Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myocyte-specific enhancer factor 2A

Gene

MEF2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT]4TAR-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.8 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi58 – 86Mef2-typeSequence analysisAdd BLAST29

GO - Molecular functioni

  • activating transcription factor binding Source: UniProtKB
  • chromatin binding Source: UniProtKB
  • histone acetyltransferase binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription coactivator activity Source: BHF-UCL
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • sequence-specific DNA binding Source: UniProtKB
  • SMAD binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: Ensembl
  • transcription factor activity, sequence-specific DNA binding Source: BHF-UCL

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cardiac conduction Source: UniProtKB
  • cellular response to calcium ion Source: UniProtKB
  • dendrite morphogenesis Source: UniProtKB
  • ERK5 cascade Source: UniProtKB
  • heart development Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • mitochondrial genome maintenance Source: UniProtKB
  • mitochondrion distribution Source: UniProtKB
  • muscle organ development Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of cardiac muscle hypertrophy Source: BHF-UCL
  • positive regulation of muscle cell differentiation Source: Reactome
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB
  • ventricular cardiac myofibril assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000068305-MONOMER.
ReactomeiR-HSA-198753. ERK/MAPK targets.
R-HSA-375170. CDO in myogenesis.
SignaLinkiQ02078.
SIGNORiQ02078.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocyte-specific enhancer factor 2A
Alternative name(s):
Serum response factor-like protein 1
Gene namesi
Name:MEF2A
Synonyms:MEF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:6993. MEF2A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Coronary artery disease, autosomal dominant, 1 (ADCAD1)
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:608320

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi176D → A: Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3. 1 Publication1
Mutagenesisi213D → A: Abolishes cleavage at sites 2 and 3 by caspase 7. 1 Publication1
Mutagenesisi255S → A: Slightly increased MEF2A protein level. 1 Publication1
Mutagenesisi255S → D: Decreased MEF2A protein level. 1 Publication1
Mutagenesisi269R → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-270. 1 Publication1
Mutagenesisi270K → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-269. 1 Publication1
Mutagenesisi273L → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-275. 1 Publication1
Mutagenesisi275V → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-273. 1 Publication1
Mutagenesisi277I → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-278. 1 Publication1
Mutagenesisi278P → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-277. 1 Publication1
Mutagenesisi312T → A: Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation; when associated with A-319. 2 Publications1
Mutagenesisi319T → A: Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation; when associated with A-312. 2 Publications1
Mutagenesisi355S → A: No effect on p38-mediated transcriptional activity. 2 Publications1
Mutagenesisi387S → A: No effect on p38-mediated phosphorylation. 1
Mutagenesisi403K → R: Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression. 2 Publications1
Mutagenesisi408S → A: Loss of sumoylation. 2 Publications1
Mutagenesisi408S → D: Rescues sumoylation. 2 Publications1
Mutagenesisi453S → A: No effect on p38-mediated phosphorylation. 1 Publication1
Mutagenesisi479S → A: No effect on p38-mediated phosphorylation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4205.
MalaCardsiMEF2A.
MIMi608320. phenotype.
OpenTargetsiENSG00000068305.
PharmGKBiPA30731.

Polymorphism and mutation databases

BioMutaiMEF2A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001994281 – 507Myocyte-specific enhancer factor 2AAdd BLAST507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei59Phosphoserine; by CK2By similarity1
Modified residuei98PhosphoserineCombined sources1
Modified residuei235PhosphoserineCombined sources1
Modified residuei249N6-acetyllysineCombined sources1
Modified residuei255Phosphoserine; by MAPK14Combined sources1 Publication1
Modified residuei312Phosphothreonine; by MAPK7 and MAPK145 Publications1
Modified residuei312Phosphothreonine; by NLK5 Publications1
Modified residuei319Phosphothreonine; by MAPK7 and MAPK144 Publications1
Modified residuei355Phosphoserine; by MAPK71 Publication1
Modified residuei403N6-acetyllysine; alternateBy similarity1
Cross-linki403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei408Phosphoserine; by CDK54 Publications1
Modified residuei415PhosphothreonineBy similarity1
Modified residuei453Phosphoserine; by MAPK1 Publication1
Isoform 7 (identifier: Q02078-7)
Modified residuei30PhosphoserineCombined sources1
Isoform 8 (identifier: Q02078-8)
Modified residuei30PhosphoserineCombined sources1
Isoform MEFA (identifier: Q02078-2)
Modified residuei98PhosphoserineCombined sources1
Isoform RSRFC9 (identifier: Q02078-4)
Modified residuei98PhosphoserineCombined sources1
Isoform 6 (identifier: Q02078-6)
Modified residuei98PhosphoserineCombined sources1

Post-translational modificationi

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.11 Publications
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).By similarity
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.By similarity
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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei176 – 177CleavageCurated2
Sitei213 – 214CleavageCurated2
Sitei466 – 467CleavageCurated2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ02078.
MaxQBiQ02078.
PaxDbiQ02078.
PeptideAtlasiQ02078.
PRIDEiQ02078.

PTM databases

iPTMnetiQ02078.
PhosphoSitePlusiQ02078.

Miscellaneous databases

PMAP-CutDBQ02078.

Expressioni

Tissue specificityi

Isoform MEF2 and isoform MEFA are expressed only in skeletal and cardiac muscle and in the brain. Isoform RSRFC4 and isoform RSRFC9 are expressed in all tissues examined.2 Publications

Gene expression databases

BgeeiENSG00000068305.
CleanExiHS_MEF2A.
ExpressionAtlasiQ02078. baseline and differential.
GenevisibleiQ02078. HS.

Organism-specific databases

HPAiCAB004499.
HPA046597.
HPA056563.

Interactioni

Subunit structurei

Binds DNA as a homo- or heterodimer. Dimerizes with MEF2D. Interacts with HDAC7 (By similarity). 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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PITX2Q99697-32EBI-2656305,EBI-1175243

GO - Molecular functioni

  • activating transcription factor binding Source: UniProtKB
  • histone acetyltransferase binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • SMAD binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110369. 53 interactors.
DIPiDIP-40711N.
IntActiQ02078. 36 interactors.
MINTiMINT-104848.
STRINGi9606.ENSP00000346389.

Structurei

Secondary structure

1507
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 38Combined sources25
Beta strandi42 – 48Combined sources7
Turni50 – 52Combined sources3
Beta strandi54 – 60Combined sources7
Helixi62 – 71Combined sources10
Beta strandi77 – 80Combined sources4
Helixi81 – 90Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7UNMR-A/B2-86[»]
1EGWX-ray1.50A/B/C/D2-78[»]
1LEWX-ray2.30B269-280[»]
3KOVX-ray2.90A/B/I/J2-91[»]
3MU6X-ray2.43A/B/C/D2-70[»]
3P57X-ray2.19A/B/C/D/I/J2-91[»]
ProteinModelPortaliQ02078.
SMRiQ02078.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02078.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 57MADS-boxPROSITE-ProRule annotationAdd BLAST55

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni266 – 283Required for interaction with MAPKsAdd BLAST18
Regioni289 – 296Beta domain8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 31Lys-rich (basic)Add BLAST28
Compositional biasi141 – 186Ser/Thr-richAdd BLAST46
Compositional biasi420 – 446Gln/Pro-richAdd BLAST27

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.
GeneTreeiENSGT00390000011828.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ02078.
KOiK09260.
OMAiPATLHRN.
OrthoDBiEOG091G05BY.
PhylomeDBiQ02078.
TreeFamiTF314067.

Family and domain databases

CDDicd00265. MADS_MEF2_like. 1 hit.
InterProiIPR022102. HJURP_C.
IPR033896. MADS_MEF2-like.
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]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform MEF2 (identifier: Q02078-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS
60 70 80 90 100
SNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD
110 120 130 140 150
PDTSYVLTPH TEEKYKKINE EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS
160 170 180 190 200
PNALSYTNPG SSLVSPSLAA SSTLTDSSML SPPQTTLHRN VSPGAPQRPP
210 220 230 240 250
STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG ATGANSLGKV
260 270 280 290 300
MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLSE EEELELNTQR
310 320 330 340 350
ISSSQATQPL ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL
360 370 380 390 400
QGFNSPGMLS LGQVSAWQQH HLGQAALSSL VAGGQLSQGS NLSINTNQNI
410 420 430 440 450
SIKSEPISPP RDRMTPSGFQ QQQQQQQQQQ PPPPPQPQPQ PPQPQPRQEM
460 470 480 490 500
GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP IVLGRPPNTE DRESPSVKRM

RMDAWVT
Length:507
Mass (Da):54,811
Last modified:November 1, 1995 - v1
Checksum:i362BA4FBCC792CE2
GO
Isoform MEFA (identifier: Q02078-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP

Show »
Length:505
Mass (Da):54,442
Checksum:iE0032FA6F955D7F7
GO
Isoform RSRFC4 (identifier: Q02078-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-296: Missing.
     420-421: Missing.

Show »
Length:497
Mass (Da):53,596
Checksum:iA255A8EDC8B07FB0
GO
Isoform RSRFC9 (identifier: Q02078-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP
     289-296: Missing.
     420-421: Missing.

Show »
Length:495
Mass (Da):53,227
Checksum:i3C083C4EFC3872F0
GO
Isoform 5 (identifier: Q02078-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-296: Missing.

Note: No experimental confirmation available.
Show »
Length:499
Mass (Da):53,852
Checksum:iFE3A83DDCE477C27
GO
Isoform 6 (identifier: Q02078-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP
     289-296: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:497
Mass (Da):53,483
Checksum:iF4A61D805AE448AF
GO
Isoform 7 (identifier: Q02078-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-86: Missing.
     87-132: ALNKKEHRGC...DNMMRNHKIA → TLRKKGLNGC...DSDFIFKRGP

Note: No experimental confirmation available.Combined sources
Show »
Length:437
Mass (Da):46,529
Checksum:iD28A536D0F0188BE
GO
Isoform 8 (identifier: Q02078-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-62: VTFTKRKFGL...KLFQYASTDM → TLRKKGLNGC...DSDFIFKRGP
     63-132: Missing.
     289-296: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:429
Mass (Da):45,570
Checksum:iB356416F17385FCD
GO

Sequence cautioni

The sequence AAH53871 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD92222 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti430Missing in AAB17195 (Ref. 4) Curated1
Sequence conflicti430Missing in AAB17196 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038407263N → S.1 PublicationCorresponds to variant rs121918530dbSNPEnsembl.1
Natural variantiVAR_038408279P → L.3 PublicationsCorresponds to variant rs121918529dbSNPEnsembl.1
Natural variantiVAR_038409283G → D.1 Publication1
Natural variantiVAR_017743440 – 446Missing Loss of nuclear localization; 66% decrease in transcription activation; loss of synergistic activation by MEF2A and GATA1 through a dominant-negative mechanism. 7

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04333819 – 86Missing in isoform 7. 1 PublicationAdd BLAST68
Alternative sequenceiVSP_04601819 – 62VTFTK…ASTDM → TLRKKGLNGCESPDADDYFE HSPLSEDRFSKLNEDSDFIF KRGP in isoform 8. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_04601963 – 132Missing in isoform 8. 1 PublicationAdd BLAST70
Alternative sequenceiVSP_00624087 – 132ALNKK…NHKIA → TLRKKGLNGCESPDADDYFE HSPLSEDRFSKLNEDSDFIF KRGP in isoform MEFA, isoform RSRFC9, isoform 6 and isoform 7. 5 PublicationsAdd BLAST46
Alternative sequenceiVSP_006241289 – 296Missing in isoform RSRFC4, isoform RSRFC9, isoform 5, isoform 6 and isoform 8. 5 Publications8
Alternative sequenceiVSP_006242420 – 421Missing in isoform RSRFC4 and isoform RSRFC9. 3 Publications2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16312 mRNA. Translation: CAA76175.1.
X63381 mRNA. Translation: CAA44979.1.
X68503 mRNA. Translation: CAA48516.1.
X68505 mRNA. Translation: CAA48517.1.
U49020
, U44889, U49012, U49013, U49015, U49016, U49017, U49018, U49019 Genomic DNA. Translation: AAB17195.1.
U49020
, U44889, U49012, U49013, U49015, U49016, U49017, U49018, U49019 Genomic DNA. Translation: AAB17196.1.
AK294207 mRNA. Translation: BAG57518.1.
AB208985 mRNA. Translation: BAD92222.1. Different initiation.
AC015660 Genomic DNA. No translation available.
AC022692 Genomic DNA. No translation available.
AC103967 Genomic DNA. No translation available.
BC013437 mRNA. Translation: AAH13437.1.
BC053871 mRNA. Translation: AAH53871.1. Different initiation.
CCDSiCCDS45362.1. [Q02078-5]
CCDS45363.1. [Q02078-7]
CCDS53978.1. [Q02078-6]
CCDS58401.1. [Q02078-8]
CCDS81920.1. [Q02078-2]
PIRiC39481.
S25831.
RefSeqiNP_001124399.1. NM_001130927.2. [Q02078-7]
NP_001124400.1. NM_001130928.2. [Q02078-8]
NP_001165365.1. NM_001171894.2. [Q02078-6]
NP_001306135.1. NM_001319206.1. [Q02078-2]
NP_005578.2. NM_005587.3. [Q02078-5]
XP_011519883.1. XM_011521581.2. [Q02078-1]
XP_011519884.1. XM_011521582.2. [Q02078-1]
XP_011519888.1. XM_011521586.2. [Q02078-7]
XP_016877679.1. XM_017022190.1. [Q02078-1]
XP_016877680.1. XM_017022191.1. [Q02078-1]
XP_016877682.1. XM_017022193.1. [Q02078-5]
XP_016877683.1. XM_017022194.1. [Q02078-5]
UniGeneiHs.268675.

Genome annotation databases

EnsembliENST00000338042; ENSP00000337202; ENSG00000068305. [Q02078-6]
ENST00000354410; ENSP00000346389; ENSG00000068305. [Q02078-5]
ENST00000449277; ENSP00000399460; ENSG00000068305. [Q02078-8]
ENST00000557785; ENSP00000453441; ENSG00000068305. [Q02078-6]
ENST00000557942; ENSP00000453095; ENSG00000068305. [Q02078-2]
ENST00000558812; ENSP00000454120; ENSG00000068305. [Q02078-7]
GeneIDi4205.
KEGGihsa:4205.
UCSCiuc002bve.4. human. [Q02078-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16312 mRNA. Translation: CAA76175.1.
X63381 mRNA. Translation: CAA44979.1.
X68503 mRNA. Translation: CAA48516.1.
X68505 mRNA. Translation: CAA48517.1.
U49020
, U44889, U49012, U49013, U49015, U49016, U49017, U49018, U49019 Genomic DNA. Translation: AAB17195.1.
U49020
, U44889, U49012, U49013, U49015, U49016, U49017, U49018, U49019 Genomic DNA. Translation: AAB17196.1.
AK294207 mRNA. Translation: BAG57518.1.
AB208985 mRNA. Translation: BAD92222.1. Different initiation.
AC015660 Genomic DNA. No translation available.
AC022692 Genomic DNA. No translation available.
AC103967 Genomic DNA. No translation available.
BC013437 mRNA. Translation: AAH13437.1.
BC053871 mRNA. Translation: AAH53871.1. Different initiation.
CCDSiCCDS45362.1. [Q02078-5]
CCDS45363.1. [Q02078-7]
CCDS53978.1. [Q02078-6]
CCDS58401.1. [Q02078-8]
CCDS81920.1. [Q02078-2]
PIRiC39481.
S25831.
RefSeqiNP_001124399.1. NM_001130927.2. [Q02078-7]
NP_001124400.1. NM_001130928.2. [Q02078-8]
NP_001165365.1. NM_001171894.2. [Q02078-6]
NP_001306135.1. NM_001319206.1. [Q02078-2]
NP_005578.2. NM_005587.3. [Q02078-5]
XP_011519883.1. XM_011521581.2. [Q02078-1]
XP_011519884.1. XM_011521582.2. [Q02078-1]
XP_011519888.1. XM_011521586.2. [Q02078-7]
XP_016877679.1. XM_017022190.1. [Q02078-1]
XP_016877680.1. XM_017022191.1. [Q02078-1]
XP_016877682.1. XM_017022193.1. [Q02078-5]
XP_016877683.1. XM_017022194.1. [Q02078-5]
UniGeneiHs.268675.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7UNMR-A/B2-86[»]
1EGWX-ray1.50A/B/C/D2-78[»]
1LEWX-ray2.30B269-280[»]
3KOVX-ray2.90A/B/I/J2-91[»]
3MU6X-ray2.43A/B/C/D2-70[»]
3P57X-ray2.19A/B/C/D/I/J2-91[»]
ProteinModelPortaliQ02078.
SMRiQ02078.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110369. 53 interactors.
DIPiDIP-40711N.
IntActiQ02078. 36 interactors.
MINTiMINT-104848.
STRINGi9606.ENSP00000346389.

PTM databases

iPTMnetiQ02078.
PhosphoSitePlusiQ02078.

Polymorphism and mutation databases

BioMutaiMEF2A.

Proteomic databases

EPDiQ02078.
MaxQBiQ02078.
PaxDbiQ02078.
PeptideAtlasiQ02078.
PRIDEiQ02078.

Protocols and materials databases

DNASUi4205.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338042; ENSP00000337202; ENSG00000068305. [Q02078-6]
ENST00000354410; ENSP00000346389; ENSG00000068305. [Q02078-5]
ENST00000449277; ENSP00000399460; ENSG00000068305. [Q02078-8]
ENST00000557785; ENSP00000453441; ENSG00000068305. [Q02078-6]
ENST00000557942; ENSP00000453095; ENSG00000068305. [Q02078-2]
ENST00000558812; ENSP00000454120; ENSG00000068305. [Q02078-7]
GeneIDi4205.
KEGGihsa:4205.
UCSCiuc002bve.4. human. [Q02078-1]

Organism-specific databases

CTDi4205.
DisGeNETi4205.
GeneCardsiMEF2A.
H-InvDBHIX0012611.
HGNCiHGNC:6993. MEF2A.
HPAiCAB004499.
HPA046597.
HPA056563.
MalaCardsiMEF2A.
MIMi600660. gene.
608320. phenotype.
neXtProtiNX_Q02078.
OpenTargetsiENSG00000068305.
PharmGKBiPA30731.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0014. Eukaryota.
COG5068. LUCA.
GeneTreeiENSGT00390000011828.
HOGENOMiHOG000230620.
HOVERGENiHBG053944.
InParanoidiQ02078.
KOiK09260.
OMAiPATLHRN.
OrthoDBiEOG091G05BY.
PhylomeDBiQ02078.
TreeFamiTF314067.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000068305-MONOMER.
ReactomeiR-HSA-198753. ERK/MAPK targets.
R-HSA-375170. CDO in myogenesis.
SignaLinkiQ02078.
SIGNORiQ02078.

Miscellaneous databases

ChiTaRSiMEF2A. human.
EvolutionaryTraceiQ02078.
GeneWikiiMyocyte-specific_enhancer_factor_2A.
GenomeRNAii4205.
PMAP-CutDBQ02078.
PROiQ02078.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000068305.
CleanExiHS_MEF2A.
ExpressionAtlasiQ02078. baseline and differential.
GenevisibleiQ02078. HS.

Family and domain databases

CDDicd00265. MADS_MEF2_like. 1 hit.
InterProiIPR022102. HJURP_C.
IPR033896. MADS_MEF2-like.
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...

Entry informationi

Entry nameiMEF2A_HUMAN
AccessioniPrimary (citable) accession number: Q02078
Secondary accession number(s): B4DFQ7
, F6XG23, O43814, Q14223, Q14224, Q59GX4, Q7Z6C9, Q96D14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.