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Q02078

- MEF2A_HUMAN

UniProt

Q02078 - MEF2A_HUMAN

Protein

Myocyte-specific enhancer factor 2A

Gene

MEF2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei176 – 1772CleavageCurated
    Sitei213 – 2142CleavageCurated
    Sitei466 – 4672CleavageCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi58 – 8629Mef2-typeSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. activating transcription factor binding Source: UniProtKB
    2. chromatin binding Source: UniProtKB
    3. histone acetyltransferase binding Source: UniProtKB
    4. histone deacetylase binding Source: UniProtKB
    5. protein binding Source: BHF-UCL
    6. protein heterodimerization activity Source: UniProtKB
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    9. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
    10. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
    11. RNA polymerase II transcription coactivator activity Source: BHF-UCL
    12. RNA polymerase II transcription factor binding Source: BHF-UCL
    13. sequence-specific DNA binding Source: UniProtKB
    14. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    15. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    16. SMAD binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cardiac conduction Source: UniProtKB
    3. cellular response to calcium ion Source: UniProtKB
    4. dendrite morphogenesis Source: UniProtKB
    5. ERK5 cascade Source: UniProtKB
    6. heart development Source: UniProtKB
    7. innate immune response Source: Reactome
    8. MAPK cascade Source: UniProtKB
    9. mitochondrial genome maintenance Source: UniProtKB
    10. mitochondrion distribution Source: UniProtKB
    11. muscle cell differentiation Source: Reactome
    12. muscle organ development Source: UniProtKB
    13. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    14. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. neurotrophin TRK receptor signaling pathway Source: Reactome
    17. positive regulation of muscle cell differentiation Source: Reactome
    18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. stress-activated MAPK cascade Source: Reactome
    20. toll-like receptor 10 signaling pathway Source: Reactome
    21. toll-like receptor 2 signaling pathway Source: Reactome
    22. toll-like receptor 3 signaling pathway Source: Reactome
    23. toll-like receptor 4 signaling pathway Source: Reactome
    24. toll-like receptor 5 signaling pathway Source: Reactome
    25. toll-like receptor 9 signaling pathway Source: Reactome
    26. toll-like receptor signaling pathway Source: Reactome
    27. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    28. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    29. transcription, DNA-templated Source: UniProtKB
    30. transcription from RNA polymerase II promoter Source: GOC
    31. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    32. ventricular cardiac myofibril assembly Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_12599. ERK/MAPK targets.
    REACT_21402. CDO in myogenesis.
    SignaLinkiQ02078.

    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
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6993. MEF2A.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear chromatin Source: BHF-UCL
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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 mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761D → A: Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3. 1 Publication
    Mutagenesisi213 – 2131D → A: Abolishes cleavage at sites 2 and 3 by caspase 7. 1 Publication
    Mutagenesisi255 – 2551S → A: Slightly increased MEF2A protein level. 1 Publication
    Mutagenesisi255 – 2551S → D: Decreased MEF2A protein level. 1 Publication
    Mutagenesisi269 – 2691R → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-270. 1 Publication
    Mutagenesisi270 – 2701K → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-269. 1 Publication
    Mutagenesisi273 – 2731L → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-275. 1 Publication
    Mutagenesisi275 – 2751V → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-273. 1 Publication
    Mutagenesisi277 – 2771I → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-278. 1 Publication
    Mutagenesisi278 – 2781P → A: Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-277. 1 Publication
    Mutagenesisi312 – 3121T → A: Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation; when associated with A-319. 2 Publications
    Mutagenesisi319 – 3191T → A: Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation; when associated with A-312. 2 Publications
    Mutagenesisi355 – 3551S → A: No effect on p38-mediated transcriptional activity. 2 Publications
    Mutagenesisi387 – 3871S → A: No effect on p38-mediated phosphorylation.
    Mutagenesisi403 – 4031K → R: Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression. 2 Publications
    Mutagenesisi408 – 4081S → A: Loss of sumoylation. 2 Publications
    Mutagenesisi408 – 4081S → D: Rescues sumoylation. 2 Publications
    Mutagenesisi453 – 4531S → A: No effect on p38-mediated phosphorylation. 1 Publication
    Mutagenesisi479 – 4791S → A: No effect on p38-mediated phosphorylation. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi608320. phenotype.
    PharmGKBiPA30731.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 507507Myocyte-specific enhancer factor 2APRO_0000199428Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591Phosphoserine; by CK2By similarity
    Modified residuei98 – 981Phosphoserine1 Publication
    Modified residuei235 – 2351Phosphoserine1 Publication
    Modified residuei249 – 2491N6-acetyllysine2 Publications
    Modified residuei255 – 2551Phosphoserine; by MAPK142 Publications
    Modified residuei312 – 3121Phosphothreonine; by MAPK7 and MAPK14; alternate5 Publications
    Modified residuei312 – 3121Phosphothreonine; by NLK; alternate5 Publications
    Modified residuei319 – 3191Phosphothreonine; by MAPK7 and MAPK144 Publications
    Modified residuei355 – 3551Phosphoserine; by MAPK71 Publication
    Modified residuei403 – 4031N6-acetyllysine; alternateBy similarity
    Cross-linki403 – 403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Modified residuei408 – 4081Phosphoserine; by CDK54 Publications
    Modified residuei453 – 4531Phosphoserine; by MAPK1 Publication

