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Protein

Myocyte-specific enhancer factor 2C

Gene

MEF2C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). Isoform 3 and isoform 4, which lack the repressor domain, are more active than isoform 1 and isoform 2.By similarity6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei432 – 4332CleavageCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi58 – 8629Mef2-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_12599. ERK/MAPK targets.
REACT_21402. CDO in myogenesis.
REACT_24941. Circadian Clock.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
SignaLinkiQ06413.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2C
Gene namesi
Name:MEF2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6996. MEF2C.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Alzheimers_University_of_Toronto
  • intracellular membrane-bounded organelle Source: HPA
  • nuclear speck Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 20 (MRD20)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by severe mental retardation, absent speech, hypotonia, poor eye contact and stereotypic movements. Dysmorphic features include high broad forehead with variable small chin, short nose with anteverted nares, large open mouth, upslanted palpebral fissures and prominent eyebrows. Some patients have seizures.

See also OMIM:613443

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1161K → R: Reduced acetylation. Further reduction in acetylation; when associated with R-119. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-119; R-234; R-239; R-252 and R-262. 1 Publication
Mutagenesisi119 – 1191K → R: Reduced acetylation. Further reduction in acetylation; when associated with R-119. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-234; R-239; R-252 and R-262. 1 Publication
Mutagenesisi234 – 2341K → R: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-239; R-252 and R-264. 1 Publication
Mutagenesisi239 – 2391K → R: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-252 and R-264. 1 Publication
Mutagenesisi252 – 2521K → R: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-239 and R-264. 1 Publication
Mutagenesisi264 – 2641K → R: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-239 and R-252. 1 Publication
Mutagenesisi271 – 2711S → A: No effect on transcriptional activation. 1 Publication
Mutagenesisi272 – 2721E → Q: Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with N-273 and N-275. 1 Publication
Mutagenesisi273 – 2731D → N: Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with Q-272 and N-275. 1 Publication
Mutagenesisi275 – 2751D → N: Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with Q-272 and N-273. 1 Publication
Mutagenesisi293 – 2931T → A: Abolishes MAPK14-mediated phosphorylation. No effect on MAPK7-mediated phosphorylation; when associated with A-300. 2 Publications
Mutagenesisi300 – 3001T → A: Abolishes MAPK14-mediated phosphorylation. No effect on MAPK7-mediated phosphorylation; when associated with A-293. 2 Publications
Mutagenesisi387 – 3871S → A: No change in transactivational activation for isoforms with or without the beta domain. 1 Publication
Mutagenesisi391 – 3911K → R: Abolishes sumoylation. 1 Publication
Mutagenesisi396 – 3961S → A or C: Abolishes sumoylation. Enhanced transcriptional activity. 3 Publications
Mutagenesisi396 – 3961S → A: No change in transactivational activation for isoforms with or without the beta domain. 3 Publications
Mutagenesisi396 – 3961S → E: No effect on sumoylation. No effect on transcriptional activity. 3 Publications
Mutagenesisi419 – 4191S → A: No effect on MAPK14-mediated phosphorylation. Abolishes MAPK7-mediated phosphorylation and reduces transactivation activity. 2 Publications
Mutagenesisi432 – 4321D → A: Abolishes cleavage by caspase 7. 1 Publication

Keywords - Diseasei

Epilepsy, Mental retardation

Organism-specific databases

MIMi613443. phenotype.
Orphaneti228384. 5q14.3 microdeletion syndrome.
PharmGKBiPA30734.

Polymorphism and mutation databases

BioMutaiMEF2C.
DMDMi2500875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Myocyte-specific enhancer factor 2CPRO_0000199433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41N6-acetyllysineBy similarity
Modified residuei59 – 591Phosphoserine; by CK2By similarity
Modified residuei116 – 1161N6-acetyllysine1 Publication
Modified residuei119 – 1191N6-acetyllysine1 Publication
Modified residuei234 – 2341N6-acetyllysine1 Publication
Modified residuei239 – 2391N6-acetyllysine1 Publication
Modified residuei252 – 2521N6-acetyllysine1 Publication
Modified residuei264 – 2641N6-acetyllysine1 Publication
Modified residuei293 – 2931Phosphothreonine; by MAPK142 Publications
Modified residuei300 – 3001Phosphothreonine; by MAPK142 Publications
Cross-linki391 – 391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei396 – 3961Phosphoserine; by CDK51 Publication
Modified residuei419 – 4191Phosphoserine; by MAPK72 Publications

Post-translational modificationi

Phosphorylation on Ser-59 enhances DNA binding activity (By similarity). Phosphorylation on Ser-396 is required for Lys-391 sumoylation and inhibits transcriptional activity.By similarity7 Publications
Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity).By similarity
Sumoylated on Lys-391 with SUMO2 but not by SUMO1 represses transcriptional activity.3 Publications
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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ06413.
PaxDbiQ06413.
PRIDEiQ06413.

PTM databases

PhosphoSiteiQ06413.

Expressioni

Tissue specificityi

Expressed in brain and skeletal muscle.1 Publication

Developmental stagei

Expression is highest during the early stages of postnatal development, at later stages levels greatly decrease.

Gene expression databases

BgeeiQ06413.
CleanExiHS_MEF2C.
ExpressionAtlasiQ06413. baseline and differential.
GenevisibleiQ06413. HS.

Organism-specific databases

HPAiCAB068196.
CAB068197.
HPA003214.
HPA005533.

Interactioni

Subunit structurei

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 MYOCD (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MYLK2Q9H1R32EBI-2684075,EBI-356910

Protein-protein interaction databases

BioGridi110372. 26 interactions.
DIPiDIP-40857N.
IntActiQ06413. 16 interactions.
MINTiMINT-125556.
STRINGi9606.ENSP00000340874.

Structurei

3D structure databases

ProteinModelPortaliQ06413.
SMRiQ06413. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 5755MADS-boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 2788Beta domain
Regioni368 – 39932Transcription repressorAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 3128Lys-rich (basic)Add
BLAST
Compositional biasi146 – 18338Ser-richAdd
BLAST

Domaini

The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity.By similarity

Sequence similaritiesi

Belongs to the MEF2 family.Curated
Contains 1 MADS-box domain.PROSITE-ProRule annotation
Contains 1 Mef2-type DNA-binding domain.Curated

Phylogenomic databases

eggNOGiCOG5068.
GeneTreeiENSGT00390000011828.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ06413.
KOiK04454.
OMAiCAVPPSN.
OrthoDBiEOG793B7D.
PhylomeDBiQ06413.
TreeFamiTF314067.

Family and domain databases

InterProiIPR022102. HJURP_C.
IPR002100. TF_MADSbox.
[Graphical view]
PfamiPF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSiPR00404. MADSDOMAIN.
SMARTiSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMiSSF55455. SSF55455. 1 hit.
PROSITEiPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q06413-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS
60 70 80 90 100
TNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD
110 120 130 140 150
PDADDSVGHS PESEDKYRKI NEDIDLMISR QRLCAVPPPN FEMPVSIPVS
160 170 180 190 200
SHNSLVYSNP VSSLGNPNLL PLAHPSLQRN SMSPGVTHRP PSAGNTGGLM
210 220 230 240 250
GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNMQAKS PPPMNLGMNN
260 270 280 290 300
RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT
310 320 330 340 350
PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW
360 370 380 390 400
QQQHLHNMPP SALSQLGACT STHLSQSSNL SLPSTQSLNI KSEPVSPPRD
410 420 430 440 450
RTTTPSRYPQ HTRHEAGRSP VDSLSSCSSS YDGSDREDHR NEFHSPIGLT
460 470
RPSPDERESP SVKRMRLSEG WAT
Length:473
Mass (Da):51,221
Last modified:November 1, 1997 - v1
Checksum:iA7982020BB8C8949
GO
Isoform 2 (identifier: Q06413-2) [UniParc]FASTAAdd to basket

Also known as: Muscle

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

Show »
Length:465
Mass (Da):50,336
Checksum:iA2059C6AACB2F07B
GO
Isoform 3 (identifier: Q06413-3) [UniParc]FASTAAdd to basket

Also known as: hMEF2C-delta32, Brain

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

Show »
Length:441
Mass (Da):47,872
Checksum:iBF94FD79A54FEEB1
GO
Isoform 4 (identifier: Q06413-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-134: Missing.
     271-278: Missing.

Show »
Length:417
Mass (Da):44,935
Checksum:i35B8B495FAB6FA3C
GO
Isoform 5 (identifier: Q06413-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     107-134: VGHSPESEDKYRKINEDIDLMISRQRLC → ALNKKENKGCESPDPDSSYALTPRTEEKYKKINEEFDNMIKSHKIP
     271-278: Missing.

Note: No experimental confirmation available.
Show »
Length:483
Mass (Da):52,328
Checksum:i54ECDC4D04211C48
GO
Isoform 6 (identifier: Q06413-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-134: TLRKKGLNGC...DLMISRQRLC → ALNKKENKGC...DNMIKSHKIP
     271-278: Missing.

Note: No experimental confirmation available.
Show »
Length:463
Mass (Da):50,242
Checksum:iB78282622DC98CE5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3901I → T in AL833268 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei87 – 13448Missing in isoform 4. 1 PublicationVSP_043339Add
BLAST
Alternative sequencei87 – 13448TLRKK…RQRLC → ALNKKENKGCESPDPDSSYA LTPRTEEKYKKINEEFDNMI KSHKIP in isoform 6. 1 PublicationVSP_046251Add
BLAST
Alternative sequencei107 – 13428VGHSP…RQRLC → ALNKKENKGCESPDPDSSYA LTPRTEEKYKKINEEFDNMI KSHKIP in isoform 5. 1 PublicationVSP_045478Add
BLAST
Alternative sequencei271 – 2788Missing in isoform 2, isoform 4, isoform 5 and isoform 6. 4 PublicationsVSP_006248
Alternative sequencei368 – 39932Missing in isoform 3. 1 PublicationVSP_006249Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08895 mRNA. Translation: AAA59578.1.
S57212 mRNA. Translation: AAB25838.1.
FM163484 mRNA. Translation: CAQ57795.2.
AL833268 mRNA. No translation available.
AL833274 mRNA. No translation available.
AC008525 Genomic DNA. No translation available.
AC008835 Genomic DNA. No translation available.
CCDSiCCDS47244.1. [Q06413-6]
CCDS47245.1. [Q06413-1]
CCDS54877.1. [Q06413-4]
CCDS54878.1. [Q06413-5]
PIRiA47284.
RefSeqiNP_001124477.1. NM_001131005.2. [Q06413-6]
NP_001180276.1. NM_001193347.1. [Q06413-5]
NP_001180277.1. NM_001193348.1. [Q06413-4]
NP_001180278.1. NM_001193349.1.
NP_001180279.1. NM_001193350.1. [Q06413-1]
NP_002388.2. NM_002397.4. [Q06413-1]
XP_005248568.1. XM_005248511.1. [Q06413-1]
XP_006714681.1. XM_006714618.1. [Q06413-1]
XP_006714682.1. XM_006714619.1. [Q06413-1]
XP_006714688.1. XM_006714625.2. [Q06413-5]
UniGeneiHs.649965.

Genome annotation databases

EnsembliENST00000340208; ENSP00000340874; ENSG00000081189. [Q06413-5]
ENST00000424173; ENSP00000389610; ENSG00000081189. [Q06413-6]
ENST00000437473; ENSP00000396219; ENSG00000081189. [Q06413-1]
ENST00000504921; ENSP00000421925; ENSG00000081189. [Q06413-1]
ENST00000508569; ENSP00000423597; ENSG00000081189. [Q06413-2]
ENST00000514015; ENSP00000424606; ENSG00000081189. [Q06413-3]
ENST00000514028; ENSP00000426665; ENSG00000081189. [Q06413-3]
ENST00000625674; ENSP00000487430; ENSG00000081189. [Q06413-6]
ENST00000628656; ENSP00000487311; ENSG00000081189. [Q06413-4]
ENST00000629612; ENSP00000486554; ENSG00000081189. [Q06413-2]
GeneIDi4208.
KEGGihsa:4208.
UCSCiuc003kji.2. human. [Q06413-2]
uc003kjj.3. human. [Q06413-1]
uc021ybh.1. human. [Q06413-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08895 mRNA. Translation: AAA59578.1.
S57212 mRNA. Translation: AAB25838.1.
FM163484 mRNA. Translation: CAQ57795.2.
AL833268 mRNA. No translation available.
AL833274 mRNA. No translation available.
AC008525 Genomic DNA. No translation available.
AC008835 Genomic DNA. No translation available.
CCDSiCCDS47244.1. [Q06413-6]
CCDS47245.1. [Q06413-1]
CCDS54877.1. [Q06413-4]
CCDS54878.1. [Q06413-5]
PIRiA47284.
RefSeqiNP_001124477.1. NM_001131005.2. [Q06413-6]
NP_001180276.1. NM_001193347.1. [Q06413-5]
NP_001180277.1. NM_001193348.1. [Q06413-4]
NP_001180278.1. NM_001193349.1.
NP_001180279.1. NM_001193350.1. [Q06413-1]
NP_002388.2. NM_002397.4. [Q06413-1]
XP_005248568.1. XM_005248511.1. [Q06413-1]
XP_006714681.1. XM_006714618.1. [Q06413-1]
XP_006714682.1. XM_006714619.1. [Q06413-1]
XP_006714688.1. XM_006714625.2. [Q06413-5]
UniGeneiHs.649965.

