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Q8CFN5 (MEF2C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myocyte-specific enhancer factor 2C
Gene names
Name:Mef2c
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.14

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 processApoptosis
Differentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB 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 cell differentiation

Non-traceable author statement PubMed 21556048. Source: UniProtKB

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

cell fate commitment

Inferred from mutant phenotype PubMed 19169261. 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: Ensembl

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: Ensembl

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: Ensembl

embryonic skeletal system morphogenesis

Inferred from mutant phenotype PubMed 17420000. Source: MGI

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 development

Inferred from mutant phenotype PubMed 10395786Ref.7. Source: MGI

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

myotube differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB

negative regulation of gene expression

Inferred from mutant phenotype PubMed 16680724. 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

neuron differentiation

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 cardiac muscle hypertrophy

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation in bone marrow

Inferred from genetic interaction PubMed 18278031. Source: MGI

positive regulation of gene expression

Inferred from direct assay PubMed 18579729. Source: UniProtKB

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 cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of skeletal muscle tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15890826PubMed 20181743. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11554755PubMed 14515274PubMed 21610032. 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

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12130539. Source: MGI

renal tubule morphogenesis

Inferred from mutant phenotype PubMed 20181743. Source: UniProtKB

response to virus

Inferred from electronic annotation. Source: Ensembl

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

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

Non-traceable author statement PubMed 21556048. Source: UniProtKB

skeletal muscle tissue development

Inferred from mutant phenotype PubMed 17786239. Source: MGI

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_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear speck

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11554755PubMed 15998798PubMed 20181743PubMed 21610032. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

sarcomere

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionAT DNA binding

Inferred from electronic annotation. Source: Ensembl

DNA binding

Inferred from direct assay PubMed 14762206PubMed 16140986PubMed 19477969. Source: MGI

HMG box domain binding

Inferred from physical interaction PubMed 11554755PubMed 21610032. Source: UniProtKB

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

histone deacetylase binding

Inferred from physical interaction PubMed 10983972. Source: BHF-UCL

miRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 21556048PubMed 21610032. Source: UniProtKB

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 21610032. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12130539. Source: MGI

transcription regulatory region DNA binding

Inferred from direct assay PubMed 8035824. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AclyQ91V923EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Myocyte-specific enhancer factor 2C
PRO_0000199434

Regions

Domain3 – 5755MADS-box
DNA binding58 – 8629Mef2-type Potential
Region271 – 2788Beta domain By similarity
Region368 – 39932Transcription repressor By similarity
Compositional bias4 – 3128Lys-rich (basic)
Compositional bias146 – 18338Ser-rich

Sites

Site433 – 4342Cleavage Probable

Amino acid modifications

Modified residue41N6-acetyllysine Ref.14
Modified residue591Phosphoserine; by CK2 Ref.5
Modified residue1161N6-acetyllysine By similarity
Modified residue1191N6-acetyllysine By similarity
Modified residue2341N6-acetyllysine By similarity
Modified residue2391N6-acetyllysine By similarity
Modified residue2521N6-acetyllysine By similarity
Modified residue2641N6-acetyllysine By similarity
Modified residue2931Phosphothreonine; by MAPK14 By similarity
Modified residue3001Phosphothreonine; by MAPK14 By similarity
Modified residue3961Phosphoserine; by CDK5 By similarity
Modified residue4201Phosphoserine; by MAPK7
Cross-link391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence87 – 9711TLRKKGLNGCD → ALNKKENKGSE in isoform 4 and isoform 5.
VSP_012501
Alternative sequence103 – 11816ADDSV…EDKYR → SSYALTPRTEEKYK in isoform 4 and isoform 5.
VSP_012502
Alternative sequence123 – 13412DIDLM…RQRLC → EFDNMIKSHKIP in isoform 4 and isoform 5.
VSP_012503
Alternative sequence271 – 2788Missing in isoform 2 and isoform 4.
VSP_012504
Alternative sequence368 – 39932Missing in isoform 3 and isoform 4.
VSP_012505

