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Q60929

- MEF2A_MOUSE

UniProt

Q60929 - MEF2A_MOUSE

Protein

Myocyte-specific enhancer factor 2A

Gene

Mef2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei174 – 1752CleavageCurated
    Sitei211 – 2122CleavageCurated
    Sitei457 – 4582CleavageCurated

    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: MGI
    3. DNA binding Source: MGI
    4. histone acetyltransferase binding Source: UniProtKB
    5. histone deacetylase binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. protein kinase binding Source: UniProtKB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    10. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
    11. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
    12. RNA polymerase II transcription coactivator activity Source: Ensembl
    13. sequence-specific DNA binding Source: MGI
    14. sequence-specific DNA binding transcription factor activity Source: MGI
    15. 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. ERK5 cascade Source: UniProtKB
    5. MAPK cascade Source: UniProtKB
    6. mitochondrial genome maintenance Source: UniProtKB
    7. mitochondrion distribution Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. nervous system development Source: UniProtKB-KW
    10. positive regulation of transcription, DNA-templated Source: MGI
    11. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    12. regulation of transcription, DNA-templated Source: MGI
    13. 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_215063. ERK/MAPK targets.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myocyte-specific enhancer factor 2A
    Gene namesi
    Name:Mef2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:99532. Mef2a.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear chromatin Source: BHF-UCL
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498Myocyte-specific enhancer factor 2APRO_0000199429Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591Phosphoserine; by CK2By similarity
    Modified residuei98 – 981PhosphoserineBy similarity
    Modified residuei233 – 2331PhosphoserineBy similarity
    Modified residuei247 – 2471N6-acetyllysine1 Publication
    Modified residuei253 – 2531PhosphoserineBy similarity
    Modified residuei310 – 3101Phosphothreonine; by MAPK7; alternateBy similarity
    Modified residuei310 – 3101Phosphothreonine; by NLK; alternate1 Publication
    Modified residuei317 – 3171Phosphothreonine; by MAPK7By similarity
    Modified residuei353 – 3531Phosphoserine; by MAPK7By similarity
    Modified residuei401 – 4011N6-acetyllysine; alternateBy similarity
    Cross-linki401 – 401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei406 – 4061PhosphoserineBy similarity
    Modified residuei444 – 4441PhosphoserineBy similarity

    Post-translational modificationi

    Constitutive phosphorylation on Ser-406 promotes Lys-401 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-406 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 By similarity. Isoform 3 is phosphorylated on Ser-98 and Thr-108.By similarity2 Publications
    Sumoylation on Lys-401 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-406 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-401 activates transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation. Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure By similarity.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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ60929.
    PRIDEiQ60929.

    PTM databases

    PhosphoSiteiQ60929.

    Expressioni

    Tissue specificityi

    Widely expressed though mainly restricted to skeletal and cardiac muscle, brain, neurons and lymphocytes. Differentially expressed depending on if isoforms contain the beta domain or not, with the total expression of the beta domain-lacking isoforms vastly exceding that of the beta domain-containing isoforms. Isoforms containing the beta domain are expressed primarily in skeletal and cardiac muscle and in brain. Also present in lung and testis. Splicing to include the beta domain is induced in differentiating myocytes. Isoforms lacking the beta domain are expressed less abundantly in skeletal muscle, brain and lymphocytes, and are uniquely found in ovary, liver, spleen and kidney. In embryos, the beta domain-containing and beta domain-lacking isoforms are equally expressed. Also expressed cerebellar granule neurons and other regions of the CNS. Highest levels in the olfactory bulb, cortex, hippocampus, thalamus and cerebellum.2 Publications

    Developmental stagei

    In the developing cerebellum, increasing levels after birth. The majority of this increase occurs around postnataL day 9 reaching a peak at postnatal day 15-18 which is maintained in adults.1 Publication

    Gene expression databases

    ArrayExpressiQ60929.
    BgeeiQ60929.
    CleanExiMM_MEF2A.
    GenevestigatoriQ60929.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NfixP70257-22EBI-2639094,EBI-2639084

    Protein-protein interaction databases

    BioGridi201381. 3 interactions.
    IntActiQ60929. 2 interactions.
    MINTiMINT-3155471.
    STRINGi10090.ENSMUSP00000117496.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60929.
    SMRiQ60929. 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
    Regioni264 – 28118Required for interaction with MAPKsBy similarityAdd
    BLAST
    Regioni287 – 2948Beta domainBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi254 – 2574Poly-Pro
    Compositional biasi288 – 2936Poly-Glu
    Compositional biasi418 – 43922Gln/Pro-richAdd
    BLAST
    Compositional biasi448 – 4558Poly-Ser

