Q02078 · MEF2A_HUMAN
- ProteinMyocyte-specific enhancer factor 2A
- GeneMEF2A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids507 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for dna binding, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 58-86 | Mef2-type | ||||
Sequence: ASTDMDKVLLKYTEYNEPHESRTNSDIVE | ||||||
Site | 176-177 | Cleavage | ||||
Sequence: DS | ||||||
Site | 213-214 | Cleavage | ||||
Sequence: DL | ||||||
Site | 466-467 | Cleavage | ||||
Sequence: DG |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyocyte-specific enhancer factor 2A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ02078
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Coronary artery disease, autosomal dominant, 1 (ADCAD1)
- Note
- DescriptionA 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.
- See alsoMIM:608320
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 176 | Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3. | ||||
Sequence: D → A | ||||||
Mutagenesis | 213 | Abolishes cleavage at sites 2 and 3 by caspase 7. | ||||
Sequence: D → A | ||||||
Mutagenesis | 255 | Slightly increased MEF2A protein level. | ||||
Sequence: S → A | ||||||
Mutagenesis | 255 | Decreased MEF2A protein level. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_038407 | 263 | in dbSNP:rs121918530 | |||
Sequence: N → S | ||||||
Mutagenesis | 269 | Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-270. | ||||
Sequence: R → A | ||||||
Mutagenesis | 270 | Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-269. | ||||
Sequence: K → A | ||||||
Mutagenesis | 273 | Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-275. | ||||
Sequence: L → A | ||||||
Mutagenesis | 275 | Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-273. | ||||
Sequence: V → A | ||||||
Mutagenesis | 277 | Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-278. | ||||
Sequence: I → A | ||||||
Mutagenesis | 278 | Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-277. | ||||
Sequence: P → A | ||||||
Natural variant | VAR_038408 | 279 | in dbSNP:rs121918529 | |||
Sequence: P → L | ||||||
Natural variant | VAR_038409 | 283 | in dbSNP:rs121918531 | |||
Sequence: G → D | ||||||
Mutagenesis | 312 | Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation; when associated with A-319. | ||||
Sequence: T → A | ||||||
Mutagenesis | 319 | Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation; when associated with A-312. | ||||
Sequence: T → A | ||||||
Mutagenesis | 355 | No effect on p38-mediated transcriptional activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 387 | No effect on p38-mediated phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 403 | Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression. | ||||
Sequence: K → R | ||||||
Mutagenesis | 408 | Loss of sumoylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 408 | Rescues sumoylation. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_017743 | 440-446 | loss of nuclear localization; 66% decrease in transcription activation; loss of synergistic activation by MEF2A and GATA1 through a dominant-negative mechanism | |||
Sequence: Missing | ||||||
Mutagenesis | 453 | No effect on p38-mediated phosphorylation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 479 | No effect on p38-mediated phosphorylation. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 475 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000199428 | 1-507 | UniProt | Myocyte-specific enhancer factor 2A | |||
Sequence: MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT | |||||||
Modified residue | 30 | UniProt | In isoform Q02078-7; Phosphoserine | ||||
Sequence: K | |||||||
Modified residue | 30 | UniProt | In isoform Q02078-8; Phosphoserine | ||||
Sequence: K | |||||||
Modified residue | 59 | UniProt | Phosphoserine; by CK2 | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | In isoform Q02078-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | In isoform Q02078-4; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | In isoform Q02078-6; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 108 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 235 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 235 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 249 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 253 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 255 | UniProt | Phosphoserine; by MAPK14 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 312 | UniProt | Phosphothreonine; by MAPK7 and MAPK14 | ||||
Sequence: T | |||||||
Modified residue | 312 | UniProt | Phosphothreonine; by NLK | ||||
Sequence: T | |||||||
Modified residue | 319 | UniProt | Phosphothreonine; by MAPK7 and MAPK14 | ||||
Sequence: T | |||||||
Modified residue | 355 | UniProt | Phosphoserine; by MAPK7 | ||||
Sequence: S | |||||||
Modified residue | 403 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 403 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Modified residue | 408 | UniProt | Phosphoserine; by CDK5 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 415 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 453 | UniProt | Phosphoserine; by MAPK | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 479 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with PIAS1; the interaction enhances sumoylation. Interacts with HDAC4, HDAC9 and SLC2A4RG. Interacts (via the N-terminal) with MAPK7; the interaction results in the phosphorylation and transcriptional activity of MEF2A
