Q14814 · MEF2D_HUMAN
- ProteinMyocyte-specific enhancer factor 2D
- GeneMEF2D
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids521 (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: ASTDMDKVLLKYTEYNEPHESRTNADIIE | ||||||
Site | 288-289 | Cleavage | ||||
Sequence: DH |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyocyte-specific enhancer factor 2D
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14814
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 180 | Abolishes MAPK7- and EGF-mediated transcriptional activation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 286 | Same transcriptional activity as for isoforms with beta domain. | ||||
Sequence: T → A | ||||||
Mutagenesis | 287 | Abolishes transcriptional activity; when associated with N-288 and N-291. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 288 | Abolishes cleavage by caspase 7. | ||||
Sequence: D → A | ||||||
Mutagenesis | 288 | Abolishes transcriptional activity; when associated with Q-287 and N-291. | ||||
Sequence: D → N | ||||||
Mutagenesis | 289 | Same transcriptional activity as for isoforms with beta domain. | ||||
Sequence: H → A | ||||||
Mutagenesis | 291 | Abolishes transcriptional activity; when associated with Q-287 and N-288. | ||||
Sequence: D → N | ||||||
Natural variant | VAR_022155 | 434 | in dbSNP:rs2274315 | |||
Sequence: P → S | ||||||
Mutagenesis | 437 | No effect on MAPK7- or EGF-mediated transcriptional activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 438 | Abolishes K-439 sumoylation. | ||||
Sequence: I → A | ||||||
Mutagenesis | 439 | Abolishes sumoylation and acetylation. | ||||
Sequence: K → R | ||||||
Mutagenesis | 444 | Abolishes K-439 sumoylation. Reduced neurotoxin-induced apoptosis of neuronal cells. More resistant to degradation. | ||||
Sequence: S → A | ||||||
Mutagenesis | 444 | No effect on K-439 sumoylation. | ||||
Sequence: S → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 479 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000199435 | 1-521 | UniProt | Myocyte-specific enhancer factor 2D | |||
Sequence: MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSTVPAPNFAMPVTVPVSNQSSLQFSNPSGSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGGDLNSANGACPSPVGNGYVSARASPGLLPVANGNSLNKVIPAKSPPPPTHSTQLGAPSRKPDLRVITSQAGKGLMHHLTEDHLDLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFSSMPTAYNTDYQLTSAELSSLPAFSSPGGLSLGNVTAWQQPQQPQQPQQPQPPQQQPPQPQQPQPQQPQQPQQPPQQQSHLVPVSLSNLIPGSPLPHVGAALTVTTHPHISIKSEPVSPSRERSPAPPPPAVFPAARPEPGDGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK | |||||||
Modified residue | 98 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 106 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 110 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 121 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 180 | UniProt | Phosphoserine; by MAPK7 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 180 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 190 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 219 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 231 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 242 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 245 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 251 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 439 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 439 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Modified residue | 444 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 444 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 450 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 472 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 508 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Gene expression databases
Organism-specific databases
Interaction
Subunit
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 HDAC4 (in undifferentiating cells); the interaction translocates MEF2D to nuclear dots. Forms a heterodimer with MEF2A. Interacts with MAPK7; the interaction phosphorylates but does not activate MEF2D (By similarity).
Interacts with CCAR2 and HDAC3
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-57 | MADS-box | ||||
Sequence: RKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQY | ||||||
Compositional bias | 174-196 | Polar residues | ||||
Sequence: TDPRLLSPQQPALQRNSVSPGLP | ||||||
Region | 174-207 | Disordered | ||||
Sequence: TDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLG | ||||||
Region | 244-266 | Disordered | ||||
Sequence: NKVIPAKSPPPPTHSTQLGAPSR | ||||||
Region | 286-292 | Beta domain | ||||
Sequence: TEDHLDL | ||||||
Region | 357-407 | Disordered | ||||
Sequence: SLGNVTAWQQPQQPQQPQQPQPPQQQPPQPQQPQPQQPQQPQQPPQQQSHL | ||||||
Compositional bias | 371-398 | Pro residues | ||||
Sequence: QQPQQPQPPQQQPPQPQQPQPQQPQQPQ | ||||||
Region | 437-521 | Disordered | ||||
Sequence: SIKSEPVSPSRERSPAPPPPAVFPAARPEPGDGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK | ||||||
Compositional bias | 447-462 | Pro residues | ||||
Sequence: RERSPAPPPPAVFPAA |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
Q14814-1
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.
- NameMEF2DAB
- Length521
- Mass (Da)55,938
- Last updated1997-11-01 v1
- Checksum5C9790AD598619BA
Q14814-2
- NameMEF2DA'B
- Differences from canonical
- 87-132: TLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYG → ALHKKHRECESPEVDEVFALTPQTEEKYKKIDEEFDKMMQSYRLA
Q14814-3
- NameMEF2D0B
- Differences from canonical
- 87-132: Missing
Q14814-4
- NameMEF2DA0
- Differences from canonical
- 286-292: Missing
Q14814-5
- NameMEF2DA'0
Q14814-6
- NameMEF2D00
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q05BX2 | Q05BX2_HUMAN | MEF2D | 139 | ||
A0A0G2JLL8 | A0A0G2JLL8_HUMAN | MEF2D | 10 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_006251 | 87-132 | in isoform MEF2D0B and isoform MEF2D00 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006250 | 87-132 | in isoform MEF2DA'B and isoform MEF2DA'0 | |||
Sequence: TLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYG → ALHKKHRECESPEVDEVFALTPQTEEKYKKIDEEFDKMMQSYRLA | ||||||
Compositional bias | 174-196 | Polar residues | ||||
Sequence: TDPRLLSPQQPALQRNSVSPGLP | ||||||
Alternative sequence | VSP_006252 | 286-292 | in isoform MEF2DA0, isoform MEF2DA'0 and isoform MEF2D00 | |||
Sequence: Missing | ||||||
Compositional bias | 371-398 | Pro residues | ||||
Sequence: QQPQQPQPPQQQPPQPQQPQPQQPQQPQ | ||||||
Compositional bias | 447-462 | Pro residues | ||||
Sequence: RERSPAPPPPAVFPAA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L16794 EMBL· GenBank· DDBJ | AAA93194.1 EMBL· GenBank· DDBJ | mRNA | ||
L16795 EMBL· GenBank· DDBJ | AAA59579.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL139412 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471121 EMBL· GenBank· DDBJ | EAW52948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW52952.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC040949 EMBL· GenBank· DDBJ | AAH40949.1 EMBL· GenBank· DDBJ | mRNA | ||
BC054520 EMBL· GenBank· DDBJ | AAH54520.1 EMBL· GenBank· DDBJ | mRNA |