    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.12 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

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ02078.
    PaxDbiQ02078.
    PRIDEiQ02078.

    PTM databases

    PhosphoSiteiQ02078.

    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

    ArrayExpressiQ02078.
    BgeeiQ02078.
    CleanExiHS_MEF2A.
    GenevestigatoriQ02078.

    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

    Protein-protein interaction databases

    BioGridi110369. 26 interactions.
    DIPiDIP-40711N.
    IntActiQ02078. 11 interactions.
    MINTiMINT-104848.
    STRINGi9606.ENSP00000346389.

    Structurei

    Secondary structure

    1
    507
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 3825
    Beta strandi42 – 487
    Turni50 – 523
    Beta strandi54 – 607
    Helixi62 – 7110
    Beta strandi77 – 804
    Helixi81 – 9010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-91.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02078.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 5755MADS-boxPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni266 – 28318Required for interaction with MAPKsAdd
    BLAST
    Regioni289 – 2968Beta domain

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 3128Lys-rich (basic)Add
    BLAST
    Compositional biasi141 – 18646Ser/Thr-richAdd
    BLAST
    Compositional biasi420 – 44627Gln/Pro-richAdd
    BLAST

    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

    eggNOGiCOG5068.
    HOGENOMiHOG000230620.
    HOVERGENiHBG053944.
    InParanoidiQ02078.
    KOiK09260.
    PhylomeDBiQ02078.
    TreeFamiTF314067.

    Family and domain databases

    InterProiIPR022102. HJURP_C.
    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. Align

    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

    MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS    50
    SNKLFQYAST DMDKVLLKYT EYNEPHESRT NSDIVEALNK KEHRGCDSPD 100
    PDTSYVLTPH TEEKYKKINE EFDNMMRNHK IAPGLPPQNF SMSVTVPVTS 150
    PNALSYTNPG SSLVSPSLAA SSTLTDSSML SPPQTTLHRN VSPGAPQRPP 200
    STGNAGGMLS TTDLTVPNGA GSSPVGNGFV NSRASPNLIG ATGANSLGKV 250
    MPTKSPPPPG GGNLGMNSRK PDLRVVIPPS SKGMMPPLSE EEELELNTQR 300
    ISSSQATQPL ATPVVSVTTP SLPPQGLVYS AMPTAYNTDY SLTSADLSAL 350
    QGFNSPGMLS LGQVSAWQQH HLGQAALSSL VAGGQLSQGS NLSINTNQNI 400
    SIKSEPISPP RDRMTPSGFQ QQQQQQQQQQ PPPPPQPQPQ PPQPQPRQEM 450
    GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP IVLGRPPNTE DRESPSVKRM 500
    RMDAWVT 507
    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.

    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. Contains a phosphoserine at position 30.

    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. Contains a phosphoserine at position 30.

    Show »
    Length:429
    Mass (Da):45,570
    Checksum:iB356416F17385FCD
    GO

    Sequence cautioni

    The sequence AAH53871.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD92222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti430 – 4301Missing in AAB17195. 1 PublicationCurated
    Sequence conflicti430 – 4301Missing in AAB17196. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti263 – 2631N → S.1 Publication
    Corresponds to variant rs121918530 [ dbSNP | Ensembl ].
    VAR_038407
    Natural varianti279 – 2791P → L.3 Publications
    Corresponds to variant rs121918529 [ dbSNP | Ensembl ].
    VAR_038408
    Natural varianti283 – 2831G → D.1 Publication
    VAR_038409
    Natural varianti440 – 4467Missing Loss of nuclear localization; 66% decrease in transcription activation; loss of synergistic activation by MEF2A and GATA1 through a dominant-negative mechanism.
    VAR_017743

