MEF2C_HUMAN
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 03-AUG-2022, entry version 201.
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}.
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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. [Q06413-5]
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; 35.
DR DIP; DIP-40857N; -.
DR ELM; Q06413; -.
DR IntAct; Q06413; 27.
DR MINT; Q06413; -.
DR STRING; 9606.ENSP00000340874; -.
DR GlyGen; Q06413; 1 site, 1 O-linked glycan (1 site).
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 PeptideAtlas; Q06413; -.
DR PRIDE; 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 Antibodypedia; 755; 1349 antibodies from 36 providers.
DR DNASU; 4208; -.
DR Ensembl; ENST00000340208.9; ENSP00000340874.5; ENSG00000081189.16. [Q06413-5]
DR Ensembl; ENST00000424173.6; ENSP00000389610.2; ENSG00000081189.16. [Q06413-6]
DR Ensembl; ENST00000437473.6; ENSP00000396219.2; ENSG00000081189.16. [Q06413-1]
DR Ensembl; ENST00000504921.7; ENSP00000421925.5; ENSG00000081189.16. [Q06413-1]
DR Ensembl; ENST00000508569.5; ENSP00000423597.2; ENSG00000081189.16. [Q06413-2]
DR Ensembl; ENST00000514015.5; ENSP00000424606.1; ENSG00000081189.16. [Q06413-3]
DR Ensembl; ENST00000514028.5; ENSP00000426665.2; ENSG00000081189.16. [Q06413-3]
DR Ensembl; ENST00000625674.2; ENSP00000487430.1; ENSG00000081189.16. [Q06413-6]
DR Ensembl; ENST00000628656.2; ENSP00000487311.1; ENSG00000081189.16. [Q06413-4]
DR Ensembl; ENST00000629612.2; ENSP00000486554.1; ENSG00000081189.16. [Q06413-2]
DR Ensembl; ENST00000636294.1; ENSP00000490473.1; ENSG00000081189.16. [Q06413-1]
DR Ensembl; ENST00000636998.1; ENSP00000490630.1; ENSG00000081189.16. [Q06413-3]
DR Ensembl; ENST00000637732.1; ENSP00000490241.1; ENSG00000081189.16. [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 CTD; 4208; -.
DR DisGeNET; 4208; -.
DR GeneCards; MEF2C; -.
DR HGNC; HGNC:6996; MEF2C.
DR HPA; ENSG00000081189; Group enriched (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 PharmGKB; PA30734; -.
DR VEuPathDB; HostDB:ENSG00000081189; -.
DR eggNOG; KOG0014; Eukaryota.
DR GeneTree; ENSGT00940000157492; -.
DR InParanoid; Q06413; -.
DR OMA; RITEGWA; -.
DR OrthoDB; 729387at2759; -.
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 SignaLink; Q06413; -.
DR SIGNOR; Q06413; -.
DR BioGRID-ORCS; 4208; 41 hits in 1106 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 198 other tissues.
DR ExpressionAtlas; Q06413; baseline and differential.
DR Genevisible; Q06413; HS.
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: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:0043406; P:positive regulation of MAP kinase activity; 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:0045893; P:positive regulation of transcription, DNA-templated; 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: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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; -; 1.
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 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 (probable disease-associated variant found in
FT a patient with infantile onset epileptic encephalopathy and
FT autism spectrum disorder)"
FT /evidence="ECO:0000269|PubMed:27864847"
FT /id="VAR_078228"
FT VARIANT 39
FT /note="C -> R (probable disease-associated variant found in
FT a patient with infantile onset epileptic encephalopathy and
FT autism spectrum disorder; 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; R-
FT 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; R-
FT 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; R-
FT 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; R-
FT 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; R-
FT 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; R-
FT 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
