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Q8CFN5

- MEF2C_MOUSE

UniProt

Q8CFN5 - MEF2C_MOUSE

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
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    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. protein binding Source: IntAct
    10. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    11. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
    12. RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Source: UniProtKB
    13. RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
    14. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
    15. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    16. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
    17. sequence-specific DNA binding Source: UniProtKB
    18. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    19. sequence-specific DNA binding transcription factor activity Source: MGI
    20. 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

    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.

    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

    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. 1 Publication
    Mutagenesisi59 – 602ST → DD: Enhanced DNA binding activity. 1 Publication
    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

    ArrayExpressiQ8CFN5.
    BgeeiQ8CFN5.
    CleanExiMM_MEF2C.
    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.
    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

    MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS    50
    TNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD 100
    PDADDSVGHS PESEDKYRKI NEDIDLMISR QRLCAVPPPS FEMPVTIPVS 150
    SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN SMSPGVTHRP PSAGNTGGLM 200
    GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS PPPMNLGMNN 250
    RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT 300
    PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW 350
    QQQHLHNMPP SALSQLGACT STHLSQSSNL SLPSTQSLSI KSEPVSPPRD 400
    RTTTPSRYPQ HTTRHEAGRS PVDSLSSCSS SYDGSDREDH RNEFHSPIGL 450
    TRPSPDERES PSVKRMRLSE GWAT 474

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    KOi K04454.
    OMAi MQHSALS.
    OrthoDBi EOG793B7D.
    PhylomeDBi Q8CFN5.
    TreeFami TF314067.

    Enzyme and pathway databases

    Reactomei REACT_215063. ERK/MAPK targets.

    Miscellaneous databases

    NextBioi 291752.
    PROi Q8CFN5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CFN5.
    Bgeei Q8CFN5.
    CleanExi MM_MEF2C.
    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

    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: October 1, 2014
    This is version 116 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