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei19 – 8668Missing in isoform 7. 1 PublicationVSP_043338Add
    BLAST
    Alternative sequencei19 – 6244VTFTK…ASTDM → TLRKKGLNGCESPDADDYFE HSPLSEDRFSKLNEDSDFIF KRGP in isoform 8. 1 PublicationVSP_046018Add
    BLAST
    Alternative sequencei63 – 13270Missing in isoform 8. 1 PublicationVSP_046019Add
    BLAST
    Alternative sequencei87 – 13246ALNKK…NHKIA → TLRKKGLNGCESPDADDYFE HSPLSEDRFSKLNEDSDFIF KRGP in isoform MEFA, isoform RSRFC9, isoform 6 and isoform 7. 5 PublicationsVSP_006240Add
    BLAST
    Alternative sequencei289 – 2968Missing in isoform RSRFC4, isoform RSRFC9, isoform 5, isoform 6 and isoform 8. 5 PublicationsVSP_006241
    Alternative sequencei420 – 4212Missing in isoform RSRFC4 and isoform RSRFC9. 3 PublicationsVSP_006242

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    PIRiC39481.
    S25831.
    RefSeqiNP_001124398.1. NM_001130926.1. [Q02078-6]
    NP_001124399.1. NM_001130927.1. [Q02078-7]
    NP_001124400.1. NM_001130928.1. [Q02078-8]
    NP_001165365.1. NM_001171894.1. [Q02078-6]
    NP_005578.2. NM_005587.2. [Q02078-5]
    XP_005254972.1. XM_005254915.1. [Q02078-6]
    UniGeneiHs.268675.

    Genome annotation databases

    EnsembliENST00000354410; 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.3. human. [Q02078-2]
    uc002bvf.3. human. [Q02078-5]
    uc002bvg.3. human. [Q02078-6]
    uc010urv.2. human. [Q02078-7]
    uc010urw.2. human. [Q02078-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS45362.1. [Q02078-5 ]
    CCDS45363.1. [Q02078-7 ]
    CCDS53978.1. [Q02078-6 ]
    CCDS58401.1. [Q02078-8 ]
    PIRi C39481.
    S25831.
    RefSeqi NP_001124398.1. NM_001130926.1. [Q02078-6 ]
    NP_001124399.1. NM_001130927.1. [Q02078-7 ]
    NP_001124400.1. NM_001130928.1. [Q02078-8 ]
    NP_001165365.1. NM_001171894.1. [Q02078-6 ]
    NP_005578.2. NM_005587.2. [Q02078-5 ]
    XP_005254972.1. XM_005254915.1. [Q02078-6 ]
    UniGenei Hs.268675.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C7U NMR - A/B 2-86 [» ]
    1EGW X-ray 1.50 A/B/C/D 2-78 [» ]
    1LEW X-ray 2.30 B 269-280 [» ]
    3KOV X-ray 2.90 A/B/I/J 2-91 [» ]
    3MU6 X-ray 2.43 A/B/C/D 2-70 [» ]
    3P57 X-ray 2.19 A/B/C/D/I/J 2-91 [» ]
    ProteinModelPortali Q02078.
    SMRi Q02078. Positions 2-91.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110369. 26 interactions.
    DIPi DIP-40711N.
    IntActi Q02078. 11 interactions.
    MINTi MINT-104848.
    STRINGi 9606.ENSP00000346389.

    PTM databases

    PhosphoSitei Q02078.

    Proteomic databases

    MaxQBi Q02078.
    PaxDbi Q02078.
    PRIDEi Q02078.

    Protocols and materials databases

    DNASUi 4205.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli 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 ]
    GeneIDi 4205.
    KEGGi hsa:4205.
    UCSCi uc002bve.3. human. [Q02078-2 ]
    uc002bvf.3. human. [Q02078-5 ]
    uc002bvg.3. human. [Q02078-6 ]
    uc010urv.2. human. [Q02078-7 ]
    uc010urw.2. human. [Q02078-1 ]

    Organism-specific databases

    CTDi 4205.
    GeneCardsi GC15P100107.
    H-InvDB HIX0012611.
    HGNCi HGNC:6993. MEF2A.
    HPAi CAB004499.
    HPA046597.
    HPA056563.
    MIMi 600660. gene.
    608320. phenotype.
    neXtProti NX_Q02078.
    PharmGKBi PA30731.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5068.
    HOGENOMi HOG000230620.
    HOVERGENi HBG053944.
    InParanoidi Q02078.
    KOi K09260.
    PhylomeDBi Q02078.
    TreeFami TF314067.

