419 FT /note="S->A: No effect on MAPK14-mediated phosphorylation. FT Abolishes MAPK7-mediated phosphorylation and reduces FT transactivation activity." FT /evidence="ECO:0000269|PubMed:9069290, FT ECO:0000269|PubMed:9384584" FT MUTAGEN 432 FT /note="D->A: Abolishes cleavage by caspase 7." FT /evidence="ECO:0000269|PubMed:11904443" FT CONFLICT 390 FT /note="I -> T (in Ref. 4; AL833268)" FT /evidence="ECO:0000305" SQ SEQUENCE 473 AA; 51221 MW; A7982020BB8C8949 CRC64; MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI NEDIDLMISR QRLCAVPPPN FEMPVSIPVS SHNSLVYSNP VSSLGNPNLL PLAHPSLQRN SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNMQAKS PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP SALSQLGACT STHLSQSSNL SLPSTQSLNI KSEPVSPPRD RTTTPSRYPQ HTRHEAGRSP VDSLSSCSSS YDGSDREDHR NEFHSPIGLT RPSPDERESP SVKRMRLSEG WAT //