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Q8CFN5

- MEF2C_MOUSE

UniProt

Q8CFN5 - MEF2C_MOUSE

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Protein

Myocyte-specific enhancer factor 2C

Gene

Mef2c

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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.By similarity7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei433 – 4342CleavageCurated

Regions

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

GO - Molecular functioni

  1. AT DNA binding Source: Ensembl
  2. chromatin binding Source: MGI
  3. core promoter proximal region sequence-specific DNA binding Source: MGI
  4. core promoter sequence-specific DNA binding Source: UniProtKB
  5. DNA binding Source: MGI
  6. histone deacetylase binding Source: BHF-UCL
  7. HMG box domain binding Source: UniProtKB
  8. miRNA binding Source: UniProtKB
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  10. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
  11. RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Source: UniProtKB
  12. RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
  13. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
  14. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  15. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  16. sequence-specific DNA binding Source: UniProtKB
  17. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  18. sequence-specific DNA binding transcription factor activity Source: MGI
  19. transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. B cell homeostasis Source: UniProtKB
  3. B cell proliferation Source: UniProtKB
  4. B cell receptor signaling pathway Source: UniProtKB
  5. blood vessel development Source: MGI
  6. blood vessel remodeling Source: MGI
  7. cardiac muscle cell differentiation Source: UniProtKB
  8. cardiac muscle hypertrophy in response to stress Source: MGI
  9. cardiac ventricle formation Source: UniProtKB
  10. cartilage morphogenesis Source: MGI
  11. cell fate commitment Source: MGI
  12. cell morphogenesis involved in neuron differentiation Source: Alzheimers_University_of_Toronto
  13. cellular response to calcium ion Source: UniProtKB
  14. cellular response to drug Source: UniProtKB
  15. cellular response to fluid shear stress Source: UniProtKB
  16. cellular response to glucose stimulus Source: Ensembl
  17. cellular response to lipopolysaccharide Source: UniProtKB
  18. cellular response to parathyroid hormone stimulus Source: UniProtKB
  19. cellular response to retinoic acid Source: Ensembl
  20. cellular response to transforming growth factor beta stimulus Source: UniProtKB
  21. cellular response to trichostatin A Source: UniProtKB
  22. chondrocyte differentiation Source: MGI
  23. dentate gyrus development Source: Ensembl
  24. embryonic skeletal system morphogenesis Source: MGI
  25. embryonic viscerocranium morphogenesis Source: MGI
  26. endochondral ossification Source: MGI
  27. epithelial cell proliferation involved in renal tubule morphogenesis Source: UniProtKB
  28. germinal center formation Source: UniProtKB
  29. glomerulus morphogenesis Source: UniProtKB
  30. heart development Source: MGI
  31. heart looping Source: UniProtKB
  32. humoral immune response Source: UniProtKB
  33. learning or memory Source: UniProtKB
  34. MAPK cascade Source: UniProtKB
  35. melanocyte differentiation Source: UniProtKB
  36. monocyte differentiation Source: MGI
  37. muscle cell fate determination Source: MGI
  38. myotube differentiation Source: Ensembl
  39. negative regulation of epithelial cell proliferation Source: UniProtKB
  40. negative regulation of gene expression Source: UniProtKB
  41. negative regulation of neuron apoptotic process Source: UniProtKB
  42. negative regulation of ossification Source: UniProtKB
  43. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  44. nephron tubule epithelial cell differentiation Source: UniProtKB
  45. neural crest cell differentiation Source: UniProtKB
  46. neuron development Source: UniProtKB
  47. neuron differentiation Source: UniProtKB
  48. neuron migration Source: Alzheimers_University_of_Toronto
  49. osteoblast differentiation Source: UniProtKB
  50. outflow tract morphogenesis Source: MGI
  51. palate development Source: MGI
  52. platelet formation Source: UniProtKB
  53. positive regulation of alkaline phosphatase activity Source: UniProtKB
  54. positive regulation of B cell proliferation Source: UniProtKB
  55. positive regulation of behavioral fear response Source: UniProtKB
  56. positive regulation of bone mineralization Source: UniProtKB
  57. positive regulation of cardiac muscle cell differentiation Source: UniProtKB
  58. positive regulation of cardiac muscle cell proliferation Source: UniProtKB
  59. positive regulation of cardiac muscle hypertrophy Source: Ensembl
  60. positive regulation of cell proliferation in bone marrow Source: MGI
  61. positive regulation of gene expression Source: UniProtKB
  62. positive regulation of macrophage apoptotic process Source: UniProtKB
  63. positive regulation of MAP kinase activity Source: Alzheimers_University_of_Toronto
  64. positive regulation of myoblast differentiation Source: UniProtKB
  65. positive regulation of neuron differentiation Source: UniProtKB
  66. positive regulation of osteoblast differentiation Source: UniProtKB
  67. positive regulation of protein homodimerization activity Source: MGI
  68. positive regulation of skeletal muscle cell differentiation Source: Ensembl
  69. positive regulation of skeletal muscle tissue development Source: UniProtKB
  70. positive regulation of transcription, DNA-templated Source: UniProtKB
  71. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  72. primary heart field specification Source: UniProtKB
  73. regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: Alzheimers_University_of_Toronto
  74. regulation of dendritic spine development Source: Alzheimers_University_of_Toronto
  75. regulation of excitatory postsynaptic membrane potential Source: Alzheimers_University_of_Toronto
  76. regulation of germinal center formation Source: UniProtKB
  77. regulation of megakaryocyte differentiation Source: UniProtKB
  78. regulation of neuron apoptotic process Source: Alzheimers_University_of_Toronto
  79. regulation of neurotransmitter secretion Source: Alzheimers_University_of_Toronto
  80. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: Alzheimers_University_of_Toronto
  81. regulation of sarcomere organization Source: MGI
  82. regulation of synapse assembly Source: Alzheimers_University_of_Toronto
  83. regulation of synaptic activity Source: UniProtKB
  84. regulation of synaptic plasticity Source: Alzheimers_University_of_Toronto
  85. regulation of synaptic transmission, glutamatergic Source: Alzheimers_University_of_Toronto
  86. regulation of transcription, DNA-templated Source: MGI
  87. renal tubule morphogenesis Source: UniProtKB
  88. response to ischemia Source: Alzheimers_University_of_Toronto
  89. response to virus Source: Ensembl
  90. response to vitamin E Source: Ensembl
  91. secondary heart field specification Source: UniProtKB
  92. sinoatrial valve morphogenesis Source: UniProtKB
  93. skeletal muscle cell differentiation Source: UniProtKB
  94. skeletal muscle tissue development Source: MGI
  95. smooth muscle cell differentiation Source: MGI
  96. ventricular cardiac muscle cell differentiation Source: UniProtKB
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_215063. ERK/MAPK targets.
REACT_258600. CDO in myogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2C
Gene namesi
Name:Mef2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:99458. Mef2c.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Alzheimers_University_of_Toronto
  3. nuclear speck Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. protein complex Source: UniProtKB
  6. sarcomere Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31R → T: Increased mobility in differentiating cells. Greatly reduced DNA binding. 1 Publication
Mutagenesisi4 – 41K → Q: 7-fold increase in DNA binding. 1 Publication
Mutagenesisi4 – 41K → R: Reduced acetylation by 30%. Some loss of DNA binding and transactivation activity. 1 Publication
Mutagenesisi59 – 602ST → CR: Reduced DNA binding activity.
Mutagenesisi59 – 602ST → DD: Enhanced DNA binding activity.
Mutagenesisi59 – 591S → A: Reduced DNA binding activity. 1 Publication
Mutagenesisi59 – 591S → D: Enhanced DNA binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Myocyte-specific enhancer factor 2CPRO_0000199434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41N6-acetyllysine1 Publication
Modified residuei59 – 591Phosphoserine; by CK21 Publication
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei119 – 1191N6-acetyllysineBy similarity
Modified residuei234 – 2341N6-acetyllysineBy similarity
Modified residuei239 – 2391N6-acetyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei264 – 2641N6-acetyllysineBy similarity
Modified residuei293 – 2931Phosphothreonine; by MAPK14By similarity
Modified residuei300 – 3001Phosphothreonine; by MAPK14By similarity
Cross-linki391 – 391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei396 – 3961Phosphoserine; by CDK5By similarity
Modified residuei420 – 4201Phosphoserine; by MAPK7By similarity

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 similarity1 Publication
Acetylated by p300 on several sites in diffentiating myocytes (By similarity). Acetylation on Lys-4 increases DNA binding and transactivation.By similarity1 Publication
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).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8CFN5.
PaxDbiQ8CFN5.
PRIDEiQ8CFN5.

PTM databases

PhosphoSiteiQ8CFN5.

Expressioni

Tissue specificityi

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.6 Publications

Developmental stagei

Expressed in developing endothelial cells and smooth muscle cells, as well as in surrounding mesenchyme, during embryogenesis. Up-regulated during myogenesis.1 Publication

Gene expression databases

BgeeiQ8CFN5.
CleanExiMM_MEF2C.
ExpressionAtlasiQ8CFN5. baseline and differential.
GenevestigatoriQ8CFN5.

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 LPIN1. Interacts with MYOCD.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AclyQ91V923EBI-643822,EBI-644049

Protein-protein interaction databases

BioGridi201383. 10 interactions.
DIPiDIP-49524N.
IntActiQ8CFN5. 6 interactions.
MINTiMINT-1551742.

Structurei

3D structure databases

ProteinModelPortaliQ8CFN5.
SMRiQ8CFN5. 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 domainBy similarity
Regioni368 – 39932Transcription repressorBy similarityAdd
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.
InParanoidiQ8CFN5.
KOiK04454.
OMAiMQHSALS.
OrthoDBiEOG793B7D.
PhylomeDBiQ8CFN5.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q8CFN5-1) [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 QRLCAVPPPS FEMPVTIPVS
160 170 180 190 200
SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN SMSPGVTHRP PSAGNTGGLM
210 220 230 240 250
GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS 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 SLPSTQSLSI KSEPVSPPRD
410 420 430 440 450
RTTTPSRYPQ HTTRHEAGRS PVDSLSSCSS SYDGSDREDH RNEFHSPIGL
460 470
TRPSPDERES PSVKRMRLSE GWAT

Note: No experimental confirmation available.

Length:474
Mass (Da):51,278
Last modified:January 4, 2005 - v2
Checksum:iCEFC2DB21E89632A
GO
Isoform 2 (identifier: Q8CFN5-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:466
Mass (Da):50,393
Checksum:iF06A89C9ACD779AE
GO
Isoform 3 (identifier: Q8CFN5-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:442
Mass (Da):47,956
Checksum:i40EFBF02BF3E775C
GO
Isoform 4 (identifier: Q8CFN5-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:432
Mass (Da):46,961
Checksum:iDCB2EBCE61A35215
GO
Isoform 5 (identifier: Q8CFN5-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:472
Mass (Da):51,168
Checksum:i1B618AB137809260
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411F → L in AAH37731. (PubMed:15489334)Curated
Sequence conflicti211 – 2111S → P(PubMed:8506376)Curated
Sequence conflicti428 – 4281C → S(PubMed:8506376)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei87 – 9711TLRKKGLNGCD → ALNKKENKGSE in isoform 4 and isoform 5. 2 PublicationsVSP_012501Add
BLAST
Alternative sequencei103 – 11816ADDSV…EDKYR → SSYALTPRTEEKYK in isoform 4 and isoform 5. 2 PublicationsVSP_012502Add
BLAST
Alternative sequencei123 – 13412DIDLM…RQRLC → EFDNMIKSHKIP in isoform 4 and isoform 5. 2 PublicationsVSP_012503Add
BLAST
Alternative sequencei271 – 2788Missing in isoform 2 and isoform 4. 2 PublicationsVSP_012504
Alternative sequencei368 – 39932Missing in isoform 3 and isoform 4. 2 PublicationsVSP_012505Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009139 mRNA. Translation: BAB26099.1.
BC026841 mRNA. Translation: AAH26841.1.
BC037731 mRNA. Translation: AAH37731.1.
BC057650 mRNA. Translation: AAH57650.1.
CCDSiCCDS26664.1. [Q8CFN5-4]
CCDS49320.1. [Q8CFN5-2]
RefSeqiNP_079558.1. NM_025282.3. [Q8CFN5-4]
XP_006517183.1. XM_006517120.1. [Q8CFN5-1]
XP_006517184.1. XM_006517121.1. [Q8CFN5-1]
XP_006517185.1. XM_006517122.1. [Q8CFN5-1]
XP_006517186.1. XM_006517123.1. [Q8CFN5-1]
XP_006517187.1. XM_006517124.1. [Q8CFN5-1]
XP_006517188.1. XM_006517125.1. [Q8CFN5-1]
XP_006517189.1. XM_006517126.1. [Q8CFN5-5]
XP_006517192.1. XM_006517129.1. [Q8CFN5-3]
XP_006517195.1. XM_006517132.1. [Q8CFN5-4]
UniGeneiMm.24001.
Mm.451574.
Mm.487610.

Genome annotation databases

EnsembliENSMUST00000005722; ENSMUSP00000005722; ENSMUSG00000005583. [Q8CFN5-4]
ENSMUST00000163888; ENSMUSP00000132547; ENSMUSG00000005583. [Q8CFN5-2]
ENSMUST00000185052; ENSMUSP00000138826; ENSMUSG00000005583. [Q8CFN5-3]
GeneIDi17260.
KEGGimmu:17260.
UCSCiuc007rie.2. mouse. [Q8CFN5-4]
uc007rih.2. mouse. [Q8CFN5-5]
uc007rii.3. mouse. [Q8CFN5-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009139 mRNA. Translation: BAB26099.1 .
BC026841 mRNA. Translation: AAH26841.1 .
BC037731 mRNA. Translation: AAH37731.1 .
BC057650 mRNA. Translation: AAH57650.1 .
CCDSi CCDS26664.1. [Q8CFN5-4 ]
CCDS49320.1. [Q8CFN5-2 ]
RefSeqi NP_079558.1. NM_025282.3. [Q8CFN5-4 ]
XP_006517183.1. XM_006517120.1. [Q8CFN5-1 ]
XP_006517184.1. XM_006517121.1. [Q8CFN5-1 ]
XP_006517185.1. XM_006517122.1. [Q8CFN5-1 ]
XP_006517186.1. XM_006517123.1. [Q8CFN5-1 ]
XP_006517187.1. XM_006517124.1. [Q8CFN5-1 ]
XP_006517188.1. XM_006517125.1. [Q8CFN5-1 ]
XP_006517189.1. XM_006517126.1. [Q8CFN5-5 ]
XP_006517192.1. XM_006517129.1. [Q8CFN5-3 ]
XP_006517195.1. XM_006517132.1. [Q8CFN5-4 ]
UniGenei Mm.24001.
Mm.451574.
Mm.487610.

3D structure databases

ProteinModelPortali Q8CFN5.
SMRi Q8CFN5. Positions 2-73.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201383. 10 interactions.
DIPi DIP-49524N.
IntActi Q8CFN5. 6 interactions.
MINTi MINT-1551742.

PTM databases

PhosphoSitei Q8CFN5.

Proteomic databases

MaxQBi Q8CFN5.
PaxDbi Q8CFN5.
PRIDEi Q8CFN5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005722 ; ENSMUSP00000005722 ; ENSMUSG00000005583 . [Q8CFN5-4 ]
ENSMUST00000163888 ; ENSMUSP00000132547 ; ENSMUSG00000005583 . [Q8CFN5-2 ]
ENSMUST00000185052 ; ENSMUSP00000138826 ; ENSMUSG00000005583 . [Q8CFN5-3 ]
GeneIDi 17260.
KEGGi mmu:17260.
UCSCi uc007rie.2. mouse. [Q8CFN5-4 ]
uc007rih.2. mouse. [Q8CFN5-5 ]
uc007rii.3. mouse. [Q8CFN5-3 ]

Organism-specific databases

CTDi 4208.
MGIi MGI:99458. Mef2c.

Phylogenomic databases

eggNOGi COG5068.
GeneTreei ENSGT00390000011828.
HOGENOMi HOG000230620.
HOVERGENi HBG053944.
InParanoidi Q8CFN5.
KOi K04454.
OMAi MQHSALS.
OrthoDBi EOG793B7D.
PhylomeDBi Q8CFN5.
TreeFami TF314067.

Enzyme and pathway databases

Reactomei REACT_215063. ERK/MAPK targets.
REACT_258600. CDO in myogenesis.

Miscellaneous databases

NextBioi 291752.
PROi Q8CFN5.
SOURCEi Search...

Gene expression databases

Bgeei Q8CFN5.
CleanExi MM_MEF2C.
ExpressionAtlasi Q8CFN5. baseline and differential.
Genevestigatori Q8CFN5.

Family and domain databases

InterProi IPR022102. HJURP_C.
IPR002100. TF_MADSbox.
[Graphical view ]
Pfami PF12347. HJURP_C. 1 hit.
PF00319. SRF-TF. 1 hit.
[Graphical view ]
PRINTSi PR00404. MADSDOMAIN.
SMARTi SM00432. MADS. 1 hit.
[Graphical view ]
SUPFAMi SSF55455. SSF55455. 1 hit.
PROSITEi PS00350. MADS_BOX_1. 1 hit.
PS50066. MADS_BOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  17. 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.

Entry informationi

Entry nameiMEF2C_MOUSE
AccessioniPrimary (citable) accession number: Q8CFN5
Secondary accession number(s): Q8R0H1, Q9D7L0, Q9QW20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: November 26, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3