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q02078 | Myod1 P10085 | 2 | EBI-2656305, EBI-4405734 | |
XENO | Q02078 | Nfix P70257-2 | 2 | EBI-2656305, EBI-2639084 | |
BINARY | Q02078 | PITX2 Q99697-3 | 2 | EBI-2656305, EBI-1175243 | |
BINARY | Q02078-1 | SUMO1 P63165 | 3 | EBI-15799584, EBI-80140 | |
BINARY | Q02078-2 | MEOX1 P50221 | 3 | EBI-16431401, EBI-2864512 | |
BINARY | Q02078-5 | HDAC4 P56524-2 | 3 | EBI-12232917, EBI-11953488 | |
BINARY | Q02078-5 | HSF2BP O75031 | 3 | EBI-12232917, EBI-7116203 | |
BINARY | Q02078-6 | MAPK7 Q13164 | 3 | EBI-16437973, EBI-1213983 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-57 | MADS-box | ||||
Sequence: RKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQY | ||||||
Region | 173-229 | Disordered | ||||
Sequence: TLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGF | ||||||
Region | 243-270 | Disordered | ||||
Sequence: GANSLGKVMPTKSPPPPGGGNLGMNSRK | ||||||
Region | 266-283 | Required for interaction with MAPKs | ||||
Sequence: MNSRKPDLRVVIPPSSKG | ||||||
Region | 289-296 | Beta domain | ||||
Sequence: SEEEELEL | ||||||
Region | 397-507 | Disordered | ||||
Sequence: NQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT | ||||||
Compositional bias | 428-448 | Pro residues | ||||
Sequence: QQQPPPPPQPQPQPPQPQPRQ | ||||||
Compositional bias | 450-466 | Polar residues | ||||
Sequence: MGRSPVDSLSSSSSSYD |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative splicing.
Q02078-1
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.
- NameMEF2
- Length507
- Mass (Da)54,811
- Last updated1995-11-01 v1
- Checksum362BA4FBCC792CE2
Q02078-2
- NameMEFA
- Differences from canonical
- 87-132: ALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIA → TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP
Q02078-3
- NameRSRFC4
Q02078-4
- NameRSRFC9
Q02078-5
- Name5
- Differences from canonical
- 289-296: Missing
Q02078-6
- Name6
Q02078-7
- Name7
Q02078-8
- Name8
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YNI2 | H0YNI2_HUMAN | MEF2A | 38 | ||
H0YM62 | H0YM62_HUMAN | MEF2A | 85 | ||
H0YKY6 | H0YKY6_HUMAN | MEF2A | 77 | ||
A0A8I5KPE6 | A0A8I5KPE6_HUMAN | MEF2A | 436 | ||
A0A8I5KVQ4 | A0A8I5KVQ4_HUMAN | MEF2A | 511 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_046018 | 19-62 | in isoform 8 | |||
Sequence: VTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDM → TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP | ||||||
Alternative sequence | VSP_043338 | 19-86 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_046019 | 63-132 | in isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006240 | 87-132 | in isoform MEFA, isoform RSRFC9, isoform 6 and isoform 7 | |||
Sequence: ALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIA → TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGP | ||||||
Alternative sequence | VSP_006241 | 289-296 | in isoform RSRFC4, isoform RSRFC9, isoform 5, isoform 6 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006242 | 420-421 | in isoform RSRFC4 and isoform RSRFC9 | |||
Sequence: Missing | ||||||
Compositional bias | 428-448 | Pro residues | ||||
Sequence: QQQPPPPPQPQPQPPQPQPRQ | ||||||
Sequence conflict | 430 | in Ref. 4; AAB17195/AAB17196 | ||||
Sequence: Missing | ||||||
Compositional bias | 450-466 | Polar residues | ||||
Sequence: MGRSPVDSLSSSSSSYD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y16312 EMBL· GenBank· DDBJ | CAA76175.1 EMBL· GenBank· DDBJ | mRNA | ||
X63381 EMBL· GenBank· DDBJ | CAA44979.1 EMBL· GenBank· DDBJ | mRNA | ||
X68503 EMBL· GenBank· DDBJ | CAA48516.1 EMBL· GenBank· DDBJ | mRNA | ||
X68505 EMBL· GenBank· DDBJ | CAA48517.1 EMBL· GenBank· DDBJ | mRNA | ||
U49020 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U44889 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49012 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49013 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49015 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49016 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49017 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49018 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49019 EMBL· GenBank· DDBJ | AAB17195.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49020 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U44889 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49012 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49013 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49015 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49016 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49017 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49018 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U49019 EMBL· GenBank· DDBJ | AAB17196.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK294207 EMBL· GenBank· DDBJ | BAG57518.1 EMBL· GenBank· DDBJ | mRNA | ||
AB208985 EMBL· GenBank· DDBJ | BAD92222.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC015660 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC022692 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC103967 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC013437 EMBL· GenBank· DDBJ | AAH13437.1 EMBL· GenBank· DDBJ | mRNA | ||
BC053871 EMBL· GenBank· DDBJ | AAH53871.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |