Q8CFN5 (MEF2C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myocyte-specific enhancer factor 2C

Gene names

Name:

Mef2c

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. May also be involved in neurogenesis and in the development of cortical architecture. Isoform 3 and isoform 4, which lack the repressor domain, are more active than isoform 1, isoform 2 and isoform 5 By similarity. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. Ref.6 Ref.7 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Subunit structure	Forms a complex with class II HDACs in undifferentiating cells. On myogenic differentiation, HDACs are released into the cytoplasm allowing MEF2s to interact with other proteins for activation. Interacts with EP300 in differentiating cells; the interaction acetylates MEF2C leading to increased DNA binding and activation. Interacts with HDAC7 and CARM1 By similarity. Interacts with HDAC4, HDAC7 AND HDAC9; the interaction WITH HDACs represses transcriptional activity. Interacts with LPIN1. Interacts with MYOCD. Ref.8 Ref.9 Ref.12 Ref.18
Subcellular location	Nucleus By similarity.
Tissue specificity	Widely expressed though mainly restricted to skeletal and cardiac muscle, brain, neurons and lymphocytes. Beta beta domain-lacking isoforms are the most predominantly expressed in all tissues including skeletal and cardiac muscle and brain. Only brain expresses all isoforms. Expression occurs primarily in the internal granule cell layer of the olfactory bulb, cortex, thalamus, hippocampus and cerebellum. Low levels in the cerebellum and hindbrain. Expressed throughout the cortex, including the frontal and entorhinal cortex, dentate gyrus, and basolateral amygdala. Selectively expressed in B-cells but not in T-cells, and its expression increases as B-cells mature. Ref.1 Ref.4 Ref.10 Ref.11 Ref.13 Ref.15
Developmental stage	Expressed in developing endothelial cells and smooth muscle cells, as well as in surrounding mesenchyme, during embryogenesis. Up-regulated during myogenesis. Ref.7
Domain	The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity By similarity.
Post-translational modification	Phosphorylation on Ser-59 enhances DNA binding activity By similarity. Phosphorylation on Ser-396 is required for Lys-391 sumoylation and inhibits transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes By similarity. Acetylation on Lys-4 increases DNA binding and transactivation. Sumoylated on Lys-391 with SUMO2 but not by SUMO1 represses transcriptional activity By similarity. Proteolytically cleaved in cerebellar granule neurons, probably by caspase 7, following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation By similarity. Ref.5
Disruption phenotype	Mice show impairment in hippocampal-dependent learning and also increase in the number of excitatory synapses and potentiation of basal and evoked synaptic transmission. Mice surviving to adulthood manifest smaller, apparently less mature neurons and smaller whole brain size, with resultant aberrant electrophysiology and behavior. Mice exhibit thrombocytopenia and a defect in B-lymphopoiesis. Ref.15 Ref.16 Ref.17
Sequence similarities	Belongs to the MEF2 family. Contains 1 MADS-box domain. Contains 1 Mef2-type DNA-binding domain.

Ontologies

Keywords
Biological process	Apoptosis Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell homeostasis Inferred from mutant phenotype Ref.17. Source: UniProtKB B cell proliferation Inferred from mutant phenotype Ref.13. Source: UniProtKB B cell receptor signaling pathway Inferred from mutant phenotype PubMed 18955699. Source: UniProtKB MAPK cascade Inferred from direct assay PubMed 14515274. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW blood vessel development Inferred from mutant phenotype PubMed 17336904Ref.7. Source: MGI blood vessel remodeling Inferred from mutant phenotype PubMed 10395786Ref.6. Source: MGI cardiac muscle hypertrophy in response to stress Inferred from mutant phenotype PubMed 10531040. Source: MGI cardiac ventricle formation Inferred from mutant phenotype PubMed 16680724. Source: UniProtKB cartilage morphogenesis Inferred from mutant phenotype PubMed 17420000. Source: MGI cellular response to calcium ion Inferred from direct assay PubMed 15998798. Source: UniProtKB cellular response to drug Inferred from direct assay PubMed 16775627. Source: UniProtKB cellular response to fluid shear stress Inferred from direct assay PubMed 20181743. Source: UniProtKB cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from direct assay PubMed 18955699. Source: UniProtKB cellular response to parathyroid hormone stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to retinoic acid Inferred from electronic annotation. Source: Compara cellular response to transforming growth factor beta stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to trichostatin A Inferred from direct assay PubMed 20181743. Source: UniProtKB chondrocyte differentiation Inferred from genetic interaction PubMed 17336904. Source: MGI dentate gyrus development Inferred from electronic annotation. Source: Compara embryonic viscerocranium morphogenesis Inferred from mutant phenotype PubMed 17420000. Source: MGI endochondral ossification Inferred from mutant phenotype PubMed 17336904. Source: MGI epithelial cell proliferation involved in renal tubule morphogenesis Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB germinal center formation Inferred from mutant phenotype PubMed 18955699. Source: UniProtKB glomerulus morphogenesis Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB heart looping Inferred from mutant phenotype PubMed 16680724. Source: UniProtKB humoral immune response Inferred from mutant phenotype PubMed 18955699. Source: UniProtKB learning or memory Inferred from mutant phenotype Ref.15. Source: UniProtKB melanocyte differentiation Inferred from mutant phenotype PubMed 21610032. Source: UniProtKB monocyte differentiation Inferred from mutant phenotype PubMed 18326819. Source: MGI muscle cell fate determination Inferred from mutant phenotype PubMed 17786239. Source: MGI negative regulation of epithelial cell proliferation Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from direct assay PubMed 18579729. Source: UniProtKB negative regulation of ossification Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB nephron tubule epithelial cell differentiation Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB neural crest cell differentiation Inferred from mutant phenotype PubMed 21610032. Source: UniProtKB neuron development Inferred from mutant phenotype Ref.16. Source: UniProtKB osteoblast differentiation Inferred from expression pattern PubMed 21652706. Source: UniProtKB outflow tract morphogenesis Inferred from genetic interaction PubMed 19035347. Source: MGI palate development Inferred from genetic interaction PubMed 17420000. Source: MGI platelet formation Inferred from mutant phenotype Ref.17. Source: UniProtKB positive regulation of B cell proliferation Inferred from mutant phenotype PubMed 18955699. Source: UniProtKB positive regulation of alkaline phosphatase activity Inferred from mutant phenotype PubMed 21652706. Source: UniProtKB positive regulation of behavioral fear response Inferred from mutant phenotype PubMed 18579729. Source: UniProtKB positive regulation of bone mineralization Inferred from mutant phenotype PubMed 21652706. Source: UniProtKB positive regulation of cardiac muscle cell differentiation Inferred from mutant phenotype PubMed 16680724. Source: UniProtKB positive regulation of cardiac muscle cell proliferation Inferred from mutant phenotype PubMed 16680724. Source: UniProtKB positive regulation of cell proliferation in bone marrow Inferred from genetic interaction PubMed 18278031. Source: MGI positive regulation of macrophage apoptotic process Inferred from mutant phenotype PubMed 16775627. Source: UniProtKB positive regulation of myoblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron differentiation Inferred from direct assay PubMed 18579729. Source: UniProtKB positive regulation of osteoblast differentiation Inferred from mutant phenotype PubMed 21652706. Source: UniProtKB positive regulation of protein homodimerization activity Inferred from direct assay PubMed 19035347. Source: MGI positive regulation of skeletal muscle tissue development Inferred from sequence or structural similarity. Source: UniProtKB primary heart field specification Inferred from mutant phenotype PubMed 16680724. Source: UniProtKB regulation of germinal center formation Inferred from mutant phenotype Ref.13. Source: UniProtKB regulation of megakaryocyte differentiation Inferred from mutant phenotype Ref.17. Source: UniProtKB regulation of sarcomere organization Inferred from mutant phenotype PubMed 17875930. Source: MGI regulation of synaptic activity Inferred from mutant phenotype Ref.15. Source: UniProtKB response to vitamin E Inferred from electronic annotation. Source: Compara secondary heart field specification Inferred from mutant phenotype PubMed 15890826. Source: UniProtKB sinoatrial valve morphogenesis Inferred from mutant phenotype PubMed 16680724. Source: UniProtKB skeletal muscle cell differentiation Inferred from expression pattern PubMed 21556048. Source: UniProtKB smooth muscle cell differentiation Inferred from mutant phenotype Ref.7. Source: MGI ventricular cardiac muscle cell differentiation Inferred from mutant phenotype PubMed 16680724. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 17420000PubMed 18093911. Source: MGI RNA polymerase II regulatory region sequence-specific DNA binding Inferred from direct assay PubMed 15890826. Source: UniProtKB chromatin binding Inferred from direct assay Ref.14. Source: MGI core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 20399744. Source: MGI core promoter sequence-specific DNA binding Inferred from direct assay PubMed 20181743. Source: UniProtKB miRNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Acly	Q91V92	3	EBI-643822,EBI-644049