3D structure databases

ProteinModelPortaliQ06413.
SMRiQ06413. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110372. 26 interactions.
DIPiDIP-40857N.
IntActiQ06413. 16 interactions.
MINTiMINT-125556.
STRINGi9606.ENSP00000340874.

PTM databases

PhosphoSiteiQ06413.

Polymorphism and mutation databases

BioMutaiMEF2C.
DMDMi2500875.

Proteomic databases

MaxQBiQ06413.
PaxDbiQ06413.
PRIDEiQ06413.

Protocols and materials databases

DNASUi4208.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340208; ENSP00000340874; ENSG00000081189. [Q06413-5]
ENST00000424173; ENSP00000389610; ENSG00000081189. [Q06413-6]
ENST00000437473; ENSP00000396219; ENSG00000081189. [Q06413-1]
ENST00000504921; ENSP00000421925; ENSG00000081189. [Q06413-1]
ENST00000508569; ENSP00000423597; ENSG00000081189. [Q06413-2]
ENST00000514015; ENSP00000424606; ENSG00000081189. [Q06413-3]
ENST00000514028; ENSP00000426665; ENSG00000081189. [Q06413-3]
ENST00000625674; ENSP00000487430; ENSG00000081189. [Q06413-6]
ENST00000628656; ENSP00000487311; ENSG00000081189. [Q06413-4]
ENST00000629612; ENSP00000486554; ENSG00000081189. [Q06413-2]
GeneIDi4208.
KEGGihsa:4208.
UCSCiuc003kji.2. human. [Q06413-2]
uc003kjj.3. human. [Q06413-1]
uc021ybh.1. human. [Q06413-4]

Organism-specific databases

CTDi4208.
GeneCardsiGC05M088013.
HGNCiHGNC:6996. MEF2C.
HPAiCAB068196.
CAB068197.
HPA003214.
HPA005533.
MIMi600662. gene.
613443. phenotype.
neXtProtiNX_Q06413.
Orphaneti228384. 5q14.3 microdeletion syndrome.
PharmGKBiPA30734.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5068.
GeneTreeiENSGT00390000011828.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ06413.
KOiK04454.
OMAiCAVPPSN.
OrthoDBiEOG793B7D.
PhylomeDBiQ06413.
TreeFamiTF314067.

Enzyme and pathway databases

ReactomeiREACT_12599. ERK/MAPK targets.
REACT_21402. CDO in myogenesis.
REACT_24941. Circadian Clock.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
SignaLinkiQ06413.

Miscellaneous databases

ChiTaRSiMEF2C. human.
GeneWikiiMEF2C.
GenomeRNAii4208.
NextBioi16578.
PROiQ06413.
SOURCEiSearch...

Gene expression databases

BgeeiQ06413.
CleanExiHS_MEF2C.
ExpressionAtlasiQ06413. baseline and differential.
GenevisibleiQ06413. HS.

Family and domain databases

InterProiIPR022102. HJURP_C.
IPR002100. TF_MADSbox.
[Graphical view]
PfamiPF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
[Graphical view]
PRINTSiPR00404. MADSDOMAIN.
SMARTiSM00432. MADS. 1 hit.
[Graphical view]
SUPFAMiSSF55455. SSF55455. 1 hit.
PROSITEiPS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MEF2C, a MADS/MEF2-family transcription factor expressed in a laminar distribution in cerebral cortex."
    Leifer D., Krainc D., Yu Y.-T., McDermott J., Breitbart R.E., Heng J., Neve R.L., Kosofsky B., Nadal-Ginard B., Lipton S.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:1546-1550(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Fetal brain and Muscle.
  2. "hMEF2C gene encodes skeletal muscle- and brain-specific transcription factors."
    McDermott J.C., Cardoso M.C., Yu Y.-T., Andres V., Leifer D., Krainc D., Lipton S.A., Nadal-Ginard B.
    Mol. Cell. Biol. 13:2564-2577(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Skeletal muscle.
  3. "Identification and characterization of a new splice variant of human MEF2C."
    Infantino V., Convertini P., Palmieri F., Iacobazzi V.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Skeletal muscle.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
    Tissue: Skeletal muscle.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C."
    Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D.
    EMBO J. 16:7054-7066(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-293; THR-300 AND SER-419, FUNCTION, MUTAGENESIS OF THR-293; THR-300 AND SER-419.
  7. "Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation."
    Han J., Jiang Y., Li Z., Kravchenko V.V., Ulevitch R.J.
    Nature 386:296-299(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-293; THR-300 AND SER-419, FUNCTION, MUTAGENESIS OF THR-293; THR-300 AND SER-419.
  8. "Characterization of myocyte enhancer factor 2 (MEF2) expression in B and T cells: MEF2C is a B cell-restricted transcription factor in lymphocytes."
    Swanson B.J., Jaeck H.-M., Lyons G.E.
    Mol. Immunol. 35:445-458(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor."
    Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J.
    Mol. Cell. Biol. 19:7816-7827(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC4.
  10. "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family."
    Kato Y., Zhao M., Morikawa A., Sugiyama T., Chakravortty D., Koide N., Yoshida T., Tapping R.I., Yang Y., Yokochi T., Lee J.D.
    J. Biol. Chem. 275:18534-18540(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAPK7.
  11. "Cloning and characterization of a histone deacetylase, HDAC9."
    Zhou X., Marks P.A., Rifkind R.A., Richon V.M.
    Proc. Natl. Acad. Sci. U.S.A. 98:10572-10577(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC9.
  12. "Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis."
    Okamoto S., Li Z., Ju C., Scholzke M.N., Mathews E., Cui J., Salvesen G.S., Bossy-Wetzel E., Lipton S.A.
    Proc. Natl. Acad. Sci. U.S.A. 99:3974-3979(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING AT ASP-432, FUNCTION, MUTAGENESIS OF ASP-432.
  13. "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: PHOSPHORYLATION AT SER-396, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-396, FUNCTION OF ISOFORMS.
  14. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
    Gocke C.B., Yu H., Kang J.
    J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  15. "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: FUNCTION OF BETA DOMAIN, MUTAGENESIS OF SER-271; GLU-272; ASP-273; ASP-275; SER-387 AND SER-396.
  16. "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors."
    Gregoire S., Yang X.-J.
    Mol. Cell. Biol. 25:2273-2287(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-391.
  17. "Myocyte enhancer factor 2 acetylation by p300 enhances its DNA binding activity, transcriptional activity, and myogenic differentiation."
    Ma K., Chan J.K., Zhu G., Wu Z.
    Mol. Cell. Biol. 25:3575-3582(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-116; LYS-119; LYS-234; LYS-239; LYS-252 AND LYS-264, INTERACTION WITH EP300, FUNCTION, DNA-BINDING, MUTAGENESIS OF LYS-116; LYS-119; LYS-234; LYS-239; LYS-252 AND LYS-264.
  18. "Phosphorylation-facilitated sumoylation of MEF2C negatively regulates its transcriptional activity."
    Kang J., Gocke C.B., Yu H.
    BMC Biochem. 7:5-5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-391, MUTAGENESIS OF LYS-391 AND SER-396.
  19. "MEF2C haploinsufficiency caused by either microdeletion of the 5q14.3 region or mutation is responsible for severe mental retardation with stereotypic movements, epilepsy and/or cerebral malformations."
    Le Meur N., Holder-Espinasse M., Jaillard S., Goldenberg A., Joriot S., Amati-Bonneau P., Guichet A., Barth M., Charollais A., Journel H., Auvin S., Boucher C., Kerckaert J.P., David V., Manouvrier-Hanu S., Saugier-Veber P., Frebourg T., Dubourg C., Andrieux J., Bonneau D.
    J. Med. Genet. 47:22-29(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRD20.

Entry informationi

Entry nameiMEF2C_HUMAN
AccessioniPrimary (citable) accession number: Q06413
Secondary accession number(s): C9JMZ0, D7F7N5, F8W7V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.