MYCD_HUMAN
ID MYCD_HUMAN Reviewed; 938 AA.
AC Q8IZQ8; Q5UBU5; Q8N7Q1;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Myocardin;
GN Name=MYOCD; Synonyms=MYCD;
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] (ISOFORM 1).
RX PubMed=12397177; DOI=10.1073/pnas.222561499;
RA Wang D.-Z., Li S., Hockemeyer D., Sutherland L., Wang Z., Schratt G.,
RA Richardson J.A., Nordheim A., Olson E.N.;
RT "Potentiation of serum response factor activity by a family of myocardin-
RT related transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14855-14860(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=12640126; DOI=10.1128/mcb.23.7.2425-2437.2003;
RA Du K.L., Ip H.S., Li J., Chen M., Dandre F., Yu W., Lu M.M., Owens G.K.,
RA Parmacek M.S.;
RT "Myocardin is a critical serum response factor cofactor in the
RT transcriptional program regulating smooth muscle cell differentiation.";
RL Mol. Cell. Biol. 23:2425-2437(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=15907818; DOI=10.1016/j.cardiores.2005.04.013;
RA van Tuyn J., Knaan-Shanzer S., van de Watering M.J., de Graaf M.,
RA van der Laarse A., Schalij M.J., van der Wall E.E., de Vries A.A.,
RA Atsma D.E.;
RT "Activation of cardiac and smooth muscle-specific genes in primary human
RT cells after forced expression of human myocardin.";
RL Cardiovasc. Res. 67:245-255(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), AND INDUCTION.
RX PubMed=12920479; DOI=10.1007/s00109-003-0470-7;
RA Torrado M., Lopez E., Centeno A., Medrano C., Castro-Beiras A.,
RA Mikhailov A.T.;
RT "Myocardin mRNA is augmented in the failing myocardium: expression
RT profiling in the porcine model and human dilated cardiomyopathy.";
RL J. Mol. Med. 81:566-577(2003).
RN [8]
RP INTERACTION WITH MLLT7.
RX PubMed=16054032; DOI=10.1016/j.devcel.2005.05.017;
RA Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N.;
RT "Phenotypic modulation of smooth muscle cells through interaction of Foxo4
RT and myocardin.";
RL Dev. Cell 9:261-270(2005).
RN [9]
RP TISSUE SPECIFICITY OF ISOFORMS.
RX PubMed=20385216; DOI=10.1016/j.gene.2010.03.012;
RA Imamura M., Long X., Nanda V., Miano J.M.;
RT "Expression and functional activity of four myocardin isoforms.";
RL Gene 464:1-10(2010).
RN [10]
RP INVOLVEMENT IN MGBL, FUNCTION, VARIANTS MGBL 115-ARG--TRP-938 DEL AND
RP GLY-530, AND CHARACTERIZATION OF VARIANTS MGBL 115-ARG--TRP-938 DEL AND
RP GLY-530.
RX PubMed=31513549; DOI=10.1172/jci128545;
RA Houweling A.C., Beaman G.M., Postma A.V., Gainous T.B., Lichtenbelt K.D.,
RA Brancati F., Lopes F.M., van der Made I., Polstra A.M., Robinson M.L.,
RA Wright K.D., Ellingford J.M., Jackson A.R., Overwater E., Genesio R.,
RA Romano S., Camerota L., D'Angelo E., Meijers-Heijboer E.J.,
RA Christoffels V.M., McHugh K.M., Black B.L., Newman W.G., Woolf A.S.,
RA Creemers E.E.;
RT "Loss-of-function variants in myocardin cause congenital megabladder in
RT humans and mice.";
RL J. Clin. Invest. 129:5374-5380(2019).
CC -!- FUNCTION: Smooth muscle cells (SM) and cardiac muscle cells-specific
CC transcriptional factor which uses the canonical single or multiple CArG
CC boxes DNA sequence. Acts as a cofactor of serum response factor (SRF)
CC with the potential to modulate SRF-target genes. Plays a crucial role
CC in cardiogenesis, urinary bladder development, and differentiation of
CC the smooth muscle cell lineage (myogenesis) (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12640126,
CC ECO:0000269|PubMed:31513549}.
CC -!- SUBUNIT: Homodimer. Interacts with SRF, its association does not depend
CC on specific DNA sequences for ternary complex formation (By
CC similarity). Interacts with MLLT7/FOXO4. Interacts (via C-terminal)
CC with EP300 (via the CREB-binding domain). Interacts with HDAC4 and
CC HDAC5 (By similarity). Interacts with MEF2C (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IZQ8; Q9HD26: GOPC; NbExp=4; IntAct=EBI-493384, EBI-349832;
CC Q8IZQ8; P11831: SRF; NbExp=2; IntAct=EBI-493384, EBI-493034;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Myocardin-A;
CC IsoId=Q8IZQ8-1; Sequence=Displayed;
CC Name=2; Synonyms=Myocardin-C;
CC IsoId=Q8IZQ8-2; Sequence=VSP_007658, VSP_007659, VSP_007660,
CC VSP_007661;
CC Name=3; Synonyms=Myocardin-B;
CC IsoId=Q8IZQ8-3; Sequence=VSP_007659;
CC -!- TISSUE SPECIFICITY: Expressed in heart, aorta, and in smooth muscle
CC cell-containing tissues: stomach, bladder, small intestine, colon,
CC lung, placenta and uterus. Very faint expression in prostate and
CC skeletal muscle. {ECO:0000269|PubMed:12640126,
CC ECO:0000269|PubMed:20385216}.
CC -!- INDUCTION: Up-regulated during heart failure.
CC {ECO:0000269|PubMed:12920479}.
CC -!- DOMAIN: The C-terminal region contains a general transcription
CC activation domain. The N-terminal region, comprising a basic and a Gln-
CC rich domain, confers transcriptional potency and specificity by
CC mediating association with the MADS box of SRF. The basic domain may be
CC required for nuclear localization. The SAP domain is important for
CC transactivation and ternary complex formation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation regulates negatively the intrinsic myocardin
CC transcriptional activity. {ECO:0000250}.
CC -!- DISEASE: Megabladder, congenital (MGBL) [MIM:618719]: An autosomal
CC dominant congenital anomaly characterized by a massively dilated
CC urinary bladder with disrupted smooth muscle in the bladder wall. MGBL
CC is a sex-limited trait with 95% male predominance, and incomplete
CC penetrance. Affected males frequently die in utero.
CC {ECO:0000269|PubMed:31513549}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
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DR EMBL; AF532596; AAN33040.1; -; mRNA.
DR EMBL; AY764180; AAV33439.1; -; mRNA.
DR EMBL; AK292885; BAF85574.1; -; mRNA.
DR EMBL; AK097821; BAC05177.1; -; mRNA.
DR EMBL; AC005358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126307; AAI26308.1; -; mRNA.
DR EMBL; BC143391; AAI43392.1; -; mRNA.
DR CCDS; CCDS11163.1; -. [Q8IZQ8-1]
DR CCDS; CCDS54091.1; -. [Q8IZQ8-3]
DR RefSeq; NP_001139784.1; NM_001146312.2. [Q8IZQ8-3]
DR RefSeq; NP_705832.1; NM_153604.3. [Q8IZQ8-1]
DR AlphaFoldDB; Q8IZQ8; -.
DR SMR; Q8IZQ8; -.
DR BioGRID; 125044; 16.
DR CORUM; Q8IZQ8; -.
DR IntAct; Q8IZQ8; 5.
DR STRING; 9606.ENSP00000401678; -.
DR iPTMnet; Q8IZQ8; -.
DR PhosphoSitePlus; Q8IZQ8; -.
DR BioMuta; MYOCD; -.
DR DMDM; 32363335; -.
DR jPOST; Q8IZQ8; -.
DR MassIVE; Q8IZQ8; -.
DR MaxQB; Q8IZQ8; -.
DR PaxDb; Q8IZQ8; -.
DR PeptideAtlas; Q8IZQ8; -.
DR PRIDE; Q8IZQ8; -.
DR ProteomicsDB; 71407; -. [Q8IZQ8-1]
DR ProteomicsDB; 71408; -. [Q8IZQ8-2]
DR ProteomicsDB; 71409; -. [Q8IZQ8-3]
DR Antibodypedia; 25055; 125 antibodies from 24 providers.
DR DNASU; 93649; -.
DR Ensembl; ENST00000343344.8; ENSP00000341835.4; ENSG00000141052.18. [Q8IZQ8-1]
DR Ensembl; ENST00000425538.6; ENSP00000401678.1; ENSG00000141052.18. [Q8IZQ8-3]
DR GeneID; 93649; -.
DR KEGG; hsa:93649; -.
DR MANE-Select; ENST00000425538.6; ENSP00000401678.1; NM_001146312.3; NP_001139784.1. [Q8IZQ8-3]
DR UCSC; uc002gnn.4; human. [Q8IZQ8-1]
DR CTD; 93649; -.
DR DisGeNET; 93649; -.
DR GeneCards; MYOCD; -.
DR HGNC; HGNC:16067; MYOCD.
DR HPA; ENSG00000141052; Low tissue specificity.
DR MalaCards; MYOCD; -.
DR MIM; 606127; gene.
DR MIM; 618719; phenotype.
DR neXtProt; NX_Q8IZQ8; -.
DR OpenTargets; ENSG00000141052; -.
DR PharmGKB; PA134946896; -.
DR VEuPathDB; HostDB:ENSG00000141052; -.
DR eggNOG; ENOG502QTAN; Eukaryota.
DR GeneTree; ENSGT00950000182979; -.
DR HOGENOM; CLU_007042_2_0_1; -.
DR InParanoid; Q8IZQ8; -.
DR OMA; HFEGMME; -.
DR OrthoDB; 190145at2759; -.
DR PhylomeDB; Q8IZQ8; -.
DR TreeFam; TF326024; -.
DR PathwayCommons; Q8IZQ8; -.
DR SignaLink; Q8IZQ8; -.
DR SIGNOR; Q8IZQ8; -.
DR BioGRID-ORCS; 93649; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; MYOCD; human.
DR GeneWiki; MYOCD; -.
DR GenomeRNAi; 93649; -.
DR Pharos; Q8IZQ8; Tbio.
DR PRO; PR:Q8IZQ8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IZQ8; protein.
DR Bgee; ENSG00000141052; Expressed in cauda epididymis and 133 other tissues.
DR ExpressionAtlas; Q8IZQ8; baseline and differential.
DR Genevisible; Q8IZQ8; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:BHF-UCL.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IDA:BHF-UCL.
DR GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; ISS:BHF-UCL.
DR GO; GO:0003231; P:cardiac ventricle development; IEA:Ensembl.
DR GO; GO:0035051; P:cardiocyte differentiation; NAS:UniProtKB.
DR GO; GO:0043954; P:cellular component maintenance; IEA:Ensembl.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0097070; P:ductus arteriosus closure; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:1900222; P:negative regulation of amyloid-beta clearance; IMP:BHF-UCL.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; IEA:Ensembl.
DR GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl.
DR GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; IEA:Ensembl.
DR GO; GO:0035065; P:regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:1900239; P:regulation of phenotypic switching; IEA:Ensembl.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; TAS:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IEP:BHF-UCL.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060157; P:urinary bladder development; IMP:UniProtKB.
DR GO; GO:0060065; P:uterus development; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR043451; Myocardin-like.
DR InterPro; IPR028721; MYOCD.
DR InterPro; IPR004018; RPEL_repeat.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR22793; PTHR22793; 1.
DR PANTHER; PTHR22793:SF11; PTHR22793:SF11; 1.