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q8CFN5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform 2 (identifier: Q8CFN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     271-278: Missing.

Isoform 3 (identifier: Q8CFN5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     368-399: Missing.

Isoform 4 (identifier: Q8CFN5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     87-97: TLRKKGLNGCD → ALNKKENKGSE
     103-118: ADDSVGHSPESEDKYR → SSYALTPRTEEKYK
     123-134: DIDLMISRQRLC → EFDNMIKSHKIP
     271-278: Missing.
     368-399: Missing.

Isoform 5 (identifier: Q8CFN5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     87-97: TLRKKGLNGCD → ALNKKENKGSE
     103-118: ADDSVGHSPESEDKYR → SSYALTPRTEEKYK
     123-134: DIDLMISRQRLC → EFDNMIKSHKIP

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 474	474	Myocyte-specific enhancer factor 2C		PRO_0000199434
Regions
	Domain	3 – 57	55	MADS-box
	DNA binding	58 – 86	29	Mef2-type Potential
	Region	271 – 278	8	Beta domain By similarity
	Region	368 – 399	32	Transcription repressor By similarity
	Compositional bias	4 – 31	28	Lys-rich (basic)
	Compositional bias	146 – 183	38	Ser-rich
Sites
	Site	433 – 434	2	Cleavage Probable
Amino acid modifications
	Modified residue	4	1	N6-acetyllysine Ref.14
	Modified residue	59	1	Phosphoserine; by CK2 Ref.5
	Modified residue	116	1	N6-acetyllysine By similarity
	Modified residue	119	1	N6-acetyllysine By similarity
	Modified residue	234	1	N6-acetyllysine By similarity
	Modified residue	239	1	N6-acetyllysine By similarity
	Modified residue	252	1	N6-acetyllysine By similarity
	Modified residue	264	1	N6-acetyllysine By similarity
	Modified residue	293	1	Phosphothreonine; by MAPK14 By similarity
	Modified residue	300	1	Phosphothreonine; by MAPK14 By similarity
	Modified residue	396	1	Phosphoserine; by CDK5 By similarity
	Modified residue	420	1	Phosphoserine; by MAPK7
	Cross-link	391		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	87 – 97	11	TLRKKGLNGCD → ALNKKENKGSE in isoform 4 and isoform 5.		VSP_012501
	Alternative sequence	103 – 118	16	ADDSV…EDKYR → SSYALTPRTEEKYK in isoform 4 and isoform 5.		VSP_012502
	Alternative sequence	123 – 134	12	DIDLM…RQRLC → EFDNMIKSHKIP in isoform 4 and isoform 5.		VSP_012503
	Alternative sequence	271 – 278	8	Missing in isoform 2 and isoform 4.		VSP_012504
	Alternative sequence	368 – 399	32	Missing in isoform 3 and isoform 4.		VSP_012505
Experimental info
	Mutagenesis	3	1	R → T: Increased mobility in differentiating cells. Greatly reduced DNA binding. Ref.14
	Mutagenesis	4	1	K → Q: 7-fold increase in DNA binding. Ref.14
	Mutagenesis	4	1	K → R: Reduced acetylation by 30%. Some loss of DNA binding and transactivation activity. Ref.14
	Mutagenesis	59 – 60	2	ST → CR: Reduced DNA binding activity. Ref.5
	Mutagenesis	59 – 60	2	ST → DD: Enhanced DNA binding activity. Ref.5
	Mutagenesis	59	1	S → A: Reduced DNA binding activity. Ref.5
	Mutagenesis	59	1	S → D: Enhanced DNA binding activity. Ref.5
	Sequence conflict	141	1	F → L in AAH37731. Ref.3
	Sequence conflict	211	1	S → P Ref.1
	Sequence conflict	428	1	C → S Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: CEFC2DB21E89632A	FASTA	474	51,278