    Enzyme and pathway databases

    Reactomei REACT_12599. ERK/MAPK targets.
    REACT_21402. CDO in myogenesis.
    SignaLinki Q02078.

    Miscellaneous databases

    EvolutionaryTracei Q02078.
    GeneWikii Myocyte-specific_enhancer_factor_2A.
    GenomeRNAii 4205.
    NextBioi 16568.
    PMAP-CutDB Q02078.
    PROi Q02078.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02078.
    Bgeei Q02078.
    CleanExi HS_MEF2A.
    Genevestigatori Q02078.

    Family and domain databases

    InterProi IPR022102. HJURP_C.
    IPR002100. TF_MADSbox.
    [Graphical view ]
    Pfami PF12347. HJURP_C. 1 hit.
    PF00319. SRF-TF. 1 hit.
    [Graphical view ]
    PRINTSi PR00404. MADSDOMAIN.
    SMARTi SM00432. MADS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55455. SSF55455. 1 hit.
    PROSITEi PS00350. MADS_BOX_1. 1 hit.
    PS50066. MADS_BOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human SRF-related proteins: DNA-binding properties and potential regulatory targets."
      Pollock R., Treisman R.
      Genes Dev. 5:2327-2341(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2; RSRFC4 AND RSRFC9), DNA-BINDING, TISSUE SPECIFICITY, DIMERIZATION.
      Tissue: Placenta.
    2. Treisman R.
      Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RSRFC9), SEQUENCE REVISION.
    3. "Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors."
      Yu Y.-T., Breitbart R.E., Smoot L.B., Lee Y., Mahdavi V., Nadal-Ginard B.
      Genes Dev. 6:1783-1798(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MEF2 AND RSRFC9), TISSUE SPECIFICITY.
      Tissue: Heart and Skeletal muscle.
    4. Suzuki E., Lowry J., Sonoda G., Testa J.R., Walsh K.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS RSRFC4 AND RSRFC9).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
      Tissue: Amygdala.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
      Tissue: Brain.
    7. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
      Tissue: Pancreas and Uterus.
    9. "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1."
      Yang C.-C., Ornatsky O.I., McDermott J.C., Cruz T.F., Prody C.A.
      Nucleic Acids Res. 26:4771-4777(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK7, PHOSPHORYLATION.
    10. "HDAC4 deacetylase associates with and represses the MEF2 transcription factor."
      Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.
      EMBO J. 18:5099-5107(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC4 AND HDAC9.
    11. "Regulation of the MEF2 family of transcription factors by p38."
      Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F., Olson E.N., Ulevitch R.J., Han J.-D.
      Mol. Cell. Biol. 19:21-30(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-312; THR-319 AND SER-453, FUNCTION, HETERODIMERIZATION, MUTAGENESIS OF THR-312; THR-319; SER-355; SER-453 AND SER-479.
    12. "Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors."
      Yang S.-H., Galanis A., Sharrocks A.D.
      Mol. Cell. Biol. 19:4028-4038(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK14, PHOSPHORYLATION AT THR-312 AND THR-319, MUTAGENESIS OF ARG-269; LYS-270; LEU-273; VAL-275; ILE-277 AND PRO-278.
    13. "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family."
      Kato Y., Zhao M., Morikawa A., Sugiyama T., Chakravortty D., Koide N., Yoshida T., Tapping R.I., Yang Y., Yokochi T., Lee J.D.
      J. Biol. Chem. 275:18534-18540(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-312; THR-319 AND SER-355, MUTAGENESIS OF THR-312; THR-319 AND SER-355.
    14. "Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosis."
      Okamoto S., Li Z., Ju C., Scholzke M.N., Mathews E., Cui J., Salvesen G.S., Bossy-Wetzel E., Lipton S.A.
      Proc. Natl. Acad. Sci. U.S.A. 99:3974-3979(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING AT ASP-176; ASP-213 AND ASP-466, FUNCTION, MUTAGENESIS OF ASP-176 AND ASP-213.
    15. "Phosphorylation motifs regulating the stability and function of myocyte enhancer factor 2A."
      Cox D.M., Du M., Marback M., Yang E.C.C., Chan J., Siu K.W.M., McDermott J.C.
      J. Biol. Chem. 278:15297-15303(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-255; THR-312; THR-319 AND SER-408, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-255.
    16. "Cdk5-mediated inhibition of the protective effects of transcription factor MEF2 in neurotoxicity-induced apoptosis."
      Gong X., Tang X., Wiedmann M., Wang X., Peng J., Zheng D., Blair L.A.C., Marshall J., Mao Z.
      Neuron 38:33-46(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-408, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-408.
    17. "Regulation of the human GLUT4 gene promoter: interaction between a transcriptional activator and myocyte enhancer factor 2A."
      Knight J.B., Eyster C.A., Griesel B.A., Olson A.L.
      Proc. Natl. Acad. Sci. U.S.A. 100:14725-14730(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC2A4RG.
    18. "Alternative pre-mRNA splicing governs expression of a conserved acidic transactivation domain in myocyte enhancer factor 2 factors of striated muscle and brain."
      Zhu B., Ramachandran B., Gulick T.
      J. Biol. Chem. 280:28749-28760(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF BETA DOMAIN.
    19. "Cyclin-dependent kinase 5 mediates neurotoxin-induced degradation of the transcription factor myocyte enhancer factor 2."
      Tang X., Wang X., Gong X., Tong M., Park D., Xia Z., Mao Z.
      J. Neurosci. 25:4823-4834(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, PHOSPHORYLATION.
    20. "SUMO-1 modification of MEF2A regulates its transcriptional activity."
      Riquelme C., Barthel K.K., Liu X.
      J. Cell. Mol. Med. 10:132-144(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-403, INTERACTION WITH PIAS1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-403.
    21. Cited for: SUMOYLATION AT LYS-403, PHOSPHORYLATION AT SER-408, FUNCTION, MUTAGENESIS OF LYS-403 AND SER-408.
    22. "A calcium-regulated MEF2 sumoylation switch controls postsynaptic differentiation."
      Shalizi A., Gaudilliere B., Yuan Z., Stegmueller J., Shirogane T., Ge Q., Tan Y., Schulman B., Harper J.W., Bonni A.
      Science 311:1012-1017(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-408, FUNCTION.
    23. "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates anterior formation in Xenopus development."
      Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T., Shibuya H.
      Mol. Cell. Biol. 27:7623-7630(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-312 BY NLK.
    24. "Quantitative control of adaptive cardiac hypertrophy by acetyltransferase p300."
      Wei J.Q., Shehadeh L.A., Mitrani J.M., Pessanha M., Slepak T.I., Webster K.A., Bishopric N.H.
      Circulation 118:934-946(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, INVOLVEMENT IN CARDIAC HYPERTROPHY.
    25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-235 AND SER-255, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORMS 7 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Identification of HZF1 as a novel target gene of the MEF2 transcription factor."
      Liu X., Jin E.Z., Zhi J.X., Li X.Q.
      Mol. Med. Report. 4:465-469(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHROMATIN BINDING.
    29. "Transcription factor MEF2A mutations in patients with coronary artery disease."
      Bhagavatula M.R.K., Fan C., Shen G.-Q., Cassano J., Plow E.F., Topol E.J., Wang Q.
      Hum. Mol. Genet. 13:3181-3188(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SER-263; LEU-279 AND ASP-283, CHARACTERIZATION OF VARIANTS SER-263; LEU-279 AND ASP-283.
    30. "The Pro279Leu variant in the transcription factor MEF2A is associated with myocardial infarction."
      Gonzalez P., Garcia-Castro M., Reguero J.R., Batalla A., Ordonez A.G., Palop R.L., Lozano I., Montes M., Alvarez V., Coto E.
      J. Med. Genet. 43:167-169(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-279, ASSOCIATION WITH SUSCEPTIBILITY TO MYOCARDIAL INFARCTION.
    31. Cited for: VARIANT LEU-279, LACK OF ASSOCIATION WITH MYOCARDIAL INFARCTION.
    32. "Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors."
      Huang K., Louis J.M., Donaldson L., Lim F.L., Sharrocks A.D., Clore G.M.
      EMBO J. 19:2615-2628(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-86 IN COMPLEX WITH DNA.
    33. "Crystal structure of MEF2A core bound to DNA at 1.5 A resolution."
      Santelli E., Richmond T.J.
      J. Mol. Biol. 297:437-449(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-78 IN COMPLEX WITH DNA, DIMERIZATION.

    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: October 1, 2014
    This is version 151 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

    External Data

    Dasty 3