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Q14814

- MEF2D_HUMAN

UniProt

Q14814 - MEF2D_HUMAN

Protein

Myocyte-specific enhancer factor 2D

Gene

MEF2D

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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, 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. Plays a critical role in the regulation of neuronal apoptosis By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei288 – 2892CleavageCurated

    Regions

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

    GO - Molecular functioni

    1. activating transcription factor binding Source: UniProtKB
    2. histone deacetylase binding Source: UniProtKB
    3. protein binding Source: BHF-UCL
    4. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
    5. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. adult heart development Source: UniProtKB
    2. apoptotic process Source: UniProtKB-KW
    3. chondrocyte differentiation Source: Ensembl
    4. endochondral ossification Source: Ensembl
    5. muscle organ development Source: ProtInc
    6. nervous system development Source: UniProtKB-KW
    7. osteoblast differentiation Source: Ensembl
    8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. skeletal muscle cell differentiation Source: Ensembl
    10. transcription from RNA polymerase II promoter Source: GOC

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Apoptosis, Differentiation, Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_21402. CDO in myogenesis.
    REACT_24941. Circadian Clock.
    SignaLinkiQ14814.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myocyte-specific enhancer factor 2D
    Gene namesi
    Name:MEF2D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6997. MEF2D.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation
    Note: Translocated by HDAC4 to nuclear dots.

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801S → A: Abolishes MAPK7- and EGF-mediated transcriptional activation. 1 Publication
    Mutagenesisi286 – 2861T → A: Same transcriptional activity as for isoforms with beta domain. 1 Publication
    Mutagenesisi287 – 2871E → Q: Abolishes transcriptional activity; when associated with N-288 and N-291. 1 Publication
    Mutagenesisi288 – 2881D → A: Abolishes cleavage by caspase 7. 2 Publications
    Mutagenesisi288 – 2881D → N: Abolishes transcriptional activity; when associated with Q-287 and N-291. 2 Publications
    Mutagenesisi289 – 2891H → A: Same transcriptional activity as for isoforms with beta domain. 1 Publication
    Mutagenesisi291 – 2911D → N: Abolishes transcriptional activity; when associated with Q-287 and N-288. 1 Publication
    Mutagenesisi437 – 4371S → A: No effect on MAPK7- or EGF-mediated transcriptional activity. 1 Publication
    Mutagenesisi438 – 4381I → A: Abolishes K-439 sumoylation. 1 Publication
    Mutagenesisi439 – 4391K → R: Abolishes sumoylation and acetylation. 2 Publications
    Mutagenesisi444 – 4441S → A: Abolishes K-439 sumoylation. Reduced neurotoxin-induced apoptosis of neuronal cells. More resistant to degradation. 3 Publications
    Mutagenesisi444 – 4441S → E: No effect on K-439 sumoylation. 3 Publications

    Organism-specific databases

    PharmGKBiPA30735.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 521521Myocyte-specific enhancer factor 2DPRO_0000199435Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei121 – 1211Phosphoserine; by PKA1 Publication
    Modified residuei180 – 1801Phosphoserine; by MAPK75 Publications
    Modified residuei190 – 1901Phosphoserine; by PKABy similarity
    Modified residuei231 – 2311Phosphoserine2 Publications
    Modified residuei245 – 2451N6-acetyllysine2 Publications
    Modified residuei251 – 2511Phosphoserine2 Publications
    Modified residuei439 – 4391N6-acetyllysine; alternate2 Publications
    Cross-linki439 – 439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Modified residuei444 – 4441Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated on Ser-444 by CDK5 is required for Lys-439 sumoylation and inhibits transcriptional activity. In neurons, enhanced CDK5 activity induced by neurotoxins promotes caspase 3-mediated cleavage leading to neuron apoptosis. Phosphorylation on Ser-180 can be enhanced by EGF. Phosphorylated and activated by CaMK4.12 Publications
    Acetylated on Lys-439 by CREBBP. Deacetylated by SIRT1.3 Publications
    Sumoylated on Lys-439 with SUMO2 but not SUMO1; which inhibits transcriptional activity and myogenic activity. Desumoylated by SENP3.3 Publications
    Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14814.
    PaxDbiQ14814.
    PRIDEiQ14814.

    PTM databases

    PhosphoSiteiQ14814.

    Miscellaneous databases

    PMAP-CutDBQ14814.