DR Pfam; PF02755; RPEL; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00707; RPEL; 3.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51073; RPEL; 3.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Disease variant; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..938
FT /note="Myocardin"
FT /id="PRO_0000126631"
FT REPEAT 18..43
FT /note="RPEL 1"
FT REPEAT 62..87
FT /note="RPEL 2"
FT REPEAT 106..131
FT /note="RPEL 3"
FT DOMAIN 371..405
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 48..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..205
FT /note="HDAC5-binding"
FT /evidence="ECO:0000250"
FT REGION 154..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 516..561
FT /evidence="ECO:0000255"
FT MOTIF 12..27
FT /note="MEF2C-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 48..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 451
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 455
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 459
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 463
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 626
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 630
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 634
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 638
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 815
FT /note="Phosphoserine; by MAPK1 AND MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 862
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 869
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT MOD_RES 896
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8VIM5"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007658"
FT VAR_SEQ 686
FT /note="Q -> QNSGAHDGHPPSFSPHSSSLHPPFSGAQADSSHGAGGNPCPKSPCVQ
FT QK (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12640126,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15907818"
FT /id="VSP_007659"
FT VAR_SEQ 730..732
FT /note="QMT -> VTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007660"
FT VAR_SEQ 733..938
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007661"
FT VARIANT 115..938
FT /note="Missing (in MGBL; loss of function in trascriptional
FT activation)"
FT /evidence="ECO:0000269|PubMed:31513549"
FT /id="VAR_083482"
FT VARIANT 530
FT /note="E -> G (in MGBL; unknown pathological significance;
FT decreased function in trascriptional activation;
FT dbSNP:rs1597809206)"
FT /evidence="ECO:0000269|PubMed:31513549"
FT /id="VAR_083483"
SQ SEQUENCE 938 AA; 101997 MW; 295F66A02725B0A5 CRC64;
MTLLGSEHSL LIRSKFRSVL QLRLQQRRTQ EQLANQGIIP PLKRPAEFHE QRKHLDSDKA
KNSLKRKARN RCNSADLVNM HILQASTAER SIPTAQMKLK RARLADDLNE KIALRPGPLE
LVEKNILPVD SAVKEAIKGN QVSFSKSTDA FAFEEDSSSD GLSPDQTRSE DPQNSAGSPP
DAKASDTPST GSLGTNQDLA SGSENDRNDS ASQPSHQSDA GKQGLGPPST PIAVHAAVKS
KSLGDSKNRH KKPKDPKPKV KKLKYHQYIP PDQKAEKSPP PMDSAYARLL QQQQLFLQLQ
ILSQQQQQQQ HRFSYLGMHQ AQLKEPNEQM VRNPNSSSTP LSNTPLSPVK NSFSGQTGVS
SFKPGPLPPN LDDLKVSELR QQLRIRGLPV SGTKTALMDR LRPFQDCSGN PVPNFGDITT
VTFPVTPNTL PNYQSSSSTS ALSNGFYHFG STSSSPPISP ASSDLSVAGS LPDTFNDASP
SFGLHPSPVH VCTEESLMSS LNGGSVPSEL DGLDSEKDKM LVEKQKVINE LTWKLQQEQR
QVEELRMQLQ KQKRNNCSEK KPLPFLAASI KQEEAVSSCP FASQVPVKRQ SSSSECHPPA
CEAAQLQPLG NAHCVESSDQ TNVLSSTFLS PQCSPQHSPL GAVKSPQHIS LPPSPNNPHF
LPSSSGAQGE GHRVSSPISS QVCTAQMAGL HSSDKVGPKF SIPSPTFSKS SSAISEVTQP
PSYEDAVKQQ MTRSQQMDEL LDVLIESGEM PADAREDHSC LQKVPKIPRS SRSPTAVLTK
PSASFEQASS GSQIPFDPYA TDSDEHLEVL LNSQSPLGKM SDVTLLKIGS EEPHFDGIMD
GFSGKAAEDL FNAHEILPGP LSPMQTQFSP SSVDSNGLQL SFTESPWETM EWLDLTPPNS
TPGFSALTTS SPSIFNIDFL DVTDLNLNSS MDLHLQQW