    Domaini

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

    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.
    GeneTreeiENSGT00390000011828.
    HOGENOMiHOG000230620.
    HOVERGENiHBG053944.
    InParanoidiQ60929.
    KOiK09260.
    OMAiRMDTWVT.
    OrthoDBiEOG793B7D.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q60929-1) [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 NSDIVETLRK KGLNGCESPD 100
    ADDYFEHSPL SEDRFSKLNE DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN 150
    ALSYTNPGSS LVSPSLAASS TLADSSMLSP PPATLHRNVS PGAPQRPPST 200
    GSASGMLSTT DLTVPNGAGN SPVGNGFVNS RASPNLIGNT GANSLGKVMP 250
    TKSPPPPGGG SLGMNSRKPD LRVVIPPSSK GMMPPLSEEE ELELNAQRIS 300
    SSQATQPLAT PVVSVTTPSL PPQGLVYSAM PTAYNTDYSL TSADLSALQG 350
    FTSPGMLSLG QASAWQQHHL GQAALSSLVA GGQLSQGSNL SINTNQNINI 400
    KSEPISPPRD RMTPSGFQQQ QQQPQQQPPP QPPQPQPRQE MGRSPVDSLS 450
    SSSSSYDGSD REDPRGDFHS PIVLGRPPNT EDRESPSVKR MRMDTWVT 498
    Length:498
    Mass (Da):53,579
    Last modified:May 29, 2007 - v2
    Checksum:iFE291C3E3E0A5E70
    GO
    Isoform 2 (identifier: Q60929-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         287-294: Missing.

    Show »
    Length:490
    Mass (Da):52,620
    Checksum:i2E15C204F58A9646
    GO
    Isoform 3 (identifier: Q60929-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         87-130: TLRKKGLNGC...DSDFIFKRGP → ALNKKEHRGC...DNMMRNHKIA
         287-294: Missing.

    Note: Contains a phosphoserine at position 98. Contains a phosphothreonine at position 108.

    Show »
    Length:492
    Mass (Da):52,990
    Checksum:i961882F1C572ACCF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981S → N in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti116 – 1161S → I in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti133 – 1331L → F in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti151 – 1511A → P in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti154 – 1541Y → D in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti174 – 1752DS → ET in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti201 – 2011G → S in BAE21297. (PubMed:16141072)Curated
    Sequence conflicti274 – 2741V → A in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti367 – 3671Q → E in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti373 – 3742AA → TT in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti419 – 4235QQQQQ → HHHHH in AAA74030. (PubMed:9013788)Curated
    Sequence conflicti478 – 4781P → A in AAA74030. (PubMed:9013788)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei87 – 13044TLRKK…FKRGP → ALNKKEHRGCDSPDPDTSYV LTPHTEEKYKKINEEFDNMM RNHKIA in isoform 3. 1 PublicationVSP_026060Add
    BLAST
    Alternative sequencei287 – 2948Missing in isoform 2 and isoform 3. 2 PublicationsVSP_026031

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30823 mRNA. Translation: AAA74030.1.
    AK132678 mRNA. Translation: BAE21297.1.
    BC061128 mRNA. Translation: AAH61128.1.
    BC096598 mRNA. Translation: AAH96598.1.
    CCDSiCCDS39981.1. [Q60929-1]
    CCDS71979.1. [Q60929-3]
    CCDS71980.1. [Q60929-2]
    RefSeqiNP_001028885.1. NM_001033713.2. [Q60929-1]
    NP_001278120.1. NM_001291191.1. [Q60929-3]
    NP_001278121.1. NM_001291192.1. [Q60929-3]
    NP_001278124.1. NM_001291195.1. [Q60929-2]
    NP_001278125.1. NM_001291196.1.
    XP_006540749.1. XM_006540686.1. [Q60929-1]
    UniGeneiMm.132788.
    Mm.426509.
    Mm.491250.