	10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI 130 140 150 160 170 180 NEDIDLMISR QRLCAVPPPS FEMPVTIPVS SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN 190 200 210 220 230 240 SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS 250 260 270 280 290 300 PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT 310 320 330 340 350 360 PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP 370 380 390 400 410 420 SALSQLGACT STHLSQSSNL SLPSTQSLSI KSEPVSPPRD RTTTPSRYPQ HTTRHEAGRS 430 440 450 460 470 PVDSLSSCSS SYDGSDREDH RNEFHSPIGL TRPSPDERES PSVKRMRLSE GWAT
	Isoform 2 [UniParc]. Checksum: F06A89C9ACD779AE	FASTA	466	50,393
	10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI 130 140 150 160 170 180 NEDIDLMISR QRLCAVPPPS FEMPVTIPVS SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN 190 200 210 220 230 240 SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS 250 260 270 280 290 300 PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV NQRINNSQSA QSLATPVVSV ATPTLPGQGM 310 320 330 340 350 360 GGYPSAISTT YGTEYSLSSA DLSSLSGFNT ASALHLGSVT GWQQQHLHNM PPSALSQLGA 370 380 390 400 410 420 CTSTHLSQSS NLSLPSTQSL SIKSEPVSPP RDRTTTPSRY PQHTTRHEAG RSPVDSLSSC 430 440 450 460 SSSYDGSDRE DHRNEFHSPI GLTRPSPDER ESPSVKRMRL SEGWAT
	Isoform 3 [UniParc]. Checksum: 40EFBF02BF3E775C	FASTA	442	47,956
	10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI 130 140 150 160 170 180 NEDIDLMISR QRLCAVPPPS FEMPVTIPVS SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN 190 200 210 220 230 240 SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS 250 260 270 280 290 300 PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT 310 320 330 340 350 360 PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP 370 380 390 400 410 420 SALSQLGDRT TTPSRYPQHT TRHEAGRSPV DSLSSCSSSY DGSDREDHRN EFHSPIGLTR 430 440 PSPDERESPS VKRMRLSEGW AT
	Isoform 4 [UniParc]. Checksum: DCB2EBCE61A35215	FASTA	432	46,961
	10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVEALNK KENKGSESPD PDSSYALTPR TEEKYKKINE 130 140 150 160 170 180 EFDNMIKSHK IPAVPPPSFE MPVTIPVSSH NSLVYSNPVS TLGNPNLLPL AHPSLQRNSM 190 200 210 220 230 240 SPGVTHRPPS AGNTGGLMGG DLTSGAGTSA GNGYGNPRNS PGLLVSPGNL NKNIQAKSPP 250 260 270 280 290 300 PMNLGMNNRK PDLRVLIPPG SKNTMPSVNQ RINNSQSAQS LATPVVSVAT PTLPGQGMGG 310 320 330 340 350 360 YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP SALSQLGDRT 370 380 390 400 410 420 TTPSRYPQHT TRHEAGRSPV DSLSSCSSSY DGSDREDHRN EFHSPIGLTR PSPDERESPS 430 VKRMRLSEGW AT
	Isoform 5 [UniParc]. Checksum: 1B618AB137809260	FASTA	472	51,168
	10 20 30 40 50 60 MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST 70 80 90 100 110 120 DMDKVLLKYT EYNEPHESRT NSDIVEALNK KENKGSESPD PDSSYALTPR TEEKYKKINE 130 140 150 160 170 180 EFDNMIKSHK IPAVPPPSFE MPVTIPVSSH NSLVYSNPVS TLGNPNLLPL AHPSLQRNSM 190 200 210 220 230 240 SPGVTHRPPS AGNTGGLMGG DLTSGAGTSA GNGYGNPRNS PGLLVSPGNL NKNIQAKSPP 250 260 270 280 290 300 PMNLGMNNRK PDLRVLIPPG SKNTMPSVSE DVDLLLNQRI NNSQSAQSLA TPVVSVATPT 310 320 330 340 350 360 LPGQGMGGYP SAISTTYGTE YSLSSADLSS LSGFNTASAL HLGSVTGWQQ QHLHNMPPSA 370 380 390 400 410 420 LSQLGACTST HLSQSSNLSL PSTQSLSIKS EPVSPPRDRT TTPSRYPQHT TRHEAGRSPV 430 440 450 460 470 DSLSSCSSSY DGSDREDHRN EFHSPIGLTR PSPDERESPS VKRMRLSEGW AT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Myocyte enhancer factor (MEF) 2C: a tissue-restricted member of the MEF-2 family of transcription factors." Martin J.F., Schwarz J.J., Olson E.N. Proc. Natl. Acad. Sci. U.S.A. 90:5282-5286(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Strain: C57BL/6J. Tissue: Tongue.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). Tissue: Eye.
[4]	"The expression of MEF2 genes is implicated in CNS neuronal differentiation." Lin X., Shah S., Bulleit R.F. Brain Res. Mol. Brain Res. 42:307-316(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"Phosphorylation of the MADS-Box transcription factor MEF2C enhances its DNA binding activity." Molkentin J.D., Li L., Olson E.N. J. Biol. Chem. 271:17199-17204(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-59, MUTAGENESIS OF SER-59.
[6]	"Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C." Lin Q., Schwarz J., Bucana C., Olson E.N. Science 276:1404-1407(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Requirement of the MADS-box transcription factor MEF2C for vascular development." Lin Q., Lu J., Yanagisawa H., Webb R., Lyons G.E., Richardson J.A., Olson E.N. Development 125:4565-4574(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[8]	"A dynamic role for HDAC7 in MEF2-mediated muscle differentiation." Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M., Muscat G.E.O. J. Biol. Chem. 276:17007-17013(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC7.
[9]	"The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2." Chen S.L., Loffler K.A., Chen D., Stallcup M.R., Muscat G.E. J. Biol. Chem. 277:4324-4333(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CARM1.
[10]	"Phosphorylation and alternative pre-mRNA splicing converge to regulate myocyte enhancer factor 2C activity." Zhu B., Gulick T. Mol. Cell. Biol. 24:8264-8275(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY OF ISOFORMS.
[11]	"Alternative pre-mRNA splicing governs expression of a conserved acidic transactivation domain in myocyte enhancer factor 2 factors of striated muscle and brain." Zhu B., Ramachandran B., Gulick T. J. Biol. Chem. 280:28749-28760(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY OF ISOFORMS.
[12]	"Coactivation of MEF2 by the SAP domain proteins myocardin and MASTR." Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N. Mol. Cell 23:83-96(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYOCD.
[13]	"Transcription factor Mef2c is required for B cell proliferation and survival after antigen receptor stimulation." Wilker P.R., Kohyama M., Sandau M.M., Albring J.C., Nakagawa O., Schwarz J.J., Murphy K.M. Nat. Immunol. 9:603-612(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[14]	"Differentiation-dependent lysine 4 acetylation enhances MEF2C binding to DNA in skeletal muscle cells." Angelelli C., Magli A., Ferrari D., Ganassi M., Matafora V., Parise F., Razzini G., Bachi A., Ferrari S., Molinari S. Nucleic Acids Res. 36:915-928(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-4, DNA-BINDING, MASS SPECTROMETRY, FUNCTION, MUTAGENESIS OF ARG-3 AND LYS-4.
