Mef2a
entrez
309957
canonical
uniprot
Q2MJT0
canonical
ensembl
ENSRNOG00000047756
resolver
ensp
ENSRNOP00000064552
resolver
ensp
ENSRNOP00000065122
resolver
ensp
ENSRNOP00000068690
resolver
ensp
ENSRNOP00000094055
resolver
enst
ENSRNOT00000070864
resolver
enst
ENSRNOT00000072915
resolver
enst
ENSRNOT00000089723
resolver
enst
ENSRNOT00000113672
resolver
genesymbol
Mef2a
resolver
uniprot
A0A0G2JSZ4
resolver
uniprot
A0A0G2JTF4
resolver
uniprot
A0A8I6AYJ3
resolver
uniprot
A0ACM8QM28
resolver
uniprot
D8X2M2
resolver
uniprot
M0R6R7
resolver
uniprot
Q66HD7
resolver
uniprot_entry
A0A0G2JTF4_RAT
resolver
uniprot_entry
A0A8I6AYJ3_RAT
resolver
uniprot_entry
A0ACM8QM28_RAT
resolver
uniprot_entry
D8X2M2_RAT
resolver
uniprot_entry
M0R6R7_RAT
resolver
uniprot_entry
MEF2A_RAT
resolver
uniprot_sec
A0A0G2JSZ4
resolver
uniprot_sec
Q66HD7
resolver
amino_acid_sequence
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLAESSMLSPPPATLHRNVSPGAPQRPPSTGSAGGMLSTTDLTVPNGAGNGPVGNGFVDSRASPNLIGNTGANSVGKVMPTKSPPPPGGGSVGMNSRKPDLRVVIPPSSKGMMPPLNAQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFTSPGMLSLGQASAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNINIKTEPISPPRDRMTPSGFQQQQQQQPQQQPPPQPPQPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNAEDRESPSVKRMRMDTWVT
uniprot
proteins
function
FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter (By similarity). {ECO:0000250, ECO:0000269|PubMed:16484498, ECO:0000269|PubMed:17367767, ECO:0000269|PubMed:17855618}.
uniprot
proteins
mass_dalton
53254
uniprot
proteins
mutagenesis
MUTAGEN 395; /note="K->R: Abolishes sumoylation."; /evidence="ECO:0000269|PubMed:16484498"; MUTAGEN 400; /note="S->A: Abolishes K-395 sumoylation. Enhances K-395 acetylation. Enhances transcriptional activity."; /evidence="ECO:0000269|PubMed:16484498
uniprot
proteins
post_translational_modification
PTM: Constitutive phosphorylation on Ser-400 promotes Lys-395 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-400 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-395 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-304 and Thr-311 are the main sites involved in p38 MAPK signaling and activate transcription. Phosphorylated on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-400 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-304, Thr-311 and Ser-347 can be induced by EGF (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-395 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-400 is required for sumoylation. Has no effect on nuclear location nor on DNA binding. Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in the cerebellar cortex and promotes their morphogenesis (By similarity). {ECO:0000250}.; PTM: Acetylation on Lys-395 activates transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity). Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure. {ECO:0000250, ECO:0000269|PubMed:16484498}.; PTM: Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16484498
uniprot
proteins
pubmed
17367767
uniprot
proteins
pubmed
17855618
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
495
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:17367767}.
uniprot
proteins