    Genome annotation databases

    EnsembliENSMUST00000032776; ENSMUSP00000032776; ENSMUSG00000030557. [Q60929-3]
    ENSMUST00000076325; ENSMUSP00000075664; ENSMUSG00000030557. [Q60929-3]
    ENSMUST00000107476; ENSMUSP00000103100; ENSMUSG00000030557. [Q60929-2]
    ENSMUST00000135493; ENSMUSP00000138566; ENSMUSG00000030557. [Q60929-1]
    ENSMUST00000156690; ENSMUSP00000117496; ENSMUSG00000030557. [Q60929-1]
    GeneIDi17258.
    KEGGimmu:17258.
    UCSCiuc009hif.2. mouse. [Q60929-1]
    uc009hih.2. mouse. [Q60929-2]
    uc009hii.2. mouse. [Q60929-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30823 mRNA. Translation: AAA74030.1 .
    AK132678 mRNA. Translation: BAE21297.1 .
    BC061128 mRNA. Translation: AAH61128.1 .
    BC096598 mRNA. Translation: AAH96598.1 .
    CCDSi CCDS39981.1. [Q60929-1 ]
    CCDS71979.1. [Q60929-3 ]
    CCDS71980.1. [Q60929-2 ]
    RefSeqi NP_001028885.1. NM_001033713.2. [Q60929-1 ]
    NP_001278120.1. NM_001291191.1. [Q60929-3 ]
    NP_001278121.1. NM_001291192.1. [Q60929-3 ]
    NP_001278124.1. NM_001291195.1. [Q60929-2 ]
    NP_001278125.1. NM_001291196.1.
    XP_006540749.1. XM_006540686.1. [Q60929-1 ]
    UniGenei Mm.132788.
    Mm.426509.
    Mm.491250.

    3D structure databases

    ProteinModelPortali Q60929.
    SMRi Q60929. Positions 2-73.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201381. 3 interactions.
    IntActi Q60929. 2 interactions.
    MINTi MINT-3155471.
    STRINGi 10090.ENSMUSP00000117496.

    PTM databases

    PhosphoSitei Q60929.

    Proteomic databases

    PaxDbi Q60929.
    PRIDEi Q60929.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032776 ; ENSMUSP00000032776 ; ENSMUSG00000030557 . [Q60929-3 ]
    ENSMUST00000076325 ; ENSMUSP00000075664 ; ENSMUSG00000030557 . [Q60929-3 ]
    ENSMUST00000107476 ; ENSMUSP00000103100 ; ENSMUSG00000030557 . [Q60929-2 ]
    ENSMUST00000135493 ; ENSMUSP00000138566 ; ENSMUSG00000030557 . [Q60929-1 ]
    ENSMUST00000156690 ; ENSMUSP00000117496 ; ENSMUSG00000030557 . [Q60929-1 ]
    GeneIDi 17258.
    KEGGi mmu:17258.
    UCSCi uc009hif.2. mouse. [Q60929-1 ]
    uc009hih.2. mouse. [Q60929-2 ]
    uc009hii.2. mouse. [Q60929-3 ]

    Organism-specific databases

    CTDi 4205.
    MGIi MGI:99532. Mef2a.

    Phylogenomic databases

    eggNOGi COG5068.
    GeneTreei ENSGT00390000011828.
    HOGENOMi HOG000230620.
    HOVERGENi HBG053944.
    InParanoidi Q60929.
    KOi K09260.
    OMAi RMDTWVT.
    OrthoDBi EOG793B7D.
    TreeFami TF314067.

    Enzyme and pathway databases

    Reactomei REACT_215063. ERK/MAPK targets.

    Miscellaneous databases

    ChiTaRSi MEF2A. mouse.
    NextBioi 291742.
    PROi Q60929.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60929.
    Bgeei Q60929.
    CleanExi MM_MEF2A.
    Genevestigatori Q60929.

    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. "The expression of MEF2 genes is implicated in CNS neuronal differentiation."
      Lin X., Shah S., Bulleit R.F.
      Brain Res. Mol. Brain Res. 42:307-316(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Cerebellum.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Testis.
    3. "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 1 AND 3).
      Strain: NMRI.
      Tissue: Brain and Mammary tumor.
    4. "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7."
      Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.
      J. Biol. Chem. 276:47496-47507(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC7.
    5. "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: TISSUE SPECIFICITY OF ISOFORMS.
    6. "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: INTERACTION WITH NLK, PHOSPHORYLATION AT THR-310.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND THR-108 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiMEF2A_MOUSE
    AccessioniPrimary (citable) accession number: Q60929
    Secondary accession number(s): Q3V155, Q4VA09, Q6P8Q3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3