[15]	"MEF2C, a transcription factor that facilitates learning and memory by negative regulation of synapse numbers and function." Barbosa A.C., Kim M.S., Ertunc M., Adachi M., Nelson E.D., McAnally J., Richardson J.A., Kavalali E.T., Monteggia L.M., Bassel-Duby R., Olson E.N. Proc. Natl. Acad. Sci. U.S.A. 105:9391-9396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[16]	"Transcription factor MEF2C influences neural stem/progenitor cell differentiation and maturation in vivo." Li H., Radford J.C., Ragusa M.J., Shea K.L., McKercher S.R., Zaremba J.D., Soussou W., Nie Z., Kang Y.J., Nakanishi N., Okamoto S., Roberts A.J., Schwarz J.J., Lipton S.A. Proc. Natl. Acad. Sci. U.S.A. 105:9397-9402(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[17]	"Mef2C is a lineage-restricted target of Scl/Tal1 and regulates megakaryopoiesis and B-cell homeostasis." Gekas C., Rhodes K.E., Gereige L.M., Helgadottir H., Ferrari R., Kurdistani S.K., Montecino-Rodriguez E., Bassel-Duby R., Olson E., Krivtsov A.V., Armstrong S., Orkin S.H., Pellegrini M., Mikkola H.K. Blood 113:3461-3471(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[18]	"Sumoylation regulates nuclear localization of lipin-1alpha in neuronal cells." Liu G.H., Gerace L. PLoS ONE 4:E7031-E7031(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LIPN1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK009139 mRNA. Translation: BAB26099.1. BC026841 mRNA. Translation: AAH26841.1. BC037731 mRNA. Translation: AAH37731.1. BC057650 mRNA. Translation: AAH57650.1.
IPI	IPI00153197. IPI00318314. IPI00408591. IPI00515347. IPI00515421.
RefSeq	NP_079558.1. NM_025282.3.
UniGene	Mm.24001. Mm.451574. Mm.484098. Mm.487610.
3D structure databases
ProteinModelPortal	Q8CFN5.
SMR	Q8CFN5. Positions 2-73.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CFN5. 5 interactions.
MINT	MINT-1551742.
PTM databases
PhosphoSite	Q8CFN5.
Proteomic databases
PaxDb	Q8CFN5.
PRIDE	Q8CFN5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005722; ENSMUSP00000005722; ENSMUSG00000005583. ENSMUST00000163888; ENSMUSP00000132547; ENSMUSG00000005583.
GeneID	17260.
KEGG	mmu:17260.
UCSC	uc007rie.2. mouse. uc007rih.2. mouse. uc007rii.3. mouse.
Organism-specific databases
CTD	4208.
MGI	MGI:99458. Mef2c.
Phylogenomic databases
eggNOG	COG5068.
GeneTree	ENSGT00390000011828.
HOGENOM	HOG000230620.
HOVERGEN	HBG053944.
KO	K04454.
OMA	GNCSSSH.
OrthoDB	EOG4DFPNH.
Gene expression databases
ArrayExpress	Q8CFN5.
Bgee	Q8CFN5.
CleanEx	MM_MEF2C.
Genevestigator	Q8CFN5.
Family and domain databases
InterPro	IPR022102. HJURP_C. IPR002100. TF_MADSbox. [Graphical view]
Pfam	PF12347. HJURP_C. 1 hit. PF00319. SRF-TF. 1 hit. [Graphical view]
PRINTS	PR00404. MADSDOMAIN.
SMART	SM00432. MADS. 1 hit. [Graphical view]
SUPFAM	SSF55455. TF_MADSbox. 1 hit.
PROSITE	PS00350. MADS_BOX_1. 1 hit. PS50066. MADS_BOX_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	291752.
SOURCE	Search...

Entry information

Entry name

MEF2C_MOUSE

Accession

Primary (citable) accession number: Q8CFN5
Secondary accession number(s): Q8R0H1, Q9D7L0, Q9QW20

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	May 29, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program