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Protein

Myocyte-specific enhancer factor 2C

Gene

MEF2C

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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).By similarity

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

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2C
Gene namesi
Name:MEF2C
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Myocyte-specific enhancer factor 2CPRO_0000366972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41N6-acetyllysineBy similarity
Modified residuei59 – 591Phosphoserine; by CK2By similarity
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei119 – 1191N6-acetyllysineBy similarity
Modified residuei222 – 2221PhosphoserineBy similarity
Modified residuei228 – 2281PhosphoserineBy similarity
Modified residuei234 – 2341N6-acetyllysineBy similarity
Modified residuei239 – 2391N6-acetyllysineBy similarity
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei264 – 2641N6-acetyllysineBy similarity
Modified residuei293 – 2931Phosphothreonine; by MAPK7 and MAPK14By similarity
Modified residuei300 – 3001Phosphothreonine; by MAPK7 and MAPK14By similarity
Modified residuei387 – 3871Phosphoserine; by MAPK7By similarity
Modified residuei413 – 4131PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation on Ser-59 enhances DNA binding activity.By similarity
Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity).By similarity
Proteolytically cleaved in cerebellar granule neurons, probably by caspase 7, following neurotoxicity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei400 – 4012CleavageCurated

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ2KIA0.

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 (By similarity). Interacts with HDAC7 and CARM1 (By similarity). Interacts with HDAC4 and HDAC9; the interaction with HDACs represses transcriptional activity (By similarity). Interacts with LPIN1. Interacts with MYOCD. Interacts with AKAP13 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000034894.

Structurei

3D structure databases

ProteinModelPortaliQ2KIA0.
SMRiQ2KIA0. Positions 2-93.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6161MADS-boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 2788Beta domainBy similarity

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

eggNOGiKOG0014. Eukaryota.
COG5068. LUCA.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ2KIA0.
KOiK04454.

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]

Sequencei

Sequence statusi: Complete.

Q2KIA0-1 [UniParc]FASTAAdd to basket

« 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
QQQHLHSMPP SALSQLGDRT TTPSRYPQHT RHEAGRSPVD SLSSCSSSYD
410 420 430 440
GSDREDHRNE FHSPIGLTRP SPDERESPSV KRMRLSEGWA T
Length:441
Mass (Da):47,844
Last modified:March 7, 2006 - v1
Checksum:i02883079B0800494
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112715 mRNA. Translation: AAI12716.1.
RefSeqiNP_001039578.1. NM_001046113.1.
UniGeneiBt.6869.

Genome annotation databases

GeneIDi512254.
KEGGibta:512254.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112715 mRNA. Translation: AAI12716.1.
RefSeqiNP_001039578.1. NM_001046113.1.
UniGeneiBt.6869.

3D structure databases

ProteinModelPortaliQ2KIA0.
SMRiQ2KIA0. Positions 2-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000034894.

Proteomic databases

PaxDbiQ2KIA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi512254.
KEGGibta:512254.

Organism-specific databases

CTDi4208.

Phylogenomic databases

eggNOGiKOG0014. Eukaryota.
COG5068. LUCA.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ2KIA0.
KOiK04454.

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

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.

Entry informationi

Entry nameiMEF2C_BOVIN
AccessioniPrimary (citable) accession number: Q2KIA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 7, 2006
Last modified: July 6, 2016
This is version 82 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.