    Expressioni

    Developmental stagei

    Present in myotubes and also in undifferentiated myoblasts.

    Gene expression databases

    ArrayExpressiQ14814.
    BgeeiQ14814.
    CleanExiHS_MEF2D.
    GenevestigatoriQ14814.

    Organism-specific databases

    HPAiHPA004807.
    HPA007114.

    Interactioni

    Subunit structurei

    Interacts with MYOG By similarity. 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.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi110373. 31 interactions.
    IntActiQ14814. 9 interactions.
    MINTiMINT-125484.
    STRINGi9606.ENSP00000271555.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14814.
    SMRiQ14814. Positions 2-73.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni286 – 2927Beta domain

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 3129Arg/Lys-rich (basic)Add
    BLAST
    Compositional biasi252 – 2554Poly-Pro
    Compositional biasi365 – 40440Gln/Pro-richAdd
    BLAST
    Compositional biasi451 – 4566Poly-Pro

    Domaini

    The beta domain, missing in a number of isoforms, is required for enhancement of transcriptional activity.

    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.
    HOVERGENiHBG053944.
    InParanoidiQ14814.
    KOiK09262.
    OMAiHHLNNAQ.
    OrthoDBiEOG793B7D.
    PhylomeDBiQ14814.
    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 (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform MEF2DAB (identifier: Q14814-1) [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

    MGRKKIQIQR ITDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNH    50
    SNKLFQYAST DMDKVLLKYT EYNEPHESRT NADIIETLRK KGFNGCDSPE 100
    PDGEDSLEQS PLLEDKYRRA SEELDGLFRR YGSTVPAPNF AMPVTVPVSN 150
    QSSLQFSNPS GSLVTPSLVT SSLTDPRLLS PQQPALQRNS VSPGLPQRPA 200
    SAGAMLGGDL NSANGACPSP VGNGYVSARA SPGLLPVANG NSLNKVIPAK 250
    SPPPPTHSTQ LGAPSRKPDL RVITSQAGKG LMHHLTEDHL DLNNAQRLGV 300
    SQSTHSLTTP VVSVATPSLL SQGLPFSSMP TAYNTDYQLT SAELSSLPAF 350
    SSPGGLSLGN VTAWQQPQQP QQPQQPQPPQ QQPPQPQQPQ PQQPQQPQQP 400
    PQQQSHLVPV SLSNLIPGSP LPHVGAALTV TTHPHISIKS EPVSPSRERS 450
    PAPPPPAVFP AARPEPGDGL SSPAGGSYET GDRDDGRGDF GPTLGLLRPA 500
    PEPEAEGSAV KRMRLDTWTL K 521
    Length:521
    Mass (Da):55,938
    Last modified:November 1, 1997 - v1
    Checksum:i5C9790AD598619BA
    GO
    Isoform MEF2DA'B (identifier: Q14814-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-132: TLRKKGFNGC...ELDGLFRRYG → ALHKKHRECE...DKMMQSYRLA

    Show »
    Length:520
    Mass (Da):56,091
    Checksum:i9B39CB2A3570EB74
    GO
    Isoform MEF2D0B (identifier: Q14814-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-132: Missing.

    Show »
    Length:475
    Mass (Da):50,680
    Checksum:iBCA6D1EF6885A467
    GO
    Isoform MEF2DA0 (identifier: Q14814-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         286-292: Missing.

    Show »
    Length:514
    Mass (Da):55,114
    Checksum:i425430A7A0F69549
    GO
    Isoform MEF2DA'0 (identifier: Q14814-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-132: TLRKKGFNGC...ELDGLFRRYG → ALHKKHRECE...DKMMQSYRLA
         286-292: Missing.

    Show »
    Length:513
    Mass (Da):55,267
    Checksum:i2CC3FD705A1C8D1F
    GO
    Isoform MEF2D00 (identifier: Q14814-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-132: Missing.
         286-292: Missing.

    Show »
    Length:468
    Mass (Da):49,856
    Checksum:iBFFEBF282D6519F7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti434 – 4341P → S.
    Corresponds to variant rs2274315 [ dbSNP | Ensembl ].
    VAR_022155

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei87 – 13246Missing in isoform MEF2D0B and isoform MEF2D00. 1 PublicationVSP_006251Add
    BLAST
    Alternative sequencei87 – 13246TLRKK…FRRYG → ALHKKHRECESPEVDEVFAL TPQTEEKYKKIDEEFDKMMQ SYRLA in isoform MEF2DA'B and isoform MEF2DA'0. 1 PublicationVSP_006250Add
    BLAST
    Alternative sequencei286 – 2927Missing in isoform MEF2DA0, isoform MEF2DA'0 and isoform MEF2D00. 2 PublicationsVSP_006252

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16794 mRNA. Translation: AAA93194.1.
    L16795 Genomic DNA. Translation: AAA59579.1.
    AL139412 Genomic DNA. Translation: CAI17184.1.
    AL139412 Genomic DNA. Translation: CAI17185.1.
    CH471121 Genomic DNA. Translation: EAW52948.1.
    CH471121 Genomic DNA. Translation: EAW52952.1.
    BC040949 mRNA. Translation: AAH40949.1.
    BC054520 mRNA. Translation: AAH54520.1.
    CCDSiCCDS1143.1. [Q14814-1]
    CCDS60304.1. [Q14814-4]
    PIRiI53124.
    RefSeqiNP_001258558.1. NM_001271629.1. [Q14814-4]
    NP_005911.1. NM_005920.3. [Q14814-1]
    XP_005245226.1. XM_005245169.2. [Q14814-1]
    XP_005245227.1. XM_005245170.1. [Q14814-1]
    XP_006711393.1. XM_006711330.1. [Q14814-1]
    XP_006711394.1. XM_006711331.1. [Q14814-1]
    XP_006711395.1. XM_006711332.1. [Q14814-2]
    XP_006711396.1. XM_006711333.1. [Q14814-4]
    XP_006711397.1. XM_006711334.1. [Q14814-5]
    UniGeneiHs.314327.
    Hs.744524.

    Genome annotation databases

    EnsembliENST00000348159; ENSP00000271555; ENSG00000116604. [Q14814-1]
    ENST00000360595; ENSP00000353803; ENSG00000116604. [Q14814-4]
    ENST00000368240; ENSP00000357223; ENSG00000116604. [Q14814-4]
    ENST00000464356; ENSP00000476788; ENSG00000116604. [Q14814-5]
    GeneIDi4209.
    KEGGihsa:4209.
    UCSCiuc001fpb.4. human. [Q14814-4]
    uc001fpc.4. human. [Q14814-1]

    Polymorphism databases

    DMDMi2500876.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16794 mRNA. Translation: AAA93194.1 .
    L16795 Genomic DNA. Translation: AAA59579.1 .
    AL139412 Genomic DNA. Translation: CAI17184.1 .
    AL139412 Genomic DNA. Translation: CAI17185.1 .
    CH471121 Genomic DNA. Translation: EAW52948.1 .
    CH471121 Genomic DNA. Translation: EAW52952.1 .
    BC040949 mRNA. Translation: AAH40949.1 .
    BC054520 mRNA. Translation: AAH54520.1 .
    CCDSi CCDS1143.1. [Q14814-1 ]
    CCDS60304.1. [Q14814-4 ]
    PIRi I53124.
    RefSeqi NP_001258558.1. NM_001271629.1. [Q14814-4 ]
    NP_005911.1. NM_005920.3. [Q14814-1 ]
    XP_005245226.1. XM_005245169.2. [Q14814-1 ]
    XP_005245227.1. XM_005245170.1. [Q14814-1 ]
    XP_006711393.1. XM_006711330.1. [Q14814-1 ]
    XP_006711394.1. XM_006711331.1. [Q14814-1 ]
    XP_006711395.1. XM_006711332.1. [Q14814-2 ]
    XP_006711396.1. XM_006711333.1. [Q14814-4 ]
    XP_006711397.1. XM_006711334.1. [Q14814-5 ]
    UniGenei Hs.314327.
    Hs.744524.

    3D structure databases

    ProteinModelPortali Q14814.
    SMRi Q14814. Positions 2-73.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110373. 31 interactions.
    IntActi Q14814. 9 interactions.
    MINTi MINT-125484.
    STRINGi 9606.ENSP00000271555.

    PTM databases

    PhosphoSitei Q14814.

    Polymorphism databases

    DMDMi 2500876.