Experimental info

Mutagenesis31R → T: Increased mobility in differentiating cells. Greatly reduced DNA binding. Ref.14
Mutagenesis41K → Q: 7-fold increase in DNA binding. Ref.14
Mutagenesis41K → R: Reduced acetylation by 30%. Some loss of DNA binding and transactivation activity. Ref.14
Mutagenesis59 – 602ST → CR: Reduced DNA binding activity. Ref.5
Mutagenesis59 – 602ST → DD: Enhanced DNA binding activity. Ref.5
Mutagenesis591S → A: Reduced DNA binding activity. Ref.5
Mutagenesis591S → D: Enhanced DNA binding activity. Ref.5
Sequence conflict1411F → L in AAH37731. Ref.3
Sequence conflict2111S → P Ref.1
Sequence conflict4281C → S Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: CEFC2DB21E89632A

FASTA47451,278
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F06A89C9ACD779AE
Show »

FASTA46650,393
Isoform 3 [UniParc].

Checksum: 40EFBF02BF3E775C
Show »

FASTA44247,956
Isoform 4 [UniParc].

Checksum: DCB2EBCE61A35215
Show »

FASTA43246,961
Isoform 5 [UniParc].

Checksum: 1B618AB137809260
Show »

FASTA47251,168

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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.
RefSeqNP_079558.1. NM_025282.3.
XP_006517183.1. XM_006517120.1.
XP_006517184.1. XM_006517121.1.
XP_006517185.1. XM_006517122.1.
XP_006517186.1. XM_006517123.1.
XP_006517187.1. XM_006517124.1.
XP_006517188.1. XM_006517125.1.
XP_006517189.1. XM_006517126.1.
XP_006517192.1. XM_006517129.1.
XP_006517195.1. XM_006517132.1.
UniGeneMm.24001.
Mm.451574.
Mm.487610.

3D structure databases

ProteinModelPortalQ8CFN5.
SMRQ8CFN5. Positions 2-73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201383. 10 interactions.
DIPDIP-49524N.
IntActQ8CFN5. 6 interactions.
MINTMINT-1551742.

PTM databases

PhosphoSiteQ8CFN5.

Proteomic databases

PaxDbQ8CFN5.
PRIDEQ8CFN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005722; ENSMUSP00000005722; ENSMUSG00000005583. [Q8CFN5-4]
ENSMUST00000163888; ENSMUSP00000132547; ENSMUSG00000005583. [Q8CFN5-2]
ENSMUST00000185052; ENSMUSP00000138826; ENSMUSG00000005583. [Q8CFN5-3]
GeneID17260.
KEGGmmu:17260.
UCSCuc007rie.2. mouse. [Q8CFN5-4]
uc007rih.2. mouse. [Q8CFN5-5]
uc007rii.3. mouse. [Q8CFN5-3]

Organism-specific databases

CTD4208.
MGIMGI:99458. Mef2c.

Phylogenomic databases

eggNOGCOG5068.
GeneTreeENSGT00390000011828.
HOGENOMHOG000230620.
HOVERGENHBG053944.
KOK04454.
OMAGNCSSSH.
OrthoDBEOG793B7D.
PhylomeDBQ8CFN5.
TreeFamTF314067.

Gene expression databases

ArrayExpressQ8CFN5.
BgeeQ8CFN5.
CleanExMM_MEF2C.
GenevestigatorQ8CFN5.

Family and domain databases

InterProIPR022102. HJURP_C.
IPR002100. TF_MADSbox.
[Graphical view]
PfamPF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSPR00404. MADSDOMAIN.
SMARTSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMSSF55455. SSF55455. 1 hit.
PROSITEPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291752.
PROQ8CFN5.
SOURCESearch...

Entry information

Entry nameMEF2C_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot