MEF2A
entrez
4205
canonical
uniprot
Q02078
canonical
ensembl
ENSG00000068305
resolver
ensp
ENSP00000337202
resolver
ensp
ENSP00000346389
resolver
ensp
ENSP00000399460
resolver
ensp
ENSP00000453095
resolver
ensp
ENSP00000453441
resolver
ensp
ENSP00000454120
resolver
ensp
ENSP00000509137
resolver
ensp
ENSP00000509537
resolver
ensp
ENSP00000509700
resolver
ensp
ENSP00000516195
resolver
ensp
ENSP00000559183
resolver
ensp
ENSP00000559185
resolver
ensp
ENSP00000559186
resolver
ensp
ENSP00000559187
resolver
ensp
ENSP00000559188
resolver
ensp
ENSP00000559189
resolver
ensp
ENSP00000559190
resolver
ensp
ENSP00000559191
resolver
ensp
ENSP00000559192
resolver
ensp
ENSP00000559193
resolver
ensp
ENSP00000559194
resolver
ensp
ENSP00000559195
resolver
ensp
ENSP00000559196
resolver
ensp
ENSP00000559197
resolver
ensp
ENSP00000559198
resolver
ensp
ENSP00000559200
resolver
ensp
ENSP00000559203
resolver
ensp
ENSP00000559204
resolver
ensp
ENSP00000559205
resolver
ensp
ENSP00000559206
resolver
ensp
ENSP00000559207
resolver
ensp
ENSP00000559209
resolver
ensp
ENSP00000559212
resolver
ensp
ENSP00000559214
resolver
ensp
ENSP00000559217
resolver
ensp
ENSP00000559218
resolver
ensp
ENSP00000559219
resolver
ensp
ENSP00000559220
resolver
ensp
ENSP00000559221
resolver
ensp
ENSP00000598394
resolver
ensp
ENSP00000617038
resolver
ensp
ENSP00000617041
resolver
ensp
ENSP00000617046
resolver
ensp
ENSP00000617047
resolver
ensp
ENSP00000617048
resolver
ensp
ENSP00000617049
resolver
ensp
ENSP00000617053
resolver
ensp
ENSP00000617057
resolver
ensp
ENSP00000617058
resolver
ensp
ENSP00000617059
resolver
ensp
ENSP00000617060
resolver
ensp
ENSP00000617063
resolver
ensp
ENSP00000617066
resolver
ensp
ENSP00000617074
resolver
ensp
ENSP00000617076
resolver
ensp
ENSP00000617081
resolver
ensp
ENSP00000617086
resolver
ensp
ENSP00000792423
resolver
ensp
ENSP00000792424
resolver
enst
ENST00000338042
resolver
enst
ENST00000690055
resolver
enst
ENST00000705985
resolver
enst
ENST00000889144
resolver
enst
ENST00000946979
resolver
genesymbol
MEF2A
resolver
genesymbol_syn
MEF2
resolver
hgnc
HGNC:6993
resolver
uniprot
A0A0S2Z417
resolver
uniprot
A0A0S2Z453
resolver
uniprot
A0A0S2Z454
resolver
uniprot
A0A0S2Z4C8
resolver
uniprot
A0A0S2Z4N0
resolver
uniprot
A0A8I5KVQ4
resolver
uniprot
A8K720
resolver
uniprot
B4DFQ7
resolver
uniprot
F6XG23
resolver
uniprot
O43814
resolver
uniprot
Q14223
resolver
uniprot
Q14224
resolver
uniprot
Q59GX4
resolver
uniprot
Q7Z6C9
resolver
uniprot
Q96D14
resolver
uniprot_entry
A0A0S2Z417_HUMAN
resolver
uniprot_entry
A0A0S2Z453_HUMAN
resolver
uniprot_entry
A0A0S2Z454_HUMAN
resolver
uniprot_entry
A0A0S2Z4C8_HUMAN
resolver
uniprot_entry
A0A0S2Z4N0_HUMAN
resolver
uniprot_entry
A0A8I5KVQ4_HUMAN
resolver
uniprot_entry
A8K720_HUMAN
resolver
uniprot_entry
MEF2A_HUMAN
resolver
uniprot_sec
B4DFQ7
resolver
uniprot_sec
F6XG23
resolver
uniprot_sec
O43814
resolver
uniprot_sec
Q14223
resolver
uniprot_sec
Q14224
resolver
uniprot_sec
Q59GX4
resolver
uniprot_sec
Q7Z6C9
resolver
uniprot_sec
Q96D14
resolver
amino_acid_sequence
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT
uniprot
proteins
disease_involvement
DISEASE: Coronary artery disease, autosomal dominant, 1 (ADCAD1) [MIM:608320]: A common heart disease characterized by reduced or absent blood flow in one or more of the arteries that encircle and supply the heart. Its most important complication is acute myocardial infarction. Note=The disease is caused by variants affecting the gene represented in this entry.
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. {ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15834131, ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:16484498, ECO:0000269|PubMed:16563226, ECO:0000269|PubMed:21468593, ECO:0000269|PubMed:9858528}.
uniprot
proteins
mass_dalton
54811
uniprot
proteins
mutagenesis
MUTAGEN 176; /note="D->A: Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3."; /evidence="ECO:0000269|PubMed:11904443"; MUTAGEN 213; /note="D->A: Abolishes cleavage at sites 2 and 3 by caspase 7."; /evidence="ECO:0000269|PubMed:11904443"; MUTAGEN 255; /note="S->A: Slightly increased MEF2A protein level."; /evidence="ECO:0000269|PubMed:12586839"; MUTAGEN 255; /note="S->D: Decreased MEF2A protein level."; /evidence="ECO:0000269|PubMed:12586839"; MUTAGEN 269; /note="R->A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-270."; /evidence="ECO:0000269|PubMed:10330143"; MUTAGEN 270; /note="K->A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-269."; /evidence="ECO:0000269|PubMed:10330143"; MUTAGEN 273; /note="L->A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-275."; /evidence="ECO:0000269|PubMed:10330143"; MUTAGEN 275; /note="V->A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-273."; /evidence="ECO:0000269|PubMed:10330143"; MUTAGEN 277; /note="I->A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-278."; /evidence="ECO:0000269|PubMed:10330143"; MUTAGEN 278; /note="P->A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-277."; /evidence="ECO:0000269|PubMed:10330143"; MUTAGEN 312; /note="T->A: Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation; when associated with A-319."; /evidence="ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:9858528"; MUTAGEN 319; /note="T->A: Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation; when associated with A-312."; /evidence="ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:9858528"; MUTAGEN 355; /note="S->A: No effect on p38-mediated transcriptional activity."; /evidence="ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:9858528"; MUTAGEN 387; /note="S->A: No effect on p38-mediated phosphorylation."; MUTAGEN 403; /note="K->R: Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression."; /evidence="ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:16563226"; MUTAGEN 408; /note="S->A: Loss of sumoylation."; /evidence="ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:16371476"; MUTAGEN 408; /note="S->D: Rescues sumoylation."; /evidence="ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:16371476"; MUTAGEN 453; /note="S->A: No effect on p38-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:9858528"; MUTAGEN 479; /note="S->A: No effect on p38-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:9858528
uniprot
proteins
post_translational_modification
PTM: Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319 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-408 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF. {ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10849446, ECO:0000269|PubMed:12586839, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:15888658, ECO:0000269|PubMed:16371476, ECO:0000269|PubMed:16484498, ECO:0000269|PubMed:16563226, ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:9753748, ECO:0000269|PubMed:9858528}.; PTM: Sumoylation on Lys-403 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-408 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-403 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}.; 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. {ECO:0000269|PubMed:11904443, ECO:0000269|PubMed:15888658}.
uniprot
proteins
protein_family
MEF2 family
uniprot
proteins
pubmed
10330143
uniprot
proteins
pubmed
10487761
uniprot
proteins
pubmed
10715212
uniprot
proteins
pubmed
10835359
uniprot
proteins
pubmed
10849446
uniprot
proteins
pubmed
11904443
uniprot
proteins
pubmed
12586839
uniprot
proteins
pubmed
12691662
uniprot
proteins
pubmed
14630949
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1516833
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15496429
uniprot
proteins
pubmed
15834131
uniprot
proteins
pubmed
15888658
uniprot
proteins
pubmed
15958500
uniprot
proteins
pubmed
16371476
uniprot
proteins
pubmed
16484498
uniprot
proteins
pubmed
16563226
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
1748287
uniprot
proteins
pubmed
17785444
uniprot
proteins
pubmed
18086930
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18697823
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21468593
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
9753748
uniprot
proteins
pubmed
9858528
uniprot
proteins
sequence_length
507
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:12691662, ECO:0000269|PubMed:16563226}.
uniprot
proteins