MEF2C_RAT
ID MEF2C_RAT Reviewed; 473 AA.
AC A0A096MJY4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Myocyte-specific enhancer factor 2C {ECO:0000305};
DE AltName: Full=Myocyte enhancer factor 2C {ECO:0000312|RGD:1563119};
GN Name=Mef2c {ECO:0000312|RGD:1563119};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, DNA-BINDING, INTERACTION WITH HABP4, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-110; SER-222 AND
RP SER-240, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcription activator which binds specifically to the MEF2
CC element present in the regulatory regions of many muscle-specific genes
CC (PubMed:15862299). Controls cardiac morphogenesis and myogenesis, and
CC is also involved in vascular development. Enhances transcriptional
CC activation mediated by SOX18. Plays an essential role in hippocampal-
CC dependent learning and memory by suppressing the number of excitatory
CC synapses and thus regulating basal and evoked synaptic transmission.
CC Crucial for normal neuronal development, distribution, and electrical
CC activity in the neocortex. Necessary for proper development of
CC megakaryocytes and platelets and for bone marrow B-lymphopoiesis.
CC Required for B-cell survival and proliferation in response to BCR
CC stimulation, efficient IgG1 antibody responses to T-cell-dependent
CC antigens and for normal induction of germinal center B-cells. May also
CC be involved in neurogenesis and in the development of cortical
CC architecture (By similarity). {ECO:0000250|UniProtKB:Q8CFN5,
CC ECO:0000269|PubMed:15862299}.
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. Interacts with HDAC7 and CARM1. Interacts with HDAC4 and
CC HDAC9; the interaction with HDACs represses transcriptional activity.
CC Interacts with LPIN1. Interacts with MYOCD. Interacts with AKAP13.
CC Interacts with FOXK1; the interaction inhibits MEF2C transactivation
CC activity (By similarity). Interacts (via N-terminus) with HABP4; this
CC interaction decreases DNA-binding activity of MEF2C in myocardial cells
CC in response to mechanical stress (PubMed:15862299). Interacts with
CC JPH2; interaction specifically takes place with the Junctophilin-2 N-
CC terminal fragment cleavage product of JPH2 (By similarity). Interacts
CC (via MADS box) with SOX18 (By similarity).
CC {ECO:0000250|UniProtKB:Q8CFN5, ECO:0000269|PubMed:15862299}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15862299}. Cytoplasm,
CC sarcoplasm {ECO:0000269|PubMed:15862299}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart (PubMed:15862299). Expressed
CC in cardiac myocytes (at protein level) (PubMed:15862299).
CC {ECO:0000269|PubMed:15862299}.
CC -!- DOMAIN: The beta domain is required for enhancement of transcriptional
CC activity. {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser-59; which enhances DNA binding activity.
CC Phosphorylated on Ser-396; which is required for Lys-391 sumoylation
CC and inhibits transcriptional activity. {ECO:0000250}.
CC -!- PTM: Acetylated by p300 on several sites in diffentiating myocytes.
CC Acetylation on Lys-4 increases DNA binding and transactivation.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated on Lys-391 with SUMO2 but not SUMO1; which represses
CC transcriptional activity. {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:0000250}.
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; AABR07007384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006224017.1; XM_006223955.3.
DR RefSeq; XP_006224019.1; XM_006223957.3.
DR RefSeq; XP_006231793.1; XM_006231731.2.
DR RefSeq; XP_006231795.1; XM_006231733.3.
DR RefSeq; XP_008758864.1; XM_008760642.2.
DR RefSeq; XP_008773249.1; XM_008775027.2.
DR RefSeq; XP_017446652.1; XM_017591163.1.
DR RefSeq; XP_017449843.1; XM_017594354.1.
DR AlphaFoldDB; A0A096MJY4; -.
DR SMR; A0A096MJY4; -.
DR STRING; 10116.ENSRNOP00000068307; -.
DR iPTMnet; A0A096MJY4; -.
DR PaxDb; A0A096MJY4; -.
DR GeneID; 499497; -.
DR KEGG; rno:499497; -.
DR CTD; 4208; -.
DR RGD; 1563119; Mef2c.
DR eggNOG; KOG0014; Eukaryota.
DR OMA; RITEGWA; -.
DR OrthoDB; 729387at2759; -.
DR Reactome; R-RNO-525793; Myogenesis.
DR PRO; PR:A0A096MJY4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000033134; Expressed in quadriceps femoris and 19 other tissues.
DR ExpressionAtlas; A0A096MJY4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0016607; C:nuclear speck; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0071837; F:HMG box domain binding; ISO:RGD.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
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; ISO:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; ISO:RGD.
DR GO; GO:0003211; P:cardiac ventricle formation; ISO:RGD.
DR GO; GO:0060536; P:cartilage morphogenesis; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; ISO:RGD.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISS:UniProtKB.
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:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS: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; ISO:RGD.
DR GO; GO:0021542; P:dentate gyrus development; IEP:RGD.
DR GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0030318; P:melanocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
DR GO; GO:0007521; P:muscle cell fate determination; ISO:RGD.
DR GO; GO:0014902; P:myotube differentiation; ISO:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0030279; P:negative regulation of ossification; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:RGD.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISO:RGD.
DR GO; GO:0072160; P:nephron tubule epithelial cell differentiation; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:2000111; P:positive regulation of macrophage apoptotic process; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS: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; ISS:UniProtKB.
DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
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:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
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:UniProtKB.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:UniProtKB.
DR GO; GO:0060297; P:regulation of sarcomere organization; ISO:RGD.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:RGD.
DR GO; GO:0060025; P:regulation of synaptic activity; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0061333; P:renal tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0003139; P:secondary heart field specification; ISS:UniProtKB.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; ISO:RGD.
DR GO; GO:0003185; P:sinoatrial valve morphogenesis; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0051145; P:smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0097492; P:sympathetic neuron axon guidance; ISO:RGD.
DR GO; GO:0060290; P:transdifferentiation; IMP:RGD.
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; Apoptosis; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; 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_0000441823"
FT DOMAIN 1..61
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..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..278
FT /note="Beta domain"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT REGION 368..399
FT /note="Transcription repressor"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
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:0000250|UniProtKB:Q06413"
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:0007744|PubMed:22673903"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CFN5"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 239
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 293
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 300
FT /note="Phosphothreonine; by MAPK14"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 396
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 419
FT /note="Phosphoserine; by MAPK7"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q06413"
SQ SEQUENCE 473 AA; 51217 MW; 3D7C3B3F641C2C1F CRC64;
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST
DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI
NEDIDLMISR QRLCAVPPPN FEMPVTIPVS SHNSLVYSNP VSSLGNPNLL PLAHPSLQRN
SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS
PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT
PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP
SALSQLGACT STHLSQSSNL SLPSTQSLNI KSEPVSPPRD RTTTPSRYPQ HTRHEAGRSP
VDSLSSCSSS YDGSDREDHR NEFHSPIGLT RPSPDERESP SVKRMRLSEG WAT