    Proteomic databases

    MaxQBi Q14814.
    PaxDbi Q14814.
    PRIDEi Q14814.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348159 ; ENSP00000271555 ; ENSG00000116604 . [Q14814-1 ]
    ENST00000360595 ; ENSP00000353803 ; ENSG00000116604 . [Q14814-4 ]
    ENST00000368240 ; ENSP00000357223 ; ENSG00000116604 . [Q14814-4 ]
    ENST00000464356 ; ENSP00000476788 ; ENSG00000116604 . [Q14814-5 ]
    GeneIDi 4209.
    KEGGi hsa:4209.
    UCSCi uc001fpb.4. human. [Q14814-4 ]
    uc001fpc.4. human. [Q14814-1 ]

    Organism-specific databases

    CTDi 4209.
    GeneCardsi GC01M156433.
    HGNCi HGNC:6997. MEF2D.
    HPAi HPA004807.
    HPA007114.
    MIMi 600663. gene.
    neXtProti NX_Q14814.
    PharmGKBi PA30735.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5068.
    HOVERGENi HBG053944.
    InParanoidi Q14814.
    KOi K09262.
    OMAi HHLNNAQ.
    OrthoDBi EOG793B7D.
    PhylomeDBi Q14814.
    TreeFami TF314067.

    Enzyme and pathway databases

    Reactomei REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_21402. CDO in myogenesis.
    REACT_24941. Circadian Clock.
    SignaLinki Q14814.

    Miscellaneous databases

    ChiTaRSi MEF2D. human.
    GeneWikii MEF2D.
    GenomeRNAii 4209.
    NextBioi 16582.
    PMAP-CutDB Q14814.
    PROi Q14814.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14814.
    Bgeei Q14814.
    CleanExi HS_MEF2D.
    Genevestigatori Q14814.

    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. "A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage."
      Breitbart R.E., Liang C.-S., Smoot L.B., Laheru D.A., Mahdavi V., Nadal-Ginard B.
      Development 118:1095-1106(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MEF2D00; MEF2D0B; MEF2DA'0; MEF2DA'B; MEF2DA0 AND MEF2DAB).
      Tissue: Myocardium.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 MEF2DA0 AND MEF2DAB).
      Tissue: Eye and Testis.
    5. "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: HETERODIMERIZATION.
    6. "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor."
      Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J.
      Mol. Cell. Biol. 19:7816-7827(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC4.
    7. "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 SER-180, FUNCTION, MUTAGENESIS OF SER-180 AND SER-437.
    8. "Ca(2+)-dependent gene expression mediated by MEF2 transcription factors."
      Blaeser F., Ho N., Prywes R., Chatila T.A.
      J. Biol. Chem. 275:197-209(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMK4.
    9. "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-288, FUNCTION, MUTAGENESIS OF ASP-288.
    10. "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-444, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-444.
    11. "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, MUTAGENESIS OF THR-286; GLU-287; ASP-288; HIS-289 AND ASP-291.
    12. "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 AT SER-444, MUTAGENESIS OF SER-444.
    13. "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors."
      Gregoire S., Yang X.-J.
      Mol. Cell. Biol. 25:2273-2287(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-439, SUBCELLULAR LOCATION, FUNCTION.
    14. "Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications."
      Zhao X., Sternsdorf T., Bolger T.A., Evans R.M., Yao T.-P.
      Mol. Cell. Biol. 25:8456-8464(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-439, ACETYLATION AT LYS-439, DEACETYLATION, MUTAGENESIS OF ILE-438 AND LYS-439.
    15. "Myocyte enhancer factor 2 acetylation by p300 enhances its DNA binding activity, transcriptional activity, and myogenic differentiation."
      Ma K., Chan J.K., Zhu G., Wu Z.
      Mol. Cell. Biol. 25:3575-3582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION.
    16. "Control of MEF2 transcriptional activity by coordinated phosphorylation and sumoylation."
      Gregoire S., Tremblay A.M., Xiao L., Yang Q., Ma K., Nie J., Mao Z., Wu Z., Giguere V., Yang X.-J.
      J. Biol. Chem. 281:4423-4433(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-439, PHOSPHORYLATION AT SER-444, MUTAGENESIS OF LYS-439 AND SER-444.
    17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMEF2D_HUMAN
    AccessioniPrimary (citable) accession number: Q14814
    Secondary accession number(s): D3DVC0
    , Q14815, Q5T9U5, Q5T9U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 139 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3